Evidence map›Paper›PMID 38105932›Full record

ArticlebioRxiv : the preprint server for biology2023

Tail Length and E525K Dilated Cardiomyopathy Mutant Alter Human β-Cardiac Myosin Super-Relaxed State.

Sebastian Duno-Miranda, Shane R Nelson, David V Rasicci, Skylar L M Bodt, Joseph A Cirilo, Duha Vang, Sivaraj Sivaramakrishnan, Christopher M Yengo, David M Warshaw

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Sebastian Duno-MirandaDepartment of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, Vermont.ORCID 0000-0002-2618-1335
Shane R NelsonDepartment of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, Vermont.
David V RasicciDepartment of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, Pennsylvania.
Skylar L M BodtDepartment of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, Pennsylvania.
Joseph A CiriloDepartment of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, Pennsylvania.ORCID 0000-0003-2135-5831
Duha VangDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota.
Sivaraj SivaramakrishnanDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota.
Christopher M YengoDepartment of Cellular and Molecular Physiology, Penn State College of Medicine, Hershey, Pennsylvania.
David M WarshawDepartment of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, Vermont.
Penn State Milton S. Hershey Medical Center · USUniversity of Vermont · USUniversity of Minnesota · US

Funding

Impact of dilated cardiomyopathy mutations on cardiac myosin structure and functionR01HL163585 · NHLBI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI Sivaraj Sivaramakrishnan, David M Warshaw · 2023 to 2026
$3.0M
Research supplement to promote diversity in Heath-related researchR01HL150953 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI SIVARAMAKRISHNAN, SIVARAJ, WARSHAW, DAVID M · 2020 to 2023
$2.4M
NHLBI NIH HHS R01 HL150953NHLBI NIH HHS R01 HL163585
6 · The paper itself

Abstract

Dilated cardiomyopathy (DCM) is characterized by impaired cardiac function due to myocardial hypo-contractility and is associated with point mutations in β-cardiac myosin, the molecular motor that powers cardiac contraction. Myocardial function can be modulated through sequestration of myosin motors into an auto-inhibited "super relaxed" state (SRX), which is further stabilized by a structural state known as the "Interacting Heads Motif" (IHM). Therefore, hypo-contractility of DCM myocardium may result from: 1) reduced function of individual myosin, and/or; 2) decreased myosin availability due to increased IHM/SRX stabilization. To define the molecular impact of an established DCM myosin mutation, E525K, we characterized the biochemical and mechanical activity of wild-type (WT) and E525K human β-cardiac myosin constructs that differed in the length of their coiled-coil tail, which dictates their ability to form the IHM/SRX state. Single-headed (S1) and a short-tailed, double-headed (2HEP) myosin constructs exhibited low (~10%) IHM/SRX content, actin-activated ATPase activity of ~5s

Identifiers

PMID38105932
PMCPMC10723396
OpenAlexW4389497845

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.