pubmed-article:12370821 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12370821 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:12370821 | lifeskim:mentions | umls-concept:C0059239 | lld:lifeskim |
pubmed-article:12370821 | lifeskim:mentions | umls-concept:C1565434 | lld:lifeskim |
pubmed-article:12370821 | lifeskim:mentions | umls-concept:C0813988 | lld:lifeskim |
pubmed-article:12370821 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:12370821 | pubmed:issue | 46 | lld:pubmed |
pubmed-article:12370821 | pubmed:dateCreated | 2002-10-8 | lld:pubmed |
pubmed-article:12370821 | pubmed:abstractText | Tyr-397 phosphorylation is important for focal adhesion kinase (FAK)-mediated signalling. In vitro FAK immunocomplex kinase experiments demonstrated that both FAK Tyr-576/577 and Tyr-863 phosphorylation regulated FAK Tyr-397 phosphorylation. While the former increased the intermolecular transphosphorylation activity of FAK, the latter was crucial for its cis-phosphorylation. This observation was further supported by the reduced complex formation between Src and 3F-FAK (576F/577F/863F-FAK) as compared to that between Src and 576F/577F-FAK or Src and 863F-FAK. Regulation of cis- and transphosphorylation activities of FAK by such a differential tyrosyl phosphorylation mechanism is unprecedented. Furthermore, in fibronectin-stimulated cells, both Tyr-576/577 and Tyr-863 phosphorylation could enhance FAK Tyr-397 phosphorylation. This observation implies that integrin-mediated FAK Tyr-397 phosphorylation was also regulated through both FAK cis- and transphosphorylation mechanisms. | lld:pubmed |
pubmed-article:12370821 | pubmed:language | eng | lld:pubmed |
pubmed-article:12370821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12370821 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12370821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12370821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12370821 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12370821 | pubmed:month | Oct | lld:pubmed |
pubmed-article:12370821 | pubmed:issn | 0950-9232 | lld:pubmed |
pubmed-article:12370821 | pubmed:author | pubmed-author:LeuTzeng-Horn... | lld:pubmed |
pubmed-article:12370821 | pubmed:author | pubmed-author:MaaMing-CheiM... | lld:pubmed |
pubmed-article:12370821 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12370821 | pubmed:day | 10 | lld:pubmed |
pubmed-article:12370821 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:12370821 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12370821 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12370821 | pubmed:pagination | 6992-7000 | lld:pubmed |
pubmed-article:12370821 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:12370821 | pubmed:meshHeading | pubmed-meshheading:12370821... | lld:pubmed |
pubmed-article:12370821 | pubmed:meshHeading | pubmed-meshheading:12370821... | lld:pubmed |
pubmed-article:12370821 | pubmed:meshHeading | pubmed-meshheading:12370821... | lld:pubmed |
pubmed-article:12370821 | pubmed:meshHeading | pubmed-meshheading:12370821... | lld:pubmed |
pubmed-article:12370821 | pubmed:meshHeading | pubmed-meshheading:12370821... | lld:pubmed |
pubmed-article:12370821 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12370821 | pubmed:articleTitle | Tyr-863 phosphorylation enhances focal adhesion kinase autophosphorylation at Tyr-397. | lld:pubmed |
pubmed-article:12370821 | pubmed:affiliation | Department of Pharmacology, College of Medicine, National Cheng Kung University, Tainan, Taiwan 70101, Republic of China. tzengleu@mail.ncku.edu.tw | lld:pubmed |
pubmed-article:12370821 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12370821 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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