Journal
NATURE COMMUNICATIONS
Volume 4, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms3575
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Funding
- Agence Nationale de la Recherche [ANR-09-MNPS-013-01, ANR-11-BSV8-021-01]
- Swiss National Science Foundation [200020_134681]
- Centre National de la Recherche Scientifique
- Human Frontier Science Program
- ETH Zurich
- European Community
- Marie Curie Actions [264508]
- Seventh Framework Program [Bio-NMR 261863]
- Lundbeck Foundation
- Fondation Bettencourt Schueller
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alpha-synuclein aggregation is implicated in a variety of diseases including Parkinson's disease, dementia with Lewy bodies, pure autonomic failure and multiple system atrophy. The association of protein aggregates made of a single protein with a variety of clinical phenotypes has been explained for prion diseases by the existence of different strains that propagate through the infection pathway. Here we structurally and functionally characterize two polymorphs of alpha-synuclein. We present evidence that the two forms indeed fulfil the molecular criteria to be identified as two strains of alpha-synuclein. Specifically, we show that the two strains have different structures, levels of toxicity, and in vitro and in vivo seeding and propagation properties. Such strain differences may account for differences in disease progression in different individuals/cell types and/or types of synucleinopathies.
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