Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors (Q24322730)

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B Margolis

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C H Heldin

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L Claesson-Welsh

Journal of Biological Chemistry

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language of work or name

English

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publication date

29 November 1996

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published in

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volume

271

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issue

48

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page(s)

30942-9

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cites work

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Signal transduction by receptors with tyrosine kinase activity

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Protein modules and signalling networks

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Structural determinants in the platelet-derived growth factor alpha-receptor implicated in modulation of chemotaxis.

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Demonstration of functionally different interactions between phospholipase C-gamma and the two types of platelet-derived growth factor receptors

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Tyrosine mutations within the alpha platelet-derived growth factor receptor kinase insert domain abrogate receptor-associated phosphatidylinositol-3 kinase activity without affecting mitogenic or chemotactic signal transduction

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High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains

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Tyr-716 in the platelet-derived growth factor beta-receptor kinase insert is involved in GRB2 binding and Ras activation

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SH2 domains recognize specific phosphopeptide sequences

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SH2 domain specificity and activity modified by a single residue

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The GRB family of SH2 domain proteins

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PDGF alpha- and beta-receptors activate unique and common signal transduction pathways

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7 January 2021

Platelet-derived growth factor: mechanism of action and possible in vivo function

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Identification of a cell retention signal in the B-chain of platelet-derived growth factor and in the long splice version of the A-chain

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Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav

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7 January 2021