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

Mdm muscular dystrophy: interactions with calpain 3 and a novel functional role for titin's N2A domain.

Human molecular genetics - 1 Oct 2005

Huebsch Kimberly A, Kudryashova Elena, Wooley Christine M, Sher Roger B, Seburn Kevin L, Spencer Melissa J, Cox Gregory A

Abstract excerpt

Human tibial muscular dystrophy and limb-girdle muscular dystrophy 2J are caused by mutations in the giant sarcomeric protein titin (TTN) adjacent to a binding site for the muscle-specific protease calpain 3 (CAPN3). Muscular dystrophy with myositis (mdm) is a recessive mouse mutation with severe and progressive muscular degeneration caused by a deletion in the N2A domain of titin (TTN-N2ADelta83), disrupting a...

Read the complete abstract on PubMed

Topics

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

Share to Calpain
Share to Connectin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Exercise Test

Share to Locomotion

Share to Muscle Contraction

Share to Muscle Proteins

Share to Muscular Dystrophies

Share to Myositis

Source

Open in PubMed Open full text

Identifiers

PMID: 16115818
DOI: 10.1093/hmg/ddi313
PMCID: PMC1350399

Genes

CAPN3
TTN

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

Mdm muscular dystrophy: interactions with calpain 3 and a novel functional role for titin's N2A domain.PMID 16115818Read ↗

Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitroSemantic proximity Read ↗

Removal of the calpain 3 protease reverses the myopathology in a mouse model for titinopathies.Semantic proximity Read ↗

Evidence for ACTN3 as a genetic modifier of Duchenne muscular dystrophy.Semantic proximity Read ↗

Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies.Semantic proximity Read ↗

Oligomer-dependent and oligomer-independent pathogenesis of muscular dystrophy-associated mutations within the penta-EF-hand domain of calpain-3.Semantic proximity Read ↗

Tropomyosin 3 (TPM3) function in skeletal muscle and in myopathy.Semantic proximity Read ↗

Pathogenity of some limb girdle muscular dystrophy mutations can result from reduced anchorage to myofibrils and altered stability of calpain 3.Semantic proximity Read ↗

Failure to up-regulate transcription of genes necessary for muscle adaptation underlies limb girdle muscular dystrophy 2A (calpainopathy).Semantic proximity Read ↗

Autolytic activation of calpain 3 proteinase is facilitated by calmodulin protein.Semantic proximity Read ↗

C3KO mouse expression analysis: downregulation of the muscular dystrophy Ky protein and alterations in muscle aging.Semantic proximity Read ↗

Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Semantic proximity Read ↗

N2A Titin: Signaling Hub and Mechanical Switch in Skeletal Muscle.Semantic proximity Read ↗

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