<?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%">Orti, L.</style></author><author><style face="normal" font="default" size="100%">Carbajo, R. J.</style></author><author><style face="normal" font="default" size="100%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Maurer, S. M.</style></author><author><style face="normal" font="default" size="100%">Rai, A. K.</style></author><author><style face="normal" font="default" size="100%">Taylor, G.</style></author><author><style face="normal" font="default" size="100%">Todd, M. H.</style></author><author><style face="normal" font="default" size="100%">Pineda-Lucena, A.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">A kernel for open source drug discovery in tropical diseases</style></title><secondary-title><style face="normal" font="default" size="100%">PLoS Negl Trop Dis</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2009</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=19381286</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">4</style></number><volume><style face="normal" font="default" size="100%">3</style></volume><pages><style face="normal" font="default" size="100%">e418</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">BACKGROUND: Conventional patent-based drug development incentives work badly for the developing world, where commercial markets are usually small to non-existent. For this reason, the past decade has seen extensive experimentation with alternative R&amp;D institutions ranging from private-public partnerships to development prizes. Despite extensive discussion, however, one of the most promising avenues-open source drug discovery-has remained elusive. We argue that the stumbling block has been the absence of a critical mass of preexisting work that volunteers can improve through a series of granular contributions. Historically, open source software collaborations have almost never succeeded without such &quot;kernels&quot;. METHODOLOGY/PRINCIPAL FINDINGS: HERE, WE USE A COMPUTATIONAL PIPELINE FOR: (i) comparative structure modeling of target proteins, (ii) predicting the localization of ligand binding sites on their surfaces, and (iii) assessing the similarity of the predicted ligands to known drugs. Our kernel currently contains 143 and 297 protein targets from ten pathogen genomes that are predicted to bind a known drug or a molecule similar to a known drug, respectively. The kernel provides a source of potential drug targets and drug candidates around which an online open source community can nucleate. Using NMR spectroscopy, we have experimentally tested our predictions for two of these targets, confirming one and invalidating the other. CONCLUSIONS/SIGNIFICANCE: The TDI kernel, which is being offered under the Creative Commons attribution share-alike license for free and unrestricted use, can be accessed on the World Wide Web at http://www.tropicaldisease.org. We hope that the kernel will facilitate collaborative efforts towards the discovery of new drugs against parasites that cause tropical diseases.</style></abstract><notes><style face="normal" font="default" size="100%">Orti, Leticia Carbajo, Rodrigo J Pieper, Ursula Eswar, Narayanan Maurer, Stephen M Rai, Arti K Taylor, Ginger Todd, Matthew H Pineda-Lucena, Antonio Sali, Andrej Marti-Renom, Marc A United States PLoS neglected tropical diseases PLoS Negl Trop Dis. 2009;3(4):e418. Epub 2009 Apr 21.</style></notes></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%">Orti, L.</style></author><author><style face="normal" font="default" size="100%">Carbajo, R. J.</style></author><author><style face="normal" font="default" size="100%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Maurer, S. M.</style></author><author><style face="normal" font="default" size="100%">Rai, A. K.</style></author><author><style face="normal" font="default" size="100%">Taylor, G.</style></author><author><style face="normal" font="default" size="100%">Todd, M. H.</style></author><author><style face="normal" font="default" size="100%">Pineda-Lucena, A.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">A kernel for the Tropical Disease Initiative</style></title><secondary-title><style face="normal" font="default" size="100%">Nat Biotechnol</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2009</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=19352362</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">4</style></number><volume><style face="normal" font="default" size="100%">27</style></volume><pages><style face="normal" font="default" size="100%">320-1</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><notes><style face="normal" font="default" size="100%">&lt;p&gt;Orti, Leticia Carbajo, Rodrigo J Pieper, Ursula Eswar, Narayanan Maurer, Stephen M Rai, Arti K Taylor, Ginger Todd, Matthew H Pineda-Lucena, Antonio Sali, Andrej Marti-Renom, Marc A P01 AI035707/AI/NIAID NIH HHS/United States P01 GM71790/GM/NIGMS NIH HHS/United States R01 GM54762/GM/NIGMS NIH HHS/United States U54 GM074945/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t United States Nature biotechnology Nat Biotechnol. 2009 Apr;27(4):320-1.&lt;/p&gt;</style></notes></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%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Webb, B. M.</style></author><author><style face="normal" font="default" size="100%">Eramian, D.</style></author><author><style face="normal" font="default" size="100%">Kelly, L.</style></author><author><style face="normal" font="default" size="100%">Barkan, D. T.</style></author><author><style face="normal" font="default" size="100%">Carter, H.</style></author><author><style face="normal" font="default" size="100%">Mankoo, P.</style></author><author><style face="normal" font="default" size="100%">Karchin, R.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Davis, F. P.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">MODBASE, a database of annotated comparative protein structure models and associated resources</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Databases</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Mutation Polymorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Genomics Humans Ligands *Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein User-Computer Interface</style></keyword><keyword><style  face="normal" font="default" size="100%">Single Nucleotide Protein Folding Protein Interaction Domains and Motifs *Protein Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Tertiary Proteins/genetics *Structural Homology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=18948282</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">Database issue</style></number><volume><style face="normal" font="default" size="100%">37</style></volume><pages><style face="normal" font="default" size="100%">D347-54</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MODBASE (http://salilab.org/modbase) is a database of annotated comparative protein structure models. The models are calculated by MODPIPE, an automated modeling pipeline that relies primarily on MODELLER for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE currently contains 5,152,695 reliable models for domains in 1,593,209 unique protein sequences; only models based on statistically significant alignments and/or models assessed to have the correct fold are included. MODBASE also allows users to calculate comparative models on demand, through an interface to the MODWEB modeling server (http://salilab.org/modweb). Other resources integrated with MODBASE include databases of multiple protein structure alignments (DBAli), structurally defined ligand binding sites (LIGBASE), predicted ligand binding sites (AnnoLyze), structurally defined binary domain interfaces (PIBASE) and annotated single nucleotide polymorphisms and somatic mutations found in human proteins (LS-SNP, LS-Mut). MODBASE models are also available through the Protein Model Portal (http://www.proteinmodelportal.org/).</style></abstract><notes><style face="normal" font="default" size="100%">Pieper, Ursula Eswar, Narayanan Webb, Ben M Eramian, David Kelly, Libusha Barkan, David T Carter, Hannah Mankoo, Parminder Karchin, Rachel Marti-Renom, Marc A Davis, Fred P Sali, Andrej GM08284/GM/NIGMS NIH HHS/United States P01 GM71790/GM/NIGMS NIH HHS/United States R01 GM54762/GM/NIGMS NIH HHS/United States U01 GM61390/GM/NIGMS NIH HHS/United States U54 GM074929/GM/NIGMS NIH HHS/United States U54 GM074945/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t Research Support, U.S. Gov’t, Non-P.H.S. England Nucleic acids research Nucleic Acids Res. 2009 Jan;37(Database issue):D347-54. Epub 2008 Oct 23.</style></notes></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%">Espadaler, J.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Querol, E.</style></author><author><style face="normal" font="default" size="100%">Aviles, F. X.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Oliva, B.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Prediction of enzyme function by combining sequence similarity and protein interactions</style></title><secondary-title><style face="normal" font="default" size="100%">BMC Bioinformatics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid *Software Structure-Activity Relationship Substrate Specificity/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence/physiology Databases</style></keyword><keyword><style  face="normal" font="default" size="100%">Automated Predictive Value of Tests Protein Interaction Mapping Proteins/analysis/metabolism Sequence Alignment Sequence Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein *Sequence Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Enzymes/analysis/*metabolism Fuzzy Logic Pattern Recognition</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2008</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=18505562</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">9</style></volume><pages><style face="normal" font="default" size="100%">249</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">BACKGROUND: A number of studies have used protein interaction data alone for protein function prediction. Here, we introduce a computational approach for annotation of enzymes, based on the observation that similar protein sequences are more likely to perform the same function if they share similar interacting partners. RESULTS: The method has been tested against the PSI-BLAST program using a set of 3,890 protein sequences from which interaction data was available. For protein sequences that align with at least 40% sequence identity to a known enzyme, the specificity of our method in predicting the first three EC digits increased from 80% to 90% at 80% coverage when compared to PSI-BLAST. CONCLUSION: Our method can also be used in proteins for which homologous sequences with known interacting partners can be detected. Thus, our method could increase 10% the specificity of genome-wide enzyme predictions based on sequence matching by PSI-BLAST alone.</style></abstract><notes><style face="normal" font="default" size="100%">Espadaler, Jordi Eswar, Narayanan Querol, Enrique Aviles, Francesc X Sali, Andrej Marti-Renom, Marc A Oliva, Baldomero GM54762/GM/NIGMS NIH HHS/United States GM71790/GM/NIGMS NIH HHS/United States GM74929/GM/NIGMS NIH HHS/United States GM74945/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t England BMC bioinformatics BMC Bioinformatics. 2008 May 27;9:249.</style></notes></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%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Madhusudhan, M. S.</style></author><author><style face="normal" font="default" size="100%">Rossi, A.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Davis, F. P.</style></author><author><style face="normal" font="default" size="100%">Fatima Al-Shahrour</style></author><author><style face="normal" font="default" size="100%">Dopazo, J.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">DBAli tools: mining the protein structure space</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Algorithms Amino Acid Sequence Computational Biology/*methods Data Interpretation</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid *Software Structure-Activity Relationship</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Internet Molecular Sequence Data Protein Conformation Proteins/*chemistry/classification/*metabolism Pseudomonas aeruginosa/*metabolism Sequence Alignment/*methods Sequence Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein/*methods Sequence Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Statistical *Databases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=17478513</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">Web Server issue</style></number><volume><style face="normal" font="default" size="100%">35</style></volume><pages><style face="normal" font="default" size="100%">W393-7</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The DBAli tools use a comprehensive set of structural alignments in the DBAli database to leverage the structural information deposited in the Protein Data Bank (PDB). These tools include (i) the DBAlit program that allows users to input the 3D coordinates of a protein structure for comparison by MAMMOTH against all chains in the PDB; (ii) the AnnoLite and AnnoLyze programs that annotate a target structure based on its stored relationships to other structures; (iii) the ModClus program that clusters structures by sequence and structure similarities; (iv) the ModDom program that identifies domains as recurrent structural fragments and (v) an implementation of the COMPARER method in the SALIGN command in MODELLER that creates a multiple structure alignment for a set of related protein structures. Thus, the DBAli tools, which are freely accessible via the World Wide Web at http://salilab.org/DBAli/, allow users to mine the protein structure space by establishing relationships between protein structures and their functions.</style></abstract><notes><style face="normal" font="default" size="100%">Marti-Renom, Marc A Pieper, Ursula Madhusudhan, M S Rossi, Andrea Eswar, Narayanan Davis, Fred P Al-Shahrour, Fatima Dopazo, Joaquin Sali, Andrej GM 62529/GM/NIGMS NIH HHS/United States GM074929/GM/NIGMS NIH HHS/United States GM54762/GM/NIGMS NIH HHS/United States GM71790/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t England Nucleic acids research Nucleic Acids Res. 2007 Jul;35(Web Server issue):W393-7. Epub 2007 May 3.</style></notes></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%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Webb, B.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Madhusudhan, M. S.</style></author><author><style face="normal" font="default" size="100%">Eramian, D.</style></author><author><style face="normal" font="default" size="100%">Shen, M. Y.</style></author><author><style face="normal" font="default" size="100%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparative protein structure modeling using Modeller</style></title><secondary-title><style face="normal" font="default" size="100%">Curr Protoc Bioinformatics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Algorithms Amino Acid Sequence Computer Simulation Crystallography/*methods *Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Chemical *Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Molecular Sequence Data Protein Conformation Protein Folding Proteins/*chemistry/*ultrastructure Sequence Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein/*methods *Software</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=18428767</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">Chapter 5</style></volume><pages><style face="normal" font="default" size="100%">Unit 5 6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Functional characterization of a protein sequence is one of the most frequent problems in biology. This task is usually facilitated by accurate three-dimensional (3-D) structure of the studied protein. In the absence of an experimentally determined structure, comparative or homology modeling can sometimes provide a useful 3-D model for a protein that is related to at least one known protein structure. Comparative modeling predicts the 3-D structure of a given protein sequence (target) based primarily on its alignment to one or more proteins of known structure (templates). The prediction process consists of fold assignment, target-template alignment, model building, and model evaluation. This unit describes how to calculate comparative models using the program MODELLER and discusses all four steps of comparative modeling, frequently observed errors, and some applications. Modeling lactate dehydrogenase from Trichomonas vaginalis (TvLDH) is described as an example. The download and installation of the MODELLER software is also described.</style></abstract><notes><style face="normal" font="default" size="100%">Eswar, Narayanan Webb, Ben Marti-Renom, Marc A Madhusudhan, M S Eramian, David Shen, Min-Yi Pieper, Ursula Sali, Andrej P01 A135707/PHS HHS/United States P01 GM71790/GM/NIGMS NIH HHS/United States R01 GM54762/GM/NIGMS NIH HHS/United States U54 GM62529/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t United States Current protocols in bioinformatics / editoral board, Andreas D. Baxevanis ... [et al.] Curr Protoc Bioinformatics. 2006 Oct;Chapter 5:Unit 5.6.</style></notes></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%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Davis, F. P.</style></author><author><style face="normal" font="default" size="100%">Braberg, H.</style></author><author><style face="normal" font="default" size="100%">Madhusudhan, M. S.</style></author><author><style face="normal" font="default" size="100%">Rossi, A.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Karchin, R.</style></author><author><style face="normal" font="default" size="100%">Webb, B. M.</style></author><author><style face="normal" font="default" size="100%">Eramian, D.</style></author><author><style face="normal" font="default" size="100%">Shen, M. Y.</style></author><author><style face="normal" font="default" size="100%">Kelly, L.</style></author><author><style face="normal" font="default" size="100%">Melo, F.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">MODBASE: a database of annotated comparative protein structure models and associated resources</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Binding Sites *Databases</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Polymorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Humans Internet Ligands *Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Systems Integration User-Computer Interface</style></keyword><keyword><style  face="normal" font="default" size="100%">Single Nucleotide Protein Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Tertiary Proteins/*chemistry/genetics/metabolism Software *Structural Homology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2006</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=16381869</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">Database issue</style></number><volume><style face="normal" font="default" size="100%">34</style></volume><pages><style face="normal" font="default" size="100%">D291-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MODBASE (http://salilab.org/modbase) is a database of annotated comparative protein structure models for all available protein sequences that can be matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on MODELLER for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE is updated regularly to reflect the growth in protein sequence and structure databases, and improvements in the software for calculating the models. MODBASE currently contains 3 094 524 reliable models for domains in 1 094 750 out of 1 817 889 unique protein sequences in the UniProt database (July 5, 2005); only models based on statistically significant alignments and models assessed to have the correct fold despite insignificant alignments are included. MODBASE also allows users to generate comparative models for proteins of interest with the automated modeling server MODWEB (http://salilab.org/modweb). Our other resources integrated with MODBASE include comprehensive databases of multiple protein structure alignments (DBAli, http://salilab.org/dbali), structurally defined ligand binding sites and structurally defined binary domain interfaces (PIBASE, http://salilab.org/pibase) as well as predictions of ligand binding sites, interactions between yeast proteins, and functional consequences of human nsSNPs (LS-SNP, http://salilab.org/LS-SNP).</style></abstract><notes><style face="normal" font="default" size="100%">Pieper, Ursula Eswar, Narayanan Davis, Fred P Braberg, Hannes Madhusudhan, M S Rossi, Andrea Marti-Renom, Marc Karchin, Rachel Webb, Ben M Eramian, David Shen, Min-Yi Kelly, Libusha Melo, Francisco Sali, Andrej GM 08284/GM/NIGMS NIH HHS/United States P50 GM62529/GM/NIGMS NIH HHS/United States R01 GM 54762/GM/NIGMS NIH HHS/United States R33 CA84699/CA/NCI NIH HHS/United States U54 GM074945/GM/NIGMS NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t England Nucleic acids research Nucleic Acids Res. 2006 Jan 1;34(Database issue):D291-5.</style></notes></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%">Espadaler, J.</style></author><author><style face="normal" font="default" size="100%">Aragues, R.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Querol, E.</style></author><author><style face="normal" font="default" size="100%">Aviles, F. X.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author><author><style face="normal" font="default" size="100%">Oliva, B.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Detecting remotely related proteins by their interactions and sequence similarity</style></title><secondary-title><style face="normal" font="default" size="100%">Proc Natl Acad Sci U S A</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid</style></keyword><keyword><style  face="normal" font="default" size="100%">Computational Biology Databases</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Protein Conformation Protein Folding Proteins/*genetics/*metabolism Proteomics/*methods *Sequence Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein *Evolution</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=15883372</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">20</style></number><volume><style face="normal" font="default" size="100%">102</style></volume><pages><style face="normal" font="default" size="100%">7151-6</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The function of an uncharacterized protein is usually inferred either from its homology to, or its interactions with, characterized proteins. Here, we use both sequence similarity and protein interactions to identify relationships between remotely related protein sequences. We rely on the fact that homologous sequences share similar interactions, and, therefore, the set of interacting partners of the partners of a given protein is enriched by its homologs. The approach was bench-marked by assigning the fold and functional family to test sequences of known structure. Specifically, we relied on 1,434 proteins with known folds, as defined in the Structural Classification of Proteins (SCOP) database, and with known interacting partners, as defined in the Database of Interacting Proteins (DIP). For this subset, the specificity of fold assignment was increased from 54% for position-specific iterative BLAST to 75% for our approach, with a concomitant increase in sensitivity for a few percentage points. Similarly, the specificity of family assignment at the e-value threshold of 10(-8) was increased from 70% to 87%. The proposed method would be a useful tool for large-scale automated discovery of remote relationships between protein sequences, given its unique reliance on sequence similarity and protein-protein interactions.</style></abstract><notes><style face="normal" font="default" size="100%">Espadaler, Jordi Aragues, Ramon Eswar, Narayanan Marti-Renom, Marc A Querol, Enrique Aviles, Francesc X Sali, Andrej Oliva, Baldomero R01 GM54762/GM/NIGMS NIH HHS/United States Comparative Study Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov’t Research Support, U.S. Gov’t, P.H.S. United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2005 May 17;102(20):7151-6. Epub 2005 May 9.</style></notes></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%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Braberg, H.</style></author><author><style face="normal" font="default" size="100%">Madhusudhan, M. S.</style></author><author><style face="normal" font="default" size="100%">Davis, F. P.</style></author><author><style face="normal" font="default" size="100%">Stuart, A. C.</style></author><author><style face="normal" font="default" size="100%">Mirkovic, N.</style></author><author><style face="normal" font="default" size="100%">Rossi, A.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Fiser, A.</style></author><author><style face="normal" font="default" size="100%">Webb, B.</style></author><author><style face="normal" font="default" size="100%">Greenblatt, D.</style></author><author><style face="normal" font="default" size="100%">Huang, C. C.</style></author><author><style face="normal" font="default" size="100%">Ferrin, T. E.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">MODBASE, a database of annotated comparative protein structure models, and associated resources</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence Animals Binding Sites *Computational Biology *Databases</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Molecular Sequence Data Polymorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Genomics Humans Internet Ligands Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Single Nucleotide Protein Binding Protein Conformation Proteins/*chemistry/genetics Sequence Alignment Software User-Computer Interface</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2004</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=14681398</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">Database issue</style></number><volume><style face="normal" font="default" size="100%">32</style></volume><pages><style face="normal" font="default" size="100%">D217-22</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">MODBASE (http://salilab.org/modbase) is a relational database of annotated comparative protein structure models for all available protein sequences matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on the MODELLER package for fold assignment, sequence-structure alignment, model building and model assessment (http:/salilab.org/modeller). MODBASE uses the MySQL relational database management system for flexible querying and CHIMERA for viewing the sequences and structures (http://www.cgl.ucsf.edu/chimera/). MODBASE is updated regularly to reflect the growth in protein sequence and structure databases, as well as improvements in the software for calculating the models. For ease of access, MODBASE is organized into different data sets. The largest data set contains 1,26,629 models for domains in 659,495 out of 1,182,126 unique protein sequences in the complete Swiss-Prot/TrEMBL database (August 25, 2003); only models based on alignments with significant similarity scores and models assessed to have the correct fold despite insignificant alignments are included. Another model data set supports target selection and structure-based annotation by the New York Structural Genomics Research Consortium; e.g. the 53 new structures produced by the consortium allowed us to characterize structurally 24,113 sequences. MODBASE also contains binding site predictions for small ligands and a set of predicted interactions between pairs of modeled sequences from the same genome. Our other resources associated with MODBASE include a comprehensive database of multiple protein structure alignments (DBALI, http://salilab.org/dbali) as well as web servers for automated comparative modeling with MODPIPE (MODWEB, http://salilab. org/modweb), modeling of loops in protein structures (MODLOOP, http://salilab.org/modloop) and predicting functional consequences of single nucleotide polymorphisms (SNPWEB, http://salilab. org/snpweb).</style></abstract><notes><style face="normal" font="default" size="100%">Pieper, Ursula Eswar, Narayanan Braberg, Hannes Madhusudhan, M S Davis, Fred P Stuart, Ashley C Mirkovic, Nebojsa Rossi, Andrea Marti-Renom, Marc A Fiser, Andras Webb, Ben Greenblatt, Daniel Huang, Conrad C Ferrin, Thomas E Sali, Andrej P41 RR01081/RR/NCRR NIH HHS/United States P50 GM62529/GM/NIGMS NIH HHS/United States R01 GM 54762/GM/NIGMS NIH HHS/United States R33 CA84699/CA/NCI NIH HHS/United States Research Support, Non-U.S. Gov’t Research Support, U.S. Gov’t, P.H.S. England Nucleic acids research Nucleic Acids Res. 2004 Jan 1;32(Database issue):D217-22.</style></notes></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%">Koh, I. Y.</style></author><author><style face="normal" font="default" size="100%">Eyrich, V. A.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Przybylski, D.</style></author><author><style face="normal" font="default" size="100%">Madhusudhan, M. S.</style></author><author><style face="normal" font="default" size="100%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">Grana, O.</style></author><author><style face="normal" font="default" size="100%">Pazos, F.</style></author><author><style face="normal" font="default" size="100%">Valencia, A.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author><author><style face="normal" font="default" size="100%">Rost, B.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">EVA: Evaluation of protein structure prediction servers</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Automation Databases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Internet *Protein Conformation Protein Folding Protein Structure</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structural Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Secondary Proteins/chemistry Reproducibility of Results *Sequence Analysis</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=12824315</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">13</style></number><volume><style face="normal" font="default" size="100%">31</style></volume><pages><style face="normal" font="default" size="100%">3311-5</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">EVA (http://cubic.bioc.columbia.edu/eva/) is a web server for evaluation of the accuracy of automated protein structure prediction methods. The evaluation is updated automatically each week, to cope with the large number of existing prediction servers and the constant changes in the prediction methods. EVA currently assesses servers for secondary structure prediction, contact prediction, comparative protein structure modelling and threading/fold recognition. Every day, sequences of newly available protein structures in the Protein Data Bank (PDB) are sent to the servers and their predictions are collected. The predictions are then compared to the experimental structures once a week; the results are published on the EVA web pages. Over time, EVA has accumulated prediction results for a large number of proteins, ranging from hundreds to thousands, depending on the prediction method. This large sample assures that methods are compared reliably. As a result, EVA provides useful information to developers as well as users of prediction methods.</style></abstract><notes><style face="normal" font="default" size="100%">Koh, Ingrid Y Y Eyrich, Volker A Marti-Renom, Marc A Przybylski, Dariusz Madhusudhan, Mallur S Eswar, Narayanan Grana, Osvaldo Pazos, Florencio Valencia, Alfonso Sali, Andrej Rost, Burkhard 1-P50-GM62413-01/GM/NIGMS NIH HHS/United States 5-P20-LM7276/LM/NLM NIH HHS/United States P50 GM62529/GM/NIGMS NIH HHS/United States R01 GM54762/GM/NIGMS NIH HHS/United States R01-GM63029-01/GM/NIGMS NIH HHS/United States Research Support, Non-U.S. Gov’t Research Support, U.S. Gov’t, Non-P.H.S. Research Support, U.S. Gov’t, P.H.S. England Nucleic acids research Nucleic Acids Res. 2003 Jul 1;31(13):3311-5.</style></notes></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%">Eswar, N.</style></author><author><style face="normal" font="default" size="100%">John, B.</style></author><author><style face="normal" font="default" size="100%">Mirkovic, N.</style></author><author><style face="normal" font="default" size="100%">Fiser, A.</style></author><author><style face="normal" font="default" size="100%">Ilyin, V. A.</style></author><author><style face="normal" font="default" size="100%">Pieper, U.</style></author><author><style face="normal" font="default" size="100%">Stuart, A. C.</style></author><author><style face="normal" font="default" size="100%">M. A. Marti-Renom</style></author><author><style face="normal" font="default" size="100%">Madhusudhan, M. S.</style></author><author><style face="normal" font="default" size="100%">Yerkovich, B.</style></author><author><style face="normal" font="default" size="100%">Sali, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Tools for comparative protein structure modeling and analysis</style></title><secondary-title><style face="normal" font="default" size="100%">Nucleic Acids Res</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid *Software *Structural Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Internet Models</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Protein Folding Proteins/chemistry Reproducibility of Results Sequence Alignment Sequence Homology</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Systems Integration</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2003</style></year></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=12824331</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">13</style></number><volume><style face="normal" font="default" size="100%">31</style></volume><pages><style face="normal" font="default" size="100%">3375-80</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The following resources for comparative protein structure modeling and analysis are described (http://salilab.org): MODELLER, a program for comparative modeling by satisfaction of spatial restraints; MODWEB, a web server for automated comparative modeling that relies on PSI-BLAST, IMPALA and MODELLER; MODLOOP, a web server for automated loop modeling that relies on MODELLER; MOULDER, a CPU intensive protocol of MODWEB for building comparative models based on distant known structures; MODBASE, a comprehensive database of annotated comparative models for all sequences detectably related to a known structure; MODVIEW, a Netscape plugin for Linux that integrates viewing of multiple sequences and structures; and SNPWEB, a web server for structure-based prediction of the functional impact of a single amino acid substitution.</style></abstract><notes><style face="normal" font="default" size="100%">Eswar, Narayanan John, Bino Mirkovic, Nebojsa Fiser, Andras Ilyin, Valentin A Pieper, Ursula Stuart, Ashley C Marti-Renom, Marc A Madhusudhan, M S Yerkovich, Bozidar Sali, Andrej P50 GM62529/GM/NIGMS NIH HHS/United States R01 GM 54762/GM/NIGMS NIH HHS/United States R33 CA84699/CA/NCI NIH HHS/United States Research Support, Non-U.S. Gov’t Research Support, U.S. Gov’t, P.H.S. England Nucleic acids research Nucleic Acids Res. 2003 Jul 1;31(13):3375-80.</style></notes></record></records></xml>