Basic residues are important for Ca2+/calmodulin binding and activation but not autoinhibition of rabbit skeletal muscle myosin light chain kinase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
1. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
2. [10] Preparation and properties of the calmodulin-binding domain of skeletal muscle myosin light chain kinase
3. Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulin
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1. Interactions of calmodulin with death-associated protein kinase peptides: experimental and modeling studies;Journal of Biomolecular Structure and Dynamics;2012-05
2. Functional Assembly of Fragments from Bisected Smooth Muscle Myosin Light Chain Kinase;Journal of Biological Chemistry;2000-09
3. Regulatory Mechanism of Ca2+/Calmodulin-dependent Protein Kinase Kinase;Journal of Biological Chemistry;2000-06
4. Conformational requirements for Ca2+/calmodulin binding and activation of myosin light chain kinase;FEBS Letters;2000-04-20
5. Regulatory Segments of Ca2+/Calmodulin-dependent Protein Kinases;Journal of Biological Chemistry;1998-04
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