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dc.creatorSickmeier, M
dc.creatorHamilton, JA
dc.creatorLeGall, T
dc.creatorVacic, V
dc.creatorCortese, MS
dc.creatorTantos, A
dc.creatorSzabo, B
dc.creatorTompa, P
dc.creatorChen, J
dc.creatorUversky, VN
dc.creatorObradovic, Z
dc.creatorDunker, AK
dc.date.accessioned2021-02-01T22:12:54Z
dc.date.available2021-02-01T22:12:54Z
dc.date.issued2007-01-01
dc.identifier.issn0305-1048
dc.identifier.issn1362-4962
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/5610
dc.identifier.other17145717 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/5628
dc.description.abstractThe Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs). Intrinsically disordered proteins do not form a fixed three-dimensional structure under physiological conditions, either in their entireties or in segments or regions. We define IDP as a protein that contains at least one experimentally determined disordered region. Although lacking fixed structure, IDPs and regions carry out important biological functions, being typically involved in regulation, signaling and control. Such functions can involve high-specificity low-affinity interactions, the multiple binding of one protein to many partners and the multiple binding of many proteins to one partner. These three features are all enabled and enhanced by protein intrinsic disorder. One of the major hindrances in the study of IDPs has been the lack of organized information. DisProt was developed to enable IDP research by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. In addition to being a unique source of biological information, DisProt opens doors for a plethora of bioinformatics studies. DisProt is openly available at http://www.disprot.org. © 2007 Oxford University Press.
dc.format.extentD786-D793
dc.language.isoen
dc.relation.haspartNucleic Acids Research
dc.relation.isreferencedbyOxford University Press (OUP)
dc.rightsCC BY-NC
dc.subjectDatabases, Protein
dc.subjectInternet
dc.subjectProtein Conformation
dc.subjectProtein Folding
dc.subjectProteins
dc.subjectUser-Computer Interface
dc.titleDisProt: The database of disordered proteins
dc.typeArticle
dc.type.genreJournal Article
dc.relation.doi10.1093/nar/gkl893
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.date.updated2021-02-01T22:12:51Z
refterms.dateFOA2021-02-01T22:12:54Z


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