ArticleBiophysical journal2008
The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 28 citations in OpenAlex.
- Ion Channel Impairment and Myofilament CaCells · 2021Review
- Altered force generation and cell-to-cell contractile imbalance in hypertrophic cardiomyopathy.Pflugers Archiv : European journal of physiology · 2019Review
- Remodeling of repolarization and arrhythmia susceptibility in a myosin-binding protein C knockout mouse model.American journal of physiology. Heart and circulatory physiology · 2017Article
- Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Ablation of cardiac myosin binding protein-C disrupts the super-relaxed state of myosin in murine cardiomyocytes.Journal of molecular and cellular cardiology · 2016Article
- The role of super-relaxed myosin in skeletal and cardiac muscle.Biophysical reviews · 2015Article
- Altered interactions between cardiac myosin binding protein-C and α-cardiac actin variants associated with cardiomyopathies.Archives of biochemistry and biophysics · 2014Article
- Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.Biophysical journal · 2014Article
- Hypertrophic and dilated cardiomyopathy: four decades of basic research on muscle lead to potential therapeutic approaches to these devastating genetic diseases.Biophysical journal · 2014Review
- Atomic model of the human cardiac muscle myosin filament.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Three-dimensional structure of the human myosin thick filament: clinical implications.Global cardiology science & practice · 2013Review
- Myosin binding protein-C phosphorylation is the principal mediator of protein kinase A effects on thick filament structure in myocardium.Journal of molecular and cellular cardiology · 2012Article
- Structure, interactions and function of the N-terminus of cardiac myosin binding protein C (MyBP-C): who does what, with what, and to whom?Journal of muscle research and cell motility · 2012Review
- A new state of cardiac myosin with very slow ATP turnover: a potential cardioprotective mechanism in the heart.Biophysical journal · 2011Article
- Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin.Journal of structural biology · 2011Article
- The role of the myosin ATPase activity in adaptive thermogenesis by skeletal muscle.Biophysical reviews · 2011Article
- Muscle myosin filaments: cores, crowns and couplings.Biophysical reviews · 2009Review
- Cytoplasmic Ig-domain proteins: cytoskeletal regulators with a role in human disease.Cell motility and the cytoskeleton · 2009Review
- Cardiac myosin binding protein-C is essential for thick-filament stability and flexural rigidity.Biophysical journal · 2009Article
- Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Mutations in the thick filament associated protein cardiac myosin binding protein-C (cMyBP-C) are a major cause of familial hypertrophic cardiomyopathy. Although cMyBP-C is thought to play both a structural and a regulatory role in the contraction of cardiac muscle, detailed information about the role of this protein in stability of the thick filament and maintenance of the ordered helical arrangement of the myosin cross-bridges is limited. To address these questions, the structure of myosin thick filaments isolated from the hearts of wild-type mice containing cMyBP-C (cMyBP-C(+/+)) were compared to those of cMyBP-C knockout mice lacking this protein (cMyBp-C(-/-)). The filaments from the knockout mice hearts lacking cMyBP-C are stable and similar in length and appearance to filaments from the wild-type mice hearts containing cMyBP-C. Both wild-type and many of the cMyBP-C(-/-) filaments display a distinct 43 nm periodicity. Fourier transforms of electron microscope images typically show helical layer lines to the sixth layer line, confirming the well-ordered arrangement of the cross-bridges in both sets of filaments. However, the "forbidden" meridional reflections, thought to derive from a perturbation from helical symmetry in the wild-type filament, are weaker or absent in the transforms of the cMyBP-C(-/-) myocardial thick filaments. In addition, the cross-bridge array in the absence of cMyBP-C appears more easily disordered.
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