Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule (Q24324749)

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A Ohtake

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K Sato

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S i Sano

Journal of Biological Chemistry

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language of work or name

English

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publication date

11 October 1996

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published in

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volume

271

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issue

41

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page(s)

25569-74

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cites work

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Cloning, expression and mutational analysis of SH-PTP2, human protein-tyrosine phosphatase

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The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp

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Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation

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Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling.

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Regulation of phosphatidylinositol 3'-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit

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Tyrosine phosphatase CD45 is required for T-cell antigen receptor and CD2-mediated activation of a protein tyrosine kinase and interleukin 2 production

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Renaturation of protein kinase activity of protein blots

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The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early Xenopus development

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Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains

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Membrane immunoglobulin and its accomplices: new lessons from an old receptor

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inferred from DOI database lookup

7 January 2021

based on heuristic

Role of the CD45 tyrosine phosphatase in signal transduction in the immune system.

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