Evidence map›Paper›PMID 38521794›Full record

ArticleNature communications2024

Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads.

Anthony L Hessel, Nichlas M Engels, Michel N Kuehn, Devin Nissen, Rachel L Sadler, Weikang Ma, Thomas C Irving, Wolfgang A Linke, Samantha P Harris

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
11.3field-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

19 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Subsarcomeric regulation of thin and thick filaments in skeletal muscle myofibrils.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Muscle Diffraction at the Life Science X-ray Scattering Beamline.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Consecutive SSCs increase the SSC effect in skinned rat muscle fibres.Pflugers Archiv : European journal of physiology · 2025
    Article
  14. Article
  15. Autoinhibition of cMyBP-C by its middle domains.Journal of molecular and cellular cardiology · 2025
    Article
  16. The distinctive mechanical and structural signatures of residual force enhancement in myofibers.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Article
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

9 authors at 4 institutions in 2 countries.

Anthony L HesselInstitute of Physiology II, University of Muenster, Muenster, Germany. anthony.hessel@uni-muenster.de.ORCID http://orcid.org/0000-0003-4278-4221
Nichlas M EngelsDepartment of Cellular and Molecular Medicine, University of Arizona, Tucson, AZ, USA.
Michel N KuehnInstitute of Physiology II, University of Muenster, Muenster, Germany.
Devin NissenBioCAT, Department of Biology, Illinois Institute of Technology, Chicago, IL, USA.
Rachel L SadlerDepartment of Physiology, University of Arizona, Tucson, AZ, USA.ORCID http://orcid.org/0000-0002-1280-1484
Weikang MaBioCAT, Department of Biology, Illinois Institute of Technology, Chicago, IL, USA.ORCID http://orcid.org/0000-0001-9535-7114
Thomas C IrvingBioCAT, Department of Biology, Illinois Institute of Technology, Chicago, IL, USA.
Wolfgang A LinkeInstitute of Physiology II, University of Muenster, Muenster, Germany.ORCID http://orcid.org/0000-0003-0801-3773
Samantha P HarrisDepartment of Physiology, University of Arizona, Tucson, AZ, USA. samharris@arizona.edu.ORCID http://orcid.org/0000-0003-0822-0238
Illinois Institute of Technology · USUniversity of Arizona · USOphthalmic Consultants of Boston · USUniversity of Münster · DE

Funding

The Biophysics Collaborative Access Team (User Training and Outreach)P30GM138395 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI THOMAS C IRVING · 2021 to 2026
$16.5M
PHYSIOLOGYT32HL007249 · NHLBI · UNIVERSITY OF ARIZONA · PI Brett A Colson, JOHN P KONHILAS · 1985 to 2026
$12.5M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
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
Mechanisms of Thin Filament Regulation by Myosin Binding Protein-CR01HL140925 · NHLBI · UNIVERSITY OF ARIZONA · PI GALKIN, VITOLD, HARRIS, SAMANTHA P · 2019 to 2022
$2.3M
Structure and function of myosin binding protein-C in skeletal musclesR01AR083970 · NIAMS · UNIVERSITY OF ARIZONA · PI Samantha P Harris · 2025 to 2026
$929k
Cut and paste of myosin binding protein-C in skeletal musclesR21AR081935 · NIAMS · UNIVERSITY OF ARIZONA · PI HARRIS, SAMANTHA P · 2023 to 2024
$366k
NHLBI NIH HHS R01 HL080367NHLBI NIH HHS R01 HL140925NHLBI NIH HHS T32 HL007249NIAMS NIH HHS R01 AR083970NIAMS NIH HHS R21 AR081935NIGMS NIH HHS P30 GM138395NIGMS NIH HHS P41 GM103622
6 · The paper itself

Abstract

Muscle contraction is produced via the interaction of myofilaments and is regulated so that muscle performance matches demand. Myosin-binding protein C (MyBP-C) is a long and flexible protein that is tightly bound to the thick filament at its C-terminal end (MyBP-C

Indexed as

Carrier ProteinsSarcomeresMuscle ContractionMuscle, SkeletalMyosin Binding Protein CMyosinsCarrier ProteinsMyosin Binding Protein CMyosins

Identifiers

PMID38521794
PMCPMC10960836
OpenAlexW4393119493

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.