Identification of a specific domain responsible for JNK2alpha2 autophosphorylation. - Wikidata - wikimedia - TriplyDB

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

http://www.wikidata.org/entity/Q40473949

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The role of the c-Jun N-terminal kinase 2-α-isoform in non-small cell lung carcinoma tumorigenesis JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships Measuring the constitutive activation of c-Jun N-terminal kinase isoforms The p38β mitogen-activated protein kinase possesses an intrinsic autophosphorylation activity, generated by a short region composed of the α-G helix and MAPK insert.Sequential protein kinase C (PKC)-dependent and PKC-independent protein kinase D catalytic activation via Gq-coupled receptors: differential regulation of activation loop Ser(744) and Ser(748) phosphorylation Tighter αC-helix-αL16-helix interactions seem to make p38α less prone to activation by autophosphorylation than Hog1.Proliferation of human HCC cells and chemically induced mouse liver cancers requires JNK1-dependent p21 downregulation.Constitutive activity of JNK2 alpha2 is dependent on a unique mechanism of MAPK activation.The complexity of signaling in host-pathogen interactions revealed by the Toxoplasma gondii-dependent modulation of JNK phosphorylation.JNK Signaling in the Control of the Tumor-Initiating Capacity Associated with Cancer Stem Cells.Poly(ADP-ribose) polymerase family member 14 (PARP14) is a novel effector of the JNK2-dependent pro-survival signal in multiple myeloma.JNKs function as CDK4-activating kinases by phosphorylating CDK4 and p21.Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts.GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.

P2860

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P2860

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

http://www.wikidata.org/entity/Q40473949

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

@en

type

label

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

@en

prefLabel

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

@en

P1433

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P2860

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P1433

Journal of Biological Chemistry

P1476

Identification of a specific domain responsible for JNK2alpha2 autophosphorylation.

@en

P2093

Albert J Wong

http://www.w3.org/2001/XMLSchema#string

Hiromasa Tsuiki

http://www.w3.org/2001/XMLSchema#string

Jian Cui

http://www.w3.org/2001/XMLSchema#string

Marina Holgado-Madruga

http://www.w3.org/2001/XMLSchema#string

Philip Wedegaertner

http://www.w3.org/2001/XMLSchema#string

Wanwen Su

http://www.w3.org/2001/XMLSchema#string

P2860

The JIP group of mitogen-activated protein kinase scaffold proteins

MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein

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

Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3

Crystal structure of JNK3: a kinase implicated in neuronal apoptosis

Signal transduction by the JNK group of MAP kinases

JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation

Signal transduction by the c-Jun N-terminal kinase (JNK)--from inflammation to development

A mammalian scaffold complex that selectively mediates MAP kinase activation

A cytoplasmic inhibitor of the JNK signal transduction pathway

P304

9913-9920

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P31

scholarly article

P356

10.1074/JBC.M412165200

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P407

P433

11

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P478

280

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2005-01-06T00:00:00Z

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P698

15637069

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