Linked Life Data

21554249

Source:http://linkedlifedata.com/resource/pubmed/id/21554249

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:21554249rdf:typepubmed:Citationlld:pubmed
pubmed-article:21554249lifeskim:mentionsumls-concept:C0007589lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C0090388lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C0243041lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C0441655lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C1421563lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C0231448lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C0877853lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C0443220lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C1511938lld:lifeskim
pubmed-article:21554249lifeskim:mentionsumls-concept:C1707271lld:lifeskim
pubmed-article:21554249pubmed:issue3lld:pubmed
pubmed-article:21554249pubmed:dateCreated2011-7-13lld:pubmed
pubmed-article:21554249pubmed:abstractTextIntracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell signalling and disease progression. The 14-3-3? isoform is a molecular chaperone, preventing the stress-induced aggregation of target proteins in a manner comparable with that of the unrelated sHsps (small heat-shock proteins). 1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3? and is similar in structure and length to the C-terminal extension of mammalian sHsps. The extension stabilizes 14-3-3?, but has no direct role in chaperone action. Lys(49) is an important functional residue within the ligand-binding groove of 14-3-3? with K49E 14-3-3? exhibiting markedly reduced binding to phosphorylated and non-phosphorylated ligands. The R18 peptide binds to the binding groove of 14-3-3? with high affinity and also reduces the interaction of 14-3-3? ligands. However, neither the K49E mutation nor the presence of the R18 peptide affected the chaperone activity of 14-3-3?, implying that the C-terminal extension and binding groove of 14-3-3? do not mediate interaction with target proteins during chaperone action. Other region(s) in 14-3-3? are most likely to be involved, i.e. the protein's chaperone and phosphoserine-binding activities are functionally and structurally separated.lld:pubmed
pubmed-article:21554249pubmed:languageenglld:pubmed
pubmed-article:21554249pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:21554249pubmed:citationSubsetIMlld:pubmed
pubmed-article:21554249pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:21554249pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:21554249pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:21554249pubmed:statusMEDLINElld:pubmed
pubmed-article:21554249pubmed:monthAuglld:pubmed
pubmed-article:21554249pubmed:issn1470-8728lld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:CarverJohn...lld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:ZhangLixinLlld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:WoodcockJoann...lld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:FuHaianHlld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:EcroydHeathHlld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:WilliamsDanie...lld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:DaiHuanqinHlld:pubmed
pubmed-article:21554249pubmed:authorpubmed-author:GoodwinKaty...lld:pubmed
pubmed-article:21554249pubmed:copyrightInfo© The Authors Journal compilation © 2011 Biochemical Societylld:pubmed
pubmed-article:21554249pubmed:issnTypeElectroniclld:pubmed
pubmed-article:21554249pubmed:day1lld:pubmed
pubmed-article:21554249pubmed:volume437lld:pubmed
pubmed-article:21554249pubmed:ownerNLMlld:pubmed
pubmed-article:21554249pubmed:authorsCompleteYlld:pubmed
pubmed-article:21554249pubmed:pagination493-503lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:meshHeadingpubmed-meshheading:21554249...lld:pubmed
pubmed-article:21554249pubmed:year2011lld:pubmed
pubmed-article:21554249pubmed:articleTitleNMR spectroscopy of 14-3-3? reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3?.lld:pubmed
pubmed-article:21554249pubmed:affiliationSchool of Chemistry and Physics, The University of Adelaide, Adelaide, SA 5005, Australia.lld:pubmed
pubmed-article:21554249pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:21554249pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:7534entrezgene:pubmedpubmed-article:21554249lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:21554249lld:entrezgene