Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Properties of Cardiac Myosin with Cardiomyopathic Mutations in Essential Light Chains.

Biochemistry. Biokhimiia - 1 Nov 2022

Yampolskaya Daria S, Kopylova Galina V, Shchepkin Daniil V, Bershitsky Sergey Y, Matyushenko Alexander M, Levitsky Dmitrii I

Abstract excerpt

The effects of cardiomyopathic mutations E56G, M149V, and E177G in the MYL3 gene encoding essential light chain of human ventricular myosin (ELCv), on the functional properties of cardiac myosin and its isolated head (myosin subfragment 1, S1) were investigated. Only the M149V mutation upregulated the actin-activated ATPase activity of S1. All mutations significantly increased the Ca2+-sensitivity of the sliding...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Actin Cytoskeleton
Share to Actins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cardiac Myosins

Share to Mutation

Share to Myosin Light Chains

Share to Myosins

Source

Identifiers

PMID: 36509720
DOI: 10.1134/S0006297922110050

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Properties of Cardiac Myosin with Cardiomyopathic Mutations in Essential Light Chains.PMID 36509720Read ↗

Early-Onset Hypertrophic Cardiomyopathy Mutations Significantly Increase the Velocity, Force, and Actin-Activated ATPase Activity of Human β-Cardiac Myosin.Semantic proximity Read ↗

Regulatory light chain mutations associated with cardiomyopathy affect myosin mechanics and kinetics.Semantic proximity Read ↗

Hypercontractile mutant of ventricular myosin essential light chain leads to disruption of sarcomeric structure and function and results in restrictive cardiomyopathy in mice.Semantic proximity Read ↗

Cardiomyopathic mutations in essential light chain reveal mechanisms regulating the super relaxed state of myosin.Semantic proximity Read ↗

Cardiomyopathy-linked myosin regulatory light chain mutations disrupt myosin strain-dependent biochemistry.Semantic proximity Read ↗

The effects of the tropomyosin cardiomyopathy mutations on the calcium regulation of actin-myosin interaction in the atrium and ventricle differ.Semantic proximity Read ↗

Effect of Cardiomyopathic Mutations in Tropomyosin on Calcium Regulation of the Actin-Myosin Interaction in Skeletal Muscle.Semantic proximity Read ↗

A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachmentSemantic proximity Read ↗

Single-molecule analysis sheds light on cardiac myosin dysfunction due to hypertrophic cardiomyopathy mutation A57D in ventricular myosin light chain-1 (MLC1v)Semantic proximity Read ↗

Effects of Cardiomyopathic Mutations on the Cytoplasmic Tropomyosin Isoform Tpm1.7.Semantic proximity Read ↗

Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro.Semantic proximity Read ↗

Tail Length and E525K Dilated Cardiomyopathy Mutant Alter Human β-Cardiac Myosin Super-Relaxed StateSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.