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dc.contributor.authorGould, CM
dc.contributor.authorDiella, F
dc.contributor.authorVia, A
dc.contributor.authorPuntervoll, P
dc.contributor.authorGemünd, C
dc.contributor.authorChabanis-Davidson, S
dc.contributor.authorMichael, S
dc.contributor.authorSayadi, A
dc.contributor.authorBryne, JC
dc.contributor.authorChica, C
dc.contributor.authorSeiler, M
dc.contributor.authorDavey, NE
dc.contributor.authorHaslam, N
dc.contributor.authorWeatheritt, RJ
dc.contributor.authorBudd, A
dc.contributor.authorHughes, T
dc.contributor.authorPas, J
dc.contributor.authorRychlewski, L
dc.contributor.authorTravé, G
dc.contributor.authorAasland, R
dc.contributor.authorHelmer-Citterich, M
dc.contributor.authorLinding, R
dc.contributor.authorGibson, TJ
dc.coverage.spatialEngland
dc.date.accessioned2018-08-24T08:25:31Z
dc.date.issued2010-01-01
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/19920119
dc.identifiergkp1016
dc.identifier.citationNucleic Acids Res, 2010, 38 (Database issue), pp. D167 - D180
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2378
dc.identifier.eissn1362-4962
dc.identifier.doi10.1093/nar/gkp1016
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 http://elm.eu.org/ 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.
dc.format.extentD167 - D180
dc.languageeng
dc.language.isoeng
dc.publisherOXFORD UNIV PRESS
dc.subjectAmino Acid Motifs
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectComputational Biology
dc.subjectDatabases, Genetic
dc.subjectDatabases, Nucleic Acid
dc.subjectDatabases, Protein
dc.subjectEukaryotic Cells
dc.subjectHumans
dc.subjectInformation Storage and Retrieval
dc.subjectInternet
dc.subjectMolecular Sequence Data
dc.subjectProtein Structure, Tertiary
dc.subjectSequence Homology, Amino Acid
dc.subjectSoftware
dc.titleELM: the status of the 2010 eukaryotic linear motif resource.
dc.typeJournal Article
rioxxterms.versionofrecord10.1093/nar/gkp1016
rioxxterms.licenseref.startdate2010-01
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfNucleic Acids Res
pubs.issueDatabase issue
pubs.notesNot known
pubs.organisational-group/ICR
pubs.organisational-group/ICR
pubs.publication-statusPublished
pubs.volume38
pubs.embargo.termsNot known
dc.contributor.icrauthorDavey, Norman


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