Solubility-determining domain of smooth muscle myosin rod
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(86)81168-1/fullpdf
Reference21 articles.
1. Adenosine Triphosphate-Induced Reversible Change in the Conformation of Chicken Gizzard Myosin and Heavy Meromyosin1
2. A bent monomeric conformation of myosin from smooth muscle.
3. Light-chain phosphorylation controls the conformation of vertebrate non-muscle and smooth muscle myosin molecules
4. Fragments Responsible for the Low Solubility of Light Meromyosin Obtained by Limited Proteolysis1
5. The proteolytic substructure of light meromyosin. Localization of a region responsible for the low ionic strength insolubility of myosin.
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