title: Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration.
abstract: The abnormal aggregation of a small number of known proteins underlies the most common human neurodegenerative diseases. In tauopathies and synucleinopathies, the normally soluble intracellular proteins tau and α-synuclein become insoluble and filamentous. In recent years, non-cell autonomous mechanisms of aggregate formation have come to the fore, suggesting that nucleation-dependent aggregation may occur in a localized fashion in human tauopathies and synucleinopathies, followed by seed-dependent propagation. There is a long prodromal phase between the formation of protein aggregates and the appearance of the first clinical symptoms, which manifest only after extensive propagation, opening novel therapeutic avenues.
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK mg@mrc-lmb.cam.ac.uk.
authors.forename: Michel
authors.initials: M
authors.lastname: Goedert
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Masami
authors.initials: M
authors.lastname: Masuda-Suzukake
authors.affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Falcon
mesh_terms: D000818:Animals; D006801:Humans; D019636:Neurodegenerative Diseases / Q000378:metabolism* / Q000503:physiopathology*; D000072002:Prion Proteins / Q000378:metabolism*; D066263:Protein Aggregation, Pathological; D051844:alpha-Synuclein / Q000378:metabolism*; D016875:tau Proteins / Q000378:metabolism*
chemical_list: D000072002:Prion Proteins; D051844:alpha-Synuclein; D016875:tau Proteins
keywords: Alzheimer’s disease; Parkinson’s disease; alpha-synuclein; prion-like; tau