Linked Life Data

10896934

Source:http://linkedlifedata.com/resource/pubmed/id/10896934

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10896934rdf:typepubmed:Citationlld:pubmed
pubmed-article:10896934lifeskim:mentionsumls-concept:C0285558lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1705328lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1705341lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C0205145lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C0031715lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1511625lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C0040005lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1416498lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C0812228lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1335204lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1418440lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1167622lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C0851285lld:lifeskim
pubmed-article:10896934lifeskim:mentionsumls-concept:C1533691lld:lifeskim
pubmed-article:10896934pubmed:issue40lld:pubmed
pubmed-article:10896934pubmed:dateCreated2000-10-23lld:pubmed
pubmed-article:10896934pubmed:abstractTextThe mechanism of outside-in signaling by integrins parallels that for growth factor receptors. In both pathways, phosphorylation of a cytoplasmic segment on tyrosine generates a docking site for proteins containing Src homology 2 (SH2) and phosphotyrosine binding domains. We recently observed that phosphorylation of a threonine (Thr-753), six amino acids proximal to tyrosine 759 in beta(3) of the platelet specific integrin alpha(IIb)beta(3), inhibits outside-in signaling through this receptor. We hypothesized that the presence of phosphothreonine 753 either renders beta(3) a poor substrate for tyrosine kinases or inhibits the docking capabilities of the tyrosyl-phosphorylated form of beta(3.) The first alternative was tested by comparing the phosphorylation of beta(3) model peptides by the tyrosine kinase pp60(c-src) and we found that the presence of a phosphate group on a residue corresponding to Thr-753 did not detectably alter the kinetics of tyrosine phosphorylation. However, the presence of phosphate on this threonine inhibited the binding of Shc to tyrosyl-phosphorylated beta(3) peptide. The inhibitory effect of the phosphate group could be mimicked by substituting an aspartic acid for Thr-753, suggesting that a negative charge at this position modulates the binding of Shc and possibly other phosphotyrosine binding domain- and SH2-containing proteins. A survey of several protein kinases revealed that Thr-753 was avidly phosphorylated by PDK1 and Akt/PKB in vitro. These observations suggest that activation of PDK1 and/or Akt/PKB in platelets may modulate the binding activity and/or specificity of beta(3) for signaling molecules.lld:pubmed
pubmed-article:10896934pubmed:languageenglld:pubmed
pubmed-article:10896934pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:citationSubsetIMlld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10896934pubmed:statusMEDLINElld:pubmed
pubmed-article:10896934pubmed:monthOctlld:pubmed
pubmed-article:10896934pubmed:issn0021-9258lld:pubmed
pubmed-article:10896934pubmed:authorpubmed-author:SandersonM...lld:pubmed
pubmed-article:10896934pubmed:authorpubmed-author:LereaK MKMlld:pubmed
pubmed-article:10896934pubmed:authorpubmed-author:KirkR IRIlld:pubmed
pubmed-article:10896934pubmed:issnTypePrintlld:pubmed
pubmed-article:10896934pubmed:day6lld:pubmed
pubmed-article:10896934pubmed:volume275lld:pubmed
pubmed-article:10896934pubmed:ownerNLMlld:pubmed
pubmed-article:10896934pubmed:authorsCompleteYlld:pubmed
pubmed-article:10896934pubmed:pagination30901-6lld:pubmed
pubmed-article:10896934pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:meshHeadingpubmed-meshheading:10896934...lld:pubmed
pubmed-article:10896934pubmed:year2000lld:pubmed
pubmed-article:10896934pubmed:articleTitleThreonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding.lld:pubmed
pubmed-article:10896934pubmed:affiliationDepartment of Cell Biology & Anatomy, New York Medical College, Valhalla, New York 10595, USA.lld:pubmed
pubmed-article:10896934pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10896934pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
entrez-gene:207entrezgene:pubmedpubmed-article:10896934lld:entrezgene
entrez-gene:3690entrezgene:pubmedpubmed-article:10896934lld:entrezgene
entrez-gene:5170entrezgene:pubmedpubmed-article:10896934lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:10896934lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:10896934lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:10896934lld:pubmed
More...