(Q40880313)

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12-O-tetradecanoylphorbol-13-acetate (TPA)-induced c-Jun N-terminal kinase (JNK) phosphatase renders immortalized or transformed epithelial cells refractory to TPA-inducible JNK activity

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Europe PubMed Central

PubMed publication ID

24 September 2017

12-O-tetradecanoylphorbol-13-acetate (TPA)-induced c-Jun N-terminal kinase (JNK) phosphatase renders immortalized or transformed epithelial cells refractory to TPA-inducible JNK activity (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

author name string

Zhou H

1

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Europe PubMed Central

PubMed publication ID

24 September 2017

Lin A

2

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Europe PubMed Central

PubMed publication ID

24 September 2017

Gu Z

3

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Chen S

4

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Europe PubMed Central

PubMed publication ID

24 September 2017

Park NH

5

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Europe PubMed Central

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24 September 2017

Chiu R

6

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24 September 2017

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publication date

1 July 2000

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24 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

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24 September 2017

275

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Europe PubMed Central

PubMed publication ID

24 September 2017

30

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Europe PubMed Central

PubMed publication ID

24 September 2017

22868-22875

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Parallel signal processing among mammalian MAPKs

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Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine

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Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain

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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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The stress-activated protein kinase subfamily of c-Jun kinases

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The MAP kinase cascade is essential for diverse signal transduction pathways

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Sounding the alarm: protein kinase cascades activated by stress and inflammation

1 reference

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How MAP kinases are regulated

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Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation

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Regulation of transcription by MAP kinase cascades

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Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells

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The stress-activated protein kinase pathway mediates cell death following injury induced by cis-platinum, UV irradiation or heat

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Use of vanadate as protein-phosphotyrosine phosphatase inhibitor

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Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases

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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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MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo

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PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase

1 reference

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Control of MAP kinase activation by the mitogen-induced threonine/tyrosine phosphatase PAC1

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

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Multiple dual specificity protein tyrosine phosphatases are expressed and regulated differentially in liver cell lines

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hVH-5: a protein tyrosine phosphatase abundant in brain that inactivates mitogen-activated protein kinase

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A novel cytoplasmic dual specificity protein tyrosine phosphatase implicated in muscle and neuronal differentiation

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Molecular cloning and functional characterization of a novel mitogen-activated protein kinase phosphatase, MKP-4

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Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5

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The retinoblastoma gene product RB stimulates Sp1-mediated transcription by liberating Sp1 from a negative regulator

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Repression of mitogen-activated protein kinases ERK1/ERK2 activity by a protein tyrosine phosphatase in rat fibroblasts transformed by upstream oncoproteins

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Involvement of p21ras in activation of extracellular signal-regulated kinase 2.

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Evidence for a Ras-dependent extracellular signal-regulated protein kinase (ERK) cascade

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Differential activation of ERK and JNK mitogen-activated protein kinases by Raf-1 and MEKK

1 reference

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All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity

1 reference

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Intestinal trefoil factor induces inactivation of extracellular signal-regulated protein kinase in intestinal epithelial cells

1 reference

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Post-translational modification of human brain type I inositol-1,4,5-trisphosphate 5-phosphatase by farnesylation

1 reference

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Phosphorylation of protein-tyrosine phosphatase PTP-1B on identical sites suggests activation of a common signaling pathway during mitosis and stress response in mammalian cells

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M909273199

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

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