Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C
- 26 February 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 286 (3), 933-949
- https://doi.org/10.1006/jmbi.1998.2522
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Isoform-specific Interaction of the Myosin-binding Proteins (MyBPs) with Skeletal and Cardiac Myosin Is a Property of the C-terminal Immunoglobulin DomainJournal of Biological Chemistry, 1997
- The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathyJournal of Muscle Research and Cell Motility, 1997
- Conservation within the myosin motor domain: implications for structure and functionStructure, 1996
- A Molecular Map of the Interactions between Titin and Myosin‐Binding Protein CEuropean Journal of Biochemistry, 1996
- Cardiac myosin binding protein–C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathyNature Genetics, 1995
- Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intracellular member of the immunoglobulin superfamily.Proceedings of the National Academy of Sciences, 1990
- The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscleJournal of Muscle Research and Cell Motility, 1986
- Heart C-protein is transiently expressed during skeletal muscle development in the embryo, but persists in cultured myogenic cellsDevelopmental Biology, 1985
- Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies.The Journal of cell biology, 1984
- Electron microscopy of thin filaments decorated with a Ca2+-regulated myosinJournal of Molecular Biology, 1980