Evidence map›Paper›PMID 19011110›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Cardiac myosin-binding protein C decorates F-actin: implications for cardiac function.

Andrew E Whitten, Cy M Jeffries, Samantha P Harris, Jill Trewhella

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
6.0field-weighted citation impact, top 3% 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

79 citing papers in PubMed, 1 synthesis or guideline pooled it, 122 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Autoinhibition of cMyBP-C by its middle domains.Journal of molecular and cellular cardiology · 2025
    Article
  4. Article
  5. Roles of cMyBP-C phosphorylation on cardiac contractile dysfunction inJournal of molecular and cellular cardiology plus · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. MyBP-C: one protein to govern them all.Journal of muscle research and cell motility · 2020
    Review
  14. Article
  15. Review
  16. Article
  17. 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 · 2019
    Article
  18. Article
  19. Review
  20. 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 · 2017
    Article

19 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

4 authors at 3 institutions in 2 countries.

Andrew E WhittenBragg Institute, Australian Nuclear Science and Technology Organisation, Lucas Heights, NSW 2234, Australia.
Cy M Jeffries
Samantha P Harris
Jill Trewhella
University of Sydney · AUAustralian Nuclear Science and Technology Organisation · AUUniversity of California, Davis · US

Funding

Role of Myosin Binding Protein-C in the Regulation of Myocardial ContractionR01HL080367 · NHLBI · UNIVERSITY OF WASHINGTON · PI Samantha P Harris · 2005 to 2026
$7.5M
NHLBI NIH HHS HL080367NHLBI NIH HHS R01 HL080367
6 · The paper itself

Abstract

Cardiac myosin-binding protein C (cMyBP-C) is an accessory protein of striated muscle sarcomeres that is vital for maintaining regular heart function. Its 4 N-terminal regulatory domains, C0-C1-m-C2 (C0C2), influence actin and myosin interactions, the basic contractile proteins of muscle. Using neutron contrast variation data, we have determined that C0C2 forms a repeating assembly with filamentous actin, where the C0 and C1 domains of C0C2 attach near the DNase I-binding loop and subdomain 1 of adjacent actin monomers. Direct interactions between the N terminus of cMyBP-C and actin thereby provide a mechanism to modulate the contractile cycle by affecting the regulatory state of the thin filament and its ability to interact with myosin.

Indexed as

Heart Function TestsActinsAnimalsCarrier ProteinsHeartMiceModels, MolecularMyosin Binding Protein CScattering, RadiationActinsCarrier ProteinsMyosin Binding Protein C

Identifiers

PMID19011110
PMCPMC2587536
OpenAlexW2078865229

What OpenQuestion holds

Textmetadata
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.