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

Biochemical characterization of cardiac α-actin mutations A21V and D26N implicated in hypertrophic cardiomyopathy.

Cytoskeleton (Hoboken, N.J.) - 1 Dec 2024

Greve Johannes N, Schwäbe Frederic V, Taft Manuel H, Manstein Dietmar J

Abstract excerpt

Familial hypertrophic cardiomyopathy (HCM) affects .2% of the world's population and is inherited in an autosomal dominant manner. Mutations in cardiac α-actin are the cause in 1%-5% of all observed cases. Here, we describe the recombinant production, purification, and characterization of the HCM-linked cardiac α-actin variants p.A21V and p.D26N. Mass spectrometric analysis of the initially purified recombinant...

Read the complete abstract on PubMed

Topics

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

Share to Actins
Share to Cardiomyopathy, Hypertrophic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Myocardium

Source

Open in PubMed Open full text

Identifiers

PMID: 38459932
DOI: 10.1002/cm.21852
PMCID: PMC11615838

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

Biochemical characterization of cardiac α-actin mutations A21V and D26N implicated in hypertrophic cardiomyopathy.PMID 38459932Read ↗

Functional Characterization of Cardiac Actin Mutants Causing Hypertrophic (p.A295S) and Dilated Cardiomyopathy (p.R312H and p.E361G).Semantic proximity Read ↗

Functional Characterization of Cardiac Actin Mutants Causing Hypertrophic (p.A295S) and Dilative Cardiomyopathy (p.R312H and p.E361G)Semantic proximity Read ↗

Distortion of the Actin A-Triad Results in Contractile Disinhibition and Cardiomyopathy.Semantic proximity Read ↗

De Novo Asp219Val Mutation in Cardiac Tropomyosin Associated with Hypertrophic Cardiomyopathy.Semantic proximity Read ↗

Functional studies of yeast actin mutants corresponding to human cardiomyopathy mutations.Semantic proximity Read ↗

Functional characterization of the human α-cardiac actin mutations Y166C and M305L involved in hypertrophic cardiomyopathy.Semantic proximity Read ↗

Myosin dilated cardiomyopathy mutation S532P disrupts actomyosin interactions, leading to altered muscle kinetics, reduced locomotion, and cardiac dilation in Drosophila.Semantic proximity Read ↗

A fluorescent folding reporter uncovers myosin misfolding as a driver of Hypertrophic CardiomyopathySemantic proximity Read ↗

Cardiomyopathy-associated variants alter the structure and function of the α-actinin-2 actin-binding domain.Semantic proximity Read ↗

Cardiomyopathy-Associated Variants Alter the Structure and Function of the α-Actinin-2 Actin-Binding DomainSemantic proximity Read ↗

Cryo-EM structures of cardiac muscle α-actin mutants M305L and A331P give insights into the structural mechanisms of hypertrophic cardiomyopathy.Semantic proximity Read ↗

Comprehensive biophysical and structural profiling of alpha-actinin-2 variants reveals mechanistic diversity in hypertrophic cardiomyopathy.Semantic proximity Read ↗

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