Ontology highlight
ABSTRACT:
SUBMITTER: Yonetani M
PROVIDER: S-EPMC2658087 | biostudies-other | 2009 Mar
REPOSITORIES: biostudies-other
The Journal of biological chemistry 20090121 12
Fibrillization or conformational change of alpha-synuclein is central in the pathogenesis of alpha-synucleinopathies, such as Parkinson disease. We found that the A30P mutant accelerates nucleation-dependent fibrillization of wild type (WT) alpha-synuclein. Electron microscopy observation and ultracentrifugation experiments revealed that shedding of fragments occurs from A30P fibrils and that these fragments accelerate fibrillization by serving as seeds. Immunochemical analysis using epitope-spe ...[more]