pubmed-article:8551236 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C1705831 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C1527940 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C1421567 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C0033713 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
pubmed-article:8551236 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:8551236 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8551236 | pubmed:dateCreated | 1996-2-22 | lld:pubmed |
pubmed-article:8551236 | pubmed:abstractText | Accumulating data show that the tyrosine protein kinase Zap-70 plays an essential role in T cell receptor-mediated signal transduction. However, the model of action, as well as the physiologically relevant substrates of Zap-70, have not been determined. We have attempted to identify a 120-kD tyrosine-phosphorylated protein (p120) that associates with Zap-70 in activated T lymphocytes. The results of our analyses showed that p120 is largely encoded by the c-cbl protooncogene. Furthermore, the association of Zap-70 with c-Cbl was shown to be induced by T cell receptor stimulation, implying that it required posttranslational modification of one or both of these products. FynT, but not Lck, also associated with c-Cbl in activated T cells. Finally, using a heterologous system, it was demonstrated that the ability of Zap-70 to cause tyrosine phosphorylation of p120c-cbl was dependent on Lck- or FynT-mediated signals. As c-Cbl can associate with several other signaling molecules, it may couple Zap-70 to downstream effectors during T cell activation. | lld:pubmed |
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pubmed-article:8551236 | pubmed:language | eng | lld:pubmed |
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pubmed-article:8551236 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8551236 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8551236 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8551236 | pubmed:issn | 0022-1007 | lld:pubmed |
pubmed-article:8551236 | pubmed:author | pubmed-author:WeilRR | lld:pubmed |
pubmed-article:8551236 | pubmed:author | pubmed-author:DavidsonDD | lld:pubmed |
pubmed-article:8551236 | pubmed:author | pubmed-author:VeilletteAA | lld:pubmed |
pubmed-article:8551236 | pubmed:author | pubmed-author:FournelMM | lld:pubmed |
pubmed-article:8551236 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8551236 | pubmed:day | 1 | lld:pubmed |
pubmed-article:8551236 | pubmed:volume | 183 | lld:pubmed |
pubmed-article:8551236 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8551236 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8551236 | pubmed:pagination | 301-6 | lld:pubmed |
pubmed-article:8551236 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8551236 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8551236 | pubmed:articleTitle | Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes. | lld:pubmed |
pubmed-article:8551236 | pubmed:affiliation | McGill Cancer Centre, McGill University, Montréal, Canada. | lld:pubmed |
pubmed-article:8551236 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8551236 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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