Protein misfolding and aggregation occur in most neurodegenerative disorders, but the concept of spreading and infectivity of aggregates in the CNS has, until recently, been confined to prion diseases such as Creutzfeldt–Jakob disease. New evidence suggests that prion-like spreading, involving proteins such as amyloid-β, tau, huntingtin and α-synuclein, can occur in other neurodegenerative disorders. In this article, Lee et al. discuss the underlying molecular mechanisms and consider the therapeutic implications of the new data.
- Seung-Jae Lee
- Paula Desplats
- Eliezer Masliah
