(Q36686508)

English

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

scientific article published on June 1993

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scholarly article

1 reference

Europe PubMed Central

15 August 2017

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

1 reference

Europe PubMed Central

15 August 2017

0 references

phosphorylation

0 references

author name string

Panayotou G

1

1 reference

Europe PubMed Central

15 August 2017

Gish G

2

1 reference

Europe PubMed Central

15 August 2017

End P

3

1 reference

Europe PubMed Central

15 August 2017

Truong O

4

1 reference

Europe PubMed Central

15 August 2017

Gout I

5

1 reference

Europe PubMed Central

15 August 2017

Dhand R

6

1 reference

Europe PubMed Central

15 August 2017

Fry MJ

7

1 reference

Europe PubMed Central

15 August 2017

Hiles I

8

1 reference

Europe PubMed Central

15 August 2017

Pawson T

9

1 reference

Europe PubMed Central

15 August 2017

Waterfield MD

10

1 reference

Europe PubMed Central

15 August 2017

language of work or name

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publication date

1 June 1993

1 reference

Europe PubMed Central

15 August 2017

Molecular and Cellular Biology

1 reference

Europe PubMed Central

15 August 2017

13

1 reference

Europe PubMed Central

15 August 2017

3567-3576

1 reference

Europe PubMed Central

15 August 2017

6

1 reference

Europe PubMed Central

15 August 2017

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

1 reference

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Direct analysis of the binding of the abl Src homology 2 domain to the activated epidermal growth factor receptor.

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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Platelet-derived growth factor (PDGF) binding promotes physical association of PDGF receptor with phospholipase C

1 reference

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Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteins

1 reference

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PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells

1 reference

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Role of phosphatidylinositol kinase in PDGF receptor signal transduction

1 reference

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

1 reference

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Interactions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptor

1 reference

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Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase

1 reference

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Activated type I phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulation

1 reference

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Signal transduction by receptors with tyrosine kinase activity

1 reference

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Binding of GAP to activated PDGF receptors

1 reference

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Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases

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cDNA cloning of a Novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor

1 reference

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Oncogenes and signal transduction

1 reference

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

1 reference

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Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase

1 reference

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30 September 2017

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

1 reference

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

1 reference

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30 September 2017

Platelet-derived growth factor (PDGF)-dependent association of phospholipase C-gamma with the PDGF receptor signaling complex

1 reference

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30 September 2017

Phosphoinositide 3-kinase: A new effector in signal transduction?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=359826

30 September 2017

A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=359826

30 September 2017

Identification of two C-terminal autophosphorylation sites in the PDGF beta-receptor: involvement in the interaction with phospholipase C-gamma

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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SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors

1 reference

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Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors

1 reference

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

1 reference

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Expression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85 beta protein by using the baculovirus expression system

1 reference

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Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes

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Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit

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Modification of the 85-kilodalton subunit of phosphatidylinositol-3 kinase in platelet-derived growth factor-stimulated cells

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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

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The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor

1 reference

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The colony stimulating factor-1 receptor associates with and activates phosphatidylinositol-3 kinase

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Direct activation of the serine/threonine kinase activity of Raf-1 through tyrosine phosphorylation by the PDGF beta-receptor

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PDGF beta-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex

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Dot-blot hybridization: quantitative analysis with direct beta counting

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

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Quantitative analysis of SH2 domain binding. Evidence for specificity and competition

1 reference

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Regulated coupling of the Neu receptor to phosphatidylinositol 3'-kinase and its release by oncogenic activation.

1 reference

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1 reference

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based on heuristic

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Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system

1 reference

https://pubmed.ncbi.nlm.nih.gov/8388538

12 December 2020

based on heuristic

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Identifiers

10.1128/MCB.13.6.3567

1 reference

Europe PubMed Central

15 August 2017

1 reference

Europe PubMed Central

15 August 2017

1 reference

Europe PubMed Central

15 August 2017

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