ArticleBiophysical journal2008
Cardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heart.
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 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent Activation.Frontiers in physiology · 2016Article
- Preserved cross-bridge kinetics in human hypertrophic cardiomyopathy patients with MYBPC3 mutations.Pflugers Archiv : European journal of physiology · 2014Article
- 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
- Protein kinase D increases maximal Ca2+-activated tension of cardiomyocyte contraction by phosphorylation of cMyBP-C-Ser315.American journal of physiology. Heart and circulatory physiology · 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
- Unique single molecule binding of cardiac myosin binding protein-C to actin and phosphorylation-dependent inhibition of actomyosin motility requires 17 amino acids of the motif domain.Journal of molecular and cellular cardiology · 2012Article
- Roles for cardiac MyBP-C in maintaining myofilament lattice rigidity and prolonging myosin cross-bridge lifetime.Biophysical journal · 2011Article
- Diastolic myofilament dysfunction in the failing human heart.Pflugers Archiv : European journal of physiology · 2011Review
- Force-generating capacity of human myosin isoforms extracted from single muscle fibre segments.The Journal of physiology · 2010Article
- Resolving myoarchitectural disarray in the mouse ventricular wall with diffusion spectrum magnetic resonance imaging.Annals of biomedical engineering · 2010Article
- The ubiquitin-proteasome system and nonsense-mediated mRNA decay in hypertrophic cardiomyopathy.Cardiovascular research · 2010Review
- PPARs, Cardiovascular Metabolism, and Function: Near- or Far-from-Equilibrium Pathways.PPAR research · 2010Article
- Cardiac myosin binding protein-C phosphorylation in a {beta}-myosin heavy chain background.Circulation · 2009Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cardiac myosin binding protein C (cMyBP-C) is an important regulator of cardiac contractility. Its precise effect on myosin cross-bridges (CBs) remains unclear. Using a cMyBP-C(-/-) mouse model, we determined how cMyBP-C modulates the cyclic interaction of CBs with actin. From papillary muscle mechanics, CB characteristics were provided using A. F. Huxley's equations. The probability of myosin being weakly bound to actin was higher in cMyBP-C(-/-) than in cMyBP-C(+/+). However, the number of CBs in strongly bound, high-force generated state and the force generated per CB were lower in cMyBP-C(-/-). Overall CB cycling and the velocity of CB tilting were accelerated in cMyBP-C(-/-). Taking advantage of the presence of cMyBP-C in cMyBP-C(+/+) myosin solution but not in cMyBP-C(-/-), we also analyzed the effects of cMyBP-C on the myosin-based sliding velocity of actin filaments. At baseline, sliding velocity and the relative isometric CB force, as determined by the amount of alpha-actinin required to arrest thin filament motility, were lower in cMyBP-C(-/-) than in cMyBP-C(+/+). cAMP-dependent protein kinase-mediated cMyBP-C phosphorylation further increased the force produced by CBs. We conclude that cMyBP-C prevents inefficient, weak binding of the myosin CB to actin and has a critical effect on the power-stroke step of the myosin molecular motor.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.