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 effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts.

Journal of cellular and molecular medicine - 1 Apr 2012

Muthu Priya, Kazmierczak Katarzyna, Jones Michelle, Szczesna-Cordary Danuta

Abstract excerpt

Phosphorylation of the myosin regulatory light chain (RLC) by Ca(2+)-calmodulin-activated myosin light chain kinase (MLCK) is known to be essential for the inotropic function of the heart. In this study, we have examined the effects of MLCK-phosphorylation of transgenic (Tg) mouse cardiac muscle preparations expressing the D166V (aspartic acid to valine)-RLC mutation, identified to cause familial hypertrophic...

Read the complete abstract on PubMed

Topics

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

Share to Cardiomyopathies
Share to Mice
Share to Mice, Transgenic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Myocardium

Share to Myosin Light Chains

Share to Phosphorylation

Source

Open in PubMed Open full text

Identifiers

PMID: 21696541
DOI: 10.1111/j.1582-4934.2011.01371.x
PMCID: PMC3193868

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

The effect of myosin RLC phosphorylation in normal and cardiomyopathic mouse hearts.PMID 21696541Read ↗

Constitutive phosphorylation of cardiac myosin regulatory light chain prevents development of hypertrophic cardiomyopathy in mice.Semantic proximity Read ↗

In vitro rescue study of a malignant familial hypertrophic cardiomyopathy phenotype by pseudo-phosphorylation of myosin regulatory light chain.Semantic proximity Read ↗

Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice.Semantic proximity Read ↗

Molecular basis of force-pCa relation in MYL2 cardiomyopathy mice: Role of the super-relaxed state of myosin.Semantic proximity Read ↗

The dilated cardiomyopathy-causing mutation ACTC E361G in cardiac muscle myofibrils specifically abolishes modulation of Ca(2+) regulation by phosphorylation of troponin I.Semantic proximity Read ↗

The E22K mutation of myosin RLC that causes familial hypertrophic cardiomyopathy increases calcium sensitivity of force and ATPase in transgenic mice.Semantic proximity Read ↗

Hypertrophic cardiomyopathy associated Lys104Glu mutation in the myosin regulatory light chain causes diastolic disturbance in mice.Semantic proximity Read ↗

Diversity and similarity of motor function and cross-bridge kinetics in papillary muscles of transgenic mice carrying myosin regulatory light chain mutations D166V and R58Q.Semantic proximity Read ↗

Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectivesSemantic proximity Read ↗

The contribution of cardiac myosin binding protein-c Ser282 phosphorylation to the rate of force generation and in vivo cardiac contractility.Semantic proximity Read ↗

Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific manner.Semantic proximity Read ↗

Mechanical defects of muscle fibers with myosin light chain mutants that cause cardiomyopathy.Semantic proximity Read ↗

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