Cardiac Myosin Binding Protein C and Its Phosphorylation Regulate Multiple Steps in the Cross-Bridge Cycle of Muscle Contraction
Author:
Affiliation:
1. Department of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi300085x
Reference66 articles.
1. The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif.
2. A Molecular Map of the Interactions between Titin and Myosin-Binding Protein C. Implications for Sarcomeric Assembly in Familial Hypertrophic Cardiomyopathy
3. The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1
4. Structural Evidence for the Interaction of C-protein (MyBP-C) with Actin and Sequence Identification of a Possible Actin-binding Domain
5. Effects of cholinergic and adrenergic agonists on phosphorylation of a 165,000-dalton myofibrillar protein in intact cardiac muscle.
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