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Volumn 8, Issue 3, 1996, Pages 394-401

Regulation of antigen receptor signal transduction by protein tyrosine kinases

Author keywords

[No Author keywords available]

Indexed keywords

LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0030175744     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(96)80130-0     Document Type: Article
Times cited : (170)

References (61)
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    • of outstanding interest. This paper and [22] analyze AgR signaling by altered-peptide ligands that lead to anergy of T cells. The authors demonstrate the provocative finding that anergic stimuli lead to altered phosphorylation TCR ζ chain. No tyrosine phosphorylation or activation of ZAP-70 is detected even though it is recruited to the TCR.
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    • of special interest. In this study, the authors propose that a major substrate of ZAP-70 is itself, and that its recruitment to the TCR complex functions to facilitate its autophosphorylation on tyrosine residues resulting in the generation of a scaffold for the recruitment of SH2 domains. Peptide mapping demonstrated that autophosphorylation generates a large variety of sites that can bind SH2-containing signaling proteins.
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    • Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function
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    • Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70
    • of outstanding interest. of outstanding interest. This paper and [31] demonstrate that catalytic activation of ZAP-70 is mediated by the phosphorylation of Tyr493 within the trans-activation loop of ZAP-70's catalytic domain. In addition, [31] provides evidence that phosphorylation of this tyrosine residue is required for AgR function.
    • of outstanding interest Wange RL, Guitian R, Isakov N, Watts JD, Aebersold R, Samelson LE. Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70. of outstanding interest J Biol Chem. 270:1995;18730-18733 This paper and [31] demonstrate that catalytic activation of ZAP-70 is mediated by the phosphorylation of Tyr493 within the trans-activation loop of ZAP-70's catalytic domain. In addition, [31] provides evidence that phosphorylation of this tyrosine residue is required for AgR function.
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    • of special interest. of special interest. Together with [31], the authors identify the sites of tyrosine phosphorylation within ZAP-70.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.