The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution-Reference-Cited by-同舟云学术

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The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution

Published:2010-12 Issue:12 Volume:18 Page:1571-1578
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Akella Radha,Min Xiaoshan,Wu Qiong,Gardner Kevin H.,Goldsmith Elizabeth J.

Funder

National Institutes of Health

Welch Foundation

U.S. Department of Energy

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference54 articles.

1. Intrinsically active variants of all human p38 isoforms;Avitzour;FEBS J.,2007

2. A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission;Bardwell;J. Biol. Chem.,2001

3. Selectivity of docking sites in MAPK kinases;Bardwell;J. Biol. Chem.,2009

4. Analysis of mitogen-activated protein kinase activation and interactions with regulators and substrates;Bardwell;Methods,2006

5. A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs;Bardwell;Trends Biochem. Sci.,1996

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1. Structural basis of a redox-dependent conformational switch that regulates the stress kinase p38α;Nature Communications;2023-12-01

2. Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases;Proceedings of the National Academy of Sciences;2023-11-21

3. Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases;2022-08-24

4. The interaction of p38 with its upstream kinase MKK6;Protein Science;2021-02-16

5. The interaction of p38 with its upstream kinase MKK6;2020-11-27

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