The tyrosine kinase activity of p56lck is increased in human T cells activated via CD2.
An early biochemical event associated with T cell activation is tyrosine phosphorylation. We have previously shown that p56lck, a lymphocyte-specific protein tyrosine kinase, is hyperphosphorylated on serine and tyrosine residues 15 minutes after activation via CD2 with a concomitant shift to a high...
المؤلفون الرئيسيون: | Danielian, S, Fagard, R, Alcover, A, Acuto, O, Fischer, S |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1991
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مواد مشابهة
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The lymphocyte-specific protein tyrosine kinase p56lck is hyperphosphorylated on serine and tyrosine residues within minutes after activation via T cell receptor or CD2.
حسب: Danielian, S, وآخرون
منشور في: (1989) -
Both T cell receptor (TcR)-CD3 complex and CD2 increase the tyrosine kinase activity of p56lck. CD2 can mediate TcR-CD3-independent and CD45-dependent activation of p56lck.
حسب: Danielian, S, وآخرون
منشور في: (1992) -
INTERACTION OF HUMAN P56LCK SH2 DOMAIN WITH THE ZAP-70 TYROSINE KINASE
حسب: Acuto, O, وآخرون
منشور في: (1994) -
The p56lck SH2 domain mediates recruitment of CD8/p56lck to the activated T cell receptor/CD3/zeta complex.
حسب: Thome, M, وآخرون
منشور في: (1996) -
INTERACTION OF SYK AND ZAP-70 WITH P56LCK/CD4
حسب: Acuto, O, وآخرون
منشور في: (1995)