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

Impact of salt concentration and free magnesium on human beta-cardiac myosin reveal important details about the conserved mechanochemical mechanism.

The Journal of biological chemistry - 1 Jun 2026

Ge Jinghua, Ebert Michael R, Bodt Skylar M L, Majumder Satyabrata, Ma Wen, Yengo Christopher M

Abstract excerpt

The myosin ATPase cycle is dramatically accelerated by the presence of actin, while the structural details of actin-activation are still unclear. We found that a dilated cardiomyopathy mutation, E525K, in human beta-cardiac myosin subfragment 1 (S1) enhanced actin-activation of phosphate release and lever arm rotation ∼3-fold. We hypothesized that abolishment of the conserved 484 to 525 salt bridge allows for...

Read the complete abstract on PubMed

Topics

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

Share to Actins
Share to Magnesium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Ventricular Myosins

Source

Open in PubMed Open full text

Identifiers

PMID: 42103214
DOI: 10.1016/j.jbc.2026.113114
PMCID: PMC13264367

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Impact of salt concentration and free magnesium on human beta-cardiac myosin reveal important details about the conserved mechanochemical mechanism.PMID 42103214Read ↗

Dilated cardiomyopathy mutation in beta-cardiac myosin enhances actin activation of the power stroke and phosphate releaseSemantic proximity Read ↗

The hypertrophic cardiomyopathy mutation G768R makes cardiac myosin a high duty ratio motorSemantic proximity Read ↗

The G256E HCM mutation prolongs relaxation via altered nucleotide handlingSemantic proximity Read ↗

The G256E HCM mutation prolongs cardiac muscle relaxation via altered nucleotide handlingSemantic proximity Read ↗

Loop 1 of human cardiac myosin regulates the rate of ATP induced actomyosin dissociation but not the rate of ADP releaseSemantic proximity Read ↗

The hypertrophic cardiomyopathy myosin mutation R453C alters ATP binding and hydrolysis of human cardiac β-myosin.Semantic proximity Read ↗

Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips.Semantic proximity Read ↗

Mutations in the catalytic domain of human β-cardiac myosin that cause early onset hypertrophic cardiomyopathy significantly increase the fundamental parameters that determine ensemble force and velocitySemantic proximity Read ↗

Hypertrophic cardiomyopathy ß-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super-relaxed stateSemantic proximity Read ↗

Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state.Semantic proximity Read ↗

Kinetic signatures of myosin-5B, the motor involved in microvillus inclusion disease.Semantic proximity Read ↗

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

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