The p56lck SH2 domain mediates recruitment of CD8/p56lck to the activated T cell receptor/CD3/ζ complex
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References (59)
SH2 domains recognize specific phosphopeptide sequences
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Signal transduction by lymphocyte antigen receptors
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The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck
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p56lck interacts via its src homology 2 domain with the ZAP-70 kinase.
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The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav.
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Activated CD8 binding to class I protein mediated by the T-cell receptor results in signalling
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The CD3 chains of the T cell antigen receptor associate with the ZAP-70 tyrosine kinase and are tyrosine phosphorylated after receptor stimulation.
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Helper T-cell development in the absence of CD4-p56 Ick association
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Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex.
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Lymphocyte activation provokes modification of a lymphocyte-specific protein tyrosine kinase (p56lck).
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GRB2 and phospholipase C-gamma 1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation.
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Both high and low avidity antibodies to the T cell receptor can have agonist or antagonist activity
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Cytotoxic T-lymphocyte activation involves a cascade of signalling and adhesion events
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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
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Activation of p56lck by p72syk through physical association and N-terminal tyrosine phosphorylation.
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1992 • 50 citations
Tyrosine kinase activity of CD4-associated p56lck may not be required for CD4-dependent T-cell activation.
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