The Pro-apoptotic Function of Death-associated Protein Kinase Is Controlled by a Unique Inhibitory Autophosphorylation-based Mechanism
Open Access
- 1 December 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (50), 47460-47467
- https://doi.org/10.1074/jbc.m105133200
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- Autophosphorylation at Thr 286 of the α Calcium-Calmodulin Kinase II in LTP and LearningScience, 1998
- Gapped BLAST and PSI-BLAST: a new generation of protein database search programsNucleic Acids Research, 1997
- Activation of Chicken Gizzard Myosin Light Chain Kinase by Ca2+/Calmodulin is Inhibited by Autophosphorylation.Cell Structure and Function, 1996
- Phosphorylation and Activation of Ca2+-Calmodulin-dependent Protein Kinase IV by Ca2+-Calmodulin-dependent Protein Kinase Ia KinaseJournal of Biological Chemistry, 1995
- Autophosphorylation of Smooth Muscle Myosin Light Chain Kinase at Its Regulatory DomainBiochemistry, 1995
- Structural Basis of the Intrasteric Regulation of Myosin Light Chain KinasesScience, 1992
- Target Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide ComplexScience, 1992
- Assessment of protein models with three-dimensional profilesNature, 1992
- Intrasteric regulation of protein kinases and phosphatasesBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1991
- Sequences of autophosphorylation sites in neuronal type II CaM kinase that control Ca2+-independent activityNeuron, 1988