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      ModBase, a database of annotated comparative protein structure models, and associated resources

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          Abstract

          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 10 355 444 reliable models for domains in 2 421 920 unique protein sequences. ModBase allows users to update comparative models on demand, and request modeling of additional sequences through an interface to the ModWeb modeling server ( http://salilab.org/modweb). ModBase models are available through the ModBase interface as well as the Protein Model Portal ( http://www.proteinmodelportal.org/). Recently developed associated resources include the SALIGN server for multiple sequence and structure alignment ( http://salilab.org/salign), the ModEval server for predicting the accuracy of protein structure models ( http://salilab.org/modeval), the PCSS server for predicting which peptides bind to a given protein ( http://salilab.org/pcss) and the FoXS server for calculating and fitting Small Angle X-ray Scattering profiles ( http://salilab.org/foxs).

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          Most cited references62

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          Identification of common molecular subsequences.

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            Helicobacter pylori infection.

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              The Universal Protein Resource (UniProt): an expanding universe of protein information

              The Universal Protein Resource (UniProt) provides a central resource on protein sequences and functional annotation with three database components, each addressing a key need in protein bioinformatics. The UniProt Knowledgebase (UniProtKB), comprising the manually annotated UniProtKB/Swiss-Prot section and the automatically annotated UniProtKB/TrEMBL section, is the preeminent storehouse of protein annotation. The extensive cross-references, functional and feature annotations and literature-based evidence attribution enable scientists to analyse proteins and query across databases. The UniProt Reference Clusters (UniRef) speed similarity searches via sequence space compression by merging sequences that are 100% (UniRef100), 90% (UniRef90) or 50% (UniRef50) identical. Finally, the UniProt Archive (UniParc) stores all publicly available protein sequences, containing the history of sequence data with links to the source databases. UniProt databases continue to grow in size and in availability of information. Recent and upcoming changes to database contents, formats, controlled vocabularies and services are described. New download availability includes all major releases of UniProtKB, sequence collections by taxonomic division and complete proteomes. A bibliography mapping service has been added, and an ID mapping service will be available soon. UniProt databases can be accessed online at or downloaded at .
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                Author and article information

                Journal
                Nucleic Acids Res
                nar
                nar
                Nucleic Acids Research
                Oxford University Press
                0305-1048
                1362-4962
                January 2011
                January 2011
                19 November 2010
                19 November 2010
                : 39
                : Database issue , Database issue
                : D465-D474
                Affiliations
                1 Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California at San Francisco, CA 94158, 2Graduate Group in Bioinformatics, University of California at San Francisco, CA, 3Graduate Group in Biophysics, University of California at San Francisco, 4Resource for Biocomputing, Visualization, and Informatics, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143-2240, 5Department of Bioengineering, QB3 Institute and Department of Plant and Microbial Biology, University of California, Berkeley, CA 94720, 6Eli Lilly and Company, San Diego, CA 92121, USA and 7Bioinformatics Institute, Singapore 138 671, Singapore
                Author notes
                *To whom correspondence should be addressed. Tel: +1 415 514 4227; Fax: +1 415 514 4231; Email: sali@ 123456salilab.org
                Article
                gkq1091
                10.1093/nar/gkq1091
                3013688
                21097780
                99b45d3b-f41e-40b0-a541-ed4c4d34db40
                © The Author(s) 2010. Published by Oxford University Press.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 15 September 2010
                : 14 October 2010
                : 15 October 2010
                Categories
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                Genetics
                Genetics

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