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Article

Pathogenic mutation R959W alters recognition dynamics of dysferlin inner DysF domain.

Molecular bioSystems - 1 Mar 2016

Espinoza-Fonseca L Michel

Abstract excerpt

Dysferlin, a 220 kD protein, plays a major role in regulating plasma membrane repair in muscle cells. Mutations in the dysferlin inner DysF domain are known to cause different types of muscular dystrophy, including limb-girdle muscular dystrophy type 2B (LGMD2B) and Miyoshi myopathy (MM). Replacement of arginine in position 959 by tryptophan has been frequently associated with both LGMD2B and MM, but the...

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Identifiers

PMID: 26806107
DOI: 10.1039/c5mb00772k

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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.

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Pathogenic mutation R959W alters recognition dynamics of dysferlin inner DysF domain.PMID 26806107Read ↗

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A novel biallelic mutation in the DYSF gene as a cause of Miyoshi myopathy.Semantic proximity Read ↗

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