(Q43546855)

English

Inactivation of JNK activity by mitogen-activated protein kinase phosphatase-2 in EAhy926 endothelial cells is dependent upon agonist-specific JNK translocation to the nucleus

scientific article published in January 2001

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scholarly article

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Europe PubMed Central

PubMed publication ID

24 November 2017

Inactivation of JNK activity by mitogen-activated protein kinase phosphatase-2 in EAhy926 endothelial cells is dependent upon agonist-specific JNK translocation to the nucleus (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

author name string

C J Robinson

1

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

C M Sloss

2

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

R Plevin

3

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

publication date

1 January 2001

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

Cellular Signalling

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Europe PubMed Central

PubMed publication ID

24 November 2017

13

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

29-41

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

The regulation of tyrosine kinase signalling pathways by growth factor and G-protein-coupled receptors.

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Stress-activated protein kinases: activation, regulation and function.

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JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain

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Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter

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Transcription factor ATF2 regulation by the JNK signal transduction pathway

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Phosphorylation of c-jun mediated by MAP kinases.

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Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase

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Integration of MAP kinase signal transduction pathways at the serum response element

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Growth factors induce nuclear translocation of MAP kinases (p42mapk and p44mapk) but not of their activator MAP kinase kinase (p45mapkk) in fibroblasts

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Efficacy of agonist-stimulated MEK activation determines the susceptibility of mitogen-activated protein (MAP) kinase to inhibition in rat aortic smooth muscle cells

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Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation

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Treatment of vascular smooth muscle cells with antisense phosphorothioate oligodeoxynucleotides directed against p42 and p44 mitogen-activated protein kinases abolishes DNA synthesis in response to platelet-derived growth factor.

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Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry

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An emerging family of dual specificity MAP kinase phosphatases

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The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation

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A novel mitogen-activated protein kinase phosphatase. Structure, expression, and regulation

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Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase

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Mitogen-activated protein kinase phosphatases inactivate stress-activated protein kinase pathways in vivo

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The dual specificity mitogen-activated protein kinase phosphatase-1 and -2 are induced by the p42/p44MAPK cascade

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Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade

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Permanent cell line expressing human factor VIII-related antigen established by hybridization

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Role of receptor desensitization, phosphatase induction and intracellular cyclic AMP in the termination of mitogen-activated protein kinase activity in UTP-stimulated EAhy 926 endothelial cells

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Regulation of lysophosphatidic acid-stimulated tyrosine phosphorylation of mitogen-activated protein kinase by protein kinase C- and pertussis toxin-dependent pathways in the endothelial cell line EAhy 926.

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Bidirectional regulation of p38 kinase and c-Jun N-terminal protein kinase by insulin-like growth factor-I.

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Three paths to stress relief

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A novel mechanism of JNK1 activation. Nuclear translocation and activation of JNK1 during ischemia and reperfusion

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Induction of c-fos expression through JNK-mediated TCF/Elk-1 phosphorylation.

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Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines.

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Phosphorylation and activation of p42 and p44 mitogen-activated protein kinase are required for the P2 purinoceptor stimulation of endothelial prostacyclin production

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Identifiers

10.1016/S0898-6568(00)00121-2

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 November 2017

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