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Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation

scientific article (publication date: 23 September 1999)

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Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation (English)

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author name string

N Jones

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1

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D J Dumont

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2

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language of work or name

English

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publication date

23 September 1999

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published in

Current Biology

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volume

9

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issue

18

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page(s)

1057-60

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cites work

p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells

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https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980458-8

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7 January 2021

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Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok

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https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980458-8

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7 January 2021

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The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R

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Crossref

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7 January 2021

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FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation

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Molecular cloning and characterization of p56dok-2 defines a new family of RasGAP-binding proteins

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Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck

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https://api.crossref.org/works/10.1016%2FS0960-9822%2899%2980458-8

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7 January 2021

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Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases

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Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein

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SV40-transformed simian cells support the replication of early SV40 mutants

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Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor

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Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain

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Autophosphorylation sites on the epidermal growth factor receptor.

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Molecular cloning of two types of GAP complementary DNA from human placenta

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Tyrosine phosphorylation of p62(Dok) induced by cell adhesion and insulin: possible role in cell migration

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Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal

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10.1016/S0960-9822(99)80458-8

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(Q28145464)

Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation

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