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Article

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

Proteins - 1 May 2012

Singh Surinder M, Molas Justine F, Kongari Narsimulu, Bandi Swati, Armstrong Geoffrey S, Winder Steve J, Mallela Krishna M G

Abstract excerpt

Muscular dystrophy (MD) is the most common genetic lethal disorder in children. Mutations in dystrophin trigger the most common form of MD, Duchenne, and its allelic variant Becker MD. Utrophin is the closest homologue and has been shown to compensate for the loss of dystrophin in human disease animal models. However, the structural and functional similarities and differences between utrophin and dystrophin are...

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Identifiers

PMID: 22275054
DOI: 10.1002/prot.24033
PMCID: PMC3439503

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.PMID 22275054Read ↗

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