A Long, Weakly Charged Actin-binding Loop Is Required for Phosphorylation-dependent Regulation of Smooth Muscle Myosin
Open Access
- 1 October 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (43), 27939-27944
- https://doi.org/10.1074/jbc.273.43.27939
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Spare the rod, spoil the regulation: Necessity for a myosin rodProceedings of the National Academy of Sciences, 1997
- The motor domain and the regulatory domain of myosin solely dictate enzymatic activity and phosphorylation-dependent regulation, respectivelyProceedings of the National Academy of Sciences, 1997
- Chimeric Substitutions of the Actin-binding Loop Activate Dephosphorylated but Not Phosphorylated Smooth Muscle Heavy MeromyosinPublished by Elsevier ,1995
- Restoration of Phosphorylation-dependent Regulation to the Skeletal Muscle Myosin Regulatory Light ChainJournal of Biological Chemistry, 1995
- Two Heads Are Required for Phosphorylation-dependent Regulation of Smooth Muscle MyosinPublished by Elsevier ,1995
- Charge replacement near the phosphorylatable serine ofthe myosin regulatory light chain mimics aspects ofphosphorylation.Proceedings of the National Academy of Sciences, 1994
- Regulation of cytoplasmic and smooth muscle myosinCurrent Opinion in Cell Biology, 1991
- Filamentous smooth muscle myosin is regulated by phosphorylation.The Journal of cell biology, 1989
- Proteolysis of smooth muscle myosin by Staphylococcus aureus protease: preparation of heavy meromyosin and subfragment 1 with intact 20,000-dalton light chainsBiochemistry, 1985
- Correlation of enzymatic properties and conformation of smooth muscle myosinBiochemistry, 1983