Myosin-binding protein C slows cardiac myofibril relaxation kinetics.

Abstract read

In one paragraph

Article in The Journal of physiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

From twitch to relaxation: Obesity dysregulates muscle contractile function.Physiological reports · 2026
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

2 authors.

Alexey V DvornikovDepartment of Physiology, University of Arizona, Tucson, AZ, USA.ORCID 0000-0003-1514-4747

Samantha P HarrisDepartment of Physiology, University of Arizona, Tucson, AZ, USA.

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

Structure and function of myosin binding protein-C in skeletal musclesR01AR083970 · NIAMS · UNIVERSITY OF ARIZONA · PI Samantha P Harris · 2025 to 2026

$929k

Expanding synchrotron applications in biomedical research: Myocardial and skeletal muscle imaging at Brookhaven National LabsR43GM156170 · NIGMS · ACCELERATED MUSCLE BIOTECHNOLOGIES CONSULTANTS, L.L.C. · PI HARRIS, SAMANTHA P, HESSEL, ANTHONY LAWRENCE CAPOZZI · 2024 to 2024

$311k

NHLBI NIH HHS R01 HL080367NIAMS NIH HHS R01 AR083970NIGMS NIH HHS R43 GM156170

6 · The paper itself

Abstract

Mutations in cardiac myosin binding protein C (cMyBP-C) are a leading cause of hypertrophic cardiomyopathy (HCM). Patients with HCM often have reduced cMyBP-C expression, reduced protein phosphorylation, and diastolic dysfunction. Relaxation of a single myofibril in response to a sudden drop in activator calcium is biphasic, consisting of a slow isometric phase (k

Indexed as

Carrier ProteinsMyofibrilsAnimalsCalciumCardiomyopathy, HypertrophicHumansKineticsMaleMiceMyosin Binding Protein CPhosphorylationCalciumCarrier ProteinsMyosin Binding Protein Ccardiac myosin binding protein‐Cmavacamtenmuscle relaxationmyofibril mechanicsphosphorylation

Identifiers

PMID40936293

DOI10.1113/JP289201

PMCPMC13073943

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.