Activation of Rabbit Skeletal Muscle Myosin Light Chain Kinase by Calmodulin- A Mechanistic Overview
- 1 January 1989
- book chapter
- Published by Springer Nature
- Vol. 255, 155-164
- https://doi.org/10.1007/978-1-4684-5679-0_17
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Stimulation of the erythrocyte Ca2+‐ATPase and of bovine brain cyclic nucleotide phosphodiesterases by chemically modified calmodulinEuropean Journal of Biochemistry, 1987
- Domain organization of chicken gizzard myosin light chain kinase deduced from a cloned cDNABiochemistry, 1986
- Activation of the multifunctional Ca2+/calmodulin-dependent protein kinase by autophosphorylation: ATP modulates production of an autonomous enzyme.Proceedings of the National Academy of Sciences, 1986
- Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formationBiochemistry, 1985
- Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase.Proceedings of the National Academy of Sciences, 1985
- The Function of Myosin and Myosin Light Chain Kinase Phosphorylation in Smooth MuscleAnnual Review of Pharmacology and Toxicology, 1985
- Phosphorylation of skeletal muscle myosin light chain kinase by the catalytic subunit of cAMP‐dependent protein kinaseFEBS Letters, 1982
- Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.Proceedings of the National Academy of Sciences, 1979
- Modulator protein as a component of the myosin light chain kinase from chicken gizzardBiochemistry, 1978
- Isolation and properties of platelet myosin light chain kinaseBiochemistry, 1976