(Q24309341)

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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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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 (English)

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author name string

Y Chu

1

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P A Solski

2

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R Khosravi-Far

3

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C J Der

4

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K Kelly

5

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publication date

15 March 1996

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Journal of Biological Chemistry

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271

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11

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6497-501

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Chromosomal localization of four human VH1-like protein-tyrosine phosphatases

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Genomic Organization and Chromosomal Localization of the DUSP2 Gene, Encoding a MAP Kinase Phosphatase, to Human 2p11.2-q11

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The sevenmaker gain-of-function mutation in p42 MAP kinase leads to enhanced signalling and reduced sensitivity to dual specificity phosphatase action

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The structure of an antigenic determinant in a protein

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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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JNK is involved in signal integration during costimulation of T lymphocytes.

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

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Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase

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

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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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Role of mitogen-activated protein kinase phosphatase during the cellular response to genotoxic stress. Inhibition of c-Jun N-terminal kinase activity and AP-1-dependent gene activation

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

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The MAPK signaling cascade

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