Evidence map›Paper›PMID 34634306›Full record

ReviewThe Journal of biological chemistry2021

Cardiac myosin contraction and mechanotransduction in health and disease.

Samantha K Barrick, Michael J Greenberg

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 69 citations in OpenAlex.

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  13. How Exceptional Is the Ear?Journal of the Association for Research in Otolaryngology : JARO · 2025
    Review
  14. Hypertrophic cardiomyopathy: insights into pathophysiology and novel therapeutic strategies from clinical studies.The Egyptian heart journal : (EHJ) : official bulletin of the Egyptian Society of Cardiology · 2025
    Review
  15. Cardiac disease mechanobiology: advances using hiPSC-CMs.Frontiers in cardiovascular medicine · 2025
    Review
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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.

Samantha K BarrickDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri, USA.
Michael J GreenbergDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri, USA. Electronic address: greenberg@wustl.edu.
Washington University in St. Louis · US

Funding

Regulation of cardiac power output in health and diseaseR01HL141086 · NHLBI · WASHINGTON UNIVERSITY · PI GREENBERG, MICHAEL J · 2018 to 2022
$2.7M
Multiscale investigation of cardiomyopathy-associated mutations in metavinculinF32HL152543 · NHLBI · WASHINGTON UNIVERSITY · PI BARRICK, SAMANTHA KIRSTIN · 2021 to 2023
$223k
NHLBI NIH HHS F32 HL152543NHLBI NIH HHS R01 HL141086
6 · The paper itself

Abstract

Cardiac myosin is the molecular motor that powers heart contraction by converting chemical energy from ATP hydrolysis into mechanical force. The power output of the heart is tightly regulated to meet the physiological needs of the body. Recent multiscale studies spanning from molecules to tissues have revealed complex regulatory mechanisms that fine-tune cardiac contraction, in which myosin not only generates power output but also plays an active role in its regulation. Thus, myosin is both shaped by and actively involved in shaping its mechanical environment. Moreover, these studies have shown that cardiac myosin-generated tension affects physiological processes beyond muscle contraction. Here, we review these novel regulatory mechanisms, as well as the roles that myosin-based force generation and mechanotransduction play in development and disease. We describe how key intra- and intermolecular interactions contribute to the regulation of myosin-based contractility and the role of mechanical forces in tuning myosin function. We also discuss the emergence of cardiac myosin as a drug target for diseases including heart failure, leading to the discovery of therapeutics that directly tune myosin contractility. Finally, we highlight some of the outstanding questions that must be addressed to better understand myosin's functions and regulation, and we discuss prospects for translating these discoveries into precision medicine therapeutics targeting contractility and mechanotransduction.

Indexed as

Mechanotransduction, CellularMyocardial ContractionAnimalsCardiac MyosinsHeart FailureHumansMyocardiumCardiac Myosinscardiac developmentcardiac musclecardiomyopathycontractile proteinheartmechanotransductionmyosin

Identifiers

PMID34634306
PMCPMC8559575
OpenAlexW3204323597

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.