(Q40947634)

English

Intensification of growth factor receptor signalling by phorbol treatment of ligand-primed cells implies a dimer-stabilizing effect of protein kinase C-dependent juxtamembrane domain phosphorylation

scientific article published on April 1999

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scholarly article

1 reference

Europe PubMed Central

25 September 2017

Intensification of growth factor receptor signalling by phorbol treatment of ligand-primed cells implies a dimer-stabilizing effect of protein kinase C-dependent juxtamembrane domain phosphorylation (English)

1 reference

Europe PubMed Central

25 September 2017

phosphorylation

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based on heuristic

inferred from title

author name string

Gulliford T

1

1 reference

Europe PubMed Central

25 September 2017

Ouyang X

2

1 reference

Europe PubMed Central

25 September 2017

Epstein RJ

3

1 reference

Europe PubMed Central

25 September 2017

publication date

1 April 1999

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Europe PubMed Central

25 September 2017

number of pages

8

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inferred from page(s)

Cellular Signalling

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Europe PubMed Central

25 September 2017

11

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Europe PubMed Central

25 September 2017

245-252

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Europe PubMed Central

25 September 2017

4

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Europe PubMed Central

25 September 2017

The epidermal growth factor receptor as a multifunctional allosteric protein

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Beta-adrenergic receptor kinase-2 and beta-arrestin-2 as mediators of odorant-induced desensitization.

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Signal transduction by the epidermal growth factor receptor after functional desensitization of the receptor tyrosine protein kinase activity

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Desensitization of the EGF receptor alters its ability to undergo EGF-induced dimerization

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Inactivation of c-Yes tyrosine kinase by elevation of intracellular calcium levels

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Activation of protein kinase C alpha inhibits signaling by members of the insulin receptor family

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Rapid and long-term effects on protein kinase C on receptor tyrosine kinase phosphorylation and degradation

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Phorbol ester-induced expression, phosphorylation, and translocation of protein-tyrosine-phosphatase 1C in HL-60 cells

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Inhibition of epidermal growth factor-dependent protein tyrosine phosphorylation by phorbol myristate acetate is mediated by protein tyrosine phosphatase activity

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Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms

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Calcium-inducible transmodulation of receptor tyrosine kinase activity

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Synthetic phosphopeptide immunogens yield activation-specific antibodies to the c-erbB-2 receptor

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Human cancer cells exhibit protein kinase C-dependent c-erbB-2 transmodulation that correlates with phosphatase sensitivity and kinase activity

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Reduced ability of transforming growth factor-alpha to induce EGF receptor heterodimerization and downregulation suggests a mechanism of oncogenic synergy with ErbB2

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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A point mutation in the neu oncogene mimics ligand induction of receptor aggregation

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Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: a mechanism of interreceptor kinase activation and transphosphorylation

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Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors

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Modulation of Epidermal Growth Factor Receptors on 3T3 Cells by Platelet-Derived Growth Factor

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Effects of Epidermal Growth Factor and 12-O-Tetradecanoylphorbol-13-Acetate on Metabolism of the Epidermal Growth Factor Receptor in Normal Human Fibroblasts

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Release of a phorbol ester-induced mitogenic block by mutation at Thr-654 of the epidermal growth factor receptor

1 reference

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7 January 2021

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Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654

1 reference

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Epidermal growth factor (EGF) promotes phosphorylation at threonine-654 of the EGF receptor: possible role of protein kinase C in homologous regulation of the EGF receptor

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Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene

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Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor.

1 reference

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Identification of serines-967/968 in the juxtamembrane region of the insulin receptor as insulin-stimulated phosphorylation sites

1 reference

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Protein kinase C--a question of specificity

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Two closely related isoforms of protein kinase C produce reciprocal effects on the growth of rat fibroblasts. Possible molecular mechanisms.

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Protein kinase C (PKC)-induced PKC down-regulation. Association with up-regulation of vesicle traffic

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Reduction of epidermal growth factor receptor affinity by heterologous ligands: Evidence for a mechanism involving the breakdown of phosphoinositides and the activation of protein kinase C

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Generation and use of antibodies to phosphothreonine

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Site-specific anti-phosphopeptide antibodies: use in assessing insulin receptor serine/threonine phosphorylation state and identification of serine-1327 as a novel site of phorbol ester-induced phosphorylation

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[23] Production of phosphorylation state-specific antibodies

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Anti-phosphoserine and anti-phosphothreonine antibodies modulate autophosphorylation of the insulin receptor but not EGF receptor

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Phorbol esters induce death in MCF-7 breast cancer cells with altered expression of protein kinase C isoforms. Role for p53-independent induction of gadd-45 in initiating death.

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Identifiers

10.1016/S0898-6568(98)00058-8

1 reference

Europe PubMed Central

25 September 2017

1 reference

Europe PubMed Central

25 September 2017

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