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

Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.

Journal of molecular and cellular cardiology - 1 Sept 2011

Midde K, Dumka V, Pinto J R, Muthu P, Marandos P, Gryczynski I, Gryczynski Z, Potter J D, Borejdo J

Abstract excerpt

Distribution of orientations of myosin was examined in ex-vivo myofibrils from hearts of transgenic (Tg) mice expressing Familial Hypertrophic Cardiomyopathy (FHC) troponin T (TnT) mutations I79N, F110I and R278C. Humans are heterozygous for sarcomeric FHC mutations and so hypertrophic myocardium contains a mixture of the wild-type (WT) and mutated (MUT) TnT. If mutations are expressed at a low level there may...

Read the complete abstract on PubMed

Topics

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

Share to Cardiomyopathy, Hypertrophic, Familial
Share to Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mice, Transgenic

Share to Mutation

Share to Myocardium

Share to Myofibrils

Share to Myosins

Share to Troponin T

Source

Open in PubMed Open full text

Identifiers

PMID: 21683708
DOI: 10.1016/j.yjmcc.2011.06.001
PMCID: PMC3150405

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 · 11 closest

Myosin cross-bridges do not form precise rigor bonds in hypertrophic heart muscle carrying troponin T mutations.PMID 21683708Read ↗

Familial hypertrophic cardiomyopathy can be characterized by a specific pattern of orientation fluctuations of actin molecules .Semantic proximity Read ↗

Sub-sarcomeric regulation of thin and thick filaments in skeletal muscle myofibrilsSemantic proximity Read ↗

Automated measurement of myofiber disarray in transgenic mice with ventricular expression ofrasSemantic proximity Read ↗

Regulatory light chain mutants linked to heart disease modify the cardiac myosin lever arm.Semantic proximity Read ↗

Probing relaxed myosin states in hypertrophic cardiomyopathy by second harmonic-generation microscopy.Semantic proximity Read ↗

Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle.Semantic proximity Read ↗

Myosin regulatory domain orientation in skeletal muscle fibers: application of novel electron paramagnetic resonance spectral decomposition and molecular modeling methods.Semantic proximity Read ↗

Phosphorylation of myosin regulatory light chain controls myosin head conformation in cardiac muscleSemantic proximity Read ↗

Direct visualisation and kinetic analysis of normal and nemaline myopathy actin polymerisation using total internal reflection microscopy.Semantic proximity Read ↗

Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscle.Semantic proximity Read ↗

Analysis of cardiomyocyte nuclei in human cardiomyopathy reveals orientation dependent defects in shapeSemantic proximity Read ↗

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