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Article

Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.

Computational and mathematical methods in medicine - 1 Jan 2016

Smaoui Mohamed R, Mazza-Anthony Cody, Waldispühl Jérôme

Abstract excerpt

Huntington's disease is a fatal autosomal genetic disorder characterized by an expanded glutamine-coding CAG repeat sequence in the huntingtin (Htt) exon 1 gene. The Htt protein associated with the disease misfolds into toxic oligomers and aggregate fibril structures. Competing models for the misfolding and aggregation phenomena have suggested the role of the Htt-N-terminal region and the CAG trinucleotide...

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Identifiers

PMID: 28096892
DOI: 10.1155/2016/6247867
PMCID: PMC5206856

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