(Q36325295)

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Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance

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scholarly article

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Europe PubMed Central

PMC publication ID

13 August 2017

Kinetics of p56lck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance (English)

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

phosphorylation

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surface plasmon resonance

1 reference

based on heuristic

inferred from title

author name string

Payne G

1

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Shoelson SE

2

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Gish GD

3

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Pawson T

4

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Walsh CT

5

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

publication date

1 June 1993

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Europe PubMed Central

PMC publication ID

13 August 2017

language of work or name

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Proceedings of the National Academy of Sciences of the United States of America

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

90

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

11

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

4902-4906

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation

1 reference

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30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

30 September 2017

SH2 domains recognize specific phosphopeptide sequences

1 reference

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30 September 2017

A photoaffinity scan maps regions of the p85 SH2 domain involved in phosphoprotein binding

1 reference

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30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

30 September 2017

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

1 reference

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Biospecific interaction analysis using biosensor technology

1 reference

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Neoplastic transformation induced by an activated lymphocyte-specific protein tyrosine kinase (pp56lck)

1 reference

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Alterations of the lymphocyte-specific protein tyrosine kinase (p56lck) during T-cell activation

1 reference

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Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction

1 reference

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

1 reference

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A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps

1 reference

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Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus.

1 reference

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A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants

1 reference

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A function for the lck proto-oncogene

1 reference

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Tyr527 is phosphorylated in pp60c-src: implications for regulation

1 reference

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30 September 2017

Src homology region 2 domains direct protein-protein interactions in signal transduction

1 reference

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Purification and characterization of phosphoinositide 3-kinase from rat liver

1 reference

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Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain

1 reference

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

1 reference

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Oncogenes and signal transduction

1 reference

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Isolation of a src homology 2-containing tyrosine phosphatase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

30 September 2017

Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

30 September 2017

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

1 reference

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

1 reference

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Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein

1 reference

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

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Regulation of the enzymatic function of the lymphocyte-specific tyrosine protein kinase p56lck by the non-catalytic SH2 and SH3 domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

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Ras GTPase-activating protein: a substrate and a potential binding protein of the protein-tyrosine kinase p56lck

1 reference

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Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=46621

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SH2 domains prevent tyrosine dephosphorylation of the EGF receptor: identification of Tyr992 as the high-affinity binding site for SH2 domains of phospholipase C gamma

1 reference

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SH2 and SH3 domains: from structure to function

1 reference

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Phosphatidylinositol 3'-kinase is activated by association with IRS-1 during insulin stimulation

1 reference

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Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro

1 reference

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

1 reference

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IRS-1 activates phosphatidylinositol 3'-kinase by associating with src homology 2 domains of p85

1 reference

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Presence of SH2 domains of phospholipase C gamma 1 enhances substrate phosphorylation by increasing the affinity toward the epidermal growth factor receptor

1 reference

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1 reference

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Tyr721 regulates specific binding of the CSF-1 receptor kinase insert to PI 3′-kinase SH2 domains: a model for SH2-mediated receptor-target interactions

1 reference

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YMXM motifs of IRS-1 define substrate specificity of the insulin receptor kinase

1 reference

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1 reference

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Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src

1 reference

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Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinase

1 reference

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PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254.

1 reference

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Simultaneous analysis of families of sigmoidal curves: application to bioassay, radioligand assay, and physiological dose-response curves

1 reference

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Interactions in the fourth dimension

1 reference

https://pubmed.ncbi.nlm.nih.gov/7685110

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/7685110

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.90.11.4902

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

1993PNAS...90.4902P

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

ResearchGate publication ID

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