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dc.contributor.authorGould, Cathryn M.
dc.contributor.authorDiella, Francesca
dc.contributor.authorVia, Allegra
dc.contributor.authorPuntervoll, Pål
dc.contributor.authorGemünd, Christine
dc.contributor.authorChabanis-Davidson, Sophie
dc.contributor.authorMichael, Sushama
dc.contributor.authorSayadi, Ahmed
dc.contributor.authorBryne, Jan Christian
dc.contributor.authorChica, Claudia
dc.contributor.authorSeiler, Markus
dc.contributor.authorDavey, Norman E.
dc.contributor.authorHaslam, Neill
dc.contributor.authorWeatheritt, Robert J.
dc.contributor.authorBudd, Aidan
dc.contributor.authorHughes, Timothy
dc.contributor.authorPas, Jakub
dc.contributor.authorRychlewski, Leszek
dc.contributor.authorTrave, Gilles Michel
dc.contributor.authorAasland, Rein
dc.contributor.authorHelmer-Citterich, Manuela
dc.contributor.authorLinding, Rune
dc.contributor.authorGibson, Toby J.
dc.PublishedNucleic Acids Research 2010, 38:D167-D180eng
dc.description.abstractLinear motifs are short segments of multidomain proteins that provide regulatory functions independently of protein tertiary structure. Much of intracellular signalling passes through protein modifications at linear motifs. Many thousands of linear motif instances, most notably phosphorylation sites, have now been reported. Although clearly very abundant, linear motifs are difficult to predict de novo in protein sequences due to the difficulty of obtaining robust statistical assessments. The ELM resource at provides an expanding knowledge base, currently covering 146 known motifs, with annotation that includes >1300 experimentally reported instances. ELM is also an exploratory tool for suggesting new candidates of known linear motifs in proteins of interest. Information about protein domains, protein structure and native disorder, cellular and taxonomic contexts is used to reduce or deprecate false positive matches. Results are graphically displayed in a ‘Bar Code’ format, which also displays known instances from homologous proteins through a novel ‘Instance Mapper’ protocol based on PHI-BLAST. ELM server output provides links to the ELM annotation as well as to a number of remote resources. Using the links, researchers can explore the motifs, proteins, complex structures and associated literature to evaluate whether candidate motifs might be worth experimental investigation.en_US
dc.publisherOxford University Press (OUP)en_US
dc.rightsAttribution CC BY-NC 2.5 UKeng
dc.titleELM: the status of the 2010 eukaryotic linear motif resourceen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright The Author(s) 2009en_US
dc.subject.nsiVDP::Matematikk og naturvitenskap: 400::Basale biofag: 470::Molekylærbiologi: 473
dc.subject.nsiVDP::Mathematics and natural scienses: 400::Basic biosciences: 470::Molecular biology: 473
dc.subject.nsiVDP::Matematikk og Naturvitenskap: 400en_US

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Attribution CC BY-NC 2.5 UK
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