<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Dang, Yan</style></author><author><style face="normal" font="default" size="100%">Holmes, Dawn E</style></author><author><style face="normal" font="default" size="100%">Zhao, Zhiqiang</style></author><author><style face="normal" font="default" size="100%">Woodard, Trevor L</style></author><author><style face="normal" font="default" size="100%">Zhang, Yaobin</style></author><author><style face="normal" font="default" size="100%">Sun, Dezhi</style></author><author><style face="normal" font="default" size="100%">Wang, Li-Ying</style></author><author><style face="normal" font="default" size="100%">Nevin, Kelly P</style></author><author><style face="normal" font="default" size="100%">Lovley, Derek R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Enhancing anaerobic digestion of complex organic waste with carbon-based conductive materials.</style></title><secondary-title><style face="normal" font="default" size="100%">Bioresour Technol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Bioresour Technol</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anaerobiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacteria</style></keyword><keyword><style  face="normal" font="default" size="100%">Bioreactors</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon Fiber</style></keyword><keyword><style  face="normal" font="default" size="100%">Charcoal</style></keyword><keyword><style  face="normal" font="default" size="100%">Dogs</style></keyword><keyword><style  face="normal" font="default" size="100%">Electric Conductivity</style></keyword><keyword><style  face="normal" font="default" size="100%">Fatty Acids, Volatile</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Methane</style></keyword><keyword><style  face="normal" font="default" size="100%">Organic Chemicals</style></keyword><keyword><style  face="normal" font="default" size="100%">Waste Products</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2016 Nov</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">220</style></volume><pages><style face="normal" font="default" size="100%">516-522</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The aim of this work was to study the methanogenic metabolism of dog food, a food waste surrogate, in laboratory-scale reactors with different carbon-based conductive materials. Carbon cloth, carbon felt, and granular activated carbon all permitted higher organic loading rates and promoted faster recovery of soured reactors than the control reactors. Microbial community analysis revealed that specific and substantial enrichments of Sporanaerobacter and Methanosarcina were present on the carbon cloth surface. These results, and the known ability of Sporanaerobacter species to transfer electrons to elemental sulfur, suggest that Sporanaerobacter species can participate in direct interspecies electron transfer with Methanosarcina species when carbon cloth is available as an electron transfer mediator.&lt;/p&gt;</style></abstract><custom1><style face="normal" font="default" size="100%">https://www.ncbi.nlm.nih.gov/pubmed/27611035?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rocha-Granados, Maria C</style></author><author><style face="normal" font="default" size="100%">Klingbeil, Michele M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Leishmania DNA Replication Timing: A Stochastic Event?</style></title><secondary-title><style face="normal" font="default" size="100%">Trends Parasitol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Trends Parasitol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication Timing</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug Delivery Systems</style></keyword><keyword><style  face="normal" font="default" size="100%">Genomic Instability</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Leishmania</style></keyword><keyword><style  face="normal" font="default" size="100%">Leishmaniasis</style></keyword><keyword><style  face="normal" font="default" size="100%">Replication Origin</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2016 10</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">32</style></volume><pages><style face="normal" font="default" size="100%">755-757</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;For eukaryotic genomes, DNA synthesis initiates at multiple discrete regions known as replication origins in a dynamic yet regulated manner to ensure genomic stability. Two recent studies using different approaches reveal few Leishmania origins and that origin firing may proceed in a mainly stochastic manner.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Wang, David T</style></author><author><style face="normal" font="default" size="100%">Gruen, Danielle S</style></author><author><style face="normal" font="default" size="100%">Lollar, Barbara Sherwood</style></author><author><style face="normal" font="default" size="100%">Hinrichs, Kai-Uwe</style></author><author><style face="normal" font="default" size="100%">Stewart, Lucy C</style></author><author><style face="normal" font="default" size="100%">Holden, James F</style></author><author><style face="normal" font="default" size="100%">Hristov, Alexander N</style></author><author><style face="normal" font="default" size="100%">Pohlman, John W</style></author><author><style face="normal" font="default" size="100%">Morrill, Penny L</style></author><author><style face="normal" font="default" size="100%">Könneke, Martin</style></author><author><style face="normal" font="default" size="100%">Delwiche, Kyle B</style></author><author><style face="normal" font="default" size="100%">Reeves, Eoghan P</style></author><author><style face="normal" font="default" size="100%">Sutcliffe, Chelsea N</style></author><author><style face="normal" font="default" size="100%">Ritter, Daniel J</style></author><author><style face="normal" font="default" size="100%">Seewald, Jeffrey S</style></author><author><style face="normal" font="default" size="100%">McIntosh, Jennifer C</style></author><author><style face="normal" font="default" size="100%">Hemond, Harold F</style></author><author><style face="normal" font="default" size="100%">Kubo, Michael D</style></author><author><style face="normal" font="default" size="100%">Cardace, Dawn</style></author><author><style face="normal" font="default" size="100%">Hoehler, Tori M</style></author><author><style face="normal" font="default" size="100%">Ono, Shuhei</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Methane cycling. Nonequilibrium clumped isotope signals in microbial methane.</style></title><secondary-title><style face="normal" font="default" size="100%">Science</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Science</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon Cycle</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon Isotopes</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Groundwater</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen</style></keyword><keyword><style  face="normal" font="default" size="100%">Methane</style></keyword><keyword><style  face="normal" font="default" size="100%">Methanomicrobiales</style></keyword><keyword><style  face="normal" font="default" size="100%">Temperature</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2015 Apr 24</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">348</style></volume><pages><style face="normal" font="default" size="100%">428-31</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Methane is a key component in the global carbon cycle, with a wide range of anthropogenic and natural sources. Although isotopic compositions of methane have traditionally aided source identification, the abundance of its multiply substituted &quot;clumped&quot; isotopologues (for example, (13)CH3D) has recently emerged as a proxy for determining methane-formation temperatures. However, the effect of biological processes on methane's clumped isotopologue signature is poorly constrained. We show that methanogenesis proceeding at relatively high rates in cattle, surface environments, and laboratory cultures exerts kinetic control on (13)CH3D abundances and results in anomalously elevated formation-temperature estimates. We demonstrate quantitatively that H2 availability accounts for this effect. Clumped methane thermometry can therefore provide constraints on the generation of methane in diverse settings, including continental serpentinization sites and ancient, deep groundwaters.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6233</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/25745067?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Shanmugam, Raghuvaran</style></author><author><style face="normal" font="default" size="100%">Aklujkar, Muktak</style></author><author><style face="normal" font="default" size="100%">Schäfer, Matthias</style></author><author><style face="normal" font="default" size="100%">Reinhardt, Richard</style></author><author><style face="normal" font="default" size="100%">Nickel, Olaf</style></author><author><style face="normal" font="default" size="100%">Reuter, Gunter</style></author><author><style face="normal" font="default" size="100%">Lovley, Derek R</style></author><author><style face="normal" font="default" size="100%">Ehrenhofer-Murray, Ann</style></author><author><style face="normal" font="default" size="100%">Nellen, Wolfgang</style></author><author><style face="normal" font="default" size="100%">Ankri, Serge</style></author><author><style face="normal" font="default" size="100%">Helm, Mark</style></author><author><style face="normal" font="default" size="100%">Jurkowski, Tomasz P</style></author><author><style face="normal" font="default" size="100%">Jeltsch, Albert</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The Dnmt2 RNA methyltransferase homolog of Geobacter sulfurreducens specifically methylates tRNA-Glu.</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Geobacter</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Methylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Nucleic Acid Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Transfer, Asp</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Transfer, Glu</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">tRNA Methyltransferases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">42</style></volume><pages><style face="normal" font="default" size="100%">6487-96</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Dnmt2 enzymes are conserved in eukaryotes, where they methylate C38 of tRNA-Asp with high activity. Here, the activity of one of the very few prokaryotic Dnmt2 homologs from Geobacter species (GsDnmt2) was investigated. GsDnmt2 was observed to methylate tRNA-Asp from flies and mice. Unexpectedly, it had only a weak activity toward its matching Geobacter tRNA-Asp, but methylated Geobacter tRNA-Glu with good activity. In agreement with this result, we show that tRNA-Glu is methylated in Geobacter while the methylation is absent in tRNA-Asp. The activities of Dnmt2 enzymes from Homo sapiens, Drosophila melanogaster, Schizosaccharomyces pombe and Dictyostelium discoideum for methylation of the Geobacter tRNA-Asp and tRNA-Glu were determined showing that all these Dnmt2s preferentially methylate tRNA-Asp. Hence, the GsDnmt2 enzyme has a swapped transfer ribonucleic acid (tRNA) specificity. By comparing the different tRNAs, a characteristic sequence pattern was identified in the variable loop of all preferred tRNA substrates. An exchange of two nucleotides in the variable loop of murine tRNA-Asp converted it to the corresponding variable loop of tRNA-Glu and led to a strong reduction of GsDnmt2 activity. Interestingly, the same loss of activity was observed with human DNMT2, indicating that the variable loop functions as a specificity determinant in tRNA recognition of Dnmt2 enzymes.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">https://www.ncbi.nlm.nih.gov/pubmed/24711368?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author><author><style face="normal" font="default" size="100%">Bertozzi, Carolyn R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mycobacterial lipid logic.</style></title><secondary-title><style face="normal" font="default" size="100%">Cell Host Microbe</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Cell Host Microbe</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Immune Evasion</style></keyword><keyword><style  face="normal" font="default" size="100%">Macrophages</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Lipids</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014 Jan 15</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">15</style></volume><pages><style face="normal" font="default" size="100%">1-2</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;During infection of the lung epithelium, Mycobacterium tuberculosis must infect and survive within macrophages long enough to be transported into deeper lung tissues. Cambier et al. (2013) show that pathogenic mycobacteria use the coordinated action of two cell wall glycolipids to regulate macrophage recruitment to initial infection sites.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/24439891?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sha, Kai</style></author><author><style face="normal" font="default" size="100%">Choi, Seung-Hoon</style></author><author><style face="normal" font="default" size="100%">Im, Jeongdae</style></author><author><style face="normal" font="default" size="100%">Lee, Gyunghee G</style></author><author><style face="normal" font="default" size="100%">Loeffler, Frank</style></author><author><style face="normal" font="default" size="100%">Park, Jae H</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Regulation of ethanol-related behavior and ethanol metabolism by the Corazonin neurons and Corazonin receptor in Drosophila melanogaster.</style></title><secondary-title><style face="normal" font="default" size="100%">PLoS One</style></secondary-title><alt-title><style face="normal" font="default" size="100%">PLoS ONE</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acetaldehyde</style></keyword><keyword><style  face="normal" font="default" size="100%">Alcohol Dehydrogenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Aldehyde Dehydrogenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Alleles</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cyclic AMP-Dependent Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Drosophila melanogaster</style></keyword><keyword><style  face="normal" font="default" size="100%">Drosophila Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Ethanol</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Reporter</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Neurons</style></keyword><keyword><style  face="normal" font="default" size="100%">Neuropeptides</style></keyword><keyword><style  face="normal" font="default" size="100%">Phenotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Neuropeptide</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Messenger</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription, Genetic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">e87062</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Impaired ethanol metabolism can lead to various alcohol-related health problems. Key enzymes in ethanol metabolism are alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH); however, neuroendocrine pathways that regulate the activities of these enzymes are largely unexplored. Here we identified a neuroendocrine system involving Corazonin (Crz) neuropeptide and its receptor (CrzR) as important physiological regulators of ethanol metabolism in Drosophila. Crz-cell deficient (Crz-CD) flies displayed significantly delayed recovery from ethanol-induced sedation that we refer to as hangover-like phenotype. Newly generated mutant lacking Crz Receptor (CrzR(01) ) and CrzR-knockdown flies showed even more severe hangover-like phenotype, which is causally associated with fast accumulation of acetaldehyde in the CrzR(01) mutant following ethanol exposure. Higher levels of acetaldehyde are likely due to 30% reduced ALDH activity in the mutants. Moreover, increased ADH activity was found in the CrzR(01) mutant, but not in the Crz-CD flies. Quantitative RT-PCR revealed transcriptional upregulation of Adh gene in the CrzR(01) . Transgenic inhibition of cyclic AMP-dependent protein kinase (PKA) also results in significantly increased ADH activity and Adh mRNA levels, indicating PKA-dependent transcriptional regulation of Adh by CrzR. Furthermore, inhibition of PKA or cAMP response element binding protein (CREB) in CrzR cells leads to comparable hangover-like phenotype to the CrzR(01) mutant. These findings suggest that CrzR-associated signaling pathway is critical for ethanol detoxification via Crz-dependent regulation of ALDH activity and Crz-independent transcriptional regulation of ADH. Our study provides new insights into the neuroendocrine-associated ethanol-related behavior and metabolism.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/24489834?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hensley, Sarah A</style></author><author><style face="normal" font="default" size="100%">Jung, Jong-Hyun</style></author><author><style face="normal" font="default" size="100%">Park, Cheon-Seok</style></author><author><style face="normal" font="default" size="100%">Holden, James F</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov. of hyperthermophilic heterotrophs from deep-sea hydrothermal vents.</style></title><secondary-title><style face="normal" font="default" size="100%">Int J Syst Evol Microbiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Int. J. Syst. Evol. Microbiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Archaeal</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrothermal Vents</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Pacific Ocean</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Polychaeta</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Ribosomal, 16S</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Analysis, DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermococcus</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2014</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2014 Nov</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">64</style></volume><pages><style face="normal" font="default" size="100%">3655-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Two heterotrophic hyperthermophilic strains, ES1(T) and CL1(T), were isolated from Paralvinella sp. polychaete worms collected from active hydrothermal vent chimneys in the north-eastern Pacific Ocean. Both were obligately anaerobic and produced H2S in the presence of elemental sulfur and H2. Complete genome sequences are available for both strains. Phylogenetic analyses based on 16S rRNA gene sequences showed that the strains are more than 97% similar to most other species of the genus Thermococcus. Therefore, overall genome relatedness index analyses were performed to establish that these strains are novel species. For each analysis, strain ES1(T) was determined to be most similar to Thermococcus barophilus MP(T), while strain CL1(T) was determined to be most similar to Thermococcus sp. 4557. The average nucleotide identity scores for these strains were 84% for strain ES1(T) and 81% for strain CL1(T), genome-to-genome direct comparison scores were 23% for strain ES1(T) and 47% for strain CL1(T), and the species identification scores were 89% for strain ES1(T) and 88% for strain CL1(T). For each analysis, strains ES1(T) and CL1(T) were below the species delineation cut-off. Therefore, based on their whole genome sequences, strains ES1(T) and CL1(T) are suggested to represent novel species of the genus Thermococcus for which the names Thermococcus paralvinellae sp. nov. and Thermococcus cleftensis sp. nov. are proposed, respectively. The type strains are ES1(T) ( =DSM 27261(T) =KACC 17923(T)) and CL1(T) ( =DSM 27260(T) =KACC 17922(T)).&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">Pt 11</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rodrigues, Jorge L M</style></author><author><style face="normal" font="default" size="100%">Pellizari, Vivian H</style></author><author><style face="normal" font="default" size="100%">Mueller, Rebecca</style></author><author><style face="normal" font="default" size="100%">Baek, Kyunghwa</style></author><author><style face="normal" font="default" size="100%">Jesus, Ederson da C</style></author><author><style face="normal" font="default" size="100%">Paula, Fabiana S</style></author><author><style face="normal" font="default" size="100%">Mirza, Babur</style></author><author><style face="normal" font="default" size="100%">Hamaoui, George S</style></author><author><style face="normal" font="default" size="100%">Tsai, Siu Mui</style></author><author><style face="normal" font="default" size="100%">Feigl, Brigitte</style></author><author><style face="normal" font="default" size="100%">Tiedje, James M</style></author><author><style face="normal" font="default" size="100%">Bohannan, Brendan J M</style></author><author><style face="normal" font="default" size="100%">Nüsslein, Klaus</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Conversion of the Amazon rainforest to agriculture results in biotic homogenization of soil bacterial communities.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Agriculture</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacteria</style></keyword><keyword><style  face="normal" font="default" size="100%">Biodiversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Brazil</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Ecosystem</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Rain</style></keyword><keyword><style  face="normal" font="default" size="100%">Soil Microbiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Trees</style></keyword><keyword><style  face="normal" font="default" size="100%">Tropical Climate</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2013 Jan 15</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">110</style></volume><pages><style face="normal" font="default" size="100%">988-93</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The Amazon rainforest is the Earth&amp;#39;s largest reservoir of plant and animal diversity, and it has been subjected to especially high rates of land use change, primarily to cattle pasture. This conversion has had a strongly negative effect on biological diversity, reducing the number of plant and animal species and homogenizing communities. We report here that microbial biodiversity also responds strongly to conversion of the Amazon rainforest, but in a manner different from plants and animals. Local taxonomic and phylogenetic diversity of soil bacteria increases after conversion, but communities become more similar across space. This homogenization is driven by the loss of forest soil bacteria with restricted ranges (endemics) and results in a net loss of diversity. This study shows homogenization of microbial communities in response to human activities. Given that soil microbes represent the majority of biodiversity in terrestrial ecosystems and are intimately involved in ecosystem functions, we argue that microbial biodiversity loss should be taken into account when assessing the impact of land use change in tropical forests.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Burand, John P</style></author><author><style face="normal" font="default" size="100%">Kim, Woojin</style></author><author><style face="normal" font="default" size="100%">Afonso, Claudio L</style></author><author><style face="normal" font="default" size="100%">Tulman, Edan R</style></author><author><style face="normal" font="default" size="100%">Kutish, Gerald F</style></author><author><style face="normal" font="default" size="100%">Lu, Zhiqiang</style></author><author><style face="normal" font="default" size="100%">Rock, Daniel L</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Analysis of the genome of the sexually transmitted insect virus Helicoverpa zea nudivirus 2.</style></title><secondary-title><style face="normal" font="default" size="100%">Viruses</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Viruses</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Baculoviridae</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Evolution</style></keyword><keyword><style  face="normal" font="default" size="100%">Consensus Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Open Reading Frames</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012 Jan</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">28-61</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The sexually transmitted insect virus Helicoverpa zea nudivirus 2 (HzNV-2) was determined to have a circular double-stranded DNA genome of 231,621 bp coding for an estimated 113 open reading frames (ORFs). HzNV-2 is most closely related to the nudiviruses, a sister group of the insect baculoviruses. Several putative ORFs that share homology with the baculovirus core genes were identified in the viral genome. However, HzNV-2 lacks several key genetic features of baculoviruses including the late transcriptional regulation factor, LEF-1 and the palindromic hrs, which serve as origins of replication. The HzNV-2 genome was found to code for three ORFs that had significant sequence homology to cellular genes which are not generally found in viral genomes. These included a presumed juvenile hormone esterase gene, a gene coding for a putative zinc-dependent matrix metalloprotease, and a major facilitator superfamily protein gene; all of which are believed to play a role in the cellular proliferation and the tissue hypertrophy observed in the malformation of reproductive organs observed in HzNV-2 infected corn earworm moths, Helicoverpa zea.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/22355451?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jung, Jong-Hyun</style></author><author><style face="normal" font="default" size="100%">Holden, James F</style></author><author><style face="normal" font="default" size="100%">Seo, Dong-Ho</style></author><author><style face="normal" font="default" size="100%">Park, Kwan-Hwa</style></author><author><style face="normal" font="default" size="100%">Shin, Hakdong</style></author><author><style face="normal" font="default" size="100%">Ryu, Sangryeol</style></author><author><style face="normal" font="default" size="100%">Lee, Ju-Hoon</style></author><author><style face="normal" font="default" size="100%">Park, Cheon-Seok</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Complete genome sequence of the hyperthermophilic archaeon Thermococcus sp. strain CL1, isolated from a Paralvinella sp. polychaete worm collected from a hydrothermal vent.</style></title><secondary-title><style face="normal" font="default" size="100%">J Bacteriol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Bacteriol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromosome Mapping</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Archaeal</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Ribosomal</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrothermal Vents</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Polychaeta</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Analysis, DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermococcus</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">194</style></volume><pages><style face="normal" font="default" size="100%">4769-70</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Thermococcus sp. strain CL1 is a hyperthermophilic, anaerobic, and heterotrophic archaeon isolated from a Paralvinella sp. polychaete worm living on an active deep-sea hydrothermal sulfide chimney on the Cleft Segment of the Juan de Fuca Ridge. To further understand the distinct characteristics of this archaeon at the genome level, its genome was completely sequenced and analyzed. Here, we announce the complete genome sequence (1,950,313 bp) of Thermococcus sp. strain CL1, with a focus on H(2)- and energy-producing capabilities and its amino acid biosynthesis and acquisition in an extreme habitat.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">17</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/22887670?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kuksin, Dmitry</style></author><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoplasm</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Fluorescence</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Assembly</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">86</style></volume><pages><style face="normal" font="default" size="100%">1555-62</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The nonenveloped polyomavirus simian virus 40 (SV40) is taken up into cells by a caveola-mediated endocytic process that delivers the virus to the endoplasmic reticulum (ER). Within the ER lumen, the capsid undergoes partial disassembly, which exposes its internal capsid proteins VP2 and VP3 to immunostaining with antibodies. We demonstrate here that the SV40 genome does not become accessible to detection while the virus is in the ER. Instead, the genome becomes accessible two distinct detection procedures, one using anti-bromodeoxyuridine antibodies and the other using a 5-ethynyl-2-deoxyuridine-based chemical reaction, only after the emergence of partially disassembled SV40 particles in the cytoplasm. These cytoplasmic particles retain some of the SV40 capsid proteins, VP1, VP2, and VP3, in addition to the viral genome. Thus, SV40 particles undergo discrete disassembly steps during entry that are separated temporally and topologically. First, a partial disassembly of the particles occurs in the ER, which exposes internal capsid proteins VP2 and VP3. Then, in the cytoplasm, disassembly progresses further to also make the genomic DNA accessible to immune detection.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/22090139?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Burand, John P</style></author><author><style face="normal" font="default" size="100%">Kim, Woojin</style></author><author><style face="normal" font="default" size="100%">Welch, Anna</style></author><author><style face="normal" font="default" size="100%">Elkinton, Joseph S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Identification of a nucleopolyhedrovirus in winter moth populations from Massachusetts.</style></title><secondary-title><style face="normal" font="default" size="100%">J Invertebr Pathol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Invertebr. Pathol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Environmental Monitoring</style></keyword><keyword><style  face="normal" font="default" size="100%">Larva</style></keyword><keyword><style  face="normal" font="default" size="100%">Massachusetts</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Nucleopolyhedrovirus</style></keyword><keyword><style  face="normal" font="default" size="100%">Viral Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Diseases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011 Nov</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">108</style></volume><pages><style face="normal" font="default" size="100%">217-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Winter moth, Operophtera brumata, originally from Europe, has invaded eastern Massachusetts causing widespread defoliation and damage to many deciduous tree species and a variety of crop plants in the infested area. We identified O. brumata nucleopolyhedrovirus (OpbuNPV) in winter moth larvae collected from field sites in Massachusetts by using PCR to amplify a 482 bp region of the baculovirus polyhedrin gene. Viral sequences were also detected in winter moth pupae that failed to emerge, suggesting that these insects may have died as a result of viral infection. This represents the first report of OpbuNPV in winter moth populations in the US.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/21893065?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Xu, Guang</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Resolving the phylogeny of malaria parasites.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Parasites</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2011 Aug 9</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">108</style></volume><pages><style face="normal" font="default" size="100%">12973-4</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">32</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/21804030?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sandler, Simon J I</style></author><author><style face="normal" font="default" size="100%">Figaji, Anthony A</style></author><author><style face="normal" font="default" size="100%">Adelson, P David</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Clinical applications of biomarkers in pediatric traumatic brain injury.</style></title><secondary-title><style face="normal" font="default" size="100%">Childs Nerv Syst</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Childs Nerv Syst</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Markers</style></keyword><keyword><style  face="normal" font="default" size="100%">Brain Injuries</style></keyword><keyword><style  face="normal" font="default" size="100%">Child</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">26</style></volume><pages><style face="normal" font="default" size="100%">205-13</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">INTRODUCTION: The diagnosis, treatment, and prediction of outcome in pediatric traumatic brain injury (TBI) present significant challenges to the treating clinician. Clinical and radiological tools for assessing injury severity and predicting outcome, in particular, lack sensitivity and specificity. In patients with mild TBI, often there is uncertainty about which patients should undergo radiological imaging and who is at risk for long term neurological sequelae. In severe TBI, often there is uncertainty about which patients will experience secondary insults and what the outcome for individual patients will be. In several other clinical specialties, biomarkers are used to diagnose disease, direct treatment, and prognosticate. However, an ideal biomarker for brain injury has not been found.

METHODS: In this review, we examine the various factors that must be taken into account in the search for a reliable biomarker in brain injury. We review the important studies that have investigated common biomarkers of structural brain injury, in particular S100B, neuron-specific enolase, myelin basic protein, and glial fibrillary acid protein.

DISCUSSION: The potential uses and limitations of these biomarkers in the context of TBI are discussed.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19902222?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ver Eecke, Helene C</style></author><author><style face="normal" font="default" size="100%">Kelley, Deborah S</style></author><author><style face="normal" font="default" size="100%">Holden, James F</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Abundances of hyperthermophilic autotrophic Fe(III) oxide reducers and heterotrophs in hydrothermal sulfide chimneys of the northeastern Pacific Ocean.</style></title><secondary-title><style face="normal" font="default" size="100%">Appl Environ Microbiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Appl. Environ. Microbiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Biodiversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Ferric Compounds</style></keyword><keyword><style  face="normal" font="default" size="100%">Hot Springs</style></keyword><keyword><style  face="normal" font="default" size="100%">Methane</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Pacific Ocean</style></keyword><keyword><style  face="normal" font="default" size="100%">Polychaeta</style></keyword><keyword><style  face="normal" font="default" size="100%">Seawater</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Jan</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">75</style></volume><pages><style face="normal" font="default" size="100%">242-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The abundances of hyperthermophilic heterotrophs, methanogens, and autotrophic reducers of amorphous Fe(III) oxide in 18 samples of deep-sea hydrothermal vent sulfide chimneys of the Endeavour Segment were measured. The results indicate that conditions favor the growth of iron reducers toward the interiors of these deposits and that of heterotrophs toward the outer surfaces near high-temperature polychaete worms (Paralvinella sulfincola).&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/18978076?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Walk, Seth T</style></author><author><style face="normal" font="default" size="100%">Xu, Guang</style></author><author><style face="normal" font="default" size="100%">Stull, Jason W</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Correlation between tick density and pathogen endemicity, New Hampshire.</style></title><secondary-title><style face="normal" font="default" size="100%">Emerg Infect Dis</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Emerging Infect. Dis.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anaplasma phagocytophilum</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Arachnid Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">Babesia microti</style></keyword><keyword><style  face="normal" font="default" size="100%">Babesiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Biosurveillance</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia burgdorferi</style></keyword><keyword><style  face="normal" font="default" size="100%">Communicable Diseases, Emerging</style></keyword><keyword><style  face="normal" font="default" size="100%">Ehrlichiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Ixodes</style></keyword><keyword><style  face="normal" font="default" size="100%">Lyme Disease</style></keyword><keyword><style  face="normal" font="default" size="100%">New Hampshire</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">15</style></volume><pages><style face="normal" font="default" size="100%">585-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">To assess the endemicity of tick-borne pathogens in New Hampshire, we surveyed adult tick vectors. Pathogens were more prevalent in areas of high tick density, suggesting a correlation between tick establishment and pathogen endemicity. Infection rates in ticks correlated with disease frequency in humans.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19331738?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ishikawa, Eri</style></author><author><style face="normal" font="default" size="100%">Ishikawa, Tetsuaki</style></author><author><style face="normal" font="default" size="100%">Morita, Yasu S</style></author><author><style face="normal" font="default" size="100%">Toyonaga, Kenji</style></author><author><style face="normal" font="default" size="100%">Yamada, Hisakata</style></author><author><style face="normal" font="default" size="100%">Takeuchi, Osamu</style></author><author><style face="normal" font="default" size="100%">Kinoshita, Taroh</style></author><author><style face="normal" font="default" size="100%">Akira, Shizuo</style></author><author><style face="normal" font="default" size="100%">Yoshikai, Yasunobu</style></author><author><style face="normal" font="default" size="100%">Yamasaki, Sho</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle.</style></title><secondary-title><style face="normal" font="default" size="100%">J Exp Med</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Exp. Med.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cord Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Granuloma</style></keyword><keyword><style  face="normal" font="default" size="100%">Lectins, C-Type</style></keyword><keyword><style  face="normal" font="default" size="100%">Ligands</style></keyword><keyword><style  face="normal" font="default" size="100%">Lung Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Macrophage Activation</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Inbred C57BL</style></keyword><keyword><style  face="normal" font="default" size="100%">Myeloid Differentiation Factor 88</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, IgG</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Dec 21</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">206</style></volume><pages><style face="normal" font="default" size="100%">2879-88</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Tuberculosis remains a fatal disease caused by Mycobacterium tuberculosis, which contains various unique components that affect the host immune system. Trehalose-6,6'-dimycolate (TDM; also called cord factor) is a mycobacterial cell wall glycolipid that is the most studied immunostimulatory component of M. tuberculosis. Despite five decades of research on TDM, its host receptor has not been clearly identified. Here, we demonstrate that macrophage inducible C-type lectin (Mincle) is an essential receptor for TDM. Heat-killed mycobacteria activated Mincle-expressing cells, but the activity was lost upon delipidation of the bacteria; analysis of the lipid extracts identified TDM as a Mincle ligand. TDM activated macrophages to produce inflammatory cytokines and nitric oxide, which are completely suppressed in Mincle-deficient macrophages. In vivo TDM administration induced a robust elevation of inflammatory cytokines in sera and characteristic lung inflammation, such as granuloma formation. However, no TDM-induced lung granuloma was formed in Mincle-deficient mice. Whole mycobacteria were able to activate macrophages even in MyD88-deficient background, but the activation was significantly diminished in Mincle/MyD88 double-deficient macrophages. These results demonstrate that Mincle is an essential receptor for the mycobacterial glycolipid, TDM.</style></abstract><issue><style face="normal" font="default" size="100%">13</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20008526?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Junglen, S</style></author><author><style face="normal" font="default" size="100%">Kurth, A</style></author><author><style face="normal" font="default" size="100%">Kuehl, H</style></author><author><style face="normal" font="default" size="100%">Quan, P-L</style></author><author><style face="normal" font="default" size="100%">Ellerbrok, H</style></author><author><style face="normal" font="default" size="100%">Pauli, G</style></author><author><style face="normal" font="default" size="100%">Nitsche, A</style></author><author><style face="normal" font="default" size="100%">Nunn, C</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Lipkin, W I</style></author><author><style face="normal" font="default" size="100%">Briese, T</style></author><author><style face="normal" font="default" size="100%">Leendertz, F H</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Examining landscape factors influencing relative distribution of mosquito genera and frequency of virus infection.</style></title><secondary-title><style face="normal" font="default" size="100%">Ecohealth</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Ecohealth</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Africa, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Culicidae</style></keyword><keyword><style  face="normal" font="default" size="100%">Ecosystem</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Population Surveillance</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Trees</style></keyword><keyword><style  face="normal" font="default" size="100%">Tropical Climate</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">6</style></volume><pages><style face="normal" font="default" size="100%">239-49</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Mosquito-borne infections cause some of the most debilitating human diseases, including yellow fever and malaria, yet we lack an understanding of how disease risk scales with human-driven habitat changes. We present an approach to study variation in mosquito distribution and concomitant viral infections on the landscape level. In a pilot study we analyzed mosquito distribution along a 10-km transect of a West African rainforest area, which included primary forest, secondary forest, plantations, and human settlements. Variation was observed in the abundance of Anopheles, Aedes, Culex, and Uranotaenia mosquitoes between the different habitat types. Screening of trapped mosquitoes from the different habitats led to the isolation of five uncharacterized viruses of the families Bunyaviridae, Coronaviridae, Flaviviridae, and Rhabdoviridae, as well as an unclassified virus. Polymerase chain reaction screening for these five viruses in individual mosquitoes indicated a trend toward infection with specific viruses in specific mosquito genera that differed by habitat. Based on these initial analyses, we believe that further work is indicated to investigate the impact of anthropogenic landscape changes on mosquito distribution and accompanying arbovirus infection.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19915916?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Abd-Alla, Adly M M</style></author><author><style face="normal" font="default" size="100%">Vlak, J M</style></author><author><style face="normal" font="default" size="100%">Bergoin, M</style></author><author><style face="normal" font="default" size="100%">Maruniak, J E</style></author><author><style face="normal" font="default" size="100%">Parker, A</style></author><author><style face="normal" font="default" size="100%">Burand, J P</style></author><author><style face="normal" font="default" size="100%">Jehle, J A</style></author><author><style face="normal" font="default" size="100%">Boucias, D G</style></author></authors><translated-authors><author><style face="normal" font="default" size="100%">Hytrosavirus Study Group of the ICTV</style></author></translated-authors></contributors><titles><title><style face="normal" font="default" size="100%">Hytrosaviridae: a proposal for classification and nomenclature of a new insect virus family.</style></title><secondary-title><style face="normal" font="default" size="100%">Arch Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Arch. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Diptera</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Circular</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Salivary Glands</style></keyword><keyword><style  face="normal" font="default" size="100%">Terminology as Topic</style></keyword><keyword><style  face="normal" font="default" size="100%">Virion</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">154</style></volume><pages><style face="normal" font="default" size="100%">909-18</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Salivary gland hypertrophy viruses (SGHVs) have been identified from different dipteran species, such as the tsetse fly Glossina pallidipes (GpSGHV), the housefly Musca domestica (MdSGHV) and the narcissus bulbfly Merodon equestris (MeSGHV). These viruses share the following characteristics: (i) they produce non-occluded, enveloped, rod-shaped virions that measure 500-1,000 nm in length and 50-100 nm in diameter; (ii) they possess a large circular double-stranded DNA (dsDNA) genome ranging in size from 120 to 190 kbp and having G + C ratios ranging from 28 to 44%; (iii) they cause overt salivary gland hypertrophy (SGH) symptoms in dipteran adults and partial to complete sterility. The available information on the complete genome sequence of GpSGHV and MdSGHV indicates significant co-linearity between the two viral genomes, whereas no co-linearity was observed with baculoviruses, ascoviruses, entomopoxviruses, iridoviruses and nudiviruses, other large invertebrate DNA viruses. The DNA polymerases encoded by the SGHVs are of the type B and closely related, but they are phylogenetically distant from DNA polymerases encoded by other large dsDNA viruses. The great majority of SGHV ORFs could not be assigned by sequence comparison. Phylogenetic analysis of conserved genes clustered both SGHVs, but distantly from the nudiviruses and baculoviruses. On the basis of the available morphological, (patho)biological, genomic and phylogenetic data, we propose that the two viruses are members of a new virus family named Hytrosaviridae. This proposed family currently comprises two unassigned species, G. pallidipes salivary gland hypertrophy virus and M. domestica salivary gland hypertrophy virus, and a tentative unassigned species, M. equestris salivary gland hypertrophy virus. Here, we present the characteristics and the justification for establishing this new virus family.</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19458899?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Siegrist, M Sloan</style></author><author><style face="normal" font="default" size="100%">Unnikrishnan, Meera</style></author><author><style face="normal" font="default" size="100%">McConnell, Matthew J</style></author><author><style face="normal" font="default" size="100%">Borowsky, Mark</style></author><author><style face="normal" font="default" size="100%">Cheng, Tan-Yun</style></author><author><style face="normal" font="default" size="100%">Siddiqi, Noman</style></author><author><style face="normal" font="default" size="100%">Fortune, Sarah M</style></author><author><style face="normal" font="default" size="100%">Moody, D Branch</style></author><author><style face="normal" font="default" size="100%">Rubin, Eric J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron</style></keyword><keyword><style  face="normal" font="default" size="100%">Macrophages</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium</style></keyword><keyword><style  face="normal" font="default" size="100%">Mycobacterium Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxazoles</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Secretory Pathway</style></keyword><keyword><style  face="normal" font="default" size="100%">Siderophores</style></keyword><keyword><style  face="normal" font="default" size="100%">Transcription, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Up-Regulation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Nov 3</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">106</style></volume><pages><style face="normal" font="default" size="100%">18792-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The Esx secretion pathway is conserved across Gram-positive bacteria. Esx-1, the best-characterized system, is required for virulence of Mycobacterium tuberculosis, although its precise function during infection remains unclear. Esx-3, a paralogous system present in all mycobacterial species, is required for growth in vitro. Here, we demonstrate that mycobacteria lacking Esx-3 are defective in acquiring iron. To compete for the limited iron available in the host and the environment, these organisms use mycobactin, high-affinity iron-binding molecules. In the absence of Esx-3, mycobacteria synthesize mycobactin but are unable to use the bound iron and are impaired severely for growth during macrophage infection. Mycobacteria thus require a specialized secretion system for acquiring iron from siderophores.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">44</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19846780?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Leendertz, Fabian H</style></author><author><style face="normal" font="default" size="100%">Xu, Guang</style></author><author><style face="normal" font="default" size="100%">LeBreton, Matthew</style></author><author><style face="normal" font="default" size="100%">Djoko, Cyrille F</style></author><author><style face="normal" font="default" size="100%">Aminake, Makoah N</style></author><author><style face="normal" font="default" size="100%">Takang, Eric E</style></author><author><style face="normal" font="default" size="100%">Diffo, Joseph L D</style></author><author><style face="normal" font="default" size="100%">Pike, Brian L</style></author><author><style face="normal" font="default" size="100%">Rosenthal, Benjamin M</style></author><author><style face="normal" font="default" size="100%">Formenty, Pierre</style></author><author><style face="normal" font="default" size="100%">Boesch, Christophe</style></author><author><style face="normal" font="default" size="100%">Ayala, Francisco J</style></author><author><style face="normal" font="default" size="100%">Wolfe, Nathan D</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The origin of malignant malaria.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">N-Acetylneuraminic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Pan troglodytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Infections, Animal</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Sep 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">106</style></volume><pages><style face="normal" font="default" size="100%">14902-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Plasmodium falciparum, the causative agent of malignant malaria, is among the most severe human infectious diseases. The closest known relative of P. falciparum is a chimpanzee parasite, Plasmodium reichenowi, of which one single isolate was previously known. The co-speciation hypothesis suggests that both parasites evolved separately from a common ancestor over the last 5-7 million years, in parallel with the divergence of their hosts, the hominin and chimpanzee lineages. Genetic analysis of eight new isolates of P. reichenowi, from wild and wild-born captive chimpanzees in Cameroon and Côte d'Ivoire, shows that P. reichenowi is a geographically widespread and genetically diverse chimpanzee parasite. The genetic lineage comprising the totality of global P. falciparum is fully included within the much broader genetic diversity of P. reichenowi. This finding is inconsistent with the co-speciation hypothesis. Phylogenetic analysis indicates that all extant P. falciparum populations originated from P. reichenowi, likely by a single host transfer, which may have occurred as early as 2-3 million years ago, or as recently as 10,000 years ago. The evolutionary history of this relationship may be explained by two critical genetic mutations. First, inactivation of the CMAH gene in the human lineage rendered human ancestors unable to generate the sialic acid Neu5Gc from its precursor Neu5Ac, and likely made humans resistant to P. reichenowi. More recently, mutations in the dominant invasion receptor EBA 175 in the P. falciparum lineage provided the parasite with preference for the overabundant Neu5Ac precursor, accounting for its extreme human pathogenicity.</style></abstract><issue><style face="normal" font="default" size="100%">35</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19666593?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Welch, Anna</style></author><author><style face="normal" font="default" size="100%">Drummond, Francis</style></author><author><style face="normal" font="default" size="100%">Tewari, Sunil</style></author><author><style face="normal" font="default" size="100%">Averill, Anne</style></author><author><style face="normal" font="default" size="100%">Burand, John P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Presence and prevalence of viruses in local and migratory honeybees (Apis mellifera) in Massachusetts.</style></title><secondary-title><style face="normal" font="default" size="100%">Appl Environ Microbiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Appl. Environ. Microbiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Beekeeping</style></keyword><keyword><style  face="normal" font="default" size="100%">Bees</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Massachusetts</style></keyword><keyword><style  face="normal" font="default" size="100%">Reverse Transcriptase Polymerase Chain Reaction</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Dec</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">75</style></volume><pages><style face="normal" font="default" size="100%">7862-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Migratory and local bees in Massachusetts were analyzed for seven viruses. Three were detected: black queen cell virus (BQCV), deformed wing virus (DWV), and sacbrood virus (SBV). DWV was most common, followed closely by BQCV and then by SBV. BQCV and SBV were present at significantly higher rates in the migratory bees assayed, bringing into question the impact that these bees have on the health of local bee populations.</style></abstract><issue><style face="normal" font="default" size="100%">24</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19854916?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Garcia-Maruniak, Alejandra</style></author><author><style face="normal" font="default" size="100%">Abd-Alla, Adly M M</style></author><author><style face="normal" font="default" size="100%">Salem, Tamer Z</style></author><author><style face="normal" font="default" size="100%">Parker, Andrew G</style></author><author><style face="normal" font="default" size="100%">Lietze, Verena-Ulrike</style></author><author><style face="normal" font="default" size="100%">van Oers, Monique M</style></author><author><style face="normal" font="default" size="100%">Maruniak, James E</style></author><author><style face="normal" font="default" size="100%">Kim, Woojin</style></author><author><style face="normal" font="default" size="100%">Burand, John P</style></author><author><style face="normal" font="default" size="100%">Cousserans, François</style></author><author><style face="normal" font="default" size="100%">Robinson, Alan S</style></author><author><style face="normal" font="default" size="100%">Vlak, Just M</style></author><author><style face="normal" font="default" size="100%">Bergoin, Max</style></author><author><style face="normal" font="default" size="100%">Boucias, Drion G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Two viruses that cause salivary gland hypertrophy in Glossina pallidipes and Musca domestica are related and form a distinct phylogenetic clade.</style></title><secondary-title><style face="normal" font="default" size="100%">J Gen Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Gen. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromosome Mapping</style></keyword><keyword><style  face="normal" font="default" size="100%">Conserved Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytomegalovirus</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Houseflies</style></keyword><keyword><style  face="normal" font="default" size="100%">Hypertrophy</style></keyword><keyword><style  face="normal" font="default" size="100%">Open Reading Frames</style></keyword><keyword><style  face="normal" font="default" size="100%">Salivary Glands</style></keyword><keyword><style  face="normal" font="default" size="100%">Tsetse Flies</style></keyword><keyword><style  face="normal" font="default" size="100%">Virion</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">90</style></volume><pages><style face="normal" font="default" size="100%">334-46</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Glossina pallidipes and Musca domestica salivary gland hypertrophy viruses (GpSGHV and MdSGHV) replicate in the nucleus of salivary gland cells causing distinct tissue hypertrophy and reduction of host fertility. They share general characteristics with the non-occluded insect nudiviruses, such as being insect-pathogenic, having enveloped, rod-shaped virions, and large circular double-stranded DNA genomes. MdSGHV measures 65x550 nm and contains a 124 279 bp genome (approximately 44 mol% G+C content) that codes for 108 putative open reading frames (ORFs). GpSGHV, measuring 50x1000 nm, contains a 190 032 bp genome (28 mol% G+C content) with 160 putative ORFs. Comparative genomic analysis demonstrates that 37 MdSGHV ORFs have homology to 42 GpSGHV ORFs, as some MdSGHV ORFs have homology to two different GpSGHV ORFs. Nine genes with known functions (dnapol, ts, pif-1, pif-2, pif-3, mmp, p74, odv-e66 and helicase-2), a homologue of the conserved baculovirus gene Ac81 and at least 13 virion proteins are present in both SGHVs. The amino acid identity ranged from 19 to 39 % among ORFs. An (A/T/G)TAAG motif, similar to the baculovirus late promoter motif, was enriched 100 bp upstream of the ORF transcription initiation sites of both viruses. Six and seven putative microRNA sequences were found in MdSGHV and GpSGHV genomes, respectively. There was genome. Collinearity between the two SGHVs, but not between the SGHVs and the nudiviruses. Phylogenetic analysis of conserved genes clustered both SGHVs in a single clade separated from the nudiviruses and baculoviruses. Although MdSGHV and GpSGHV are different viruses, their pathology, host range and genome composition indicate that they are related.</style></abstract><issue><style face="normal" font="default" size="100%">Pt 2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19141442?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Klingbeil, Michele M</style></author><author><style face="normal" font="default" size="100%">Shapiro, Theresa A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Unraveling the secrets of regulating mitochondrial DNA replication.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Cell</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Helicases</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Kinetoplast</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Mitochondrial</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Peptide Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2009 Aug 28</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">35</style></volume><pages><style face="normal" font="default" size="100%">398-400</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In this issue, Liu et al. (2009) report that maxicircle DNA copy number in trypanosomes is regulated by proteolysis of a helicase; the complex kinetoplast DNA system yields a clear view of how mitochondrial DNA replication can be regulated.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/19716784?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chandler, Julian</style></author><author><style face="normal" font="default" size="100%">Vandoros, Anthula V</style></author><author><style face="normal" font="default" size="100%">Mozeleski, Brian</style></author><author><style face="normal" font="default" size="100%">Klingbeil, Michele M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stem-loop silencing reveals that a third mitochondrial DNA polymerase, POLID, is required for kinetoplast DNA replication in trypanosomes.</style></title><secondary-title><style face="normal" font="default" size="100%">Eukaryot Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Eukaryotic Cell</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Kinetoplast</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA-Directed DNA Polymerase</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondrial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA Interference</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Double-Stranded</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2008 Dec</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">2141-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Kinetoplast DNA (kDNA), the mitochondrial genome of trypanosomes, is a catenated network containing thousands of minicircles and tens of maxicircles. The topological complexity dictates some unusual features including a topoisomerase-mediated release-and-reattachment mechanism for minicircle replication and at least six mitochondrial DNA polymerases (Pols) for kDNA transactions. Previously, we identified four family A DNA Pols from Trypanosoma brucei with similarity to bacterial DNA Pol I and demonstrated that two (POLIB and POLIC) were essential for maintaining the kDNA network, while POLIA was not. Here, we used RNA interference to investigate the function of POLID in procyclic T. brucei. Stem-loop silencing of POLID resulted in growth arrest and the progressive loss of the kDNA network. Additional defects in kDNA replication included a rapid decline in minicircle and maxicircle abundance and a transient accumulation of minicircle replication intermediates before loss of the kDNA network. These results demonstrate that POLID is a third essential DNA Pol required for kDNA replication. While other eukaryotes utilize a single DNA Pol (Pol gamma) for replication of mitochondrial DNA, T. brucei requires at least three to maintain the complex kDNA network.</style></abstract><issue><style face="normal" font="default" size="100%">12</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/18849470?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Li, Xiaohong</style></author><author><style face="normal" font="default" size="100%">Foulkes, Andrea S</style></author><author><style face="normal" font="default" size="100%">Yucel, Recai M</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">An expectation maximization approach to estimate malaria haplotype frequencies in multiply infected children.</style></title><secondary-title><style face="normal" font="default" size="100%">Stat Appl Genet Mol Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Stat Appl Genet Mol Biol</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Child</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Frequency</style></keyword><keyword><style  face="normal" font="default" size="100%">Genotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Likelihood Functions</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria Vaccines</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2007</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">6</style></volume><pages><style face="normal" font="default" size="100%">Article33</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Characterizing genetic variability in the human pathogenic Plasmodium species, the group of parasites that cause Malaria, may have broad global health implications. Specifically, discerning the combinations of mutations that lead to viable parasites and the population level frequencies of these clonal sequences will allow for targeted vaccine development and individualized treatment choices. This presents an analytical challenge, however, since haplotypic phase (i.e. the alignment of bases on a single DNA strand) is generally unobservable in multiply infected individuals. This manuscript describes an expectation maximization (EM) approach to maximum likelihood estimation of haplotype frequencies in this missing data setting. The approach is applied to a cohort of N=341 malaria infected children in Uganda, Cameroon and Sudan to characterize regional differences. A simulation study is also presented to characterize method performance and assess sensitivity to distributional assumptions.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/18052916?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Stern, Adi</style></author><author><style face="normal" font="default" size="100%">Doron-Faigenboim, Adi</style></author><author><style face="normal" font="default" size="100%">Erez, Elana</style></author><author><style face="normal" font="default" size="100%">Martz, Eric</style></author><author><style face="normal" font="default" size="100%">Bacharach, Eran</style></author><author><style face="normal" font="default" size="100%">Pupko, Tal</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach.</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Nucleic Acids Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Algorithms</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Substitution</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bayes Theorem</style></keyword><keyword><style  face="normal" font="default" size="100%">Computational Biology</style></keyword><keyword><style  face="normal" font="default" size="100%">Computer Simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Internet</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Analysis, Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Software</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2007 Jul</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">35</style></volume><pages><style face="normal" font="default" size="100%">W506-11</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Biologically significant sites in a protein may be identified by contrasting the rates of synonymous (K(s)) and non-synonymous (K(a)) substitutions. This enables the inference of site-specific positive Darwinian selection and purifying selection. We present here Selecton version 2.2 (http://selecton.bioinfo.tau.ac.il), a web server which automatically calculates the ratio between K(a) and K(s) (omega) at each site of the protein. This ratio is graphically displayed on each site using a color-coding scheme, indicating either positive selection, purifying selection or lack of selection. Selecton implements an assembly of different evolutionary models, which allow for statistical testing of the hypothesis that a protein has undergone positive selection. Specifically, the recently developed mechanistic-empirical model is introduced, which takes into account the physicochemical properties of amino acids. Advanced options were introduced to allow maximal fine tuning of the server to the user's specific needs, including calculation of statistical support of the omega values, an advanced graphic display of the protein's 3-dimensional structure, use of different genetic codes and inputting of a pre-built phylogenetic tree. Selecton version 2.2 is an effective, user-friendly and freely available web server which implements up-to-date methods for computing site-specific selection forces, and the visualization of these forces on the protein's sequence and structure.</style></abstract><issue><style face="normal" font="default" size="100%">Web Server issue</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/17586822?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hong, Yeonchul</style></author><author><style face="normal" font="default" size="100%">Nagamune, Kisaburo</style></author><author><style face="normal" font="default" size="100%">Morita, Yasu S</style></author><author><style face="normal" font="default" size="100%">Nakatani, Fumiki</style></author><author><style face="normal" font="default" size="100%">Ashida, Hisashi</style></author><author><style face="normal" font="default" size="100%">Maeda, Yusuke</style></author><author><style face="normal" font="default" size="100%">Kinoshita, Taroh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Removal or maintenance of inositol-linked acyl chain in glycosylphosphatidylinositol is critical in trypanosome life cycle.</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cloning, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosylphosphatidylinositols</style></keyword><keyword><style  face="normal" font="default" size="100%">Inositol</style></keyword><keyword><style  face="normal" font="default" size="100%">Life Cycle Stages</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Glycoproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphoric Monoester Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Messenger</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2006 Apr 28</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">281</style></volume><pages><style face="normal" font="default" size="100%">11595-602</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The protozoan parasite Trypanosoma brucei is coated by glycosylphosphatidylinositol (GPI)-anchored proteins. During GPI biosynthesis, inositol in phosphatidylinositol becomes acylated. Inositol is deacylated prior to attachment to variant surface glycoproteins in the bloodstream form, whereas it remains acylated in procyclins in the procyclic form. We have cloned a T. brucei GPI inositol deacylase (GPIdeAc2). In accordance with the acylation/deacylation profile, the level of GPIdeAc2 mRNA was 6-fold higher in the bloodstream form than in the procyclic form. Knockdown of GPIdeAc2 in the bloodstream form caused accumulation of an inositol-acylated GPI, a decreased VSG expression on the cell surface and slower growth, indicating that inositol-deacylation is essential for the growth of the bloodstream form. Overexpression of GPIdeAc2 in the procyclic form caused an accumulation of GPI biosynthetic intermediates lacking inositol-linked acyl chain and decreased cell surface procyclins because of release into the culture medium, indicating that overexpression of GPIdeAc2 is deleterious to the surface coat of the procyclic form. Therefore, the GPI inositol deacylase activity must be tightly regulated in trypanosome life cycle.</style></abstract><issue><style face="normal" font="default" size="100%">17</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16510441?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Daniels, Robert</style></author><author><style face="normal" font="default" size="100%">Rusan, Nasser M</style></author><author><style face="normal" font="default" size="100%">Wilbuer, Anne-Kathrin</style></author><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Wadsworth, Patricia</style></author><author><style face="normal" font="default" size="100%">Hebert, Daniel N</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsid Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Death</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane Permeability</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Nuclear Envelope</style></keyword><keyword><style  face="normal" font="default" size="100%">Permeability</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2006 Jul</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">80</style></volume><pages><style face="normal" font="default" size="100%">6575-87</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Many nonenveloped viruses have evolved an infectious cycle that culminates in the lysis or permeabilization of the host to enable viral release. How these viruses initiate the lytic event is largely unknown. Here, we demonstrated that the simian virus 40 progeny accumulated at the nuclear envelope prior to the permeabilization of the nuclear, endoplasmic reticulum, and plasma membranes at a time which corresponded with the release of the progeny. The permeabilization of these cellular membranes temporally correlated with late protein expression and was not observed upon the inhibition of their synthesis. To address whether one or more of the late proteins possessed an inherent capacity to induce membrane permeabilization, we examined the permeability of Escherichia coli that separately expressed the late proteins. VP2 and VP3, but not VP1, caused the permeabilization of bacterial membranes. Additionally, VP3 expression resulted in bacterial cell lysis. These findings demonstrate that VP3 possesses an inherent lytic property that is independent of eukaryotic signaling or cell death pathways.</style></abstract><issue><style face="normal" font="default" size="100%">13</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16775344?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hong, Yeonchul</style></author><author><style face="normal" font="default" size="100%">Nagamune, Kisaburo</style></author><author><style face="normal" font="default" size="100%">Ohishi, Kazuhito</style></author><author><style face="normal" font="default" size="100%">Morita, Yasu S</style></author><author><style face="normal" font="default" size="100%">Ashida, Hisashi</style></author><author><style face="normal" font="default" size="100%">Maeda, Yusuke</style></author><author><style face="normal" font="default" size="100%">Kinoshita, Taroh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei.</style></title><secondary-title><style face="normal" font="default" size="100%">FEBS Lett</style></secondary-title><alt-title><style face="normal" font="default" size="100%">FEBS Lett.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acyltransferases</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Disulfides</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Targeting</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Glycoproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Multiprotein Complexes</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Subunits</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2006 Jan 23</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">580</style></volume><pages><style face="normal" font="default" size="100%">603-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16405969?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Kuksin, Dmitry</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The caveolae-mediated sv40 entry pathway bypasses the golgi complex en route to the endoplasmic reticulum.</style></title><secondary-title><style face="normal" font="default" size="100%">Virol J</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Virol. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolae</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Fibroblasts</style></keyword><keyword><style  face="normal" font="default" size="100%">Golgi Apparatus</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunohistochemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2005</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">2</style></volume><pages><style face="normal" font="default" size="100%">38</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">BACKGROUND: Simian virus 40 (SV40) enters cells via an atypical caveolae-mediated endocytic pathway, which delivers the virus to a new intermediary compartment, the caveosome. The virus then is believed to go directly from the caveosome to the endoplasmic reticulum. Cholera toxin likewise enters via caveolae and traffics to caveosomes. But, in contrast to SV40, cholera toxin is transported from caveosomes to the endoplasmic reticulum via the Golgi. For that reason, and because the caveosome and Golgi may have some common markers, we revisited the issue of whether SV40 might access the endoplasmic reticulum via the Golgi.

RESULTS: We confirmed our earlier finding that SV40 co localizes with the Golgi marker beta-COP. However, we show that the virus does not co localize with the more discriminating Golgi markers, golgin 97 and BODIPY-ceramide.

CONCLUSION: The caveolae-mediated SV40 entry pathway does not intersect the Golgi. SV40 is seen to co localize with beta-COP because that protein is a marker for caveosomes as well as the Golgi. Moreover, these results are consistent with the likelihood that the caveosome is a sorting organelle. In addition, there are at least two distinct but related routes by which a ligand might traffic from the caveosome to the ER; one route involving transport through the Golgi, and another pathway that does not involve the Golgi.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15840166?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Burand, John P</style></author><author><style face="normal" font="default" size="100%">Tan, Weijia</style></author><author><style face="normal" font="default" size="100%">Kim, Woojin</style></author><author><style face="normal" font="default" size="100%">Nojima, Satoshi</style></author><author><style face="normal" font="default" size="100%">Roelofs, Wendell</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Infection with the insect virus Hz-2v alters mating behavior and pheromone production in female Helicoverpa zea moths.</style></title><secondary-title><style face="normal" font="default" size="100%">J Insect Sci</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Insect Sci.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Infectious Disease Transmission, Vertical</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Pheromones</style></keyword><keyword><style  face="normal" font="default" size="100%">Sexual Behavior, Animal</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Vocalization, Animal</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2005</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">5</style></volume><pages><style face="normal" font="default" size="100%">6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The effect of Hz-2V virus infection on the reproductive physiology and behavior of infected Helicoverpa zea female moths was examined. In the absence of males, infected females exhibited calling behavior and called as often but for shorter periods on average than control females. As expected, control females mated with males for extend periods when they were present and did not call after mating, while virus-infected females made many frequent contacts with males and continued to call even after these contacts. Virus-infected females were found to produce five to seven times more pheromone than control females and attracted twice as many males as did control females in flight tunnel experiments. The ability of Hz-2V to alter the physiology and behavior of infected females observed here may serve to facilitate the transmission of virus in insect populations.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/16299596?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kang, Ji Young</style></author><author><style face="normal" font="default" size="100%">Hong, Yeongjin</style></author><author><style face="normal" font="default" size="100%">Ashida, Hisashi</style></author><author><style face="normal" font="default" size="100%">Shishioh, Nobue</style></author><author><style face="normal" font="default" size="100%">Murakami, Yoshiko</style></author><author><style face="normal" font="default" size="100%">Morita, Yasu S</style></author><author><style face="normal" font="default" size="100%">Maeda, Yusuke</style></author><author><style face="normal" font="default" size="100%">Kinoshita, Taroh</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol.</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line, Tumor</style></keyword><keyword><style  face="normal" font="default" size="100%">CHO Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Cloning, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Conserved Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetinae</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">Glioma</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycosylphosphatidylinositols</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mannose</style></keyword><keyword><style  face="normal" font="default" size="100%">Mannosyltransferases</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Open Reading Frames</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Restriction Mapping</style></keyword><keyword><style  face="normal" font="default" size="100%">Saccharomyces cerevisiae</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2005 Mar 11</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">280</style></volume><pages><style face="normal" font="default" size="100%">9489-97</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Glycosylphosphatidylinositol (GPI) is a glycolipid that anchors many proteins to the eukaryotic cell surface. The biosynthetic pathway of GPI is mediated by sequential additions of sugars and other components to phosphatidylinositol. Four mannoses in the GPI are transferred from dolichol-phosphate-mannose (Dol-P-Man) and are linked through different glycosidic linkages. Therefore, four Dol-P-Man-dependent mannosyltransferases, GPI-MT-I, -MT-II, -MT-III, and -MT-IV for the first, second, third, and fourth mannoses, respectively, are required for generation of GPI. GPI-MT-I (PIG-M), GPI-MT-III (PIG-B), and GPI-MT-IV (SMP3) were previously reported, but GPI-MT-II remains to be identified. Here we report the cloning of PIG-V involved in transferring the second mannose in the GPI anchor. Human PIG-V encodes a 493-amino acid, endoplasmic reticulum (ER) resident protein with eight putative transmembrane regions. Saccharomyces cerevisiae protein encoded in open reading frame YBR004c, which we termed GPI18, has 25% amino acid identity to human PIG-V. Viability of the yeast gpi18 deletion mutant was restored by human PIG-V cDNA. PIG-V has two functionally important conserved regions facing the ER lumen. Taken together, we suggest that PIG-V is the second mannosyltransferase in GPI anchor biosynthesis.</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15623507?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Webley, Wilmore C</style></author><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Stuart, Elizabeth S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Caveolin-2 associates with intracellular chlamydial inclusions independently of caveolin-1.</style></title><secondary-title><style face="normal" font="default" size="100%">BMC Infect Dis</style></secondary-title><alt-title><style face="normal" font="default" size="100%">BMC Infect. Dis.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 2</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cells, Cultured</style></keyword><keyword><style  face="normal" font="default" size="100%">Chlamydia</style></keyword><keyword><style  face="normal" font="default" size="100%">Fluorescent Antibody Technique</style></keyword><keyword><style  face="normal" font="default" size="100%">Golgi Apparatus</style></keyword><keyword><style  face="normal" font="default" size="100%">Guinea Pigs</style></keyword><keyword><style  face="normal" font="default" size="100%">HeLa Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Confocal</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Vacuoles</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Jul 22</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">23</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">BACKGROUND: Lipid raft domains form in plasma membranes of eukaryotic cells by the tight packing of glycosphingolipids and cholesterol. Caveolae are invaginated structures that form in lipid raft domains when the protein caveolin-1 is expressed. The Chlamydiaceae are obligate intracellular bacterial pathogens that replicate entirely within inclusions that develop from the phagocytic vacuoles in which they enter. We recently found that host cell caveolin-1 is associated with the intracellular vacuoles and inclusions of some chlamydial strains and species, and that entry of those strains depends on intact lipid raft domains. Caveolin-2 is another member of the caveolin family of proteins that is present in caveolae, but of unknown function.

METHODS: We utilized a caveolin-1 negative/caveolin-2 positive FRT cell line and laser confocal immunofluorescence techniques to visualize the colocalization of caveolin-2 with the chlamydial inclusions.

RESULTS: We show here that in infected HeLa cells, caveolin-2, as well as caveolin-1, colocalizes with inclusions of C. pneumoniae (Cp), C. caviae (GPIC), and C. trachomatis serovars E, F and K. In addition, caveolin-2 also associates with C. trachomatis serovars A, B and C, although caveolin-1 did not colocalize with these organisms. Moreover, caveolin-2 appears to be specifically, or indirectly, associated with the pathogens at the inclusion membranes. Using caveolin-1 deficient FRT cells, we show that although caveolin-2 normally is not transported out of the Golgi in the absence of caveolin-1, it nevertheless colocalizes with chlamydial inclusions in these cells. However, our results also show that caveolin-2 did not colocalize with UV-irradiated Chlamydia in FRT cells, suggesting that in these caveolin-1 negative cells, pathogen viability and very likely pathogen gene expression are necessary for the acquisition of caveolin-2 from the Golgi.

CONCLUSION: Caveolin-2 associates with the chlamydial inclusion independently of caveolin-1. The function of caveolin-2, either in the uninfected cell or in the chlamydial developmental cycle, remains to be elucidated. Nevertheless, this second caveolin protein can now be added to the small number of host proteins that are associated with the inclusions of this obligate intracellular pathogen.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15271223?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Klingbeil, Michele M</style></author><author><style face="normal" font="default" size="100%">Englund, Paul T</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Closing the gaps in kinetoplast DNA network replication.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Crithidia fasciculata</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Ligases</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Kinetoplast</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Mitochondrial</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Electron</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Mar 30</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">101</style></volume><pages><style face="normal" font="default" size="100%">4333-4</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">13</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15070715?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Yan, Bin</style></author><author><style face="normal" font="default" size="100%">Methé, Barbara A</style></author><author><style face="normal" font="default" size="100%">Lovley, Derek R</style></author><author><style face="normal" font="default" size="100%">Krushkal, Julia</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Computational prediction of conserved operons and phylogenetic footprinting of transcription regulatory elements in the metal-reducing bacterial family Geobacteraceae.</style></title><secondary-title><style face="normal" font="default" size="100%">J Theor Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Theor. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Computational Biology</style></keyword><keyword><style  face="normal" font="default" size="100%">Conserved Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Footprinting</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Regulator</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Geobacter</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Operon</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Sep 7</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">230</style></volume><pages><style face="normal" font="default" size="100%">133-44</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Members of the family Geobacteraceae are an important group of microorganisms from the delta subdivision of Proteobacteria that couple the oxidation of organic compounds to metal reduction. In order to uncover transcription regulatory interactions in these organisms, we used computational methods to identify conserved operons and putative cis-regulatory transcription elements. We identified 26 putative operons with gene order and function conserved among two species of Geobacteraceae, Geobacter sulfurreducens and Geobacter metallireducens. Most of these operons were also conserved in Desulfovibrio vulgaris, an additional metal reducing organism from family Desulfovibrionaceae of the delta subdivision of Proteobacteria. The predicted conserved operons were investigated for the presence of transcription factor binding sites by two different methods, (i) comparison of non-coding regions in conserved operons, and (ii) neural network promoter prediction. Predicted motifs were screened to identify most likely transcription factor binding sites and ribosome-binding sites. We provide information on motifs in Geobacteraceae similar to known transcription factor binding sites in Escherichia coli, conserved motifs in other bacterial species, putative palindromic sites, and predicted ribosome-binding sites. These predictions will aid in further elucidation of regulatory networks of gene interactions in Geobacteraceae.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15276006?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Burand, John P</style></author><author><style face="normal" font="default" size="100%">Rallis, Christopher P</style></author><author><style face="normal" font="default" size="100%">Tan, Weijia</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Horizontal transmission of Hz-2V by virus infected Helicoverpa zea moths.</style></title><secondary-title><style face="normal" font="default" size="100%">J Invertebr Pathol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Invertebr. Pathol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Abdomen</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Entomology</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Genitalia</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Sexual Behavior, Animal</style></keyword><keyword><style  face="normal" font="default" size="100%">Tissue Distribution</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">85</style></volume><pages><style face="normal" font="default" size="100%">128-31</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Helicoverpa zea female moths productively infected with Hz-2V have malformed reproductive tissues and are sterile. Virus replication in infected females occurs primarily in the reproductive tissues and culminates with the accumulation of virus-filled vesicles, which form plugs of virus covering the reproductive openings of these insects. The location of this large concentration of virus particles at the terminal abdominal segment of infected females suggests that it may serve as a source of virus that can be transmitted horizontally between moths during mating. In mating experiments it was found that healthy males are attracted to and attempt to mate with infected females, and that these males are able transmit Hz-2V to healthy females during subsequent matings, giving rise to virus infected progeny.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15050843?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Burand, John P</style></author><author><style face="normal" font="default" size="100%">Rallis, Christopher P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">In vivo dose-response of insects to Hz-2V infection.</style></title><secondary-title><style face="normal" font="default" size="100%">Virol J</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Virol. J.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Ovum</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Diseases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1</style></volume><pages><style face="normal" font="default" size="100%">15</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">BACKGROUND: Hz-2V infection of female Helicoverpa zea moths is manifested as insects that are either sterile &quot;agonadal&quot; individuals with malformed reproductive tissues or fertile asymptomatic carriers which are capable of transmitting virus on to their progeny. Virus infected progeny arising from eggs laid by asymptomatic carrier females may themselves be either sterile agonadals or asymptomatic carriers.

RESULTS: By injecting virus into female moths, a correlation was established between virus doses administered to the females and the levels of resulting asymptomatic and sterile progeny.

CONCLUSIONS: The results of these experiments indicate that high virus doses produced a higher level of agonadal progeny and lower doses produced higher levels of asymptomatic carriers.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15613241?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Gov, Yael</style></author><author><style face="normal" font="default" size="100%">Borovok, Ilya</style></author><author><style face="normal" font="default" size="100%">Korem, Moshe</style></author><author><style face="normal" font="default" size="100%">Singh, Vineet K</style></author><author><style face="normal" font="default" size="100%">Jayaswal, Radheshyam K</style></author><author><style face="normal" font="default" size="100%">Wilkinson, Brian J</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Balaban, Naomi</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Quorum sensing in Staphylococci is regulated via phosphorylation of three conserved histidine residues.</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Northern</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Communication</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrophoresis, Polyacrylamide Gel</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Histidine</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutagenesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutagenesis, Site-Directed</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Phenotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphorylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmids</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Tertiary</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Antisense</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Staphylococcus aureus</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Apr 9</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">279</style></volume><pages><style face="normal" font="default" size="100%">14665-72</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Staphylococcus aureus cause infections by producing toxins, a process regulated by cell-cell communication (quorum sensing) through the histidine-phosphorylation of the target of RNAIII-activating protein (TRAP). We show here that TRAP is highly conserved in staphylococci and contains three completely conserved histidine residues (His-66, His-79, His-154) that are phosphorylated and essential for its activity. This was tested by constructing a TRAP(-) strain with each of the conserved histidine residues changed to alanine by site-directed mutagenesis. All mutants were tested for pathogenesis in vitro (expression of RNAIII and hemolytic activity) and in vivo (murine cellulitis model). Results show that RNAIII is not expressed in the TRAP(-) strain, that it is non hemolytic, and that it does not cause disease in vivo. These pathogenic phenotypes could be rescued in the strain containing the recovered traP, confirming the importance of TRAP in S. aureus pathogenesis. The phosphorylation of TRAP mutated in any of the conserved histidine residues was significantly reduced, and mutants defective in any one of these residues were non-pathogenic in vitro or in vivo, whereas those mutated in a non-conserved histidine residue (His-124) were as pathogenic as the wild type. These results confirm the importance of the three conserved histidine residues in TRAP activity. The phosphorylation pattern, structure, and gene organization of TRAP deviates from signaling molecules known to date, suggesting that TRAP belongs to a novel class of signal transducers.</style></abstract><issue><style face="normal" font="default" size="100%">15</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/14726534?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The unpredictable past of Plasmodium vivax revealed in its genome.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Evolution</style></keyword><keyword><style  face="normal" font="default" size="100%">Culicidae</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetics, Population</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Genomics</style></keyword><keyword><style  face="normal" font="default" size="100%">Haplorhini</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria, Vivax</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium vivax</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2004 Nov 2</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">101</style></volume><pages><style face="normal" font="default" size="100%">15547-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">44</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/15505201?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Tumwine, James K</style></author><author><style face="normal" font="default" size="100%">Kekitiinwa, Addy</style></author><author><style face="normal" font="default" size="100%">Nabukeera, Nicolette</style></author><author><style face="normal" font="default" size="100%">Akiyoshi, Donna E</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Widmer, Giovanni</style></author><author><style face="normal" font="default" size="100%">Feng, Xiaochuan</style></author><author><style face="normal" font="default" size="100%">Tzipori, Saul</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Cryptosporidium parvum in children with diarrhea in Mulago Hospital, Kampala, Uganda.</style></title><secondary-title><style face="normal" font="default" size="100%">Am J Trop Med Hyg</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Am. J. Trop. Med. Hyg.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Case-Control Studies</style></keyword><keyword><style  face="normal" font="default" size="100%">Child, Preschool</style></keyword><keyword><style  face="normal" font="default" size="100%">Cross-Sectional Studies</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidium parvum</style></keyword><keyword><style  face="normal" font="default" size="100%">Diarrhea</style></keyword><keyword><style  face="normal" font="default" size="100%">Diarrhea, Infantile</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Hospitalization</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Infant</style></keyword><keyword><style  face="normal" font="default" size="100%">Infant, Newborn</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Nutrition Disorders</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Restriction Fragment Length</style></keyword><keyword><style  face="normal" font="default" size="100%">Prevalence</style></keyword><keyword><style  face="normal" font="default" size="100%">Uganda</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2003 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">68</style></volume><pages><style face="normal" font="default" size="100%">710-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">A cross-sectional case-control study (ratio = 3:1) was conducted over a 15-month period to determine the prevalence and consequences of cryptosporidiosis in hospitalized diarrheic children (0-5 years old) at Mulago Hospital in Kampala, Uganda. Cryptosporidium parvum was detected and genotyped among 2,446 children of whom 1,779 (72.7%) had diarrhea, and 667 (27.3%) were age- and sex-matched controls. Of the 1,779 children with diarrhea, 532 (29.9%) had persistent (&gt; 14 days) diarrhea and 1,247 (70.1%) had acute diarrhea. Overall, 444 (25.0%) of the 1,779 children with diarrhea had C. parvum, compared with only 57 (8.5%) of the 667 children without diarrhea (chi2 = 80.2, P &lt; or = 0.0001). Within this group of infected children, 72.8% were infected with genotype 1, 18.4% with genotype 2, and 4.1% with a mixture of both genotypes, and 4.1% isolates were either unclassified or C. meleagridis. The prevalence was highest during the rainy months of April to June. Of the 532 children with persistent diarrhea, 166 (31.2%) had C. parvum compared with 278 (22.3%) of the 1,247 children with acute diarrhea (chi2 = 15.8, P &lt; or = 0.0001). There was a significant association between C. parvum and malnutrition including stunting, being underweight, and wasting. Unfavorable outcome (death or failure to resolve within 14 days) occurred in 139 (72.8%) of the 191 children with C. parvum, and in only 65.1% of the 545 without (odds ratio = 1.117, 95% confidence interval = 1.005-1.243, P = 0.05), Of the 191 children with C. parvum, 24 (12.6%) died, compared with 34 (6.2%) of the 545 without C. parvum (P = 0.005). Mortality rates were higher among children with severe dehydration and persistent diarrhea, and in stunted or underweight children infected with C. parvum. Among Ugandan children, cryptosporidiosis, which remains untreatable, is frequently associated with diarrhea and other serious and unfavorable consequences.</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12887032?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Ayala, Francisco J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Progress in malaria research: the case for phylogenetics.</style></title><secondary-title><style face="normal" font="default" size="100%">Adv Parasitol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Adv. Parasitol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Biomedical Research</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2003</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">54</style></volume><pages><style face="normal" font="default" size="100%">255-80</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Malaria, from the Italian for &quot;bad air&quot;, is a term used to describe a human disease caused by any of four parasites of the genus, Plasmodium. There are in fact over 200 described species of Plasmodium that parasitize reptiles, birds, and mammals, and may or may not cause disease in these various hosts. In this chapter, we highlight important evolutionary studies that have been undertaken to determine the relatedness among these species and their place in the taxonomic hierarchy. We begin by providing an overview of our present understanding of the phylum to which malaria parasites belong--Apicomplexa. The unique characteristics of these parasites reflect both their adaptation to the parasitic life style as well as some vestigial remnants of their pre-parasitic evolutionary past. Phylogenetic analyses provide the means for discerning the means by which these characteristics have come into existence. We next discuss the systematics of the genus Plasmodium. Morphology, genomic structure and content as well as host affiliation of these parasites are all traits that have been used for establishing taxonomic arrangements. Molecular phylogenetics has proven to be an invaluable tool in this regard and so we discuss the current phylogenetic picture of the genus as well as the correspondence among the various datasets (morphology, molecules, and host-preference). Lastly, we present a detailed account of our current understanding of the evolutionary past of the most deadly of the human malaria species--P. falciparum.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/14711087?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ferreira, Marcelo U</style></author><author><style face="normal" font="default" size="100%">Ribeiro, Weber L</style></author><author><style face="normal" font="default" size="100%">Tonon, Angela P</style></author><author><style face="normal" font="default" size="100%">Kawamoto, Fumihiko</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Sequence diversity and evolution of the malaria vaccine candidate merozoite surface protein-1 (MSP-1) of Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Gene</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Gene</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alleles</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Brazil</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Variation</style></keyword><keyword><style  face="normal" font="default" size="100%">Haplotypes</style></keyword><keyword><style  face="normal" font="default" size="100%">Linkage Disequilibrium</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria Vaccines</style></keyword><keyword><style  face="normal" font="default" size="100%">Merozoite Surface Protein 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Single Nucleotide</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombination, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Analysis, DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Tanzania</style></keyword><keyword><style  face="normal" font="default" size="100%">Thailand</style></keyword><keyword><style  face="normal" font="default" size="100%">Vietnam</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2003 Jan 30</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">304</style></volume><pages><style face="normal" font="default" size="100%">65-75</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The merozoite surface protein-1 (MSP-1) of the malaria parasite Plasmodium falciparum is a major blood-stage antigen containing highly polymorphic tripeptide repeats in the domain known as block 2 and several non-repetitive domains that are essentially dimorphic. We have analyzed sequence variation in block 2 repeats and in non-repetitive block 17, as well as other polymorphisms within the MSP-1 gene, in clinical isolates of P. falciparum. Repeat haplotypes were defined as unique combinations of repeat motifs within block 2, whereas block 17 haplotypes were defined as unique combinations of single nucleotide replacements in this domain. A new block 17 haplotype, E-TNG-L, was found in one isolate from Vietnam. MSP-1 alleles, defined as unique combinations of haplotypes in blocks 2 and 17 and other polymorphisms within the molecule, were characterized in 60 isolates from hypoendemic Brazil and 37 isolates from mesoendemic Vietnam. Extensive diversity has been created in block 2 and elsewhere in the molecule, while maintaining significant linkage disequilibrium between polymorphisms across the non-telomeric MSP-1 locus separated by a map distance of more than 4 kb, suggesting that low meiotic recombination rates occur in both parasite populations. These results indicate a role for non-homologous recombination, such as strand-slippage mispairing during mitosis and gene conversion, in creating variation in a malarial antigen under strong diversifying selection.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12568716?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Saxowsky, Tina T</style></author><author><style face="normal" font="default" size="100%">Choudhary, Gunjan</style></author><author><style face="normal" font="default" size="100%">Klingbeil, Michele M</style></author><author><style face="normal" font="default" size="100%">Englund, Paul T</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Trypanosoma brucei has two distinct mitochondrial DNA polymerase beta enzymes.</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Polymerase beta</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2003 Dec 5</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">278</style></volume><pages><style face="normal" font="default" size="100%">49095-101</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In higher eukaryotes, DNA polymerase (pol) beta resides in the nucleus and participates primarily in DNA repair. The DNA polymerase beta from the trypanosomatid Crithidia fasciculata, however, was the first mitochondrial enzyme of this type described. Upon searching the nearly completed genome data base of the related parasite Trypanosoma brucei, we discovered genes for two pol beta-like proteins. One is approximately 70% identical to the C. fasciculata pol beta and is likely the homolog of this enzyme. The other, although approximately 30% identical within the polymerase region, has unusual structural features including a short C-terminal tail and a long N-terminal extension rich in prolines, alanines, and lysines. Both proteins, when expressed recombinantly, are active as DNA polymerases and deoxyribose phosphate lyases, but their polymerase activity optima differ with respect to pH and KCl and MgCl2 concentrations. Remarkably, green fluorescent protein fusion proteins and immunofluorescence demonstrate that both are mitochondrial, but their locations with respect to the mitochondrial DNA (kinetoplast DNA network) in this organism are strikingly different.</style></abstract><issue><style face="normal" font="default" size="100%">49</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12966090?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Burke, William D</style></author><author><style face="normal" font="default" size="100%">Malik, Harmit S</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Eickbush, Thomas H</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Ancient lineages of non-LTR retrotransposons in the primitive eukaryote, Giardia lamblia.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biol Evol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Biol. Evol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Giardia lamblia</style></keyword><keyword><style  face="normal" font="default" size="100%">Long Interspersed Nucleotide Elements</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Open Reading Frames</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Repetitive Sequences, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Telomere</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">19</style></volume><pages><style face="normal" font="default" size="100%">619-30</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Mobile elements that use reverse transcriptase to make new copies of themselves are found in all major lineages of eukaryotes. The non-long terminal repeat (non-LTR) retrotransposons have been suggested to be the oldest of these eukaryotic elements. Phylogenetic analysis of non-LTR elements suggests that they have predominantly undergone vertical transmission, as opposed to the frequent horizontal transmissions found for other mobile elements. One prediction of this vertical model of inheritance is that the oldest lineages of eukaryotes should exclusively harbor the oldest lineages of non-LTR retrotransposons. Here we characterize the non-LTR retrotransposons present in one of the most primitive eukaryotes, the diplomonad Giardia lamblia. Two families of elements were detected in the WB isolate of G. lamblia currently being used for the genome sequencing project. These elements are clearly distinct from all other previously described non-LTR lineages. Phylogenetic analysis indicates that these Genie elements (for Giardia early non-LTR insertion element) are among the oldest known lineages of non-LTR elements consistent with strict vertical descent. Genie elements encode a single open reading frame with a carboxyl terminal endonuclease domain. Genie 1 is site specific, as seven to eight copies are present in a single tandem array of a 771-bp repeat near the telomere of one chromosome. The function of this repeat is not known. One additional, highly divergent, element within the Genie 1 lineage is not located in this tandem array but is near a second telomere. Four different telomere addition sites could be identified within or near the Genie elements on each of these chromosomes. The second lineage of non-LTR elements, Genie 2, is composed of about 10 degenerate copies. Genie 2 elements do not appear to be site specific in their insertion. An unusual aspect of Genie 2 is that all copies contain inverted repeats up to 172 bp in length.</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11961096?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, Leonard C</style></author><author><style face="normal" font="default" size="100%">Anderson, Howard A</style></author><author><style face="normal" font="default" size="100%">Wolfrom, Scott A</style></author><author><style face="normal" font="default" size="100%">Oppenheim, Ariella</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antiviral Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Brefeldin A</style></keyword><keyword><style  face="normal" font="default" size="100%">Capsid</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolae</style></keyword><keyword><style  face="normal" font="default" size="100%">Coatomer Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Endoplasmic Reticulum</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">76</style></volume><pages><style face="normal" font="default" size="100%">5156-66</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) enters cells by atypical endocytosis mediated by caveolae that transports the virus to the endoplasmic reticulum (ER) instead of to the endosomal-lysosomal compartment, which is the usual destination for viruses and other cargo that enter by endocytosis. We show here that SV4O is transported to the ER via an intermediate compartment that contains beta-COP, which is best known as a component of the COPI coatamer complexes that are required for the retrograde retrieval pathway from the Golgi to the ER. Additionally, transport of SV40 to the ER, as well as infection, is sensitive to brefeldin A. This drug acts by specifically inhibiting the ARF1 GTPase, which is known to regulate assembly of COPI coat complexes on Golgi cisternae. Moreover, some beta-COP colocalizes with intracellular caveolin-1, which was previously shown to be present on a new organelle (termed the caveosome) that is an intermediate in the transport of SV40 to the ER (L. Pelkmans, J. Kartenbeck, and A. Helenius, Nat. Cell Biol. 3:473-483, 2001). We also show that the internal SV40 capsid proteins VP2 and VP3 become accessible to immunostaining starting at about 5 h. Most of that immunostaining overlays the ER, with some appearing outside of the ER. In contrast, immunostaining with anti-SV40 antisera remains confined to the ER.</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11967331?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Feng, Xiaochuan</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Tzipori, Saul</style></author><author><style face="normal" font="default" size="100%">Widmer, Giovanni</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Experimental evidence for genetic recombination in the opportunistic pathogen Cryptosporidium parvum.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biochem Parasitol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Biochem. Parasitol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Conserved Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Crosses, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidium parvum</style></keyword><keyword><style  face="normal" font="default" size="100%">Deer</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Genotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Microsatellite Repeats</style></keyword><keyword><style  face="normal" font="default" size="100%">Opportunistic Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombination, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Survival Rate</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 Jan</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">119</style></volume><pages><style face="normal" font="default" size="100%">55-62</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Cryptosporidium parvum is an intracellular protozoan parasite causing intestinal malabsorption and diarrhea in humans. The infection is usually self-limiting, although persistent cryptosporidosis is observed in immunocompromised and malnourished individuals. As with other Apicomplexa, the life cycle of Cryptosporidium is thought to comprise a sexual phase, during which a motile microgamont fuses with a sessile macrogamont. The four sporozoites found within each oocyst (the infectious form excreted in the feces) are thought to be the product of a meiotic division taking place immediately following fertilization, but the existence of a meiotic cycle in this genus has not been tested experimentally. To substantiate the occurrence of meiotic recombination in this species, we performed a genetic cross between two distinct isolates of C. parvum co-infected in INF-gamma knockout mice. We found that mixed infections produced recombinant progeny characterized by multilocus genotypes comprising alleles inherited from each parental line. This observation represents the first demonstration of sexual recombination in this pathogen. Together with the occurrence of genetically heterogeneous infections, this finding suggests that outcrossing between genotypes may occur in nature. Experimental crosses among Cryptosporidium populations will facilitate mapping of clinically relevant genes, the delineation of Cryptosporidium species, and defining the taxonomical status of C. parvum subtypes and host-specific genotypes.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11755186?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mukherjee, Jean</style></author><author><style face="normal" font="default" size="100%">Chios, Kerry</style></author><author><style face="normal" font="default" size="100%">Fishwild, Dianne</style></author><author><style face="normal" font="default" size="100%">Hudson, Deborah</style></author><author><style face="normal" font="default" size="100%">O'Donnell, Susan</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Donohue-Rolfe, Arthur</style></author><author><style face="normal" font="default" size="100%">Tzipori, Saul</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Human Stx2-specific monoclonal antibodies prevent systemic complications of Escherichia coli O157:H7 infection.</style></title><secondary-title><style face="normal" font="default" size="100%">Infect Immun</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Infect. Immun.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibodies, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibodies, Monoclonal</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibody Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Models, Animal</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli O157</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Germ-Free Life</style></keyword><keyword><style  face="normal" font="default" size="100%">HeLa Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemolytic-Uremic Syndrome</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunization, Passive</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin G</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin Isotypes</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin kappa-Chains</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Neutralization Tests</style></keyword><keyword><style  face="normal" font="default" size="100%">Shiga Toxin 2</style></keyword><keyword><style  face="normal" font="default" size="100%">Swine</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">70</style></volume><pages><style face="normal" font="default" size="100%">612-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Hemolytic-uremic syndrome (HUS) is a serious complication predominantly associated with infection by enterohemorrhagic Escherichia coli (EHEC), such as E. coli O157:H7. EHEC can produce Shiga toxin 1 (Stx1) and/or Shiga toxin 2 (Stx2), both of which are exotoxins comprised of active (A) and binding (B) subunits. In piglets and mice, Stx can induce fatal neurological symptoms. Polyclonal Stx2 antiserum can prevent these effects in piglets infected with the Stx2-producing E. coli O157:H7 strain 86-24. Human monoclonal antibodies (HuMAbs) against Stx2 were developed as potential passive immunotherapeutic reagents for the prevention and/or treatment of HUS. Transgenic mice bearing unrearranged human immunoglobulin (Ig) heavy and kappa light chain loci (HuMAb___Mouse) were immunized with formalin-inactivated Stx2. Thirty-seven stable hybridomas secreting Stx2-specific HuMAbs were isolated: 33 IgG1kappa A-subunit-specific and 3 IgG1kappa and 1 IgG3kappa B-subunit-specific antibodies. Six IgG1kappa A-subunit-specific (1G3, 2F10, 3E9, 4H9, 5A4, and 5C12) and two IgG1kappa B-subunit-specific (5H8 and 6G3) HuMAbs demonstrated neutralization of &gt; 95% activity of 1 ng of Stx2 in the presence of 0.04 microg of HuMAb in vitro and significant prolongation of survival of mice given 50 microg of HuMAb intraperitoneally (i.p.) and 25 ng of Stx2 intravenously. When administered i.p. to gnotobiotic piglets 6 or 12 h after infection with E. coli O157:H7 strain 86-24, HuMAbs 2F10, 3E9, 5H8, and 5C12 prolonged survival and prevented development of fatal neurological signs and cerebral lesions. The Stx2-neutralizing ability of these HuMAbs could potentially be used clinically to passively protect against HUS development in individuals infected with Stx-producing bacteria, including E. coli O157:H7.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11796590?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Okhuysen, Pablo C</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Chappell, Cynthia L</style></author><author><style face="normal" font="default" size="100%">Grimes, Kevin A</style></author><author><style face="normal" font="default" size="100%">Widmer, Giovanni</style></author><author><style face="normal" font="default" size="100%">Feng, Xiaochuan</style></author><author><style face="normal" font="default" size="100%">Tzipori, Saul</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Infectivity of a Cryptosporidium parvum isolate of cervine origin for healthy adults and interferon-gamma knockout mice.</style></title><secondary-title><style face="normal" font="default" size="100%">J Infect Dis</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Infect. Dis.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adult</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Body Weight</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidium parvum</style></keyword><keyword><style  face="normal" font="default" size="100%">Deer</style></keyword><keyword><style  face="normal" font="default" size="100%">Diarrhea</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Susceptibility</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Interferon-gamma</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 May 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">185</style></volume><pages><style face="normal" font="default" size="100%">1320-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The infectivity of a Cryptosporidium parvum isolate of cervine origin (type 2, Moredun) propagated in calves was investigated simultaneously in healthy adult human volunteers and in interferon-gamma knockout (GKO) mice. After exposure to 100-3000 oocysts, 16 volunteers recorded, for a duration of 6 weeks, the number and form of stools that they passed and any symptoms that they experienced. Oocyst excretion was assessed by enzyme-linked immunosorbent assay and direct immunofluorescence assay. Eleven subjects (69%) became ill, and 8 subjects (50%) shed oocysts in stool. The median duration of illness was 169 h, and the median number of unformed stools passed was 24. The duration and intensity of symptoms were more severe than were those associated with previously studied isolates. The median infectious dose was estimated to be 300 oocysts for humans and 1 oocyst for the GKO mouse model. The Moredun isolate was more pathogenic than the reference GCH-1 isolate. The GKO mouse model of cryptosporidiosis is useful for discerning isolate-specific differences in pathogenicity.</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12001050?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Klingbeil, Michele M</style></author><author><style face="normal" font="default" size="100%">Motyka, Shawn A</style></author><author><style face="normal" font="default" size="100%">Englund, Paul T</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multiple mitochondrial DNA polymerases in Trypanosoma brucei.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Cell</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Kinetoplast</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA-Directed DNA Polymerase</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Tertiary</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Double-Stranded</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Messenger</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 Jul</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">175-86</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Kinetoplast DNA (kDNA), the unusual mitochondrial DNA of Trypanosoma brucei, is a network containing thousands of catenated circles. Database searching for a kDNA replicative polymerase (pol) revealed no mitochondrial pol gamma homolog. Instead, we identified four proteins (TbPOLIA, IB, IC, and ID) related to bacterial pol I. Remarkably, all four localized to the mitochondrion. TbPOLIB and TbPOLIC localized beside the kDNA where replication occurs, and their knockdown by RNA interference caused kDNA network shrinkage. Furthermore, silencing of TbPOLIC caused loss of both minicircles and maxicircles and accumulation of minicircle replication intermediates, consistent with a role in replication. While typical mitochondria contain one DNA polymerase, pol gamma, trypanosome mitochondria contain five such enzymes, including the previously characterized pol beta.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12150917?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rallis, Christopher P</style></author><author><style face="normal" font="default" size="100%">Burand, John P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Pathology and ultrastructure of Hz-2V infection in the agonadal female corn earworm, Helicoverpa zea.</style></title><secondary-title><style face="normal" font="default" size="100%">J Invertebr Pathol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Invertebr. Pathol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Electron</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Diseases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">81</style></volume><pages><style face="normal" font="default" size="100%">33-44</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The pathology and ultrastructure of the reproductive tract of Hz-2V-infected female corn earworm moths, Helicoverpa zea, were studied. The identity of malformed reproductive tissues found in virus-infected moths was determined by examining these tissues in moths that were infected with the virus at different life stages. Malformation of reproductive tissues in the progeny of virus-infected female moths was first observed by 3 days post-pupation (dpp), indicating that virus replication had altered the differentiation of these tissues very early on in their development. The ultrastructure of the grossly malformed agonadal reproductive tissues from insects aged 3-10dpp revealed the absence of the cuticular lining found in the oviducts of normal moths, and the proliferation of epithelial cells in these infected oviduct tissues. In addition, large quantities of virus were found aggregated into a large mass in the lumen of the malformed cervix bursa of 10dpp agonadal female pharate adult moths. Prior to eclosion, the virus in the cervix bursa was observed separated into spherical masses, which are thought to exude through the ductus bursa and collect over the vulva, forming a viral &quot;waxy plug&quot; that is likely to play an important role in virus transmission.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12417211?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rallis, Christopher P</style></author><author><style face="normal" font="default" size="100%">Burand, John P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Pathology and ultrastructure of the insect virus, Hz-2V, infecting agonadal male corn earworms, Helicoverpa zea.</style></title><secondary-title><style face="normal" font="default" size="100%">J Invertebr Pathol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Invertebr. Pathol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Insect Viruses</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Moths</style></keyword><keyword><style  face="normal" font="default" size="100%">Testis</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Diseases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">80</style></volume><pages><style face="normal" font="default" size="100%">81-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The pathology of the reproductive tract of Hz-2V-infected agonadal male corn earworm moths, Helicoverpa zea, was studied. The examination of the reproductive tissues of adult agonadal males infected with Hz-2V during different lifestages allowed us to positively correlate the grossly malformed tissues of typical agonadal male moths to the corresponding normal tissues in uninfected males. The reproductive tissues responsible for producing sperm, a pheromonostatic peptide (PSP), and the spermatophore in normal male moths were absent or grossly malformed in the agonadal male moths. Hz-2V was observed replicating in one area of these malformed reproductive tissues in pharate adult males as early as 7 days post-pupation. Interestingly, reproductive tissues essential for initiation of copulation and transfer of reproductive fluids into a female moth during mating appear to be intact and may be functional. These data suggest that agonadal adult males are able to mate with healthy female moths and transfer Hz-2V particles, without fertilizing female moths or altering their sexual receptivity to further mating with other male moths.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12383433?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mukherjee, Jean</style></author><author><style face="normal" font="default" size="100%">Chios, Kerry</style></author><author><style face="normal" font="default" size="100%">Fishwild, Dianne</style></author><author><style face="normal" font="default" size="100%">Hudson, Deborah</style></author><author><style face="normal" font="default" size="100%">O'Donnell, Susan</style></author><author><style face="normal" font="default" size="100%">Rich, Stephen M</style></author><author><style face="normal" font="default" size="100%">Donohue-Rolfe, Arthur</style></author><author><style face="normal" font="default" size="100%">Tzipori, Saul</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Production and characterization of protective human antibodies against Shiga toxin 1.</style></title><secondary-title><style face="normal" font="default" size="100%">Infect Immun</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Infect. Immun.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibodies, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibodies, Monoclonal</style></keyword><keyword><style  face="normal" font="default" size="100%">Child</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">HeLa Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemolytic-Uremic Syndrome</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hybridomas</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunization, Passive</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin G</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoglobulin M</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Neutralization Tests</style></keyword><keyword><style  face="normal" font="default" size="100%">Shiga Toxin 1</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2002 Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">70</style></volume><pages><style face="normal" font="default" size="100%">5896-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Hemolytic-uremic syndrome (HUS) is a serious complication which is predominantly associated in children with infection by Shiga toxin-producing Escherichia coli (STEC). By using HuMAb-Mouse (Medarex) animals, human monoclonal antibodies (Hu-MAbs) were developed against Shiga toxin 1 (Stx1) for passive immunotherapy of HUS. Ten stable hybridomas comprised of fully human heavy- and light-chain immunoglobulin elements and secreting Stx1-specific Hu-MAbs (seven immunoglobulin M(kappa)() [IgM(kappa)] elements [one specific for the A subunit and six specific for the B subunit] and three IgG1(kappa) elements specific for subunit B) were isolated. Two IgM(kappa) Hu-MAbs (2D9 and 15G9) and three IgG1(kappa) Hu-MAbs (5A4, 10F4, and 15G2), all specific for subunit B, demonstrated marked neutralization of Stx1 in vitro and significant prolongation of survival in a murine model of Stx1 toxicosis.</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12228326?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author><author><style face="normal" font="default" size="100%">Wolfrom, S A</style></author><author><style face="normal" font="default" size="100%">Stuart, E S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Association of caveolin with Chlamydia trachomatis inclusions at early and late stages of infection.</style></title><secondary-title><style face="normal" font="default" size="100%">Exp Cell Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Exp. Cell Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Chlamydia trachomatis</style></keyword><keyword><style  face="normal" font="default" size="100%">Epithelium</style></keyword><keyword><style  face="normal" font="default" size="100%">Filipin</style></keyword><keyword><style  face="normal" font="default" size="100%">HeLa Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Inclusion Bodies</style></keyword><keyword><style  face="normal" font="default" size="100%">Macrophages</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Microdomains</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Nystatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Phagosomes</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 Jun 10</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">266</style></volume><pages><style face="normal" font="default" size="100%">229-38</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The mechanism by which the intracellular bacterial pathogen Chlamydia trachomatis enters eukaryotic cells is poorly understood. There are conflicting reports of entry occurring by clathrin-dependent and clathrin-independent processes. We report here that C. trachomatis serovar K enters HEp-2 and HeLa 229 epithelial cells and J-774A.1 mouse macrophage/monocyte cells via caveolin-containing sphingolipid and cholesterol-enriched raft microdomains in the host cell plasma membranes. First, filipin and nystatin, drugs that specifically disrupt raft function by cholesterol chelation, each impaired entry of C. trachomatis serovar K. In control experiments, filipin did not impair entry of the same organism by an antibody-mediated opsonic process, nor did it impair entry of BSA-coated microspheres. Second, the chlamydia-containing endocytic vesicles specifically reacted with antisera against the caveolae marker protein caveolin. These vesicles are known to become the inclusions in which parasite replication occurs. They avoid fusion with lysosomes and instead traffic to the Golgi region, where they intercept Golgi-derived vesicles that recycle sphingolipids and cholesterol to the plasma membrane. We also report that late-stage C. trachomatis inclusions continue to display high levels of caveolin, which they likely acquire from the exocytic Golgi vesicles. We suggest that the atypical raft-mediated entry process may have important consequences for the host-pathogen interaction well after entry has occurred. These consequences include enabling the chlamydial vesicle to avoid acidification and fusion with lysosomes, to traffic to the Golgi region, and to intercept sphingolipid-containing vesicles from the Golgi.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11399051?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Caveolae in the uptake and targeting of infectious agents and secreted toxins.</style></title><secondary-title><style face="normal" font="default" size="100%">Adv Drug Deliv Rev</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Adv. Drug Deliv. Rev.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolae</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Toxins, Biological</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Diseases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 Jul 28</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">49</style></volume><pages><style face="normal" font="default" size="100%">301-15</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">A variety of microbial pathogens, including viruses, intracellular bacteria, and prions, as well as certain secreted bacterial toxins, can now be added to the list of ligands that enter cells via caveolae or caveolae-like membrane domains. In general, the caveolae-mediated entry pathway results in transport of these microbes and toxins to intracellular destinations that are different from that of cargo entering by other means. As a result, the caveolae-mediated entry pathway can profoundly affect the host cell-pathogen interaction long after entry has occurred. Furthermore, some microbes such as SV40 that enter via cavolae will be valuable as probes to analyze certain poorly understood intracellular trafficking pathways, such as retrograde transport to the ER. Also, viruses that enter via caveolae may have unique potential as gene and drug delivery vectors. In addition, some extracellular microbial pathogens, such as Pneumocystis carinii, may also interact with host cells via caveolae. Finally, caveolae may play a role in host immune defense mechanisms.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11551401?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Armstrong, P M</style></author><author><style face="normal" font="default" size="100%">Smith, R D</style></author><author><style face="normal" font="default" size="100%">Telford, S R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lone star tick-infecting borreliae are most closely related to the agent of bovine borreliosis.</style></title><secondary-title><style face="normal" font="default" size="100%">J Clin Microbiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Clin. Microbiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Flagellin</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Lyme Disease</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Relapsing Fever</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Ribosomal, 16S</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Tick-Borne Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Ticks</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">39</style></volume><pages><style face="normal" font="default" size="100%">494-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Although Borrelia theileri, the agent of bovine borreliosis, was described at the turn of the century (in 1903), its relationship with borreliae causing Lyme disease or relapsing fever remains undescribed. We tested the previously published hypothesis that spirochetes infecting Lone Star ticks (Amblyomma americanum) may comprise B. theileri by analyzing the 16S ribosomal DNAs (rDNAs) and flagellin genes of these spirochetes. B. theileri, the Amblyomma agent, and B. miyamotoi formed a natural group or clade distinct from but most closely related to that of the relapsing fever spirochetes. B. theileri and the Amblyomma agent were 97 and 98% similar at the nucleotide level within the analyzed portions of the 16S rDNA and the flagellin gene respectively, suggesting a recent divergence. The agent of bovine borreliosis might be explored as a surrogate antigen for the as-yet-uncultivatable Amblyomma agent in studies designed to explore the etiology of a Lyme disease-like infection associated with Lone Star ticks.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11158095?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Morris, J C</style></author><author><style face="normal" font="default" size="100%">Drew, M E</style></author><author><style face="normal" font="default" size="100%">Klingbeil, M M</style></author><author><style face="normal" font="default" size="100%">Motyka, S A</style></author><author><style face="normal" font="default" size="100%">Saxowsky, T T</style></author><author><style face="normal" font="default" size="100%">Wang, Z</style></author><author><style face="normal" font="default" size="100%">Englund, P T</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Replication of kinetoplast DNA: an update for the new millennium.</style></title><secondary-title><style face="normal" font="default" size="100%">Int J Parasitol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Int. J. Parasitol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Crithidia fasciculata</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Kinetoplast</style></keyword><keyword><style  face="normal" font="default" size="100%">Forecasting</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 May 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">31</style></volume><pages><style face="normal" font="default" size="100%">453-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">In this review we will describe the replication of kinetoplast DNA, a subject that our lab has studied for many years. Our knowledge of kinetoplast DNA replication has depended mostly upon the investigation of the biochemical properties and intramitochondrial localisation of replication proteins and enzymes as well as a study of the structure and dynamics of kinetoplast DNA replication intermediates. We will first review the properties of the characterised kinetoplast DNA replication proteins and then describe our current model for kinetoplast DNA replication.</style></abstract><issue><style face="normal" font="default" size="100%">5-6</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11334929?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lu, H</style></author><author><style face="normal" font="default" size="100%">Burand, J P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Replication of the gonad-specific virus Hz-2V in Ld652Y cells mimics replication in vivo.</style></title><secondary-title><style face="normal" font="default" size="100%">J Invertebr Pathol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Invertebr. Pathol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Baculoviridae</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">Lepidoptera</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Mimicry</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Cultivation</style></keyword><keyword><style  face="normal" font="default" size="100%">Virus Replication</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 Jan</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">77</style></volume><pages><style face="normal" font="default" size="100%">44-50</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">A newly discovered, nonoccluded insect virus, known as gonad-specific virus or Hz-2V, was found to replicate differently in two insect cell lines derived from ovarian tissues (Tn-368 cells from Trichoplusia ni and Ld652Y from Lymantria dispar). Differences between these two cell lines were observed in virus plaque forming ability, rate of viral DNA replication, time course of infectious virus production, and the mechanism of virus release from infected cells. Replication of Hz-2V in Ld652Y cells was more productive and more closely resembled in vivo virus replication.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11161993?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Klingbeil, M M</style></author><author><style face="normal" font="default" size="100%">Drew, M E</style></author><author><style face="normal" font="default" size="100%">Liu, Y</style></author><author><style face="normal" font="default" size="100%">Morris, J C</style></author><author><style face="normal" font="default" size="100%">Motyka, S A</style></author><author><style face="normal" font="default" size="100%">Saxowsky, T T</style></author><author><style face="normal" font="default" size="100%">Wang, Z</style></author><author><style face="normal" font="default" size="100%">Englund, P T</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Unlocking the secrets of trypanosome kinetoplast DNA network replication.</style></title><secondary-title><style face="normal" font="default" size="100%">Protist</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Protist</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Replication</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Kinetoplast</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Trypanosoma brucei brucei</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2001</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2001 Dec</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">152</style></volume><pages><style face="normal" font="default" size="100%">255-62</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11822657?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Widmer, G</style></author><author><style face="normal" font="default" size="100%">Akiyoshi, D</style></author><author><style face="normal" font="default" size="100%">Buckholt, M A</style></author><author><style face="normal" font="default" size="100%">Feng, X</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Deary, K M</style></author><author><style face="normal" font="default" size="100%">Bowman, C A</style></author><author><style face="normal" font="default" size="100%">Xu, P</style></author><author><style face="normal" font="default" size="100%">Wang, Y</style></author><author><style face="normal" font="default" size="100%">Wang, X</style></author><author><style face="normal" font="default" size="100%">Buck, G A</style></author><author><style face="normal" font="default" size="100%">Tzipori, S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Animal propagation and genomic survey of a genotype 1 isolate of Cryptosporidium parvum.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biochem Parasitol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Biochem. Parasitol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidium parvum</style></keyword><keyword><style  face="normal" font="default" size="100%">Genome, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Genotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Germ-Free Life</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Restriction Fragment Length</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Analysis, DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">Swine</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2000 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">108</style></volume><pages><style face="normal" font="default" size="100%">187-97</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Human cryptosporidiosis is attributed to two major Cryptosporidium parvum genotypes of which type 1 appears to be the predominant. Most laboratory investigations however are performed using genotype 2 isolates, the only type which readily infects laboratory animals. So far type 1 has only been identified in humans and primates. A type 1 isolate, obtained from an individual with HIV and cryptosporidiosis, was successfully adapted to propagate in gnotobiotic piglets. Genotypic characterization of oocyst DNA from this isolate using multiple restriction fragment length polymorphisms, a genotype-specific PCR marker, and direct sequence analysis of two polymorphic loci confirmed that this isolate, designated NEMC1, is indeed type 1. No changes in the genetic profile were identified during multiple passages in piglets. In contrast, the time period between infection and onset of fecal oocyst shedding, an indicator of adaptation, decreased with increasing number of passages. Consistent with other type 1 isolates, NEMC1 failed to infect mice. A preliminary survey of the NEMC1 genome covering approximately 2% of the genome and encompassing 200 kb of unique sequence showed an average similarity of approximately 95% between type 1 and 2 sequences. Twenty-four percent of the NEMC1 sequences were homologous to previously determined genotype 2 C. parvum sequences. To our knowledge, this is the first successful serial propagation of genotype 1 in animals, which should facilitate characterization of the unique features of this human pathogen.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10838221?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Craig, S A</style></author><author><style face="normal" font="default" size="100%">Holden, J F</style></author><author><style face="normal" font="default" size="100%">Khaled, M Y</style></author><author><style face="normal" font="default" size="100%">Craig, S A</style></author><author><style face="normal" font="default" size="100%">Holden, J F</style></author><author><style face="normal" font="default" size="100%">Khaled, M Y</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Determination of polydextrose as dietary fiber in foods.</style></title><secondary-title><style face="normal" font="default" size="100%">J AOAC Int</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J AOAC Int</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Anions</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Beverages</style></keyword><keyword><style  face="normal" font="default" size="100%">Cacao</style></keyword><keyword><style  face="normal" font="default" size="100%">Candy</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromatography, Ion Exchange</style></keyword><keyword><style  face="normal" font="default" size="100%">Dietary Fiber</style></keyword><keyword><style  face="normal" font="default" size="100%">Ethanol</style></keyword><keyword><style  face="normal" font="default" size="100%">Food Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Glucan 1,4-alpha-Glucosidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Glucans</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoside Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrolysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoamylase</style></keyword><keyword><style  face="normal" font="default" size="100%">Tea</style></keyword><keyword><style  face="normal" font="default" size="100%">Ultrafiltration</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2000 Jul-Aug</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">83</style></volume><pages><style face="normal" font="default" size="100%">1006-12</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Polydextrose (Litesse) provides physiological effects consistent with dietary fiber. However, AOAC methods for measuring total dietary fiber (TDF) in foods include an ethanol precipitation step in which polydextrose and similar carbohydrates are discarded and therefore not quantitated. This study describes a method developed to quantitate polydextrose in foods. The new method includes water extraction, centrifugal ultrafiltration, multienzyme hydrolysis, and anion exchange chromatography with electrochemical detection. Six foods were prepared with 4 levels of polydextrose to test the ruggedness of the method. Internal validation demonstrated the ruggedness of the method with recoveries ranging from 83 to 104% with an average of 95% (n = 24) and relative standard deviation of recoveries ranging from 0.7 to 13% with an average of 3.3% (n = 24). The value is added to that obtained for dietary fiber content of foods using the AOAC methods, to determine the TDF content of the food.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10995130?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Feng, X</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Akiyoshi, D</style></author><author><style face="normal" font="default" size="100%">Tumwine, J K</style></author><author><style face="normal" font="default" size="100%">Kekitiinwa, A</style></author><author><style face="normal" font="default" size="100%">Nabukeera, N</style></author><author><style face="normal" font="default" size="100%">Tzipori, S</style></author><author><style face="normal" font="default" size="100%">Widmer, G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Extensive polymorphism in Cryptosporidium parvum identified by multilocus microsatellite analysis.</style></title><secondary-title><style face="normal" font="default" size="100%">Appl Environ Microbiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Appl. Environ. Microbiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Cryptosporidium parvum</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Karyotyping</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Knockout</style></keyword><keyword><style  face="normal" font="default" size="100%">Microsatellite Repeats</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Analysis, DNA</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2000 Aug</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">3344-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Restriction fragment length polymorphism and DNA sequence analysis discern two main types of Cryptosporidium parvum. We present a survey of length polymorphism at several microsatellite loci for type 1 and type 2 isolates. A total of 14 microsatellite loci were identified from C. parvum DNA sequences deposited in public databases. All repeats were mono-, di-, and trinucleotide repeats of A, AT, and AAT, reflecting the high AT content of the C. parvum genome. Several of these loci showed significant length polymorphism, with as many as seven alleles identified for a single locus. Differences between alleles ranged from 1 to 27 bp. Karyotype analysis using probes flanking three microsatellites localized each marker to an individual chromosomal band, suggesting that these markers are single copy. In a sample of 19 isolates for which at least three microsatellites were typed, a majority of isolates displayed a unique multilocus fingerprint. Microsatellite analysis of isolates passaged between different host species identified genotypic changes consistent with changes in parasite populations.</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10919789?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ayala, F J</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Genetic variation and the recent worldwide expansion of Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Gene</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Gene</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Variation</style></keyword><keyword><style  face="normal" font="default" size="100%">Merozoite Surface Protein 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Repetitive Sequences, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Ribosomal</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Nucleic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2000 Dec 30</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">261</style></volume><pages><style face="normal" font="default" size="100%">161-70</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Plasmodium falciparum, the agent of human malignant malaria, diverged from Plasmodium reichenowi, the chimpanzee parasite, about the time the human and chimpanzee lineages diverged from each other. The absence of synonymous nucleotide variation at ten loci indicates that the world populations of P. falciparum derive most recently from one single strain, or 'cenancestor,' which lived a few thousand years ago. Antigenic genes of P. falciparum (such as Csp, Msp-1, and Msp-2) exhibit numerous polymorphisms that have been estimated to be millions of years old. We have discovered in these antigenic genes short repetitive sequences that distort the alignment of alleles and account for the apparent old age of the polymorphisms. The processes of intragenic recombination that generate the repeats occur at rates about 10(-3) to 10(-2), several orders of magnitude greater than the typical mutational process of nucleotide substitutions. We conclude that the antigenic polymorphisms of P. falciparum are consistent with a recent expansion of the world populations of the parasite from a cenancestor that lived in tropical Africa a few thousand years ago.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/11164047?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Ferreira, M U</style></author><author><style face="normal" font="default" size="100%">Ayala, F J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The origin of antigenic diversity in Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Parasitol Today</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Parasitol. Today (Regul. Ed.)</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Variation</style></keyword><keyword><style  face="normal" font="default" size="100%">Merozoite Surface Protein 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2000 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">16</style></volume><pages><style face="normal" font="default" size="100%">390-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Most studies of genetic variability of Plasmodium falciparum have focused on protein antigens and the genes that encode them. The consensus is that populations exhibit high levels of genetic polymorphism, most notably the genes encoding surface proteins of the merozoite (Msp1, Msp2) and the sporozoite (Csp). The age and derivation of this variation is a subject that warrants further careful consideration, as discussed here by Stephen Rich, Marcelo Ferreira and Francisco Ayala.</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10951599?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Ayala, F J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Population structure and recent evolution of Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Evolution</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetics, Population</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2000 Jun 20</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">97</style></volume><pages><style face="normal" font="default" size="100%">6994-7001</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Plasmodium falciparum is the agent of malignant malaria, one of mankind's most severe maladies. The parasite exhibits antigenic polymorphisms that have been postulated to be ancient. We have proposed that the extant world populations of P. falciparum have derived from one single parasite, a cenancestor, within the last 5, 000-50,000 years. This inference derives from the virtual or complete absence of synonymous nucleotide polymorphisms at genes not involved in immune or drug responses. Seeking to conciliate this claim with extensive antigenic polymorphism, we first note that allele substitutions or polymorphisms can arise very rapidly, even in a single generation, in large populations subject to strong natural selection. Second, new alleles can arise not only by single-nucleotide mutations, but also by duplication/deletion of short simple-repeat DNA sequences, a process several orders of magnitude faster than single-nucleotide mutation. We analyze three antigenic genes known to be extremely polymorphic: Csp, Msp-1, and Msp-2. We identify regions consisting of tandem or proximally repetitive short DNA sequences, including some previously unnoticed. We conclude that the antigenic polymorphisms are consistent with the recent origin of the world populations of P. falciparum inferred from the analysis of nonantigenic genes.</style></abstract><issue><style face="normal" font="default" size="100%">13</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10860962?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ayala, F J</style></author><author><style face="normal" font="default" size="100%">Escalante, A A</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Evolution of Plasmodium and the recent origin of the world populations of Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Parassitologia</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Parassitologia</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Hominidae</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Merozoite Surface Protein 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1999 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">41</style></volume><pages><style face="normal" font="default" size="100%">55-68</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We have investigated the evolution of Plasmodium parasites by analyzing DNA sequences of several genes. We reach the following conclusions: (1) The four human parasites, P. falciparum, P. malariae, P. ovale, and P. vivax are very remotely related to each other, so that their evolutionary divergence predates the origin of the hominids; several of these parasites became associated with the human lineage by lateral transfer from other hosts. (2) P. falciparum diverged from P. reichenowi about 8 million years ago, consistently with the time of divergence of the human lineage from the apes; a parsimonious inference is that falciparum has been associated with humans since the origin of the hominids. (3) P. malariae is genetically indistinguishable from P. brasilianum, a parasite of New World monkeys; and, similarly. (4) P. vivax is genetically indistinguishable from the New World monkey parasite P. simium. We infer in each of these two cases a very recent lateral transfer between the human and monkey hosts, and explore alternative hypotheses about the direction of the transfer. We have also investigated the population structure of P. falciparum by analyzing 10 genes and conclude that the extant world populations of this parasite have evolved from a single strain within the last several thousand years. The extensive polymorphisms observed in the highly repetitive central region of the Csp gene, as well as the apparently very divergent two classes of alleles at the Msa-1 gene, are consistent with this conclusion.</style></abstract><issue><style face="normal" font="default" size="100%">1-3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10697834?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Chen, Y</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Extracellular simian virus 40 transmits a signal that promotes virus enclosure within caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Exp Cell Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Exp. Cell Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Northern</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Cholesterol</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, myc</style></keyword><keyword><style  face="normal" font="default" size="100%">Genistein</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Microscopy, Electron</style></keyword><keyword><style  face="normal" font="default" size="100%">Nystatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Octoxynol</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Solubility</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1999 Jan 10</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">246</style></volume><pages><style face="normal" font="default" size="100%">83-90</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">It was reported earlier that entry of simian virus 40 (SV40) into cells is promoted by a signal transmitted by the virus from the cell surface and that SV40 enters cells through caveolae. It is shown here that bound SV40 begins to partition into a caveolae-enriched Triton X-100-insoluble membrane fraction at 30 min postadsorption. Maximal levels of SV40 were seen in that fraction at 1 h. The sterol-binding agent nystatin, which selectively disrupts the cholesterol-enriched caveolae-containing membrane microdomain, selectively blocked the SV40-induced signal. This implies that the SV40 signal is transmitted from that membrane microdomain. The tyrosine kinase inhibitor genistein, which was earlier shown to block the SV40-induced signal and infectious entry, did not block the partitioning of SV40 into the detergent-insoluble membrane fraction. This shows that the signal is not required for the translocation of SV40 to the detergent-insoluble membrane and is consistent with the finding that the signal is likely transmitted from that membrane microdomain. However, electron microscopy of the Triton X-100-insoluble membrane fraction showed that genistein caused SV40 particles to accumulate at the annuli or mouths of the caveolae. In contrast, most SV40 particles were found enclosed within caveolae in parallel samples from untreated control cells. Together, these results imply that SV40 initially binds to flat detergent-soluble membrane. The virus then translocates to a caveolae-containing detergent-insoluble membrane microdomain. From the flat portion of that membrane microdomain the virus induces a signal which promotes its entry into caveolae.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9882517?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Simian virus 40 infection via MHC class I molecules and caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Immunol Rev</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Immunol. Rev.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Papillomavirus Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Tumor Virus Infections</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1999 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">168</style></volume><pages><style face="normal" font="default" size="100%">13-22</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MHC class I molecules are a necessary component of the cell surface receptor for simian virus 40 (SV40). After binding to class I molecules, SV40 enters cells via a unique endocytic pathway that involves caveolae, rather than clathrin-coated pits. This pathway is dependent on a transmembrane signal that SV40 transmits from the cell surface. Furthermore, it delivers SV40 to the endoplasmic reticulum, rather than to the endosomal/lysosomal compartment, which is the usual target for endocytic traffic. The glycosphingolipid and cholesterol-enriched plasma membrane domains that contain caveolae are also enriched for class I molecules, relative to whole plasma membrane. Nevertheless, although class I molecules bind SV40, they do not enter with SV40, nor do they enter spontaneously into uninfected SV40 host cells. Instead, they are shed from the cell surface by the activity of a metalloprotease. These results imply the existence of a putative secondary receptor for SV40 that might mediate SV40 entry. It is not yet clear whether class I molecules are active in transmitting the SV40 signal. Monoclonal antibodies against class I molecules also induce a signal in the SV40 host cells. However, the antibody-induced signal is mediated by mitogen-activated protein kinase (MAP kinase), whereas the SV40 signal is independent of MAP kinase.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10399061?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Licht, M C</style></author><author><style face="normal" font="default" size="100%">Hudson, R R</style></author><author><style face="normal" font="default" size="100%">Ayala, F J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Malaria's Eve: evidence of a recent population bottleneck throughout the world populations of Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Africa</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Asia</style></keyword><keyword><style  face="normal" font="default" size="100%">Climate</style></keyword><keyword><style  face="normal" font="default" size="100%">Demography</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Life Cycle Stages</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Malaria, Falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Netherlands</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">South America</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetrahydrofolate Dehydrogenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Time</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1998</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1998 Apr 14</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">95</style></volume><pages><style face="normal" font="default" size="100%">4425-30</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We have analyzed DNA sequences from world-wide geographic strains of Plasmodium falciparum and found a complete absence of synonymous DNA polymorphism at 10 gene loci. We hypothesize that all extant world populations of the parasite have recently derived (within several thousand years) from a single ancestral strain. The upper limit of the 95% confidence interval for the time when this most recent common ancestor lived is between 24,500 and 57,500 years ago (depending on different estimates of the nucleotide substitution rate); the actual time is likely to be much more recent. The recent origin of the P. falciparum populations could have resulted from either a demographic sweep (P. falciparum has only recently spread throughout the world from a small geographically confined population) or a selective sweep (one strain favored by natural selection has recently replaced all others). The selective sweep hypothesis requires that populations of P. falciparum be effectively clonal, despite the obligate sexual stage of the parasite life cycle. A demographic sweep that started several thousand years ago is consistent with worldwide climatic changes ensuing the last glaciation, increased anthropophilia of the mosquito vectors, and the spread of agriculture. P. falciparum may have rapidly spread from its African tropical origins to the tropical and subtropical regions of the world only within the last 6,000 years. The recent origin of the world-wide P. falciparum populations may account for its virulence, as the most malignant of human malarial parasites.</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9539753?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Anderson, H A</style></author><author><style face="normal" font="default" size="100%">Chen, Y</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">MHC class I molecules are enriched in caveolae but do not enter with simian virus 40.</style></title><secondary-title><style face="normal" font="default" size="100%">J Gen Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Gen. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1998</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1998 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">79 ( Pt 6)</style></volume><pages><style face="normal" font="default" size="100%">1469-77</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) binds to MHC class I molecules anywhere on the cell surface and then enters through caveolae. The fate of class I molecules after SV40 binding is not known. Sensitivity of 125I-surface-labelled class I molecules to papain cleavage was used to distinguish internalized class I molecules from class I molecules remaining at the cell surface. Whereas the caveolae-enriched membrane microdomain was found to also be enriched for class I molecules, no internalized papain-resistant 125I-surface-labelled class I molecules could be detected at any time in either control cells or in cells preadsorbed with saturating amounts of SV40. Instead, 125I-surface-labelled class I molecules, as well as preadsorbed 125I-labelled anti-class I antibodies, accumulated in the medium, coincident with the turnover of class I molecules at the cell surface. The class I heavy chains that accumulated in the medium were truncated and their release was specifically prevented by the metalloprotease inhibitor 1,10-phenanthroline. Thus, whereas class I molecules mediate SV40 binding, they do not appear to mediate SV40 entry.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9634090?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Ayala, F J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The recent origin of allelic variation in antigenic determinants of Plasmodium falciparum.</style></title><secondary-title><style face="normal" font="default" size="100%">Genetics</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Genetics</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Alleles</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Epitopes</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Variation</style></keyword><keyword><style  face="normal" font="default" size="100%">Merozoite Surface Protein 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1998</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1998 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">150</style></volume><pages><style face="normal" font="default" size="100%">515-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9841225?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Klingbeil, M M</style></author><author><style face="normal" font="default" size="100%">Walker, D J</style></author><author><style face="normal" font="default" size="100%">Huang, Y J</style></author><author><style face="normal" font="default" size="100%">Komuniecki, R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Altered phosphorylation/inactivation of a novel pyruvate dehydrogenase in adult Ascaris suum muscle.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biochem Parasitol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Biochem. Parasitol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Ascaris suum</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscles</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphorylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein-Serine-Threonine Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Pyruvate Dehydrogenase (Lipoamide)</style></keyword><keyword><style  face="normal" font="default" size="100%">Pyruvate Dehydrogenase Complex</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1997</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1997 Dec 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">90</style></volume><pages><style face="normal" font="default" size="100%">323-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9497054?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Brendel, V</style></author><author><style face="normal" font="default" size="100%">Brocchieri, L</style></author><author><style face="normal" font="default" size="100%">Sandler, S J</style></author><author><style face="normal" font="default" size="100%">Clark, A J</style></author><author><style face="normal" font="default" size="100%">Karlin, S</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms.</style></title><secondary-title><style face="normal" font="default" size="100%">J Mol Evol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Mol. Evol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Archaeal Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacteria</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Cycle Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Consensus Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Conserved Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA-Binding Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Evolution, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Rad51 Recombinase</style></keyword><keyword><style  face="normal" font="default" size="100%">Rec A Recombinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1997</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1997 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">44</style></volume><pages><style face="normal" font="default" size="100%">528-41</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Protein sequences with similarities to Escherichia coli RecA were compared across the major kingdoms of eubacteria, archaebacteria, and eukaryotes. The archaeal sequences branch monophyletically and are most closely related to the eukaryotic paralogous Rad51 and Dmc1 groups. A multiple alignment of the sequences suggests a modular structure of RecA-like proteins consisting of distinct segments, some of which are conserved only within subgroups of sequences. The eukaryotic and archaeal sequences share an N-terminal domain which may play a role in interactions with other factors and nucleic acids. Several positions in the alignment blocks are highly conserved within the eubacteria as one group and within the eukaryotes and archaebacteria as a second group, but compared between the groups these positions display nonconservative amino acid substitutions. Conservation within the RecA-like core domain identifies possible key residues involved in ATP-induced conformational changes. We propose that RecA-like proteins derive evolutionarily from an assortment of independent domains and that the functional homologs of RecA in noneubacteria comprise an array of RecA-like proteins acting in series or cooperatively.</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9115177?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Rosenthal, B M</style></author><author><style face="normal" font="default" size="100%">Telford, S R</style></author><author><style face="normal" font="default" size="100%">Spielman, A</style></author><author><style face="normal" font="default" size="100%">Hartl, D L</style></author><author><style face="normal" font="default" size="100%">Ayala, F J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Heterogeneity of the internal transcribed spacer (ITS-2) region within individual deer ticks.</style></title><secondary-title><style face="normal" font="default" size="100%">Insect Mol Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Insect Mol. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Deer</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Ribosomal</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Heterogeneity</style></keyword><keyword><style  face="normal" font="default" size="100%">Ixodes</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1997</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1997 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">6</style></volume><pages><style face="normal" font="default" size="100%">123-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">To determine whether nuclear rDNA sequences provide a useful means for assessing the structure of populations of Ixodes ticks, we compared variability among copies of an internal transcribed spacer (ITS-2) sequence within individual ticks to the variability between ticks. At least 4% of the nucleotides comprising this sequence vary among the copies present within individual ticks. ITS-2 diversity in each of two ticks is nearly half as great as that reported between ticks from geographically disparate populations. Because individual ticks retain ancestral polymorphism, ITS-2 variation does not accurately reflect descent relationships among these ticks. Sequencing single copies of PCR-amplified ITS-2 therefore does not permit assessment of the phylogenetic relationships among the I. ricinus-like ticks in eastern North America. We recommend caution in future analyses, and emphasize the importance of procedures designed to ensure that the many paralogous copies of the rDNA cistron have been sufficiently homogenized by concerted evolutionary processes. Such precautionary measures will make certain that phylogenetic trees based on these gene sequences reflect the phyletic relatedness of the biological species.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9099576?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Hudson, R R</style></author><author><style face="normal" font="default" size="100%">Ayala, F J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Plasmodium falciparum antigenic diversity: evidence of clonal population structure.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Protozoan</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasmodium falciparum</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymorphism, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Protozoan Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombination, Genetic</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1997</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1997 Nov 25</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">94</style></volume><pages><style face="normal" font="default" size="100%">13040-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Plasmodium falciparum, the agent of malignant malaria, is one of mankind's most severe scourges. Efforts to develop preventive vaccines or remedial drugs are handicapped by the parasite's rapid evolution of drug resistance and protective antigens. We examine 25 DNA sequences of the gene coding for the highly polymorphic antigenic circumsporozoite protein. We observe total absence of silent nucleotide variation in the two nonrepeated regions of the gene. We propose that this absence reflects a recent origin (within several thousand years) of the world populations of P. falciparum from a single individual; the amino acid polymorphisms observed in these nonrepeat regions would result from strong natural selection. Analysis of these polymorphisms indicates that: (i) the incidence of recombination events does not increase with nucleotide distance; (ii) the strength of linkage disequilibrium between nucleotides is also independent of distance; and (iii) haplotypes in the two nonrepeat regions are correlated with one another, but not with the central repeat region they span. We propose two hypotheses: (i) variation in the highly polymorphic central repeat region arises by mitotic intragenic recombination, and (ii) the population structure of P. falciparum is clonal--a state of affairs that persists in spite of the necessary stage of physiological sexuality that the parasite must sustain in the mosquito vector to complete its life cycle.</style></abstract><issue><style face="normal" font="default" size="100%">24</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/9371796?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Anderson, H A</style></author><author><style face="normal" font="default" size="100%">Chen, Y</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Biol Cell</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Biol. Cell</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Polyomavirus Transforming</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolin 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Caveolins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Coated Vesicles</style></keyword><keyword><style  face="normal" font="default" size="100%">Endocytosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Membrane Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Nystatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Organelles</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetradecanoylphorbol Acetate</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996 Nov</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">1825-34</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) entry leading to infection occurred only after the virus was at the cell surface for 1.5 to 2 h. SV40 infectious entry was not sensitive to cytosol acidification, a treatment that blocks endocytosis via clathrin-coated vesicles. Instead, SV40 infectious entry was blocked by treating cells with the phorbol ester PMA or nystatin, which selectively disrupts caveolae. In control experiments, transferrin internalization was sensitive to cytosol acidification but was not sensitive to PMA or nystatin. Also, absorbed transferrin entered cells within minutes. Finally, bound SV40 translocated to caveolin-enriched membrane complexes isolated by a Triton X-100 insolubility protocol. Treatment with nystatin did not impair SV40 binding but did block the partitioning of virus into the caveolin-enriched complexes.</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8930903?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Dangoria, N S</style></author><author><style face="normal" font="default" size="100%">Breau, W C</style></author><author><style face="normal" font="default" size="100%">Anderson, H A</style></author><author><style face="normal" font="default" size="100%">Cishek, D M</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Extracellular simian virus 40 induces an ERK/MAP kinase-independent signalling pathway that activates primary response genes and promotes virus entry.</style></title><secondary-title><style face="normal" font="default" size="100%">J Gen Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Gen. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium-Calmodulin-Dependent Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Cycle Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Cercopithecus aethiops</style></keyword><keyword><style  face="normal" font="default" size="100%">Dual Specificity Phosphatase 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Inhibitors</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Viral</style></keyword><keyword><style  face="normal" font="default" size="100%">Genistein</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Immediate-Early Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoflavones</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitogen-Activated Protein Kinase 3</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitogen-Activated Protein Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Naphthalenes</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphoprotein Phosphatases</style></keyword><keyword><style  face="normal" font="default" size="100%">Platelet-Derived Growth Factor</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Kinase C</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Phosphatase 1</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Tyrosine Phosphatases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein-Serine-Threonine Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-jun</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-myc</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-raf</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-sis</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Up-Regulation</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">77 ( Pt 9)</style></volume><pages><style face="normal" font="default" size="100%">2173-82</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Simian virus 40 (SV40) binding to growth-arrested cells activated an intracellular signalling pathway that induced the up-regulation of the primary response genes c-myc, c-jun and c-sis within 30 min and of JE within 90 min. The up-regulation of the primary response genes occurred in the presence of cycloheximide and when UV-inactivated SV40 was adsorbed to cells. SV40 binding did not activate Raf or mitogen-activated protein kinase (MAP/ERK1), or mobilize intracellular Ca2+. The SV40-induced up-regulation of c-myc and c-jun was blocked by the tyrosine kinase inhibitor, genistein, and by the protein kinase C (PKC) inhibitor, calphostin C, but not by expression of the MAP kinase-specific phosphatase, MKP-1. These results suggest that the SV40-induced signalling pathway includes the activities of a tyrosine kinase and a Ca(2+)-independent isoform of PKC, but not of Raf or MAP kinase. Finally, SV40 infectious entry into cells was specifically and reversibly blocked by genistein.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8811017?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Klingbeil, M M</style></author><author><style face="normal" font="default" size="100%">Walker, D J</style></author><author><style face="normal" font="default" size="100%">Arnette, R</style></author><author><style face="normal" font="default" size="100%">Sidawy, E</style></author><author><style face="normal" font="default" size="100%">Hayton, K</style></author><author><style face="normal" font="default" size="100%">Komuniecki, P R</style></author><author><style face="normal" font="default" size="100%">Komuniecki, R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Identification of a novel dihydrolipoyl dehydrogenase-binding protein in the pyruvate dehydrogenase complex of the anaerobic parasitic nematode, Ascaris suum.</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Anaerobiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Ascaris suum</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Carrier Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Dihydrolipoamide Dehydrogenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrophoresis, Polyacrylamide Gel</style></keyword><keyword><style  face="normal" font="default" size="100%">Flavin-Adenine Dinucleotide</style></keyword><keyword><style  face="normal" font="default" size="100%">Helminth Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Larva</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">NAD</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Pyruvate Dehydrogenase Complex</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996 Mar 8</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">271</style></volume><pages><style face="normal" font="default" size="100%">5451-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">A novel dihydrolipoyl dehydrogenase-binding protein (E3BP) which lacks an amino-terminal lipoyl domain, p45, has been identified in the pyruvate dehydrogenase complex (PDC) of the adult parasitic nematode, Ascaris suum. Sequence at the amino terminus of p45 exhibited significant similarity with internal E3-binding domains of dihydrolipoyl transacetylase (E2) and E3BP. Dissociation and resolution of a pyruvate dehydrogenase-depleted adult A. suum PDC in guanidine hydrochloride resulted in two E3-depleted E2 core preparations which were either enriched or substantially depleted of p45. Following reconstitution, the p45-enriched E2 core exhibited enhanced E3 binding, whereas, the p45-depleted E2 core exhibited dramatically reduced E3 binding. Reconstitution of either the bovine kidney or A. suum PDCs with the A. suum E3 suggested that the ascarid E3 was more sensitive to NADH inhibition when bound to the bovine kidney core. The expression of p45 was developmentally regulated and p45 was most abundant in anaerobic muscle. In contrast, E3s isolated from anaerobic muscle or aerobic second-stage larvae were identical. These results suggest that during the transition to anaerobic metabolism, E3 remains unchanged, but it appears that a novel E3BP, p45, is expressed which may help to maintain the activity of the PDC in the face of the elevated intramitochondrial NADH/NAD+ ratios associated with anaerobiosis.</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8621401?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author><author><style face="normal" font="default" size="100%">Anderson, H A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multiple stages of virus-receptor interactions as shown by simian virus 40.</style></title><secondary-title><style face="normal" font="default" size="100%">Adv Exp Med Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Adv. Exp. Med. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">408</style></volume><pages><style face="normal" font="default" size="100%">159-67</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8895788?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Armstrong, P M</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Smith, R D</style></author><author><style face="normal" font="default" size="100%">Hartl, D L</style></author><author><style face="normal" font="default" size="100%">Spielman, A</style></author><author><style face="normal" font="default" size="100%">Telford, S R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">A new Borrelia infecting Lone Star ticks.</style></title><secondary-title><style face="normal" font="default" size="100%">Lancet</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Lancet</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Deer</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">Maryland</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Ticks</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996 Jan 6</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">347</style></volume><pages><style face="normal" font="default" size="100%">67-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">8993</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8531586?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Caporale, D A</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Spielman, A</style></author><author><style face="normal" font="default" size="100%">Telford, S R</style></author><author><style face="normal" font="default" size="100%">Kocher, T D</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Discriminating between Ixodes ticks by means of mitochondrial DNA sequences.</style></title><secondary-title><style face="normal" font="default" size="100%">Mol Phylogenet Evol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Mol. Phylogenet. Evol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Arachnid Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Dermacentor</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Mitochondrial</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Ixodes</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Ribosomal, 16S</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1995 Dec</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">361-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Ticks of the genus Ixodes have recently assumed prominence because they frequently serve as vectors of important zoonoses, including Lyme disease and babesiosis. The morphological characteristics that have been used in their identification often are ambiguous and are useful solely at a particular stage of development. Here we report the DNA sequence of the mitochondrially encoded 16S rRNA gene of nine different Ixodes ticks and an outgroup from another genus, Dermacentor. The sequences readily discriminate between these ticks. Samples of I. dammini from the northeastern and upper midwestern United States differ from southeastern I. scapularis at about 2% of the nucleotides. This difference is about half that separating other members of the I. ricinus group of species, but exceeds typical levels of intraspecific variation. Two major clades exist within the I. ricinus complex. One includes I. cookei, I. hexagonus, and I. angustus. The other includes I. persulcatus, I. pacificus, I. muris, I. ricinus, I. scapularis, and I. dammini. We conclude that mtDNA sequences are useful for unravelling the systematics of these important vectors of human disease.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8747292?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Caporale, D A</style></author><author><style face="normal" font="default" size="100%">Telford, S R</style></author><author><style face="normal" font="default" size="100%">Kocher, T D</style></author><author><style face="normal" font="default" size="100%">Hartl, D L</style></author><author><style face="normal" font="default" size="100%">Spielman, A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Distribution of the Ixodes ricinus-like ticks of eastern North America.</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Proc. Natl. Acad. Sci. U.S.A.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Demography</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Mitochondrial</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Ribosomal</style></keyword><keyword><style  face="normal" font="default" size="100%">Geography</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Phylogeny</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Population</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Ribosomal, 16S</style></keyword><keyword><style  face="normal" font="default" size="100%">Ticks</style></keyword><keyword><style  face="normal" font="default" size="100%">United States</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1995 Jul 3</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">92</style></volume><pages><style face="normal" font="default" size="100%">6284-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">We analyzed the geographic distribution of the Ixodes ricinus-like ticks in eastern North America by comparing the mitochondrial 16S rDNA sequences of specimens sampled directly from the field during the 1990s. Two distinct lineages are evident. The southern clade includes ticks from the southeastern and middle-eastern regions of the United States. The range of the northern clade, which appears to have been restricted to the northeastern region until the mid-1900s, now extends throughout the northeastern and middle-eastern regions. These phyletic units correspond to northern and southern taxa that have previously been assigned specific status as Ixodes dammini and Ixodes scapularis, respectively. The expanding range of I. dammini appears to drive the present outbreaks of zoonotic disease in eastern North America that include Lyme disease and human babesiosis.</style></abstract><issue><style face="normal" font="default" size="100%">14</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/7603983?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lafond, R E</style></author><author><style face="normal" font="default" size="100%">Giammalvo, J T</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Relationship between expression of epidermal growth factor and simian virus 40 T antigen in a line of transgenic mice.</style></title><secondary-title><style face="normal" font="default" size="100%">Transgenic Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Transgenic Res.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adenocarcinoma</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antigens, Viral, Tumor</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Choroid Plexus</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetinae</style></keyword><keyword><style  face="normal" font="default" size="100%">Epidermal Growth Factor</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Neoplastic</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney Tubules, Distal</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice, Transgenic</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Submandibular Gland</style></keyword><keyword><style  face="normal" font="default" size="100%">Submandibular Gland Neoplasms</style></keyword><keyword><style  face="normal" font="default" size="100%">Wnt Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Wnt1 Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Zebrafish Proteins</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1995 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">306-14</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The pattern of expression of the simian virus 40 (SV40) T antigen gene and resultant dysplasia were re-examined in a line of transgenic mice in which the T antigen gene was under the control of the SV40 early promoter. We found that T antigen expression in the kidney, and resulting dysplastic lesions, occurred exclusively in the distal convoluted tubules and the ascending limbs of Henle. Epidermal growth factor (EGF) expression in the kidney of normal mice was similarly immunolocalized. The correlation between high EGF immunoreactivity in normal mouse tissues and T antigen expression in the transgenic counterpart was also seen in the choroid plexus epithelium and in the submandibular glands of male mice. T antigen was not found in the submandibular gland of transgenic females. Similarly, EGF was only rarely detected in the normal female submandibular gland. In contrast to the correlation between T antigen expression in the transgenic mice and EGF expression in the corresponding tissues of the normal mice, within the dysplastic lesions of the transgenic mice EGF expression was severely diminished. Adenocarcinomas of the male submandibular gland from another line of transgenic mice that expresses the Int-1 transgene, showed similarly reduced levels of immunostaining for EGF. Thus, reduced expression of EGF might be a general feature of dysplasia and tumorigenesis in those tissues that normally express EGF.</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8589733?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Duran, E</style></author><author><style face="normal" font="default" size="100%">Komuniecki, R W</style></author><author><style face="normal" font="default" size="100%">Komuniecki, P R</style></author><author><style face="normal" font="default" size="100%">Wheelock, M J</style></author><author><style face="normal" font="default" size="100%">Klingbeil, M M</style></author><author><style face="normal" font="default" size="100%">Ma, Y C</style></author><author><style face="normal" font="default" size="100%">Johnson, K R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Characterization of cDNA clones for the 2-methyl branched-chain enoyl-CoA reductase. An enzyme involved in branched-chain fatty acid synthesis in anaerobic mitochondria of the parasitic nematode Ascaris suum.</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Biol. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Anaerobiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Ascaris suum</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Cloning, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Consensus Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Complementary</style></keyword><keyword><style  face="normal" font="default" size="100%">Fatty Acid Desaturases</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Library</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondria</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Oligonucleotides, Antisense</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidoreductases</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidoreductases Acting on CH-CH Group Donors</style></keyword><keyword><style  face="normal" font="default" size="100%">Poly A</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA</style></keyword><keyword><style  face="normal" font="default" size="100%">RNA, Messenger</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1993</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1993 Oct 25</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">268</style></volume><pages><style face="normal" font="default" size="100%">22391-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The 2-methyl branched-chain enoyl-CoA reductase plays a pivotal role in the reversal of beta-oxidation operating in anaerobic mitochondria of the parasitic nematode Ascaris suum. An affinity-purified polyclonal anti-serum against the reductase was used to screen a cDNA library constructed in lambda gt11 with poly(A)+ RNA from adult A. suum muscle. A 1.2-kilobase partial cDNA clone was isolated, subcloned, and sequenced in both directions. Additional sequence at the 5' end of the mRNA was determined by the RACE (rapid amplification of cDNA ends) procedure. Nucleotide sequence analysis of the cDNAs revealed the 22-nucleotide trans-spliced leader sequence characteristic of many nematode mRNAs, an open reading frame of 1236 nucleotides and a 3'-untranslated sequence of 109 nucleotides including a short poly(A) tail 14 nucleotides from a polyadenylation signal (AATAAA). The open reading frame encoded a 396-amino acid sequence (M(r) 43,046) including a 16-amino acid leader peptide. Two-dimensional gel electrophoresis of the purified reductase yielded multiple spots with two distinct but overlapping amino-terminal amino acid sequences. Both sequences overlapped with the sequence predicted from the mRNA, and one of the sequences was identical to the predicted sequence. Comparison of the ascarid sequence with that of mammalian acyl-CoA dehydrogenases revealed a high degree of sequence identity, suggesting that these enzymes may have evolved from a common ancestral gene even though the ascarid enzyme functions as a reductase, not as a dehydrogenase. Immunoblotting of A. suum larval stages and adult tissues with antisera that cross-reacted with each of the spots separated on two-dimensional gels suggested that the reductase was only found in adult muscle. Northern blotting using the partial cDNA revealed a hybridization band of about 1.5 kilobases and also suggested that the enzyme was tissue-specific and developmentally regulated in agreement with the results of the immunoblotting.</style></abstract><issue><style face="normal" font="default" size="100%">30</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/7693666?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rand, P W</style></author><author><style face="normal" font="default" size="100%">Lacombe, E H</style></author><author><style face="normal" font="default" size="100%">Smith, R P</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Kilpatrick, C W</style></author><author><style face="normal" font="default" size="100%">Dragoni, C A</style></author><author><style face="normal" font="default" size="100%">Caporale, D</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Competence of Peromyscus maniculatus (Rodentia: Cricetidae) as a reservoir host for Borrelia burgdorferi (Spirochaetares: Spirochaetaceae) in the wild.</style></title><secondary-title><style face="normal" font="default" size="100%">J Med Entomol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Med. Entomol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia burgdorferi Group</style></keyword><keyword><style  face="normal" font="default" size="100%">Host-Parasite Interactions</style></keyword><keyword><style  face="normal" font="default" size="100%">Lyme Disease</style></keyword><keyword><style  face="normal" font="default" size="100%">Peromyscus</style></keyword><keyword><style  face="normal" font="default" size="100%">Ticks</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1993</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1993 May</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">614-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Although capable of maintaining and transmitting Borrelia burgdorferi Johnson, Schmidt, Hyde, Steigerwalt &amp; Brenner, the causative spirochete of Lyme disease, in the laboratory, the specific ability of deer mice, Peromyscus maniculatus Le Conte, to support this zoonosis has not been established. Demonstration that P. maniculatus is a competent reservoir host in the wild would indicate that the spread of Lyme disease is not limited to the range of the primary reservoir host, P. leucopus Rafinesque. Isle au Haut, an offshore Maine island upon which the vector tick Ixodes dammini Spielman, Clifford, Piesman &amp; Corwin has become established, supports an isolated population of mice that are exclusively P. maniculatus. We examined the reservoir competence of this species by comparing infection rates of B. burgdorferi among juvenile ticks removed from livetrapped mice on this island with those removed from P. leucopus obtained at a mainland site endemic for Lyme disease. Equivalent rates of infection among engorged larval ticks, survival of infection through the larval-nymphal molt, and the isolation of B. burgdorferi from mice at both sites attest to the reservoir competence of P. maniculatus.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8510121?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Smith, R P</style></author><author><style face="normal" font="default" size="100%">Rand, P W</style></author><author><style face="normal" font="default" size="100%">Lacombe, E H</style></author><author><style face="normal" font="default" size="100%">Telford, S R</style></author><author><style face="normal" font="default" size="100%">Rich, S M</style></author><author><style face="normal" font="default" size="100%">Piesman, J</style></author><author><style face="normal" font="default" size="100%">Spielman, A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Norway rats as reservoir hosts for Lyme disease spirochetes on Monhegan Island, Maine.</style></title><secondary-title><style face="normal" font="default" size="100%">J Infect Dis</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Infect. Dis.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals, Domestic</style></keyword><keyword><style  face="normal" font="default" size="100%">Antibodies, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Borrelia burgdorferi Group</style></keyword><keyword><style  face="normal" font="default" size="100%">Cats</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Reservoirs</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Vectors</style></keyword><keyword><style  face="normal" font="default" size="100%">Dogs</style></keyword><keyword><style  face="normal" font="default" size="100%">Geography</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Incidence</style></keyword><keyword><style  face="normal" font="default" size="100%">Lyme Disease</style></keyword><keyword><style  face="normal" font="default" size="100%">Maine</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Ticks</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1993</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1993 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">168</style></volume><pages><style face="normal" font="default" size="100%">687-91</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">To determine whether the agent of Lyme disease, Borrelia burgdorferi, may be maintained in the absence of its usual white-footed mouse reservoir host, Ixodes dammini ticks from an island where mice are absent were examined. Prevalence of spirochetal infection was described for ticks removed from mammals, birds, and vegetation on Monhegan Island, Maine. Forty percent of adult I. dammini removed from vegetation were infected. Norway rats were heavily infested with ticks, and &gt; 60% of such ticks contained spirochetes. Other hosts were less frequently infested by ticks, and few such ticks were infected by spirochetes. The prevalence of antibody to B. burgdorferi was 23% in dogs and cats; 4% of island residents had Lyme disease. Thus, rats maintain Lyme disease spirochetes on Monhegan Island, and there may be transmission of this agent by I. dammini to island residents and their pets.</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8354910?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Breau, W C</style></author><author><style face="normal" font="default" size="100%">Atwood, W J</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Class I major histocompatibility proteins are an essential component of the simian virus 40 receptor.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding, Competitive</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Flow Cytometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Precipitin Tests</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Transfection</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1992</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1992 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">2037-45</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The class I molecules encoded by the major histocompatibility complex (MHC) present endogenously synthesized antigenic peptide fragments to cytotoxic T lymphocytes. We show here that these proteins are an essential component of the cell surface receptor for simian virus 40 (SV40). First, SV40 binding to cells can be blocked by two monoclonal antibodies against class I human lymphocyte antigen (HLA) proteins but not by monoclonal antibodies specific for other cell surface proteins. Second, SV40 does not bind to cells of two different human lymphoblastoid cell lines which do not express surface class I MHC proteins because of genetic defects in the beta 2-microglobulin gene in one line and in the HLA complex in the other. Transfection of these cell lines with cloned genes for beta 2-microglobulin and HLA-B8, respectively, restored expression of their surface class I MHC proteins and resulted in concomitant SV40 binding. Finally, SV40 binds to purified HLA proteins in vitro and selectively binds to class I MHC proteins in a cell surface extract.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/1312619?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Lovley, D R</style></author><author><style face="normal" font="default" size="100%">Greening, R C</style></author><author><style face="normal" font="default" size="100%">Ferry, J G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Rapidly growing rumen methanogenic organism that synthesizes coenzyme M and has a high affinity for formate.</style></title><secondary-title><style face="normal" font="default" size="100%">Appl Environ Microbiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Appl. Environ. Microbiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Culture Media</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Induction</style></keyword><keyword><style  face="normal" font="default" size="100%">Euryarchaeota</style></keyword><keyword><style  face="normal" font="default" size="100%">Formates</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mercaptoethanol</style></keyword><keyword><style  face="normal" font="default" size="100%">Mesna</style></keyword><keyword><style  face="normal" font="default" size="100%">Rumen</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1984</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1984 Jul</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">48</style></volume><pages><style face="normal" font="default" size="100%">81-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Methanogenic bacteria with a coccobacillus morphology similar to Methanobrevibacter ruminantium were isolated from the bovine rumen. One isolate, 10-16B, represented a previously undescribed rumen population that, unlike M. ruminantium, synthesized coenzyme M, grew rapidly (mu = 0.24 h-1) on H2-CO2 in a complex medium, had simple nutritional requirements, and metabolized formate at reported rumen concentrations. H2 was metabolized to partial pressures 10-fold lower than those reported for the rumen. After H2 starvation for 26 h, strain 10-16B rapidly resumed growth when H2 was made available. The minimum concentrations of acetate (6 mM) and ammonia (less than 7 mM) that were required for optimal growth were lower than the reported acetate and ammonia concentrations in the rumen. Isoleucine and leucine stimulated growth, but only at concentrations (greater than 50 microM) higher than those reported for the rumen. Another coccobacillary methanogenic organism that synthesized coenzyme M was isolated from a different animal as were organisms that required an exogenous supply of coenzyme M. In general, methanogenic bacteria that required an exogenous supply of coenzyme M had lower maximum growth rates and more complex nutritional requirements than organisms that synthesized the cofactor. The ability of all isolates to metabolize formate below the detection limit of 10 microM indicated that, in contrast to previous reports, methanogenic bacteria have the potential to directly metabolize formate in the rumen. This study demonstrated that there are physiologically diverse populations of coccobacillary methanogenic bacteria in the rumen that can interact competitively and cooperatively.</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/6433795?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Weitzman, P D</style></author><author><style face="normal" font="default" size="100%">Danson, M J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Citrate synthase.</style></title><secondary-title><style face="normal" font="default" size="100%">Curr Top Cell Regul</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Curr. Top. Cell. Regul.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adenosine Diphosphate</style></keyword><keyword><style  face="normal" font="default" size="100%">Adenosine Monophosphate</style></keyword><keyword><style  face="normal" font="default" size="100%">Adenosine Triphosphate</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacteria</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Cations, Divalent</style></keyword><keyword><style  face="normal" font="default" size="100%">Cations, Monovalent</style></keyword><keyword><style  face="normal" font="default" size="100%">Citrate (si)-Synthase</style></keyword><keyword><style  face="normal" font="default" size="100%">Dithionitrobenzoic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Ketoglutaric Acids</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Weight</style></keyword><keyword><style  face="normal" font="default" size="100%">NAD</style></keyword><keyword><style  face="normal" font="default" size="100%">NADP</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxo-Acid-Lyases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1976</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1976</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">10</style></volume><pages><style face="normal" font="default" size="100%">161-204</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/3389?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Misra, A L</style></author><author><style face="normal" font="default" size="100%">Bloch, R</style></author><author><style face="normal" font="default" size="100%">Vardy, J</style></author><author><style face="normal" font="default" size="100%">Mulé, S J</style></author><author><style face="normal" font="default" size="100%">Verebely, K</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Disposition of (15,16-3H)naltrexone in the central nervous system of the rat.</style></title><secondary-title><style face="normal" font="default" size="100%">Drug Metab Dispos</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Drug Metab. Dispos.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blood-Brain Barrier</style></keyword><keyword><style  face="normal" font="default" size="100%">Brain</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromatography, Thin Layer</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Naloxone</style></keyword><keyword><style  face="normal" font="default" size="100%">Naltrexone</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1976</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1976 May-Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">276-80</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;After injection of (15,16-3H)naltrexone (10 mg/kg s.c.) in male Wistar rats, peak concentrations of drug occurred in brain and plasma within 0.5 hr. Levels of naltrexone were sustained in brain between 2 and 24 hr and were barely detectable at 48 hr. Significant amounts of metabolities were present in brain and plasma at longer time periods. The t1/2 of naltrexone in brain and plasma were approximately 8.0 and 11.4 hr. respectively. The brain/plasma ratios of naltrexone at earlier times (0.5-1 hr) were higher than those at later times. The binding of naltrexone in vitro with rat plasma proteins in concentrations of 1-10 mug/ml ranged between 41 and 59% 6beta-Naltrexol was present in very small amounts in brain but not in plasma. In addition to 7,8-dihydro-14-hydroxynormophinone and 7,8-dihydro-14-hydroxynormophine, tentative evidence was obtained for three other metabolites of naltrexone in brain. These metabolites were also present in plasma in addition to free and conjugated naltrexone and its N-dealkylated metabolites.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/6233?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Rodier, F</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">[Spectral properties of porcine plasminogen: study of the acidic transition (author's transl)].</style></title><secondary-title><style face="normal" font="default" size="100%">Eur J Biochem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Eur. J. Biochem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Guanidines</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasminogen</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrometry, Fluorescence</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrophotometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrophotometry, Ultraviolet</style></keyword><keyword><style  face="normal" font="default" size="100%">Swine</style></keyword><keyword><style  face="normal" font="default" size="100%">Temperature</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1976</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1976 Apr 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">63</style></volume><pages><style face="normal" font="default" size="100%">553-62</style></pages><language><style face="normal" font="default" size="100%">fre</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The acidic transition of porcine plasminogen, prepared by affinity chromatography, was studied by non-destructive methods. These methods are based on the analysis of the behaviour of the tryptophyls under various conditions. The perturbation of the absorption and emission spectra by pH or temperature and the dynamic quenching of the intrinsic fluorescence are used to obtain information on structural changes which affect the environment of these residues. It is shown that by decreasing pH the fluorescence emission spectra are shifted toward the long wavelengths, with a broadening of the fluorescence band. The same effect can be obtained at constant pH by heating the protein solution. In order to analyze these phenomena, it is assumed that the fluorescence intensities at 355 nm and 328 nm reflect the proportion of the tryptophans which are exposed to the solvent, and buried, respectively. The plot of the ratio of the fluorescence intensities at these wavelengths versus pH or temperature leads to a titration curve showing an unmasking of tryptophans. The proportion of exposed tryptophans is measured by the dynamic fluorescence quenching technique and the data analyzed according to Lehrer. The plot of the fraction of exposed tryptophyls versus pH also shows the unmasking of these chromophores. Thermal perturbation of a solution of plaminogen at neutral pH induces a difference absorption spectrum whose amplitudes at the maxima are proportional to the number of exposed aromatic residues. The comparison with a solution of fully denatured plasminogen in 6 M guanidium chloride, where all the tryptophyls are exposed, shows that the percentage of exposure is equal to 59%. This number is significantly higher than the percentage found by the fluorescence quenching technique (20%), indicating that some tryptophyls are located in crevices, exposed to the solvent but not to the iodide. At acidic pH the absorption difference spectra induced by thermal perturbation are not classical, since they show an inversion and a new band between 300 nm and 305 nm. This band is mentioned in the literature as a minor band of tryptophan which appears when this chromophore is located in an asymmetric environment. On plotting the maximum amplitude of these spectra obtained at acidic pH versus temperature, we obtain a curve indicating that two types of antagonistic interactions are involved in the perturbation of the chromophores spectra. The spectrophotometric titration of plasminogen gives classical absorption difference spectra. By plotting the maximum amplitude at 292 nm versus pH, we obtain a titration curve with an apparent pK of 2.9 units. This pK is acidic which respect to the pK value of a normal carboxyl. This low value can be due to a positively charged group in the neighbourhood of a carboxyl, which interacts with one or more chromophores. When the carboxyl becomes protonated, this positively charged group is free and available to perturb the environment of some chromophores...&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/4326?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Miller, D D</style></author><author><style face="normal" font="default" size="100%">Hsu, F L</style></author><author><style face="normal" font="default" size="100%">Ruffolo, R R</style></author><author><style face="normal" font="default" size="100%">Patil, P N</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Stereochemical studies of adrenergic drugs. Optically active derivatives of imidazolines.</style></title><secondary-title><style face="normal" font="default" size="100%">J Med Chem</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Med. Chem.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Aorta</style></keyword><keyword><style  face="normal" font="default" size="100%">Histamine H1 Antagonists</style></keyword><keyword><style  face="normal" font="default" size="100%">Imidazoles</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle, Smooth</style></keyword><keyword><style  face="normal" font="default" size="100%">Naphazoline</style></keyword><keyword><style  face="normal" font="default" size="100%">Phenylephrine</style></keyword><keyword><style  face="normal" font="default" size="100%">Rabbits</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Adrenergic</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Adrenergic, alpha</style></keyword><keyword><style  face="normal" font="default" size="100%">Stereoisomerism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1976</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1976 Dec</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">19</style></volume><pages><style face="normal" font="default" size="100%">1382-4</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The synthesis of (R)-(+)-4-methyl-2-(1-naphthylmethyl)imidazoline hydrochloride (2) and (S)-(-)-4-methyl-2-(1-naphthylmethyl)imidazoline hydrochloride (3) is presented. The synthesis involves the preparation of (R)-(+)- and (S)-(-)-1,2-diaminopropane dihydrochloride and then allowing the appropriate diaminopropane to react with ethyl 1-naphthyliminoacetate hydrochloride in the presence of triethylamine. The parent compound, naphazoline, is a potent alpha-adrenoreceptor agonist (-log ED50 = 7.22), whereas the methylated derivatives, 2 and 3, were moderately potent antagonists (pA2 = 5.6 and 5.8, respectively) of the alpha-adrenoreceptor. Compounds 2 and 3 also produced blockade of the response to histamine on the rabbit aorta, but at concentrations approximately 20 times higher than necessary to produce equal blockade of the alpha-adrenoreceptor.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">12</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/12368?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Simonian, M A</style></author><author><style face="normal" font="default" size="100%">Nalbandian, R M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">[Acid and alkaline denaturation of superoxide dismutase].</style></title><secondary-title><style face="normal" font="default" size="100%">Biofizika</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biofizika</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Erythrocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Denaturation</style></keyword><keyword><style  face="normal" font="default" size="100%">Superoxide Dismutase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep-Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">783-7</style></pages><language><style face="normal" font="default" size="100%">rus</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Optical and ESR spectra of erythrocyte superoxide dismutase denaturated with acid and alkali are described. Sharp changes in activity and spectra were found. &quot;Residual&quot; activity of alkaline denaturated protein was higher than of acidic denaturated sample. It is suggested that covalent bonding copper-nitrogen is essential for superoxide dismutase activity of the protein or synthetic copper complexes.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/1099?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Silen, W</style></author><author><style face="normal" font="default" size="100%">Machen, T E</style></author><author><style face="normal" font="default" size="100%">Forte, J G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Acid-base balance in amphibian gastric mucosa.</style></title><secondary-title><style face="normal" font="default" size="100%">Am J Physiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Am. J. Physiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acid-Base Equilibrium</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Anura</style></keyword><keyword><style  face="normal" font="default" size="100%">Bicarbonates</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon Dioxide</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrophysiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Gastric Mucosa</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphates</style></keyword><keyword><style  face="normal" font="default" size="100%">Potassium</style></keyword><keyword><style  face="normal" font="default" size="100%">Rana catesbeiana</style></keyword><keyword><style  face="normal" font="default" size="100%">Solutions</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">229</style></volume><pages><style face="normal" font="default" size="100%">721-30</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;It has been established that H+ secretion can be maintained in frog stomach in the absence of exogenous CO2 by using a nutrient bathing fluid containing 25 mM H2PO4 (pH approximately equal to 4.5) or by lowering the pH of a nonbuffered nutrient solution to about 3.0-3.6. Exogenous CO2 in the presence of these nutrient solutions uniformly caused a marked decrease in H+ secretion, PD, adn short-circuit current (Isc) and an increase in transmucosal resistance (R). Elevation of nutrient [k+] to 83 mM reduced R significantly but transiently without change in H+ when nutrient pH less than 5.0, whereas R returned to base line and H+ increased when nutrient pH greater than 5.0. Acidification of the nutrient medium in the presence of exogenous CO2 results in inhibition of the secretory pump, probably by decreasing intracellular pH, and also interferes with conductance at the nutrient membrane. Removal of exogenous CO2 from standard bicarbonate nutrient solution reduced by 50% the H+, PD, and Isc without change in R; K+-free nutrient solutions reverse these changes in Isc and PD but not in H+. The dropping PD and rising R induced by K+-free nutrient solutions in 5% CO2 - 95% O2 are returned toward normal by 100% O2. Our findings support an important role for exogenous CO2 in maintaining normal acid-base balance in frog mucosa by acting as an acidifying agent.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/2015?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hendrickson, W A</style></author><author><style face="normal" font="default" size="100%">Ward, K B</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Atomic models for the polypeptide backbones of myohemerythrin and hemerythrin.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Biophys Res Commun</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem. Biophys. Res. Commun.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cnidaria</style></keyword><keyword><style  face="normal" font="default" size="100%">Computers</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemerythrin</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloproteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct 27</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">1349-56</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/5?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ali, S S</style></author><author><style face="normal" font="default" size="100%">Elliott, W H</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Bile acids. XLVII. 12alpha-Hydroxylation of precursors of allo bile acids by rabbit liver microsomes.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochim Biophys Acta</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochim. Biophys. Acta</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aging</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bile Acids and Salts</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Microsomes, Liver</style></keyword><keyword><style  face="normal" font="default" size="100%">Mixed Function Oxygenases</style></keyword><keyword><style  face="normal" font="default" size="100%">NADP</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Rabbits</style></keyword><keyword><style  face="normal" font="default" size="100%">Sex Factors</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Nov 21</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">409</style></volume><pages><style face="normal" font="default" size="100%">249-57</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Rabbit liver microsomal preparations fortified with 0.1 mM NADPH effectively promote hydroxylation of [3beta-3H]- or [24-14C]allochenodeoxycholic acid or [5alpha,6alpha-3H2]5alpha-cholestane-3alpha,7alpha-diol to their respective 12alpha-hydroxyl derivatives in yields of about 25 or 65% in 60 min. Minor amounts of other products are formed from the diol. The requirements for activity of rabbit liver microsomal 12alpha-hydroxylase resemble those of rat liver microsomes. Of a number of enzyme inhibitors studied only p-chloromercuribenzoate demonstrated a marked ability to inhibit the reaction with either tritiated substrate. There was no difference in the quantity of product produced from the tritiated acid or the 14C-labeled acid. No clear sex difference was found in activity of the enzyme, nor was an appreciable difference noted in activity of the enzyme between mature and immature animals.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/65?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Moroi, K</style></author><author><style face="normal" font="default" size="100%">Sato, T</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparison between procaine and isocarboxazid metabolism in vitro by a liver microsomal amidase-esterase.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Pharmacol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem. Pharmacol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amidohydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Esterases</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Isocarboxazid</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Metals</style></keyword><keyword><style  face="normal" font="default" size="100%">Microsomes, Liver</style></keyword><keyword><style  face="normal" font="default" size="100%">Phospholipids</style></keyword><keyword><style  face="normal" font="default" size="100%">Procaine</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Subcellular Fractions</style></keyword><keyword><style  face="normal" font="default" size="100%">Temperature</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Aug 15</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">1517-21</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">16</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Schmoldt, A</style></author><author><style face="normal" font="default" size="100%">Benthe, H F</style></author><author><style face="normal" font="default" size="100%">Haberland, G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Digitoxin metabolism by rat liver microsomes.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Pharmacol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem. Pharmacol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Chromatography, Thin Layer</style></keyword><keyword><style  face="normal" font="default" size="100%">Digitoxigenin</style></keyword><keyword><style  face="normal" font="default" size="100%">Digitoxin</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydroxylation</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Microsomes, Liver</style></keyword><keyword><style  face="normal" font="default" size="100%">NADP</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">1639-41</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">17</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kreuzer, W</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Ecological observation of the 137Cs-contamination in beef of animals from the southern-Bavarian area.</style></title><secondary-title><style face="normal" font="default" size="100%">Environ Qual Saf</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Environ Qual Saf</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Cesium Radioisotopes</style></keyword><keyword><style  face="normal" font="default" size="100%">Ecology</style></keyword><keyword><style  face="normal" font="default" size="100%">Food Contamination, Radioactive</style></keyword><keyword><style  face="normal" font="default" size="100%">Fungi</style></keyword><keyword><style  face="normal" font="default" size="100%">Germany, West</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Meat</style></keyword><keyword><style  face="normal" font="default" size="100%">Plants</style></keyword><keyword><style  face="normal" font="default" size="100%">Radioactive Pollutants</style></keyword><keyword><style  face="normal" font="default" size="100%">Soil</style></keyword><keyword><style  face="normal" font="default" size="100%">Soil Microbiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Trees</style></keyword><keyword><style  face="normal" font="default" size="100%">Weather</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">4</style></volume><pages><style face="normal" font="default" size="100%">24-36</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Certain climatic and edaphic conformations in the Bavarian sub-alpine mountains and in the Alps favor above all the development of a land utilization system and farm structures similar to those in the northern part of Scandinavia. In 1963/64, the years of the highest environmental contamination up to the present, we established in 600 beef samples from the round or shoulder of male and female cattle (mainly Highland cattle) close connections between the 137Cs-contamination of green crop and the long lastnig yearly precipitation quantities, as well as certain relations between the 137Cs-contamination of meat and differences in the feeding and keeping of the animals. During summer-seasons (April-October), beef of cattle from pastures with heavy rainfall (Alps) was contaiminated by 137Cs up to 15 times more than that of confined animals. Hereby the rate of 137Cs-contamination in the meat of grazing cattle was nearly proportional to the quantities of precipitation. When confined cattle were fed on pastures in autumn after harvesting for 2 to 3 weeks, a quick increase of 137Cs-contamination of the meat was caused within this time up to values which in this district were otherwise only observed in grazing cattle. The lower 137Cs-content in meat of cattle housed during the summer season is due to the more varied fodder, which is at that time less contaminated than green crop. During the winter season (November to March), the highest contaminations in the meat of confined (Bohemian Forest) or grazing cattle (Alps) was measured when the animals in these districts were almost exclusively fed with fodder from the own farmground or with leafy silage. The highest contamination was almost regularly noticed in January, February and March, as generally during these months the highly contaminated first cut hay is fed. Here the meat was often even more contaminated than that of grazing cattle. After the quick decrease of 137Cs in fallout noticed in the years 1964 and 1965, in 1965/66 a dependance in the 137Cs-contamination of beef on the methods of keeping and feeding could still be observed in only the extreme cases (Alps, Bavarian- and Bohemian Forest); though in general, meat of animals from districts with heavy rainfall was slightly more contaminated than meat of animals from regions with less precipitation.&lt;/p&gt;</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/229?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Flohr, H</style></author><author><style face="normal" font="default" size="100%">Breull, W</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of etafenone on total and regional myocardial blood flow.</style></title><secondary-title><style face="normal" font="default" size="100%">Arzneimittelforschung</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Arzneimittelforschung</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Anoxia</style></keyword><keyword><style  face="normal" font="default" size="100%">Blood Pressure</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon Dioxide</style></keyword><keyword><style  face="normal" font="default" size="100%">Cardiac Output</style></keyword><keyword><style  face="normal" font="default" size="100%">Coronary Circulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Coronary Vessels</style></keyword><keyword><style  face="normal" font="default" size="100%">Dogs</style></keyword><keyword><style  face="normal" font="default" size="100%">Heart Rate</style></keyword><keyword><style  face="normal" font="default" size="100%">Heart Septum</style></keyword><keyword><style  face="normal" font="default" size="100%">Heart Ventricles</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxygen</style></keyword><keyword><style  face="normal" font="default" size="100%">Propiophenones</style></keyword><keyword><style  face="normal" font="default" size="100%">Vasodilator Agents</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">25</style></volume><pages><style face="normal" font="default" size="100%">1400-3</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The distribution of blood flow to the subendocardial, medium and subepicardial layers of the left ventricular free wall was studied in anaesthetized dogs under normoxic (A), hypoxic (B) conditions and under pharmacologically induced (etafenone) coronary vasodilation (C). Regional myocardial blood flow was determined by means of the particle distribution method. In normoxia a transmural gradient of flow was observed, with the subendocardial layers receiving a significantly higher flow rate compared with the subepicardial layers. In hypoxia induced vasodilation this transmural gradient of flow was persistent. In contrast a marked redistribution of regional flow was observed under pharmacologically induced vasodilation. The transmural gradient decreased. In contrast to some findings these experiments demonstrate that a considerable vasodilatory capacity exists in all layers of the myocardium and can be utilized by drugs. The differences observed for the intramural distribution pattern of flow under hypoxia and drug induced vasodilation support the hypothesis that this pattern reflects corresponding gradients of regional myocardial metabolism.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/23?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kahn, T</style></author><author><style face="normal" font="default" size="100%">Bosch, J</style></author><author><style face="normal" font="default" size="100%">Levitt, M F</style></author><author><style face="normal" font="default" size="100%">Goldstein, M H</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Effect of sodium nitrate loading on electrolyte transport by the renal tubule.</style></title><secondary-title><style face="normal" font="default" size="100%">Am J Physiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Am. J. Physiol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Bicarbonates</style></keyword><keyword><style  face="normal" font="default" size="100%">Biological Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Chlorides</style></keyword><keyword><style  face="normal" font="default" size="100%">Chlorothiazide</style></keyword><keyword><style  face="normal" font="default" size="100%">Diuresis</style></keyword><keyword><style  face="normal" font="default" size="100%">Dogs</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrolytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Ethacrynic Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Glomerular Filtration Rate</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney Tubules</style></keyword><keyword><style  face="normal" font="default" size="100%">Nitrates</style></keyword><keyword><style  face="normal" font="default" size="100%">Potassium</style></keyword><keyword><style  face="normal" font="default" size="100%">Sodium</style></keyword><keyword><style  face="normal" font="default" size="100%">Sodium Chloride</style></keyword><keyword><style  face="normal" font="default" size="100%">Urine</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">229</style></volume><pages><style face="normal" font="default" size="100%">746-53</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Effects of sodium nitrate were compared with sodium chloride loading on transport of electrolytes by the nephron. Maximal levels of free water clearance/clomerular filtration rate (CH2O/GFR) averaged 8.4% with nitrate loading and 14.4% with saline loading. Since ethacrynic acid and chlorothiazide exert their major natriuretic effect in the distal nephron, the increment in Na ad Cl reabsorbed beyond the proximal tubule. The administration of these agents resulted in an increase in fractional sodium excretion (CNa/GFR) of 21.1%, urinary sodium excretion (UNaV) of 1,126 mueq/min, and urinary chloride excretion (UClV) of 848 mueq/min during nitrate loading compared with an increase in CNa/GFR of 37.6%, UNaV of 2,362 mueq/min, and UClV of 2,397 mueq/min during saline loading. The smaller diuretic-induced increment in Na and Cl excretion in the nitrate studies suggests, as do the hydrated studies, that less Cl and Na are reabsorbed in the distal nephron during nitrate than saline loading. At every level of UNaV, fractional bicarbonate reabsorption was higher, urine pH was lower, and urinary potassium excretion (UKV) was higher in the nitrate studies. Thus, compared with saline loading, sodium nitrate decreases chloride and sodium reabsorption in the distal nephron. The higher hydrogen and potassium secretion in the nitrate studies may be consequent to the decreased ability of the distal nephron to reabsorb chloride.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/2016?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Huijbregts, L A</style></author><author><style face="normal" font="default" size="100%">Schreurs, M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Evaluation of amplitude and frequency changes of miniature potentials with a poor signal-to-noise ratio.</style></title><secondary-title><style face="normal" font="default" size="100%">Comp Biochem Physiol C</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Comp. Biochem. Physiol. C, Comp. Pharmacol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Gallamine Triethiodide</style></keyword><keyword><style  face="normal" font="default" size="100%">Grasshoppers</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle Contraction</style></keyword><keyword><style  face="normal" font="default" size="100%">Potentiometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Sodium Chloride</style></keyword><keyword><style  face="normal" font="default" size="100%">Strychnine</style></keyword><keyword><style  face="normal" font="default" size="100%">Sucrose</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">52</style></volume><pages><style face="normal" font="default" size="100%">11-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/196?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Makar, A B</style></author><author><style face="normal" font="default" size="100%">McMartin, K E</style></author><author><style face="normal" font="default" size="100%">Palese, M</style></author><author><style face="normal" font="default" size="100%">Tephly, T R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Formate assay in body fluids: application in methanol poisoning.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Med</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem Med</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aldehyde Oxidoreductases</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Body Fluids</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbon Dioxide</style></keyword><keyword><style  face="normal" font="default" size="100%">Formates</style></keyword><keyword><style  face="normal" font="default" size="100%">Haplorhini</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Methanol</style></keyword><keyword><style  face="normal" font="default" size="100%">Methods</style></keyword><keyword><style  face="normal" font="default" size="100%">Pseudomonas</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Jun</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">13</style></volume><pages><style face="normal" font="default" size="100%">117-26</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/1?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kröger, H</style></author><author><style face="normal" font="default" size="100%">Donner, I</style></author><author><style face="normal" font="default" size="100%">Skiello, G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Influence of a new virostatic compound on the induction of enzymes in rat liver.</style></title><secondary-title><style face="normal" font="default" size="100%">Arzneimittelforschung</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Arzneimittelforschung</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adrenalectomy</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Antiviral Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Cortisone</style></keyword><keyword><style  face="normal" font="default" size="100%">Culture Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Dose-Response Relationship, Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Induction</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Imidazoles</style></keyword><keyword><style  face="normal" font="default" size="100%">Liver</style></keyword><keyword><style  face="normal" font="default" size="100%">Piperazines</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Time Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Tryptophan Oxygenase</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine Transaminase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">25</style></volume><pages><style face="normal" font="default" size="100%">1426-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The virostatic compound N,N-diethyl-4-[2-(2-oxo-3-tetradecyl-1-imidazolidinyl)-ethyl]-1-piperazinecarboxamide-hydrochloride (5531) was analyzed as to its effect on the induction of tryptophan-pyrrolase and tyrosineaminotransferase in rat liver. 1. The basic activity of the enzymes was not influenced by the substance either in normal or in adrenalectomized animals. 2. The induction of the enzymes by cortisone increased in the presence of the compound whereas the substrate induction remained unchanged. 3. The induction of tyrosine-aminotransferase by dexamethasonephosphate in tissue culture is inhibited if the dose of compound 5531 is higher than 5 mug/ml.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/24?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Reinis, Z</style></author><author><style face="normal" font="default" size="100%">Lojda, Z</style></author><author><style face="normal" font="default" size="100%">Heyrovský, A</style></author><author><style face="normal" font="default" size="100%">Horáková, D</style></author><author><style face="normal" font="default" size="100%">Reisenauer, R</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">[Influence of beta-blocking agents on experimental atherosclerosis of cocks (author's transl)].</style></title><secondary-title><style face="normal" font="default" size="100%">Cas Lek Cesk</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Cas. Lek. Cesk.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adrenergic beta-Antagonists</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Arteriosclerosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Chickens</style></keyword><keyword><style  face="normal" font="default" size="100%">Cholesterol, Dietary</style></keyword><keyword><style  face="normal" font="default" size="100%">Disease Models, Animal</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct 24</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">114</style></volume><pages><style face="normal" font="default" size="100%">1320-5</style></pages><language><style face="normal" font="default" size="100%">cze</style></language><issue><style face="normal" font="default" size="100%">43</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/146?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ris, M M</style></author><author><style face="normal" font="default" size="100%">Deitrich, R A</style></author><author><style face="normal" font="default" size="100%">Von Wartburg, J P</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Inhibition of aldehyde reductase isoenzymes in human and rat brain.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Pharmacol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem. Pharmacol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aldehyde Oxidoreductases</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Anticonvulsants</style></keyword><keyword><style  face="normal" font="default" size="100%">Barbiturates</style></keyword><keyword><style  face="normal" font="default" size="100%">Brain</style></keyword><keyword><style  face="normal" font="default" size="100%">Glutethimide</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydantoins</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Isoenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">NAD</style></keyword><keyword><style  face="normal" font="default" size="100%">NADP</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Succinimides</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct 15</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">1865-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">20</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/18?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mier, P D</style></author><author><style face="normal" font="default" size="100%">van den Hurk, J J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lysosomal hydrolases of the epidermis. 2. Ester hydrolases.</style></title><secondary-title><style face="normal" font="default" size="100%">Br J Dermatol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Br. J. Dermatol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acid Phosphatase</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Carboxylic Ester Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cerebroside-Sulfatase</style></keyword><keyword><style  face="normal" font="default" size="100%">Chondro-4-Sulfatase</style></keyword><keyword><style  face="normal" font="default" size="100%">Guinea Pigs</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Lysosomes</style></keyword><keyword><style  face="normal" font="default" size="100%">Pyrophosphatases</style></keyword><keyword><style  face="normal" font="default" size="100%">Skin</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">93</style></volume><pages><style face="normal" font="default" size="100%">391-8</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Five distinct ester hydrolases (EC 3-1) have been characterized in guinea-pig epidermis. These are carboxylic esterase, acid phosphatase, pyrophosphatase, and arylsulphatase A and B. Their properties are consistent with those of lysosomal enzymes.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/31?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mier, P D</style></author><author><style face="normal" font="default" size="100%">van den Hurk, J J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Lysosomal hydrolases of the epidermis. I. Glycosidases.</style></title><secondary-title><style face="normal" font="default" size="100%">Br J Dermatol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Br. J. Dermatol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Acetylglucosaminidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Galactosidases</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycoside Hydrolases</style></keyword><keyword><style  face="normal" font="default" size="100%">Guinea Pigs</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Lysosomes</style></keyword><keyword><style  face="normal" font="default" size="100%">Skin</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Jul</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">93</style></volume><pages><style face="normal" font="default" size="100%">1-10</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Seven distinct glycosidases (EC 3.2) have been characterized in guinea-pig epidermis. Their properties indicate them to be of lysosomal origin. The 'profile' of the epidermal glycosidases is significantly different from that reported for whole skin, the activities of beta-galactosidase and beta-acetylglucosaminidase being very high and those of the remaining enzymes relatively low in epidermis.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/30?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Anderson, T R</style></author><author><style face="normal" font="default" size="100%">Slotkin, T A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Maturation of the adrenal medulla--IV. Effects of morphine.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Pharmacol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem. Pharmacol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adrenal Medulla</style></keyword><keyword><style  face="normal" font="default" size="100%">Aging</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals, Newborn</style></keyword><keyword><style  face="normal" font="default" size="100%">Body Weight</style></keyword><keyword><style  face="normal" font="default" size="100%">Catecholamines</style></keyword><keyword><style  face="normal" font="default" size="100%">Dopamine beta-Hydroxylase</style></keyword><keyword><style  face="normal" font="default" size="100%">Epinephrine</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Maternal-Fetal Exchange</style></keyword><keyword><style  face="normal" font="default" size="100%">Metaraminol</style></keyword><keyword><style  face="normal" font="default" size="100%">Morphine</style></keyword><keyword><style  face="normal" font="default" size="100%">Morphine Dependence</style></keyword><keyword><style  face="normal" font="default" size="100%">Pregnancy</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine 3-Monooxygenase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Aug 15</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">24</style></volume><pages><style face="normal" font="default" size="100%">1469-74</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">16</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/7?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Smith, R J</style></author><author><style face="normal" font="default" size="100%">Bryant, R G</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Metal substitutions incarbonic anhydrase: a halide ion probe study.</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Biophys Res Commun</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochem. Biophys. Res. Commun.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Cadmium</style></keyword><keyword><style  face="normal" font="default" size="100%">Carbonic Anhydrases</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">Magnetic Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Mercury</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Binding</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Zinc</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct 27</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">1281-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/3?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">El Halawani, M E</style></author><author><style face="normal" font="default" size="100%">Waibel, P E</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">The relative importance of monoamine oxidase and catechol-O-methyl transferase on the physiologic response to administered norepinephrine in the turkey.</style></title><secondary-title><style face="normal" font="default" size="100%">Comp Biochem Physiol C</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Comp. Biochem. Physiol. C, Comp. Pharmacol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Blood Pressure</style></keyword><keyword><style  face="normal" font="default" size="100%">Catechol O-Methyltransferase</style></keyword><keyword><style  face="normal" font="default" size="100%">Chickens</style></keyword><keyword><style  face="normal" font="default" size="100%">Epinephrine</style></keyword><keyword><style  face="normal" font="default" size="100%">Heart</style></keyword><keyword><style  face="normal" font="default" size="100%">Kidney</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Liver</style></keyword><keyword><style  face="normal" font="default" size="100%">Monoamine Oxidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Myocardium</style></keyword><keyword><style  face="normal" font="default" size="100%">Norepinephrine</style></keyword><keyword><style  face="normal" font="default" size="100%">Organ Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Rats</style></keyword><keyword><style  face="normal" font="default" size="100%">Species Specificity</style></keyword><keyword><style  face="normal" font="default" size="100%">Turkeys</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Oct 1</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">52</style></volume><pages><style face="normal" font="default" size="100%">35-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><issue><style face="normal" font="default" size="100%">1</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/200?dopt=Abstract</style></custom1></record></records></xml>