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

Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation

8 May 2010

Abstract excerpt

Mutations in the dystrophin gene cause Duchenne muscular dystrophy (DMD) most commonly through loss of protein expression. In a small subpopulation of patients, missense mutations can cause DMD, Becker muscular dystrophy, or X-linked cardiomyopathy. Nearly one-half of disease-causing missense mutations are located in actin-binding domain 1 (ABD1) of dystrophin. To test the hypothesis that ABD1 missense mutations...

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 Genetic Neurodegenerative Diseases
Share to Muscle Physiology and Disorders

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

Source

Identifiers

PMID: 20457930
DOI: 10.1073/pnas.1001517107

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 9 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregationPMID 20457930Read ↗

Novel mutation in spectrin-like repeat 1 of dystrophin central domain causes protein misfolding and mild Becker muscular dystrophy.Semantic proximity Read ↗

Molecular mechanisms of disease-related human β-actin mutations p.R183W and p.E364K.Semantic proximity Read ↗

Disease-proportional proteasomal degradation of missense dystrophins.Semantic proximity Read ↗

Increased actin binding is a shared molecular consequence of numerous spinocerebellar ataxia mutations in β-III-spectrinSemantic proximity Read ↗

The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy.Semantic proximity Read ↗

Increased Actin Binding Is a Shared Molecular Consequence of Numerous SCA5 Mutations in β-III-Spectrin.Semantic proximity Read ↗

Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.Semantic proximity Read ↗

Proteostasis Associated Mutations in HSPB5 Destabilize the αB-crystallin DomainSemantic proximity Read ↗

A1603P and K1617del, Mutations in β-Cardiac Myosin Heavy Chain that Cause Laing Early-Onset Distal Myopathy, Affect Secondary Structure and Filament Formation In Vitro and In Vivo.Semantic proximity Read ↗

Flexibility in the N-terminal actin-binding domain: clues from in silico mutations and molecular dynamics.Semantic proximity Read ↗

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

Myopathy mutations in alpha-skeletal-muscle actin cause a range of molecular defects.Semantic proximity Read ↗

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