Low-resolution structure of a vesicle disrupting -synuclein oligomer that accumulates during fibrillation
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference37 articles.
1. The Aggregation and Fibrillation of α-Synuclein
2. Vesicle Permeabilization by Protofibrillar α-Synuclein Is Sensitive to Parkinson's Disease-Linked Mutations and Occurs by a Pore-like Mechanism
3. Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease
4. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha -synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
5. α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils
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