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- W2291424369 endingPage "397" @default.
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- W2291424369 abstract "Abstract α‐synuclein is normally situated in the nerve terminal but it accumulates and aggregates in axons and cell bodies in synucleinopathies such as Parkinson's disease. The conformational changes occurring during α‐synucleins aggregation process affects its interactions with other proteins and its subcellular localization. This review focuses on interaction partners of α‐synuclein within different compartments of the cell with a focus on those preferentially binding aggregated α‐synuclein. The aggregation state of α‐synuclein also affects its catabolism and we hypothesize impaired macroautophagy is involved neuronal excretion of α‐synuclein species responsible for the prion‐like spreading of α‐synuclein pathology." @default.
- W2291424369 created "2016-06-24" @default.
- W2291424369 creator A5008055701 @default.
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- W2291424369 creator A5024195150 @default.
- W2291424369 creator A5051399477 @default.
- W2291424369 creator A5062813947 @default.
- W2291424369 date "2016-04-25" @default.
- W2291424369 modified "2023-09-27" @default.
- W2291424369 title "Protein Partners of α-Synuclein in Health and Disease" @default.
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