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Article

Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core.

Nature communications - 24 May 2017

Lin Hsiang-Kai, Boatz Jennifer C, Krabbendam Inge E, Kodali Ravindra, Hou Zhipeng, Wetzel Ronald, Dolga Amalia M, Poirier Michelle A, van der Wel Patrick C A

Abstract excerpt

Polyglutamine expansion in the huntingtin protein is the primary genetic cause of Huntington's disease (HD). Fragments coinciding with mutant huntingtin exon1 aggregate in vivo and induce HD-like pathology in mouse models. The resulting aggregates can have different structures that affect their biochemical behaviour and cytotoxic activity. Here we report our studies of the structure and functional characteristics...

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PMID: 28537272
DOI: 10.1038/ncomms15462
PMCID: PMC5458082

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