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- W3011714189 abstract "Abstract Abnormal α-synuclein aggregation has been implicated in several diseases and is known to spread in a prion-like manner. There is a relationship between protein aggregate structure (strain) and clinical phenotype in prion diseases, however, whether differences in the strains of α-synuclein aggregates account for the different pathologies remained unclear. Here, we generated two types of α-synuclein fibrils from identical monomer and investigated their seeding and propagation ability in mice and primary-cultured neurons. One α-synuclein fibril induced marked accumulation of phosphorylated α-synuclein and ubiquitinated protein aggregates, while the other did not, indicating the formation of α-synuclein two strains. Notably, the former α-synuclein strain inhibited proteasome activity and co-precipitated with 26S proteasome complex. Further examination indicated that structural differences in the C-terminal region of α-synuclein strains lead to different effects on proteasome activity. These results provide a possible molecular mechanism to account for the different pathologies induced by different α-synuclein strains." @default.
- W3011714189 created "2020-03-23" @default.
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- W3011714189 date "2020-03-20" @default.
- W3011714189 modified "2023-10-17" @default.
- W3011714189 title "α-Synuclein strains that cause distinct pathologies differentially inhibit proteasome" @default.
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- W3011714189 doi "https://doi.org/10.1101/2020.03.19.999086" @default.
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