(Q46226598)

English

Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors

scientific article published in January 1996

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

Affinity, specificity, and kinetics of the interaction of the SHC phosphotyrosine binding domain with asparagine-X-X-phosphotyrosine motifs of growth factor receptors (English)

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

author name string

Laminet AA

1

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

Apell G

2

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

Conroy L

3

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

Kavanaugh WM

4

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

language of work or name

0 references

publication date

1 January 1996

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

271

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

1

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

264-269

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

Protein modules and signalling networks

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

An alternative to SH2 domains for binding tyrosine-phosphorylated proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction Domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

A phosphotyrosine interaction domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

SH2 domains recognize specific phosphopeptide sequences

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Oncogenes and signal transduction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Molecular cloning of a GTPase activating protein specific for the Krev-1 protein p21rap1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Complexes of polyoma virus medium T antigen and cellular proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Polyoma middle tumor antigen interacts with SHC protein via the NPTY (Asn-Pro-Thr-Tyr) motif in middle tumor antigen.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.1.264

21 January 2018

Identifiers

10.1074/JBC.271.1.264

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/8550571

ResearchGate publication ID

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