p38γ Activation Triggers Dynamical Changes in Allosteric Docking Sites-Reference-Cited by-同舟云学术

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p38γ Activation Triggers Dynamical Changes in Allosteric Docking Sites

Published:2011-02-07 Issue:8 Volume:50 Page:1384-1395
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rodriguez Limardo Ramiro G.¹²,Ferreiro Dardo N.¹²,Roitberg Adrián E.³,Marti Marcelo A.¹²,Turjanski Adrian G.¹²

Affiliation:

1. Departamento de Química Inorgánica, Analítica y Química Física/INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales

2. Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales

3. Department of Chemistry, University of Florida, Gainesville, Florida 32611-8435, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi1007518

Reference51 articles.

1. Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation

2. Mitogen-Activated Protein Kinase: Conservation of a Three-Kinase Module From Yeast to Human

3. The structure of phosphorylated P38γ is monomeric and reveals a conserved activation-loop conformation

4. Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3

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1. Stress-Activated Protein Kinases in Intervertebral Disc Degeneration: Unraveling the Impact of JNK and p38 MAPK;Biomolecules;2024-03-25

2. Resistance Evolution against Host-directed Antiviral Agents: Buffalopox Virus Switches to Use p38-ϒ under Long-term Selective Pressure of an Inhibitor Targeting p38-α;Molecular Biology and Evolution;2022-08-17

3. Kinase Activation by Small Conformational Changes;Journal of Chemical Information and Modeling;2019-11-12

4. Cell Signaling and Stress Responses;Cold Spring Harbor Perspectives in Biology;2016-10

5. Structural Analysis of α-Fetoprotein (AFP)-like Peptides with Anti-Breast-Cancer Properties;The Journal of Physical Chemistry B;2014-04-22

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