(Q30175265)

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The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes

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Europe PubMed Central

PubMed publication ID

9 June 2017

The SH3 and SH2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes (English)

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

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Summy JM

1

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Guappone AC

2

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Europe PubMed Central

PubMed publication ID

9 June 2017

Sudol M

3

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Europe PubMed Central

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9 June 2017

Flynn DC

4

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Europe PubMed Central

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9 June 2017

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1 January 2000

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Europe PubMed Central

PubMed publication ID

9 June 2017

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Europe PubMed Central

PubMed publication ID

9 June 2017

19

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Europe PubMed Central

PubMed publication ID

9 June 2017

1

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Europe PubMed Central

PubMed publication ID

9 June 2017

155-160

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Elevated c-Src tyrosine kinase activity in premalignant epithelia of ulcerative colitis

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pp60c-src activation in human colon carcinoma

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Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor

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The Src SH3 domain is required for DNA synthesis induced by platelet-derived growth factor and epidermal growth factor

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The integrity of the SH3 binding motif of AFAP-110 is required to facilitate tyrosine phosphorylation by, and stable complex formation with, Src

1 reference

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Formation of a stable src-AFAP-110 complex through either an amino-terminal or a carboxy-terminal SH2-binding motif

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Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases

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Signalling by the p60c-src family of protein-tyrosine kinases

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Modular peptide recognition domains in eukaryotic signaling

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Avian sarcoma virus Y73 genome sequence and structural similarity of its transforming gene product to that of Rous sarcoma virus

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Association between the PDGF receptor and members of the src family of tyrosine kinases

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The SRC family protein tyrosine kinase p62yes controls polymeric IgA transcytosis in vivo

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Stimulation of the protein tyrosine kinase c-Yes but not c-Src by neurotrophins in human brain-metastatic melanoma cells

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SH2 domain specificity and activity modified by a single residue

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Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase

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Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinase

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Src activity increases and Yes activity decreases during mitosis of human colon carcinoma cells

1 reference

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Elevated c-yes tyrosine kinase activity in premalignant lesions of the colon

1 reference

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Identification of Src, Fyn, Lyn, PI3K and Abl SH3 domain ligands using phage display libraries.

1 reference

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Phage display selection of ligand residues important for Src homology 3 domain binding specificity

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Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division

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Common in vitro substrate specificity and differential Src homology 2 domain accessibility displayed by two members of the Src family of protein-tyrosine kinases, c-Src and Hck.

1 reference

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Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

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Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice

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Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2.

1 reference

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Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice.

1 reference

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Cellular proteins homologous to the viral yes gene product

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From Src Homology domains to other signaling modules: proposal of the 'protein recognition code'.

1 reference

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Cellular functions regulated by Src family kinases

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Angiotensin II induces diverse signal transduction pathways via both Gq and Gi proteins in liver epithelial cells

1 reference

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Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains

1 reference

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Structure-function analysis of SH3 domains: SH3 binding specificity altered by single amino acid substitutions

1 reference

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Inactivation of c-Yes tyrosine kinase by elevation of intracellular calcium levels

1 reference

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Recognition and specificity in protein tyrosine kinase-mediated signalling

1 reference

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inferred from DOI database lookup

Identifiers

10.1038/SJ.ONC.1203265

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

Dimensions Publication ID

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

9 June 2017

ResearchGate publication ID

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