Article
Self-assembly of Mutant Huntingtin Exon-1 Fragments into Large Complex Fibrillar Structures Involves Nucleated Branching.
Journal of molecular biology - 8 Jun 2018
Wagner Anne S, Politi Antonio Z, Ast Anne, Bravo-Rodriguez Kenny, Baum Katharina, Buntru Alexander, Strempel Nadine U, Brusendorf Lydia, Hänig Christian, Boeddrich Annett, Plassmann Stephanie, Klockmeier Konrad, Ramirez-Anguita Juan M, Sanchez-Garcia Elsa, Wolf Jana, Wanker Erich E
Abstract excerpt
Huntingtin (HTT) fragments with extended polyglutamine tracts self-assemble into amyloid-like fibrillar aggregates. Elucidating the fibril formation mechanism is critical for understanding Huntington's disease pathology and for developing novel therapeutic strategies. Here, we performed systematic experimental and theoretical studies to examine the self-assembly of an aggregation-prone N-terminal HTT exon-1...
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