pubmed-article:7760813 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C1705831 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C1527940 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C1421567 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C0813988 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C1720127 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C1719914 | lld:lifeskim |
pubmed-article:7760813 | lifeskim:mentions | umls-concept:C2828406 | lld:lifeskim |
pubmed-article:7760813 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:7760813 | pubmed:dateCreated | 1995-6-28 | lld:pubmed |
pubmed-article:7760813 | pubmed:abstractText | ZAP-70 is a protein tyrosine kinase thought to play a critical role in T-cell receptor (TCR) signal transduction. During T-cell activation, ZAP-70 binds to a conserved signalling motif known as the immune receptor tyrosine activating motif (ITAM) and becomes tyrosine phosphorylated. To determine whether binding of ZAP-70 to the phosphorylated ITAM was able to activate its kinase activity, we measured the kinase activity of ZAP-70 both when it was bound and when it was unbound to phosphorylated TCR subunits. The ability of ZAP-70 to phosphorylate itself, but not exogenous substrates, was enhanced when it was bound to the tyrosine-phosphorylated TCR zeta and eta chains or to a construct that contained duplicated epsilon ITAMs. No enhanced ZAP-70 autophosphorylation was noted when it was bound to tyrosine-phosphorylated CD3 gamma or epsilon. In addition, autophosphorylation of ZAP-70 when bound to zeta or eta resulted in the generation of multiple distinct ZAP-70 phosphorylated tyrosine residues which had the capacity to bind the SH2 domains of fyn, lck, GAP, and abl. As the effect was noted only when ZAP-70 was bound to TCR subunits containing multiple ITAMs, we propose that one of the roles of the tandem ITAMs is to facilitate the autophosphorylation of ZAP-70. Tyrosine-phosphorylated ZAP-70 then mediates downstream signalling by recruiting SH2 domain-containing signalling proteins. | lld:pubmed |
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pubmed-article:7760813 | pubmed:language | eng | lld:pubmed |
pubmed-article:7760813 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7760813 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7760813 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7760813 | pubmed:month | Jun | lld:pubmed |
pubmed-article:7760813 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:7760813 | pubmed:author | pubmed-author:TerhorstCC | lld:pubmed |
pubmed-article:7760813 | pubmed:author | pubmed-author:HOPFH CHC | lld:pubmed |
pubmed-article:7760813 | pubmed:author | pubmed-author:ZinAA | lld:pubmed |
pubmed-article:7760813 | pubmed:author | pubmed-author:ShawA SAS | lld:pubmed |
pubmed-article:7760813 | pubmed:author | pubmed-author:RichardSS | lld:pubmed |
pubmed-article:7760813 | pubmed:author | pubmed-author:NeumeisterE... | lld:pubmed |
pubmed-article:7760813 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7760813 | pubmed:volume | 15 | lld:pubmed |
pubmed-article:7760813 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7760813 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7760813 | pubmed:pagination | 3171-8 | lld:pubmed |
pubmed-article:7760813 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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