A Novel Ligand for SH3 Domains (Q30039659)

24 May 2017

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H. Hanafusa

1

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24 May 2017

language of work or name

English

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publication date

31 March 1995

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Journal of Biological Chemistry

24 May 2017

published in

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24 May 2017

volume

270

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24 May 2017

issue

13

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24 May 2017

page(s)

7359-7364

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Oncogenes and signal transduction

24 May 2017

cites work

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Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3

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C. elegans cell-signalling gene sem-5 encodes a protein with SH2 and SH3 domains

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A novel transforming protein (SHC) with an SH2 domain is implicated in mitogenic signal transduction

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

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Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras

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Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases

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The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment

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Nuclear localization and regulation of erk- and rsk-encoded protein kinases

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Identification of a ten-amino acid proline-rich SH3 binding site

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An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro

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Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho

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The v-Src SH3 domain binds phosphatidylinositol 3'-kinase

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Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor

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A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.13.7359

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