pubmed-article:8096851 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8096851 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
pubmed-article:8096851 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
pubmed-article:8096851 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
pubmed-article:8096851 | pubmed:issue | 8 Pt 1 | lld:pubmed |
pubmed-article:8096851 | pubmed:dateCreated | 1993-5-12 | lld:pubmed |
pubmed-article:8096851 | pubmed:abstractText | The zeta-subunit of the TCR binds GTP and is a well characterized substrate for a TCR-activated tyrosine kinase. To examine the possible coupling of GTP-binding to zeta with TCR-mediated signal transduction, a mutant (termed J32-3.2) of the T cell line Jurkat (J32) was used. Anti-TCR/CD3 stimulation of the TCR/CD3+ J32-3.2 cells resulted in a weak stimulation of both the phosphatidyl inositol and tyrosine kinase signal transduction pathways, as measured by changes in the level of free intracellular calcium, tyrosine phosphorylation of TCR-zeta, CD3-epsilon and ZAP-70, p56lck, or p59fyn tyrosine kinase activity and IL-2 gene activation. The impaired responsiveness of J32-3.2 cells to anti-TCR/CD3 mAb correlated with a low basal level of GTP-binding to zeta. Furthermore, in J32-3.2 cells TCR activation by antibody ligation caused a weaker increase in GTP-binding to the zeta-chain, as compared with that of wild-type J32 cells, which indicates for the first time that GTP-binding to zeta can be modulated by extracellular signals and suggest that the role of GTP-binding to zeta is to couple the TCR to intracellular signal transduction mechanisms. | lld:pubmed |
pubmed-article:8096851 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:language | eng | lld:pubmed |
pubmed-article:8096851 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:citationSubset | AIM | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8096851 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8096851 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8096851 | pubmed:issn | 0022-1767 | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:ReedJ CJC | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:FagardRR | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:FrancoRR | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:TerhorstCC | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:KamounMM | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:WoodsJJ | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:SanchoJJ | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:PeterM EME | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:DanielianSS | lld:pubmed |
pubmed-article:8096851 | pubmed:author | pubmed-author:KangJ SJS | lld:pubmed |
pubmed-article:8096851 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8096851 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8096851 | pubmed:volume | 150 | lld:pubmed |
pubmed-article:8096851 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8096851 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8096851 | pubmed:pagination | 3230-42 | lld:pubmed |
pubmed-article:8096851 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8096851 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8096851 | pubmed:articleTitle | Coupling of GTP-binding to the T cell receptor (TCR) zeta-chain with TCR-mediated signal transduction. | lld:pubmed |
pubmed-article:8096851 | pubmed:affiliation | Division of Immunology, Beth Israel Hospital, Boston, MA 02215. | lld:pubmed |
pubmed-article:8096851 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8096851 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8096851 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8096851 | lld:pubmed |