MODBASE: a database of annotated comparative protein structure models and associated resources

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dc.catalogadoraba
dc.contributor.authorPieper, U.
dc.contributor.authorEswar, N.
dc.contributor.authorDavis, F. P.
dc.contributor.authorBraberg, H.
dc.contributor.authorMadhusudhan, M. S.
dc.contributor.authorRossi, A.
dc.contributor.authorMarti Renom, M.
dc.contributor.authorKarchin, R.
dc.contributor.authorWebb, B. M.
dc.contributor.authorEramian, D.
dc.contributor.authorShen, M. Y.
dc.contributor.authorKelly, L.
dc.contributor.authorMelo Ledermann, Francisco Javier
dc.contributor.authorSali, A.
dc.date.accessioned2025-02-06T19:39:57Z
dc.date.available2025-02-06T19:39:57Z
dc.date.issued2006
dc.description.abstractMODBASE (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).
dc.format.extent5 páginas
dc.fuente.origenSIPA
dc.identifier.doi10.1093/nar/gkj059
dc.identifier.eissn1362-4962
dc.identifier.issn0305-1048
dc.identifier.pubmedid16381869
dc.identifier.pubmedidPMC1347422
dc.identifier.scopusid2-s2.0-33644874394
dc.identifier.urihttps://doi.org/10.1093/nar/gkj059
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/102188
dc.identifier.wosidWOS:000239307700063
dc.information.autorucFacultad de Ciencias Biológicas; Melo Ledermann, Francisco Javier; 0000-0002-0424-5991; 82342
dc.issue.numeroSuppl. 1
dc.language.isoen
dc.nota.accesocontenido completo
dc.pagina.finalD295
dc.pagina.inicioD291
dc.revistaNucleic acids research
dc.rightsacceso abierto
dc.subject.ddc570
dc.subject.deweyBiologíaes_ES
dc.subject.ods03 Good health and well-being
dc.subject.odspa03 Salud y bienestar
dc.titleMODBASE: a database of annotated comparative protein structure models and associated resources
dc.typeartículo
dc.volumen34
sipa.codpersvinculados82342
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