ArticleJournal of biomedicine & biotechnology2010
Functional differences between the N-terminal domains of mouse and human myosin binding protein-C.
Article in Journal of biomedicine & biotechnology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 35 citations in OpenAlex.
- The role of the troponin T interactions with actin in regulation of cardiac thin filament revealed by the troponin T pathogenic variant Ile79Asn.Journal of molecular and cellular cardiology · 2025Article
- Cryo-Electron Microscopy Reveals Cardiac Myosin Binding Protein-C M-Domain Interactions with the Thin Filament.Journal of molecular biology · 2022Article
- Changes in the Cardiotoxic Effects of Lead Intoxication in Rats Induced by Muscular Exercise.International journal of molecular sciences · 2022Article
- Interaction of the C2 Ig-like Domain of Cardiac Myosin Binding Protein-C with F-actin.Journal of molecular biology · 2021Article
- Cardioinotropic Effects in Subchronic Intoxication of Rats with Lead and/or Cadmium Oxide Nanoparticles.International journal of molecular sciences · 2021Article
- MyBP-C: one protein to govern them all.Journal of muscle research and cell motility · 2020Review
- Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Revealing the mechanism of how cardiac myosin-binding protein C N-terminal fragments sensitize thin filaments for myosin binding.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- MYBPC3 truncation mutations enhance actomyosin contractile mechanics in human hypertrophic cardiomyopathy.Journal of molecular and cellular cardiology · 2019Article
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament.Structure (London, England : 1993) · 2018Article
- Hypertrophic cardiomyopathy and the myosin mesa: viewing an old disease in a new light.Biophysical reviews · 2018Review
- C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Normal cardiac contraction in mice lacking the proline-alanine rich region and C1 domain of cardiac myosin binding protein C.Journal of molecular and cellular cardiology · 2015Article
- Myosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Modulation of thin filament activation of myosin ATP hydrolysis by N-terminal domains of cardiac myosin binding protein-C.Biochemistry · 2014Article
- Earning stripes: myosin binding protein-C interactions with actin.Pflugers Archiv : European journal of physiology · 2014Review
- An endogenously produced fragment of cardiac myosin-binding protein C is pathogenic and can lead to heart failure.Circulation research · 2013Article
- A gain-of-function mutation in the M-domain of cardiac myosin-binding protein-C increases binding to actin.The Journal of biological chemistry · 2013Article
- Cardiac myosin binding protein-C: redefining its structure and function.Biophysical reviews · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The N-terminus of cMyBP-C can activate actomyosin interactions in the absence of Ca2+, but it is unclear which domains are necessary. Prior studies suggested that the Pro-Ala rich region of human cMyBP-C activated force in permeabilized human cardiomyocytes, whereas the C1 and M-domains of mouse cMyBP-C activated force in permeabilized rat cardiac trabeculae. Because the amino acid sequence of the P/A region differs between human and mouse cMyBP-C isoforms (46% identity), we investigated whether species-specific differences in the P/A region could account for differences in activating effects. Using chimeric fusion proteins containing combinations of human and mouse C0, Pro-Ala, and C1 domains, we demonstrate here that the human P/A and C1 domains activate actomyosin interactions, whereas the same regions of mouse cMyBP-C are less effective. These results suggest that species-specific differences between homologous cMyBP-C isoforms confer differential effects that could fine-tune cMyBP-C function in hearts of different species.
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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.