@article {676,
	title = {Proteopedia: a status report on the collaborative, 3D web-encyclopedia of proteins and other biomolecules.},
	journal = {J Struct Biol},
	volume = {175},
	year = {2011},
	month = {2011 Aug},
	pages = {244-52},
	abstract = {Proteopedia is a collaborative, 3D web-encyclopedia of protein, nucleic acid and other biomolecule structures. Created as a means for communicating biomolecule structures to a diverse scientific audience, Proteopedia (http://www.proteopedia.org) presents structural annotation in an intuitive, interactive format and allows members of the scientific community to easily contribute their own annotations. Here, we provide a status report on Proteopedia by describing advances in the web resource since its inception three and a half years ago, focusing on features of potential direct use to the scientific community. We discuss its progress as a collaborative 3D-encyclopedia of structures as well as its use as a complement to scientific publications and PowerPoint presentations. We also describe Proteopedia{\textquoteright}s use for 3D visualization in structure-related pedagogy.},
	keywords = {Encyclopedias as Topic, Information Dissemination, Information Management, Information Services, Models, Molecular, Molecular Biology, Online Systems, Protein Conformation, Proteins, User-Computer Interface},
	issn = {1095-8657},
	doi = {10.1016/j.jsb.2011.04.011},
	author = {Prilusky, Jaime and Hodis, Eran and Canner, David and Decatur, Wayne A and Oberholser, Karl and Martz, Eric and Berchanski, Alexander and Harel, Michal and Sussman, Joel L}
}
@article {679,
	title = {Proteopedia.Org: a scientific "Wiki" bridging the rift between 3D structure and function of biomacromolecules.},
	journal = {Biopolymers},
	volume = {92},
	year = {2009},
	month = {2009},
	pages = {76-7},
	keywords = {Computational Biology, Imaging, Three-Dimensional, Internet, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Proteins, Structure-Activity Relationship},
	issn = {0006-3525},
	doi = {10.1002/bip.21126},
	author = {Martz, Eric}
}
@article {680,
	title = {Proteopedia - a scientific {\textquoteright}wiki{\textquoteright} bridging the rift between three-dimensional structure and function of biomacromolecules.},
	journal = {Genome Biol},
	volume = {9},
	year = {2008},
	month = {2008},
	pages = {R121},
	abstract = {Many scientists lack the background to fully utilize the wealth of solved three-dimensional biomacromolecule structures. Thus, a resource is needed to present structure/function information in a user-friendly manner to a broad scientific audience. Proteopedia http://www.proteopedia.org is an interactive, wiki web-resource whose pages have embedded three-dimensional structures surrounded by descriptive text containing hyperlinks that change the appearance (view, representations, colors, labels) of the adjacent three-dimensional structure to reflect the concept explained in the text.},
	keywords = {Databases, Protein, Internet, Models, Molecular, Protein Conformation, Protein Structure, Tertiary, Proteins, Software},
	issn = {1465-6914},
	doi = {10.1186/gb-2008-9-8-r121},
	author = {Hodis, Eran and Prilusky, Jaime and Martz, Eric and Silman, Israel and Moult, John and Sussman, Joel L}
}
@article {682,
	title = {Selecton 2007: advanced models for detecting positive and purifying selection using a Bayesian inference approach.},
	journal = {Nucleic Acids Res},
	volume = {35},
	year = {2007},
	month = {2007 Jul},
	pages = {W506-11},
	abstract = {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{\textquoteright}s specific needs, including calculation of statistical support of the omega values, an advanced graphic display of the protein{\textquoteright}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{\textquoteright}s sequence and structure.},
	keywords = {Algorithms, Amino Acid Sequence, Amino Acid Substitution, Amino Acids, Animals, Bayes Theorem, Computational Biology, Computer Simulation, Humans, Internet, Models, Molecular, Molecular Sequence Data, Phylogeny, Proteins, Sequence Analysis, Protein, Software},
	issn = {1362-4962},
	doi = {10.1093/nar/gkm382},
	author = {Stern, Adi and Doron-Faigenboim, Adi and Erez, Elana and Martz, Eric and Bacharach, Eran and Pupko, Tal}
}
@article {684,
	title = {ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information.},
	journal = {Bioinformatics},
	volume = {19},
	year = {2003},
	month = {2003 Jan},
	pages = {163-4},
	abstract = {We recently developed algorithmic tools for the identification of functionally important regions in proteins of known three dimensional structure by estimating the degree of conservation of the amino-acid sites among their close sequence homologues. Projecting the conservation grades onto the molecular surface of these proteins reveals patches of highly conserved (or occasionally highly variable) residues that are often of important biological function. We present a new web server, ConSurf, which automates these algorithmic tools. ConSurf may be used for high-throughput characterization of functional regions in proteins. AVAILABILITY: The ConSurf web server is available at:http://consurf.tau.ac.il. SUPPLEMENTARY INFORMATION: A set of examples is available at http://consurf.tau.ac.il under {\textquoteright}GALLERY{\textquoteright}.},
	keywords = {Amino Acids, bcl-X Protein, Conserved Sequence, Databases, Protein, Evolution, Molecular, Internet, Phylogeny, Protein Conformation, Proteins, Proto-Oncogene Proteins c-bcl-2, Sequence Alignment, Sequence Analysis, Protein, User-Computer Interface},
	issn = {1367-4803},
	author = {Glaser, Fabian and Pupko, Tal and Paz, Inbal and Bell, Rachel E and Bechor-Shental, Dalit and Martz, Eric and Ben-Tal, Nir}
}
@article {685,
	title = {Protein Explorer: easy yet powerful macromolecular visualization.},
	journal = {Trends Biochem Sci},
	volume = {27},
	year = {2002},
	month = {2002 Feb},
	pages = {107-9},
	abstract = {Protein Explorer (PE, http://www.proteinexplorer.org) enables students, educators and other nonspecialists to visualize macromolecular structures easily. It also offers several advanced capabilities useful to protein structure specialists. Great attention has been given to making PE easy to use. Explanations, color keys and troubleshooting information are displayed automatically. There are also {\textquoteright}Frequently Asked Questions{\textquoteright}, a one-hour {\textquoteright}Quick-Tour{\textquoteright}, an alphabetical {\textquoteright}Help/Index/Glossary{\textquoteright}, and a detailed {\textquoteright}Tutorial{\textquoteright}; all making PE much easier to use than either Chime or RasMol. Moreover, it is much more powerful; in addition to basic macromolecular visualization capabilities common to most similar programs, it offers one-click visualization of interfaces between moieties ({\textquoteright}contacts{\textquoteright}), cation-pi interactions and salt bridges, as well as easy-to-use routines to visualize regions of conservation in three-dimensional protein structures based on multiple sequence alignments.},
	keywords = {Computational Biology, DNA, Evolution, Molecular, Macromolecular Substances, Protein Structure, Secondary, Proteins, Sequence Alignment, Software},
	issn = {0968-0004},
	author = {Martz, Eric}
}
