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

Cell-intrinsic functional effects of the α-cardiac myosin Arg-403-Gln mutation in familial hypertrophic cardiomyopathy.

Biophysical journal - 20 Jun 2012

Chuan Peiying, Sivaramakrishnan Sivaraj, Ashley Euan A, Spudich James A

Abstract excerpt

Human familial hypertrophic cardiomyopathy is the most common Mendelian cardiovascular disease worldwide. Among the most severe presentations of the disease are those in families heterozygous for the mutation R403Q in β-cardiac myosin. Mice heterozygous for this mutation in the α-cardiac myosin isoform display typical familial hypertrophic cardiomyopathy pathology. Here, we study cardiomyocytes from heterozygous...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Biomechanical Phenomena

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cardiomyopathy, Hypertrophic

Share to Mutation

Share to Myocytes, Cardiac

Share to Ventricular Myosins

Source

Open in PubMed Open full text

Identifiers

PMID: 22735528
DOI: 10.1016/j.bpj.2012.04.049
PMCID: PMC3379014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cell-intrinsic functional effects of the α-cardiac myosin Arg-403-Gln mutation in familial hypertrophic cardiomyopathy.PMID 22735528Read ↗

Disrupted Mechanobiology Links the Molecular and Cellular Phenotypes in Familial Dilated CardiomyopathySemantic proximity Read ↗

Molecular mechanisms of altered contraction with the β-myosin R403Q mutation in porcine ventricular muscle and a human stem cell-derived cardiomyocyte model.Semantic proximity Read ↗

Disrupted mechanobiology links the molecular and cellular phenotypes in familial dilated cardiomyopathySemantic proximity Read ↗

Molecular mechanisms of altered contraction with the β-myosin R403Q mutation in porcine ventricular muscle and a human stem cell-derived cardiomyocyte modelSemantic proximity Read ↗

Length-dependent hypercontractility decoupled from cellular adaptations is the initial phenotype in MYBPC3-haploinsufficient iPSC-derived engineered cardiac tissuesSemantic proximity Read ↗

The familial hypertrophic cardiomyopathy-associated myosin mutation R403Q accelerates tension generation and relaxation of human cardiac myofibrils.Semantic proximity Read ↗

Mechanical Resistance to Micro-Heart Tissue Contractility unveils early Structural and Functional Pathology in iPSC Models of Hypertrophic CardiomyopathySemantic proximity Read ↗

Altered crossbridge kinetics in the alphaMHC403/+ mouse model of familial hypertrophic cardiomyopathy.Semantic proximity Read ↗

Mechanical dysfunction induced by a hypertrophic cardiomyopathy mutation is the primary driver of cellular adaptationSemantic proximity Read ↗

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

Cardiomyopathy-related mutation (A30V) in mouse cardiac troponin T divergently alters the magnitude of stretch activation in α- and β-myosin heavy chain fibers.Semantic proximity Read ↗

Gene transfer of human cardiomyopathy β-MyHC mutant R403Q directly alters intact cardiac myocyte calcium homeostasis and causes hyper-contractilitySemantic proximity Read ↗

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