@article {714,
	title = {Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles.},
	journal = {J Virol},
	volume = {76},
	year = {2002},
	month = {2002 May},
	pages = {5156-66},
	abstract = {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.},
	keywords = {Animals, Antiviral Agents, Biological Transport, Brefeldin A, Capsid, Caveolae, Coatomer Protein, Endocytosis, Endoplasmic Reticulum, Simian virus 40, Virus Replication},
	issn = {0022-538X},
	author = {Norkin, Leonard C and Anderson, Howard A and Wolfrom, Scott A and Oppenheim, Ariella}
}
@article {704,
	title = {Virus receptors: implications for pathogenesis and the design of antiviral agents.},
	journal = {Clin Microbiol Rev},
	volume = {8},
	year = {1995},
	month = {1995 Apr},
	pages = {293-315},
	abstract = {A virus initiates infection by attaching to its specific receptor on the surface of a susceptible host cell. This prepares the way for the virus to enter the cell. Consequently, the expression of the receptor on specific cells and tissues of the host is a major determinant of the route of entry of the virus into the host and of the patterns of virus spread and pathogenesis in the host. This review emphasizes the virus-receptor interactions of human immunodeficiency virus, the rhinoviruses, the herpesviruses, and the coronaviruses. These interactions are often found to be complex and dynamic, involving multiple sites or factors on both the virus and the host cell. Also, the receptor may play an important role in virus entry per se in addition to its role in virus binding. In the cases of human immunodeficiency virus and the rhinoviruses, ingenious approaches to therapeutic strategies based on inhibiting virus attachment and entry are under development and in clinical trials.},
	keywords = {Antigens, CD4, Antiviral Agents, Coronavirus, Drug Design, Herpesviridae, HIV, Humans, Intercellular Adhesion Molecule-1, Models, Molecular, Picornaviridae, Receptors, Virus, Retroviridae},
	issn = {0893-8512},
	author = {Norkin, L C}
}
@article {1722,
	title = {Influence of a new virostatic compound on the induction of enzymes in rat liver.},
	journal = {Arzneimittelforschung},
	volume = {25},
	year = {1975},
	month = {1975 Sep},
	pages = {1426-9},
	abstract = {<p>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.</p>},
	keywords = {Adrenalectomy, Animals, Antiviral Agents, Cortisone, Culture Techniques, Dose-Response Relationship, Drug, Enzyme Induction, Female, Imidazoles, Liver, Piperazines, Rats, Time Factors, Tryptophan Oxygenase, Tyrosine, Tyrosine Transaminase},
	issn = {0004-4172},
	author = {Kr{\"o}ger, H and Donner, I and Skiello, G}
}
