Evidence map›Paper›PMID 40268117›Full record

ArticleJournal of molecular and cellular cardiology2025

Screening single nucleotide changes to tropomyosin to identify novel cardiomyopathy mutants.

Jian Wen, Stuart Campbell, Jeffrey Moore, William Lehman, Michael Rynkiewicz

Abstract read
In one paragraph

Article in Journal of molecular and cellular cardiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Jian WenDepartment of Pharmacology, Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Stuart CampbellDepartment of Biomedical Engineering, Yale University, New Haven, CT, USA.
Jeffrey MooreDepartment of Biological Sciences, University of Massachusetts Lowell, Lowell, MA, USA.
William LehmanDepartment of Pharmacology, Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA.
Michael RynkiewiczDepartment of Pharmacology, Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, Boston, MA, USA. Electronic address: rynkiemj@bu.edu.

Funding

THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR01HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI William J Lehman · 1986 to 2026
$6.5M
Revealing Pathomechanisms of Mutant TPM1 Through a Hybrid Computational-Experimental ApproachR01HL136590 · NHLBI · YALE UNIVERSITY · PI STUART G CAMPBELL, William J Lehman · 2017 to 2026
$5.6M
NHLBI NIH HHS R01 HL036153NHLBI NIH HHS R01 HL136590
6 · The paper itself

Abstract

Inherited cardiomyopathy is a broad class of heart disease that includes pathological cardiac remodeling such as hypertrophic and dilated cardiomyopathy, affecting 1/250-1/500 people worldwide. In many cases, mutations in proteins that make up the sarcomere, the basic subcellular unit of contraction, alter thin filament regulation and are the root cause of hypertrophic and dilated cardiomyopathy. Initially, compensations can maintain cardiac function, so patients may remain asymptomatic for years before a major cardiac episode. Early therapeutic intervention could rescue the deleterious effects of mutations thereby avoiding pathological remodeling, so prediction of potential outcomes and severity of as yet uncharacterized and known mutants of uncertain significance is critical. To accomplish this goal, we begin with the structure of the thin filament containing actin, tropomyosin, and troponin in its regulatory B- and C-states, incorporate all potential single nucleotide mutations to the tropomyosin sequence (over 1700 unique mutations), and then measure the interaction energy between tropomyosin and actin after energy minimization. Analysis of the database thus generated shows the tropomyosin residues resulting in large changes in tropomyosin-actin interaction, and therefore most likely to be deleterious to function. Some of these mutants have been observed in human patients, whereas others are novel. Global analysis further refines hotspots of mutation-sensitive, coiled-coil tropomyosin residues affecting actin interactions. Altogether, the database will allow research to focus in great depth on key candidates for functional analysis, for instance, by assaying in vitro motility and engineered heart tissue mechanics and assessing outcomes in animal models.

Indexed as

CardiomyopathiesMutationTropomyosinActinsAnimalsHumansModels, MolecularProtein BindingActinsTropomyosinActinCardiomyopathyElectrostatic interaction energySingle nucleotide substitutionTropomyosin

Identifiers

PMID40268117
PMCPMC12135046

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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.