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

The essential light chain N-terminal extension alters force and fiber kinetics in mouse cardiac muscle.

The Journal of biological chemistry - 14 Oct 2005

Miller Mark S, Palmer Bradley M, Ruch Stuart, Martin Lisa A, Farman Gerrie P, Wang Yuan, Robbins Jeffrey, Irving Thomas C, Maughan David W

Abstract excerpt

The functional significance of the actin-binding region at the N terminus of the cardiac myosin essential light chain (ELC) remains elusive. In a previous experiment, the endogenous ventricular ELC was replaced with a protein containing a 10-amino acid deletion at positions 5-14 (ELC1vDelta5-14, referred to as 1vDelta5-14), a region that interacts with actin. 1vDelta5-14 mice showed no discernable mutant...

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 Dextrans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Echocardiography

Share to Models, Chemical

Share to Myocardium

Share to Myosin Heavy Chains

Share to Osmosis

Share to X-Ray Diffraction

Source

Identifiers

PMID: 16085933
DOI: 10.1074/jbc.M508430200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The essential light chain N-terminal extension alters force and fiber kinetics in mouse cardiac muscle.PMID 16085933Read ↗

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 ↗

Ablation of the N terminus of cardiac essential light chain promotes the super-relaxed state of myosin and counteracts hypercontractility in hypertrophic cardiomyopathy mutant mice.Semantic proximity Read ↗

Subcellular Remodeling in Filamin C Deficient Mouse Hearts Impairs Myocyte Tension Development during Progression of Dilated Cardiomyopathy.Semantic proximity Read ↗

Discrete effects of A57G-myosin essential light chain mutation associated with familial hypertrophic cardiomyopathy.Semantic proximity Read ↗

Structural and functional impact of troponin C-mediated Ca2+ sensitization on myofilament lattice spacing and cross-bridge mechanics in mouse cardiac muscle.Semantic proximity Read ↗

Ablation of cardiac myosin-binding protein-C accelerates contractile kinetics in engineered cardiac tissue.Semantic proximity Read ↗

Identification of two new regions in the N-terminus of cardiac troponin T that have divergent effects on cardiac contractile function.Semantic proximity Read ↗

Essential light chain S195 phosphorylation is required for cardiac adaptation under physical stress.Semantic proximity Read ↗

Changes in end-to-end interactions of tropomyosin affect mouse cardiac muscle dynamics.Semantic proximity Read ↗

Removal of the cardiac troponin I N-terminal extension improves cardiac function in aged mice.Semantic proximity Read ↗

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

A Cardiomyopathy Mutation in the Myosin Essential Light Chain Alters Actomyosin Structure.Semantic proximity Read ↗

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