Recognition and specificity in protein tyrosine kinase-mediated signalling (Q30192978)

10 June 2017

title

Recognition and specificity in protein tyrosine kinase-mediated signalling (English)

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10 June 2017

Z Songyang

1

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10 June 2017

L C Cantley

series ordinal

2

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10 June 2017

publication date

1 November 1995

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10 June 2017

number of pages

6

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Trends in Biochemical Sciences

inferred from page(s)

published in

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10 June 2017

volume

20

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10 June 2017

issue

11

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10 June 2017

page(s)

470-475

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publication type of scholarly work

10 June 2017

review article

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cites work

Protein-tyrosine kinases

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Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling

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Modular binding domains in signal transduction proteins

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Protein modules and signalling networks

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Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors

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SH2 domains recognize specific phosphopeptide sequences

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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck

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Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

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Crystal structures of peptide complexes of the amino-terminal SH2 domain of the Syp tyrosine phosphatase

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Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide

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An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

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

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A phosphotyrosine interaction domain

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Phosphotyrosine-dependent interaction of SHC and insulin receptor substrate 1 with the NPEY motif of the insulin receptor via a novel non-SH2 domain

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A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptides

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The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif

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Use of an oriented peptide library to determine the optimal substrates of protein kinases

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

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DNA synthesis induced by some but not all growth factors requires Src family protein tyrosine kinases.

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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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Point mutation within the tyrosine kinase domain of the RET proto-oncogene in multiple endocrine neoplasia type 2B and related sporadic tumours

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Activation of RET as a dominant transforming gene by germline mutations of MEN2A and MEN2B

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Functional specificity of cytoplasmic and transmembrane tyrosine kinases: identification of 130- and 75-kilodalton substrates of c-fps/fes tyrosine kinase in macrophages

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ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain

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T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases

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Acidic residues are involved in substrate recognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1

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Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates

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Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate

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Crystal structure of human protein tyrosine phosphatase 1B

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The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase

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Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

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7 January 2021

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Identifiers

DOI

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10 June 2017

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