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• W2335432880 abstract "Abnormal protein aggregation has been postulated to explain the molecular basis for many neurodegenerative diseases, including Alzheimer's disease, Parkinson's disease and prion diseases, as well as trinucleotide repeat disorders. The recent findings that mutations in alpha-synuclein lead to autosomal-dominant, early-onset Parkinson's disease in some families and that alpha-synuclein is found in Lewy bodies of all Parkinson's disease patients prompted the hypothesis that the pathophysiology of all Parkinson's disease patients starts with an abnormal folding of alpha-synuclein, producing excessive aggregation that overwhelms the antiaggregation mechanisms of the cell. The genetics of Parkinson's disease and polyglutamine repeat disorders and the evidence of abnormal processing and aggregation of the respective target proteins for the aetiology and pathogenesis in these diseases are reviewed." @default.
• W2335432880 created "2016-06-24" @default.
• W2335432880 creator A5033794504 @default.
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• W2335432880 date "1999-08-01" @default.
• W2335432880 modified "2023-10-15" @default.
• W2335432880 title "Molecular pathogenesis of movement disorders: are protein aggregates a common link in neuronal degeneration?" @default.
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• W2335432880 doi "https://doi.org/10.1097/00019052-199908000-00010" @default.
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