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

Nemaline Myopathy-Related Skeletal Muscle α-Actin (ACTA1) Mutation, Asp286Gly, Prevents Proper Strong Myosin Binding and Triggers Muscle Weakness

20 Sept 2012

Abstract excerpt

Many mutations in the skeletal muscle α-actin gene (ACTA1) lead to muscle weakness and nemaline myopathy. Despite increasing clinical and scientific interest, the molecular and cellular pathogenesis of weakness remains unclear. Therefore, in the present study, we aimed at unraveling these mechanisms using muscles from a transgenic mouse model of nemaline myopathy expressing the ACTA1 Asp286Gly mutation. We...

Read the complete abstract on PubMed

Topics

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

Share to Cardiomyopathy and Myosin Studies
Share to Cellular Mechanics and Interactions
Share to Muscle Physiology and Disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23029319
DOI: 10.1371/journal.pone.0045923

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nemaline Myopathy-Related Skeletal Muscle α-Actin (ACTA1) Mutation, Asp286Gly, Prevents Proper Strong Myosin Binding and Triggers Muscle WeaknessPMID 23029319Read ↗

A myopathy-related actin mutation increases contractile function.Semantic proximity Read ↗

Distinct underlying mechanisms of limb and respiratory muscle fiber weaknesses in nemaline myopathy.Semantic proximity Read ↗

A role for actin flexibility in thin filament-mediated contractile regulation and myopathy.Semantic proximity Read ↗

Tropomyosin Must Interact Weakly with Actin to Effectively Regulate Thin Filament Function.Semantic proximity Read ↗

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

Skeletal and cardiac α-actin isoforms differently modulate myosin cross-bridge formation and myofibre force production.Semantic proximity Read ↗

Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy.Semantic proximity Read ↗

Multimodal MRI and (31)P-MRS investigations of the ACTA1(Asp286Gly) mouse model of nemaline myopathy provide evidence of impaired in vivo muscle function, altered muscle structure and disturbed energy metabolism.Semantic proximity Read ↗

Thin filament proteins mutations associated with skeletal myopathies: defective regulation of muscle contraction.Semantic proximity Read ↗

Acute and chronic tirasemtiv treatment improves in vivo and in vitro muscle performance in actin-based nemaline myopathy mice.Semantic proximity Read ↗

Modulating myosin restores muscle function in a mouse model of nemaline myopathySemantic proximity Read ↗

Skeletal muscle α-actin diseases (actinopathies): pathology and mechanisms.Semantic proximity Read ↗

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