Kinetically Competing Huntingtin Aggregation Pathways Control Amyloid Polymorphism and Properties
Author:
Affiliation:
1. Department of Structural Biology and ‡Pittsburgh Institute for Neurodegenerative Diseases, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi3000929
Reference68 articles.
1. Physical Chemistry of Polyglutamine: Intriguing Tales of a Monotonous Sequence
2. Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: Implications for Huntington's disease pathology
3. Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
4. An Antisense CAG Repeat Transcript at JPH3 Locus Mediates Expanded Polyglutamine Protein Toxicity in Huntington's Disease-like 2 Mice
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