Evidence map›Paper›PMID 41443503›Full record

ArticleJournal of molecular and cellular cardiology2026

Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments.

Kripa Chitre, Olga E Karpicheva, Chloe J King, Michael J Rynkiewicz, Axel J Fenwick, John F Dawson, D Brian Foster, William Lehman, Anthony Cammarato

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular and cellular cardiology, 2026. 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.

No citing paper in PubMed yet.

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

9 authors.

Kripa ChitreDepartment of Medicine, Division of Cardiology, Johns Hopkins University, 720 Rutland Avenue, Baltimore, MD 21205, USA.
Olga E KarpichevaDepartment of Pharmacology, Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, 72 E. Concord St, Boston, MA 02118, USA.
Chloe J KingDepartment Molecular and Cellular Biology, University of Guelph, Guelph, 50 Stone Rd E, ON N1G 2W1, Canada.
Michael J RynkiewiczDepartment of Pharmacology, Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, 72 E. Concord St, Boston, MA 02118, USA.
Axel J FenwickDepartment of Medicine, Division of Cardiology, Johns Hopkins University, 720 Rutland Avenue, Baltimore, MD 21205, USA.
John F DawsonDepartment Molecular and Cellular Biology, University of Guelph, Guelph, 50 Stone Rd E, ON N1G 2W1, Canada.
D Brian FosterDepartment of Medicine, Division of Cardiology, Johns Hopkins University, 720 Rutland Avenue, Baltimore, MD 21205, USA.
William LehmanDepartment of Pharmacology, Physiology & Biophysics, Boston University Chobanian & Avedisian School of Medicine, 72 E. Concord St, Boston, MA 02118, USA.
Anthony CammaratoDepartment of Medicine, Division of Cardiology, Johns Hopkins University, 720 Rutland Avenue, Baltimore, MD 21205, USA; Department of Physiology, Johns Hopkins University School of Medicine, 720 Rutland Avenue, Baltimore, MD 21205, USA. Electronic address: acammar3@jhmi.edu.

Funding

THIN FILAMENTS AND VERTEBRATE SMOOTH MUSCLE CONTRACTIONR01HL036153 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI William J Lehman · 1986 to 2026
$6.5M
PATHOGENESIS AND IN VIVO SUPPRESSION OF THIN FILAMENT-BASED CARDIOMYOPATHIESR01HL124091 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI Anthony Cammarato · 2015 to 2026
$4.3M
Tundra Cryo-EM for Boston UniversityS10OD032253 · OD · BOSTON UNIVERSITY MEDICAL CAMPUS · PI BULLITT, ESTHER · 2023 to 2023
$1.5M
NHLBI NIH HHS R01 HL036153NHLBI NIH HHS R01 HL124091NIH HHS S10 OD032253
6 · The paper itself

Abstract

Electrostatic interactions between actin residues K326 and K328 and tropomyosin bias tropomyosin to an F-actin location where it blocks myosin attachment. K326/328 acetylation neutralizes their charge, potentially disrupting thin filament-based contractile regulation. We verified acetylation of K326/328 on human cardiac actin (ACTC1) and generated recombinant K326/328Q, pseudo-acetylated ACTC1. Pseudo-acetylation reduced inhibition of myosin-driven motility of F-actin-tropomyosin and F-actin-tropomyosin-troponin at low Ca

Indexed as

Actin CytoskeletonActinsMyocardiumAcetylationCalciumHumansModels, MolecularMyosinsProtein BindingTropomyosinTroponinActinsCalciumMyosinsTropomyosinTroponinActinCryo-EM structure determinationLysine acetylationMuscleSteric regulationTropomyosin

Identifiers

PMID41443503
PMCPMC13316180

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.