SH2 domain specificity and activity modified by a single residue (Q34057752)

30 July 2017

SH2 domain specificity and activity modified by a single residue (English)

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30 July 2017

7

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30 July 2017

Marengere LE

1

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30 July 2017

Songyang Z

2

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30 July 2017

Gish GD

3

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30 July 2017

Schaller MD

4

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30 July 2017

Parsons JT

5

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30 July 2017

Stern MJ

6

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30 July 2017

Pawson T

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30 July 2017

language of work or name

English

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publication date

1 June 1994

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30 July 2017

4

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inferred from page(s)

published in

Nature

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30 July 2017

369

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30 July 2017

502-505

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30 July 2017

6480

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https://scigraph.springernature.com/pub.10.1038/369502a0

30 July 2017

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cites work

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

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7 January 2021

Oncogenes and signal transduction

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7 January 2021

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7 January 2021

SH2 domains recognize specific phosphopeptide sequences

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7 January 2021

Binding of Transforming Protein, P47 gag-crk , to a Broad Range of Phosphotyrosine-containing Proteins

1 reference

7 January 2021

Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways

1 reference

7 January 2021

SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins

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7 January 2021

The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity

1 reference

7 January 2021

Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

1 reference

7 January 2021

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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7 January 2021

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

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7 January 2021

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

1 reference

7 January 2021

A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos.

1 reference

7 January 2021

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

1 reference

7 January 2021

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling

1 reference

7 January 2021

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

1 reference

7 January 2021

The human GRB2 and Drosophila Drk genes can functionally replace the Caenorhabditis elegans cell signaling gene sem-5.

1 reference

7 January 2021

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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7 January 2021

The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

1 reference

7 January 2021

Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling

1 reference

7 January 2021

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

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7 January 2021

Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway

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7 January 2021

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions

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7 January 2021

Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin

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7 January 2021

Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK.

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7 January 2021

Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

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7 January 2021

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

1 reference

7 January 2021

SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange

1 reference

7 January 2021

Identifiers

DOI

10.1038/369502A0

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Dimensions Publication ID

30 July 2017

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