pubmed-article:9218412 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9218412 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:9218412 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
pubmed-article:9218412 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
pubmed-article:9218412 | lifeskim:mentions | umls-concept:C0017280 | lld:lifeskim |
pubmed-article:9218412 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
pubmed-article:9218412 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:9218412 | pubmed:issue | 29 | lld:pubmed |
pubmed-article:9218412 | pubmed:dateCreated | 1997-8-18 | lld:pubmed |
pubmed-article:9218412 | pubmed:abstractText | Tyrosine kinases of the Src family are regulated via their Src homology 2 (SH2) and SH3 domains. The Nef protein of human immunodeficiency virus-1 (HIV-1) has previously been shown to bind with high affinity and specificity in vitro to the SH3 domain of Hck, a Src family member expressed primarily in myeloid cells. However, the effect of Nef on Hck activity in living cells is unknown. Here we show that Rat-2 fibroblasts co-expressing Hck and Nef rapidly developed transformed foci, whereas control cells expressing either protein alone did not. Nef formed a stable complex with Hck and stimulated its tyrosine kinase activity in vivo. Mutagenesis of the Nef proline-rich motif essential for SH3 binding completely blocked complex formation, kinase activation, and transformation, indicating that the Nef SH3-binding function is required for its effects on Hck. These results provide direct evidence that SH3 engagement is sufficient to activate a Src family kinase in vivo and suggest that Hck may be activated by Nef in HIV-infected macrophages. | lld:pubmed |
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pubmed-article:9218412 | pubmed:language | eng | lld:pubmed |
pubmed-article:9218412 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9218412 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9218412 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9218412 | pubmed:month | Jul | lld:pubmed |
pubmed-article:9218412 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9218412 | pubmed:author | pubmed-author:StevensonMM | lld:pubmed |
pubmed-article:9218412 | pubmed:author | pubmed-author:SmithgallT... | lld:pubmed |
pubmed-article:9218412 | pubmed:author | pubmed-author:BriggsS DSD | lld:pubmed |
pubmed-article:9218412 | pubmed:author | pubmed-author:SharkeyMM | lld:pubmed |
pubmed-article:9218412 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9218412 | pubmed:day | 18 | lld:pubmed |
pubmed-article:9218412 | pubmed:volume | 272 | lld:pubmed |
pubmed-article:9218412 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9218412 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9218412 | pubmed:pagination | 17899-902 | lld:pubmed |
pubmed-article:9218412 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:9218412 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9218412 | pubmed:articleTitle | SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1. | lld:pubmed |
pubmed-article:9218412 | pubmed:affiliation | Eppley Institute for Research in Cancer, University of Nebraska Medical Center, Omaha, Nebraska 68198-6805, USA. | lld:pubmed |
pubmed-article:9218412 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9218412 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9218412 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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