| pubmed-article:1848666 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1848666 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:1848666 | lifeskim:mentions | umls-concept:C0080059 | lld:lifeskim |
| pubmed-article:1848666 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:1848666 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:1848666 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:1848666 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:1848666 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1848666 | pubmed:dateCreated | 1991-4-22 | lld:pubmed |
| pubmed-article:1848666 | pubmed:abstractText | When purified p60v-src was mixed with lysates of chicken embryo fibroblasts and immunoprecipitated with anti-Src antibody, phosphatidylinositol (PI)-3 kinase activity was found to be present in the Src protein immunoprecipitates. The level of bound PI-3 kinase activity was 5 to 10 times higher in lysates obtained from cells transformed by the src, fps, or yes oncogene than in lysates of uninfected cells. This increase in associated PI-3 kinase activity appears to be due to increased binding of this enzyme to p60v-src. This change most likely resulted from tyrosine phosphorylation of PI-3 kinase or an associated protein, since the PI-3 kinase activity that can bind to p60v-src was depleted by antiphosphotyrosine antibody. Binding of PI-3 kinase did not require either p60src protein kinase activity or autophosphorylation of p60v-src tyrosine residues. Furthermore, binding was markedly decreased by deletions in the N-terminal SH2 region but unchanged by deletion of the C-terminal half of p60v-src containing the catalytic domain. Taking these data together, it appears that PI-3 kinase or its associated protein is phosphorylated on tyrosine and that the phosphorylated form can bind to the N-terminal half of p60v-src, which contains the SH2 domain. | lld:pubmed |
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| pubmed-article:1848666 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1848666 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848666 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1848666 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1848666 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1848666 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1848666 | pubmed:author | pubmed-author:HanafusaHH | lld:pubmed |
| pubmed-article:1848666 | pubmed:author | pubmed-author:FukuiYY | lld:pubmed |
| pubmed-article:1848666 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1848666 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:1848666 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1848666 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1848666 | pubmed:pagination | 1972-9 | lld:pubmed |
| pubmed-article:1848666 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1848666 | pubmed:meshHeading | pubmed-meshheading:1848666-... | lld:pubmed |
| pubmed-article:1848666 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1848666 | pubmed:articleTitle | Requirement of phosphatidylinositol-3 kinase modification for its association with p60src. | lld:pubmed |
| pubmed-article:1848666 | pubmed:affiliation | Rockefeller University, New York, New York 10021-6399. | lld:pubmed |
| pubmed-article:1848666 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1848666 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1848666 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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