ReviewPflugers Archiv : European journal of physiology2014
Cardiac myosin binding protein-C: a structurally dynamic regulator of myocardial contractility.
Review in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed.
- From bedside to bench: A multimodal approach uncovering the molecular basis of theProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Transcriptome Profile Identifies Actin as an Essential Regulator of Cardiac Myosin Binding Protein C3 Hypertrophic Cardiomyopathy in a Zebrafish Model.International journal of molecular sciences · 2022Article
- Biomarkers for Heart Failure Prognosis: Proteins, Genetic Scores and Non-coding RNAs.Frontiers in cardiovascular medicine · 2020Review
- Genotypic effect of a mutation of the MYBPC3 gene and two phenotypes with different patterns of inheritance.Journal of clinical laboratory analysis · 2018Article
- Interaction between cardiac myosin-binding protein C and formin Fhod3.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathy.The Journal of general physiology · 2016Article
- Alterations in Multi-Scale Cardiac Architecture in Association With Phosphorylation of Myosin Binding Protein-C.Journal of the American Heart Association · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cardiac myosin binding protein-C (cMyBP-C) is a modular protein anchored to the thick filament through interactions mediated by its C-terminal region. The N-terminal region of cMyBPC-C regulates myocardial contractility by modifying actin-myosin association. Phosphorylation of the N-terminal region diminishes cMyBP-C's capacity to regulate actin-myosin function. Despite a substantial body of literature, many issues remain unclear regarding the structural and functional roles of cMyBP-C. While no high-resolution structures of the intact protein exist, crystallographic and nuclear magnetic resonance (NMR) structures of isolated N-terminal domains provide important molecular details regarding cMyBP-C's role in controlling contractility. In this review, we summarize the emerging structural understanding of cMyBP-C with a particular emphasis placed on describing how its dynamic molecular interactions with both thin and thick filament proteins likely contribute to contractile regulation. Furthermore, we discuss the future directions and strategies by which we may improve the mechanistic understanding of its role in modulating cardiac muscle contraction.
Indexed as
Identifiers
24469349What OpenQuestion holds
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.