p38γ MAPK contributes to left ventricular remodeling after pathologic stress and disinhibits calpain through phosphorylation of calpastatin
Author:
Affiliation:
1. School of Cardiovascular Medicine and Science, British Heart Foundation (BHF) Centre, King’s College London, London, United Kingdom;
2. University of California–San Francisco, San Francisco, California, USA
Publisher
Wiley
Subject
Genetics,Molecular Biology,Biochemistry,Biotechnology
Reference33 articles.
1. New Therapeutic Targets in Cardiology
2. Novel Homologues of CSBP/p38 MAP Kinase: Activation, Substrate Specificity and Sensitivity to Inhibition by Pyridinyl Imidazoles
3. Effect of pressure overload-induced hypertrophy on the expression and localization of p38 MAP kinase isoforms in the mouse heart
4. Cardiac Expression and Subcellular Localization of the p38 Mitogen-activated Protein Kinase Member, Stress-activated Protein Kinase-3 (SAPK3)
5. Stress-activated Protein Kinase-3 Interacts with the PDZ Domain of α1-Syntrophin
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3. Fam20c regulates the calpain proteolysis system through phosphorylating Calpasatatin to maintain cell homeostasis;Journal of Translational Medicine;2023-06-27
4. p38γ MAPK Inflammatory and Metabolic Signaling in Physiology and Disease;Cells;2023-06-21
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