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

Functional analysis of myosin missense mutations in familial hypertrophic cardiomyopathy.

Proceedings of the National Academy of Sciences of the United States of America - 18 Jan 1994

Straceski A J, Geisterfer-Lowrance A, Seidman C E, Seidman J G, Leinwand L A

Abstract excerpt

To analyze potential functional consequences of myosin heavy chain (MHC) mutations identified in patients with familial hypertrophic cardiomyopathy (FHC), we have assessed the stability of the mutant MHCs and their ability to form thick filaments. Constructs encoding wild-type rat alpha MHC and seven corresponding FHC missense mutants were transfected into COS cells. Immunoblot analysis suggested that FHC...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Microscopy, Electron

Share to Myosins

Share to Phenotype

Share to Point Mutation

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 8290568
DOI: 10.1073/pnas.91.2.589
PMCID: PMC42994

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of myosin missense mutations in familial hypertrophic cardiomyopathy.PMID 8290568Read ↗

Point Mutations in Human β Cardiac Myosin Heavy Chain Have Differential Effects on Sarcomeric Structure and Assembly: An ATP Binding Site Change Disrupts Both Thick and Thin Filaments, Whereas Hypertrophic Cardiomyopathy Mutations Display Normal AssemblySemantic proximity Read ↗

Functional consequences of mutations in the myosin heavy chain at sites implicated in familial hypertrophic cardiomyopathy.Semantic proximity Read ↗

Functional analysis of myosin mutations that cause familial hypertrophic cardiomyopathy.Semantic proximity Read ↗

A mutant tropomyosin that causes hypertrophic cardiomyopathy is expressed in vivo and associated with an increased calcium sensitivity.Semantic proximity Read ↗

Skeletal muscle expression and abnormal function of beta-myosin in hypertrophic cardiomyopathy.Semantic proximity Read ↗

Functional analyses of troponin T mutations that cause hypertrophic cardiomyopathy: Insights into disease pathogenesis and troponin functionSemantic proximity Read ↗

Molecular mechanisms regulating the myofilament response to Ca2+: implications of mutations causal for familial hypertrophic cardiomyopathy.Semantic proximity Read ↗

Altered myocyte contractility and calcium homeostasis in alpha-myosin heavy chain point mutations linked to familial dilated cardiomyopathy.Semantic proximity Read ↗

Mutations in the motor domain modulate myosin activity and myofibril organization.Semantic proximity Read ↗

Functional effects of the hypertrophic cardiomyopathy R403Q mutation are different in an alpha- or beta-myosin heavy chain backbone.Semantic proximity Read ↗

Facilitated cross-bridge interactions with thin filaments by familial hypertrophic cardiomyopathy mutations in α-tropomyosin.Semantic proximity Read ↗

Cardiac and skeletal muscle expression of mutant β-myosin heavy chains, degree of functional impairment and phenotypic heterogeneity in hypertrophic cardiomyopathy.Semantic proximity Read ↗

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