(Q24295007)

GOA release 2020-03-11

author name string

Qiang Zhang

1

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Michaela Muller

2

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Can Hao Chen

3

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Lei Zeng

4

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Amjad Farooq

5

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Ming-Ming Zhou

Journal of Molecular Biology

6

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language of work or name

English

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publication date

9 December 2005

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published in

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volume

354

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issue

4

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page(s)

777-88

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cites work

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Signal transduction through MAP kinase cascades

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Mitogen-activated protein kinase pathways

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Signal transduction. Switching off MAP kinases

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Solution structure of the MAPK phosphatase PAC-1 catalytic domain. Insights into substrate-induced enzymatic activation of MKP

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Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain

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Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase

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A conserved docking motif in MAP kinases common to substrates, activators and regulators

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

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PAC1 phosphatase is a transcription target of p53 in signalling apoptosis and growth suppression

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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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How MAP kinases are regulated

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

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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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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase

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