Both Phosphorylation and Caspase-mediated Cleavage Contribute to Regulation of the Ste20-like Protein Kinase Mst1 during CD95/Fas-induced Apoptosis
Open Access
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (18) , 14909-14915
- https://doi.org/10.1074/jbc.m010905200
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Interactions between protein kinases and proteases in cellular signaling and regulationAdvances in Enzyme Regulation, 2000
- Serine/Threonine Protein Kinases and ApoptosisExperimental Cell Research, 2000
- Lymphocyte Survival—The Struggle Against DeathAnnual Review of Cell and Developmental Biology, 1999
- Mammalian Caspases: Structure, Activation, Substrates, and Functions During ApoptosisAnnual Review of Biochemistry, 1999
- THE CENTRAL EFFECTORS OF CELL DEATH IN THE IMMUNE SYSTEMAnnual Review of Immunology, 1999
- MATURE T LYMPHOCYTE APOPTOSIS—Immune Regulation in a Dynamic and Unpredictable Antigenic EnvironmentAnnual Review of Immunology, 1999
- Caspases: Enemies WithinScience, 1998
- Programmed Cell Death in Animal DevelopmentCell, 1997
- Cloning and characterization of a member of the MST subfamily of Ste20-like kinasesGene, 1995
- Cloning and Characterization of a Human Protein Kinase with Homology to Ste20Journal of Biological Chemistry, 1995