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

Kenneth W Drombosky1, Sascha Rode2, Ravi Kodali2

  • 1Department of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA; Graduate Program in Molecular Pharmacology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA; Pittsburgh Institute for Neurodegenerative Diseases (PIND), University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.

Neurobiology of Disease
|September 2, 2018
PubMed
Summary

Huntington disease (HD) toxicity stems from huntingtin (htt) exon1 aggregation, not just polyglutamine (polyQ) length. Engineered htt analogs reveal amyloid formation drives toxicity, offering therapeutic targets.

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