Sulfhydryl groups of natural actomyosin essential for the Ca2−-sensitive response: location and properties
Author:
Publisher
Elsevier BV
Subject
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Reference44 articles.
1. Inhibition of myosin B-adenosinetriphosphatase by excess substrate
2. Interactions of calcium and native tropomyosin with myosin and heavy meromyosin
3. Interaction of Actomyosin with Adenosine Triphosphate at Low Ionic Strength
4. On the active site of myosin A-adenosine triphosphatase IV. Properties of binding of trinitrobenzenesulfonate and p-chloromercuribenzoate to myosin a
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1. Thiol reactivity as a sensor of rotation of the converter in myosin;Biochemical and Biophysical Research Communications;2008-04
2. Xestoquinone Activates Skeletal Muscle Actomyosin ATPase by Modification of the Specific Sulfhydryl Group in the Myosin Head Probably Distinct from Sulfhydryl Groups SH1 and SH2;Biochemistry;1995-10-03
3. Reversible elimination of myofibrillar Ca2+ sensitivity by diamide and other sulfhydryl reagents: comparison with reversible contracture produced in intact cells;Canadian Journal of Physiology and Pharmacology;1990-08-01
4. Mechanisms that produce rapid damage to myofilaments of amphibian skeletal muscle;Muscle & Nerve;1989-03
5. SH-1 modification of rabbit myosin interferes with calcium regulation;Journal of Muscle Research and Cell Motility;1989-02
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