Linked Life Data

7515062

Source:http://linkedlifedata.com/resource/pubmed/id/7515062

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:7515062rdf:typepubmed:Citationlld:pubmed
pubmed-article:7515062lifeskim:mentionsumls-concept:C0085536lld:lifeskim
pubmed-article:7515062lifeskim:mentionsumls-concept:C1334140lld:lifeskim
pubmed-article:7515062lifeskim:mentionsumls-concept:C1335280lld:lifeskim
pubmed-article:7515062lifeskim:mentionsumls-concept:C1158884lld:lifeskim
pubmed-article:7515062lifeskim:mentionsumls-concept:C0123658lld:lifeskim
pubmed-article:7515062pubmed:issue22lld:pubmed
pubmed-article:7515062pubmed:dateCreated1994-6-30lld:pubmed
pubmed-article:7515062pubmed:abstractTextThe phosphotyrosine (Tyr(P)) form of insulin receptor substrate 1 (IRS-1) is a key component in insulin signaling. Our previous study revealed that Tyr(P) IRS-1 binds to the widely distributed tyrosine phosphatase PTP2C through the src homology 2 (SH2) domains of the latter. In the present study, we examined the activity of this enzyme and of a truncated form lacking the SH2 domains (delta PTP2C) toward IRS-1 and also toward the cytoplasmic domain of the insulin receptor. Tyr(P) IRS-1 was prepared by phosphorylation of recombinant IRS-1 with recombinant cytoplasmic insulin receptor kinase (CIRK). PTP2C rapidly dephosphorylated Tyr(P) IRS-1; dephosphorylation by delta PTP2C was approximately one-third as fast. Other substrates, including Tyr(P) CIRK, were not dephosphorylated as rapidly by PTP2C; moreover, delta PTP2C was at least 10 times more active than PTP2C toward CIRK and other substrates. These results indicate that the binding of Tyr(P) residues on IRS-1 to the SH2 domain(s) of PTP2C enhances its activity toward IRS-1 and suggest that PTP2C is the phosphatase responsible for the dephosphorylation of IRS-1 in vivo. In addition, with the expectation that a PTP2C-resistant form of IRS-1 will be useful in investigations of IRS-1 function, we determined that IRS-1 can be thiophosphorylated with adenosine 5'-O-(3-thiotriphosphate) and CIRK and that this form of IRS-1 is resistant to PTP2C.lld:pubmed
pubmed-article:7515062pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:languageenglld:pubmed
pubmed-article:7515062pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:citationSubsetIMlld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:7515062pubmed:statusMEDLINElld:pubmed
pubmed-article:7515062pubmed:monthJunlld:pubmed
pubmed-article:7515062pubmed:issn0021-9258lld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:FischerE HEHlld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:LienhardG EGElld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:ZhaoZZlld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:ShenS HSHlld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:LavanB EBElld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:KuhnéM RMRlld:pubmed
pubmed-article:7515062pubmed:authorpubmed-author:RowleyLLlld:pubmed
pubmed-article:7515062pubmed:issnTypePrintlld:pubmed
pubmed-article:7515062pubmed:day3lld:pubmed
pubmed-article:7515062pubmed:volume269lld:pubmed
pubmed-article:7515062pubmed:ownerNLMlld:pubmed
pubmed-article:7515062pubmed:authorsCompleteYlld:pubmed
pubmed-article:7515062pubmed:pagination15833-7lld:pubmed
pubmed-article:7515062pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:meshHeadingpubmed-meshheading:7515062-...lld:pubmed
pubmed-article:7515062pubmed:year1994lld:pubmed
pubmed-article:7515062pubmed:articleTitleDephosphorylation of insulin receptor substrate 1 by the tyrosine phosphatase PTP2C.lld:pubmed
pubmed-article:7515062pubmed:affiliationDepartment of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755.lld:pubmed
pubmed-article:7515062pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7515062pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:7515062pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:7515062lld:pubmed