A folded (10 S) conformer of myosin from a striated muscle and its implications for regulation of ATPase activity
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference52 articles.
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2. Temperature Dependence of the Release of ATP Hydrolysis Products from the 10 S Conformation of Smooth Muscle Myosin;Applegate;J. Muscle Res. Cell Motil,1989
3. Characterization of Homologous Divalent Metal Ion Binding Sites of Vertebrate and Molluscan Myosins using Electron Paramagnetic Resonance Spectroscopy;Bagshaw;J. Mol. Biol,1979
4. 8-Anilino-1-Naphthalenesulphonate, a Fluorescent Probe for the Regulatory Light Chain Binding Site of Scallop Myosin;Bennett;J. Muscle Res. Cell Motil,1984
5. UV-Photometric Determination of Total Cerebrospinal Fluid Proteins with a Modified Biuret Reagent;Bürgi;Clin. Chim. Acta,1967
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1. Review on the structural understanding of the 10S myosin II in the era of Cryo-electron microscopy;Applied Microscopy;2022-10-11
2. Structural basis of the super- and hyper-relaxed states of myosin II;Journal of General Physiology;2021-12-10
3. Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro;Proceedings of the National Academy of Sciences;2020-06-22
4. The central role of the tail in switching off 10S myosin II activity;Journal of General Physiology;2019-08-06
5. The Central Role of the Tail in Switching Off Myosin II in Cells;2019-04-11
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