Title : Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease.

Pub. Date : 2018 Dec

PMID : 30171891






3 Functional Relationships(s)
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1 Additional modifications within the polyQ segment produce htt exon1 analogs that populate only spherical oligomers and are non-toxic in cells and flies. polyglutamine huntingtin Drosophila melanogaster
2 Furthermore, in mixture with expanded-polyQ htt exon1, the latter analogs in vitro suppress amyloid formation and promote oligomer formation, and in vivo rescue neurons and flies expressing mhtt exon1 from dysfunction and death. polyglutamine huntingtin Drosophila melanogaster
3 Thus, in our experiments, while htt exon1 toxicity tracks with aggregation propensity, it does so in spite of the toxic construct"s possessing polyQ tracts well below those normally considered to be disease-associated. polyglutamine huntingtin Drosophila melanogaster