Evidence map›Paper›PMID 19962384›Full record

ReviewJournal of molecular and cellular cardiology2010

Phosphorylation and function of cardiac myosin binding protein-C in health and disease.

David Barefield, Sakthivel Sadayappan

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 189 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
189citing papers in PubMed, 1 pooled it
10.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

189 citing papers in PubMed, 1 synthesis or guideline pooled it, 268 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. The CabioRxiv : the preprint server for biology · 2026
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  12. New Types of Post-Translational Modification of Proteins in Cardiovascular Diseases.Journal of cardiovascular translational research · 2025
    Review
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  15. CaJournal of molecular and cellular cardiology · 2025
    Article
  16. Molecular Regulation of Cardiomyocyte Maturation.Current cardiology reports · 2025
    Review
  17. Review
  18. Cells · 2024
    Article
  19. Article
  20. Article

129 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

David BarefieldDepartment of Cell and Molecular Physiology, Stritch School of Medicine, Loyola University Chicago, 2160 South First Avenue, Maywood, IL 60153, USA.
Sakthivel Sadayappan
Loyola University Chicago · US

Funding

Myosin binding protein H-like and its role in cardiomyopathyF32HL131304 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BAREFIELD, DAVID Y · 2016 to 2018
$155k
NHLBI NIH HHS F32 HL131304
6 · The paper itself

Abstract

During the past 5 years there has been an increasing body of literature describing the roles cardiac myosin binding protein C (cMyBP-C) phosphorylation play in regulating cardiac function and heart failure. cMyBP-C is a sarcomeric thick filament protein that interacts with titin, myosin and actin to regulate sarcomeric assembly, structure and function. Elucidating the function of cMyBP-C is clinically important because mutations in this protein have been linked to cardiomyopathy in more than sixty million people worldwide. One function of cMyBP-C is to regulate cross-bridge formation through dynamic phosphorylation by protein kinase A, protein kinase C and Ca(2+)-calmodulin-activated kinase II, suggesting that cMyBP-C phosphorylation serves as a highly coordinated point of contractile regulation. Moreover, dephosphorylation of cMyBP-C, which accelerates its degradation, has been shown to associate with the development of heart failure in mouse models and in humans. Strikingly, cMyBP-C phosphorylation presents a potential target for therapeutic development as protection against ischemic-reperfusion injury, which has been demonstrated in mouse hearts. Also, emerging evidence suggests that cMyBP-C has the potential to be used as a biomarker for diagnosing myocardial infarction. Although many aspects of cMyBP-C phosphorylation and function remain poorly understood, cMyBP-C and its phosphorylation states have significant promise as a target for therapy and for providing a better understanding of the mechanics of heart function during health and disease. In this review we discuss the most recent findings with respect to cMyBP-C phosphorylation and function and determine potential future directions to better understand the functional role of cMyBP-C and phosphorylation in sarcomeric structure, myocardial contractility and cardioprotection.

Indexed as

AnimalsCardiomyopathiesCarrier ProteinsHeart FailureHumansModels, BiologicalMyocardial ContractionMyocardiumMyosin Binding Protein CPhosphorylationSarcomeresCarrier ProteinsMyosin Binding Protein C

Identifiers

PMID19962384
PMCPMC6800196
OpenAlexW2027759264

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.