Evidence map›Paper›PMID 25619247›Full record

ArticleBiochemical Society transactions2015

The myosin mesa and a possible unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathy.

James A Spudich

Abstract read
In one paragraph

Article in Biochemical Society transactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
–field-weighted citation impact
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

94 citing papers in PubMed.

  1. Immature and mature myocardium in the pathophysiology of hypertrophic cardiomyopathy.Journal of molecular and cellular cardiology plus · 2026
    Review
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  10. A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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34 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

1 author.

James A Spudich*Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, U.S.A.

Funding

MYOSIN MOVEMENT IN VITRO: MOLECULAR CHARACTERIZATIONR01GM033289 · NIGMS · STANFORD UNIVERSITY · PI SPUDICH, JAMES · 1985 to 2024
$13.6M
Molecular Characterization of Cardiomyopathy Mutations in Human Cardiac MyosinR01HL117138 · NHLBI · UNIVERSITY OF COLORADO · PI LEINWAND, LESLIE ANNE, PERKINS, THOMAS TUPPER · 2013 to 2021
$4.2M
NHLBI NIH HHS HL117138NHLBI NIH HHS R01 HL117138NIGMS NIH HHS GM33289NIGMS NIH HHS R01 GM033289
6 · The paper itself

Abstract

No matter how many times one explores the structure of the myosin molecule, there is always something new to discover. Here, I describe the myosin mesa, a structural feature of the motor domain that has the characteristics of a binding domain for another protein, possibly myosin-binding protein C (MyBP-C). Interestingly, many well-known hypertrophic cardiomyopathy (HCM) mutations lie along this surface and may affect the putative interactions proposed here. A potential unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathy is discussed here. It involves increased power output of the cardiac muscle as a result of HCM mutations causing the release of inhibition by myosin binding protein C.

Indexed as

Amino Acid SequenceAnimalsCardiomyopathy, HypertrophicCarrier ProteinsHumansModels, MolecularMolecular Sequence DataMyosin Binding Protein CMyosinsProtein BindingProtein Interaction Domains and MotifsCarrier ProteinsMyosin Binding Protein CMyosins

Identifiers

PMID25619247
PMCPMC4349527

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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.