Implication of the GRB2-associated phosphoprotein SLP-76 in T cell receptor-mediated interleukin 2 production (Q24678315)

2

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J Wu

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L R Hendricks-Taylor

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G A Koretzky

Journal of Experimental Medicine

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language of work or name

English

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publication date

1 April 1996

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published in

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volume

183

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issue

4

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page(s)

1937-43

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cites work

Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells

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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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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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CD45-associated kinase activity requires lck but not T cell receptor expression in the Jurkat T cell line

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SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases

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The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor

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A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells

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T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases

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Signal transmission between the plasma membrane and nucleus of T lymphocytes

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Cell-mediated cytotoxicity: contact and secreted factors

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A functional T-cell receptor signaling pathway is required for p95vav activity

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Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line

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CD3 stimulation causes phosphorylation of phospholipase C-gamma 1 on serine and tyrosine residues in a human T-cell line

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Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-gamma 1.

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CD5 acts as a tyrosine kinase substrate within a receptor complex comprising T-cell receptor zeta chain/CD3 and protein-tyrosine kinases p56lck and p59fyn

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CD5 is phosphorylated on tyrosine after stimulation of the T-cell antigen receptor complex

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In vivo association of Grb2 with pp116, a substrate of the T cell antigen receptor-activated protein tyrosine kinase.

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p21ras and calcineurin synergize to regulate the nuclear factor of activated T cells

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Tyrosine phosphorylation and association with phospholipase C gamma-1 of the GAP-associated 62-kD protein after CD2 stimulation of Jurkat T cell

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Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation

30 May 2018

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p21ras mediates control of IL-2 gene promoter function in T cell activation.

30 May 2018

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Product of vav proto-oncogene defines a new class of tyrosine protein kinase substrates

30 May 2018

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T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-gamma 1

30 May 2018

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12 December 2020

Identification of ezrin as an 81-kDa tyrosine-phosphorylated protein in T cells

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12 December 2020

Multiple components of the T cell antigen receptor complex become tyrosine-phosphorylated upon activation

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12 December 2020

Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation

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12 December 2020

Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor

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12 December 2020