Linked Life Data

18796434

Source:http://linkedlifedata.com/resource/pubmed/id/18796434

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:18796434rdf:typepubmed:Citationlld:pubmed
pubmed-article:18796434lifeskim:mentionsumls-concept:C0080279lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1412097lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0000744lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0031727lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1826328lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1167622lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0013682lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0439851lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C2266681lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0007382lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0220905lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1704735lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1552596lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C2349975lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1947931lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0441712lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C1627358lld:lifeskim
pubmed-article:18796434lifeskim:mentionsumls-concept:C0332291lld:lifeskim
pubmed-article:18796434pubmed:issue46lld:pubmed
pubmed-article:18796434pubmed:dateCreated2008-11-10lld:pubmed
pubmed-article:18796434pubmed:abstractTextABL family tyrosine kinases are tightly regulated by autoinhibition and phosphorylation mechanisms. These kinases maintain an inactive conformation through intramolecular interactions involving SH3 and SH2 domains. RIN1, a downstream effector of RAS, binds to the ABL SH3 and SH2 domains and stimulates ABL tyrosine kinase activity. RIN1 binding to the ABL2 kinase resulted in a large decrease in Km and a small increase in Vmax toward an ABL consensus substrate peptide. The enzyme efficiency (k(cat)/Km) was increased more than 5-fold by RIN1. In addition, RIN1 strongly enhanced ABL-mediated phosphorylation of CRK, PSTPIP1, and DOK1, all established ABL substrates but with unique protein structures and distinct target sequences. Importantly RIN1-mediated stimulation of ABL kinase activity was independent of activation by SRC-mediated phosphorylation. RIN1 increased the kinase activity of both ABL1 and ABL2, and this occurred in the presence or absence of ABL regulatory domains outside the SH3-SH2-tyrosine kinase domain core. We further demonstrate that a catalytic site mutation associated with broad drug resistance, ABL1T315I, remains responsive to stimulation by RIN1. These findings are consistent with an allosteric kinase activation mechanism by which RIN1 binding promotes a more accessible ABL catalytic site through relief of autoinhibition. Direct disruption of RIN1 binding may therefore be a useful strategy to suppress the activity of normal and oncogenic ABL, including inhibitor-resistant mutants that confound current therapeutic strategies. Stimulation through derepression may be applicable to many other tyrosine kinases autoinhibited by coupled SH3 and SH2 domains.lld:pubmed
pubmed-article:18796434pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:commentsCorrectionshttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:languageenglld:pubmed
pubmed-article:18796434pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:citationSubsetIMlld:pubmed
pubmed-article:18796434pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:18796434pubmed:statusMEDLINElld:pubmed
pubmed-article:18796434pubmed:monthNovlld:pubmed
pubmed-article:18796434pubmed:issn0021-9258lld:pubmed
pubmed-article:18796434pubmed:authorpubmed-author:ColicelliJohn...lld:pubmed
pubmed-article:18796434pubmed:authorpubmed-author:KoleskeAnthon...lld:pubmed
pubmed-article:18796434pubmed:authorpubmed-author:TanisKeith...lld:pubmed
pubmed-article:18796434pubmed:authorpubmed-author:CaoXiaoqingXlld:pubmed
pubmed-article:18796434pubmed:issnTypePrintlld:pubmed
pubmed-article:18796434pubmed:day14lld:pubmed
pubmed-article:18796434pubmed:volume283lld:pubmed
pubmed-article:18796434pubmed:ownerNLMlld:pubmed
pubmed-article:18796434pubmed:authorsCompleteYlld:pubmed
pubmed-article:18796434pubmed:pagination31401-7lld:pubmed
pubmed-article:18796434pubmed:dateRevised2011-3-28lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
pubmed-article:18796434pubmed:meshHeadingpubmed-meshheading:18796434...lld:pubmed
More...