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- W2037794385 abstract "Abstract α-Synuclein, a natively unfolded protein aggregation which is implicated in the pathogenesis of Parkinson’s disease and several other neurodegenerative diseases, is known to interact with a great number of unrelated proteins. Some of these proteins, such as β-synuclein and DJ-1, were shown to inhibit α-synuclein aggregation in vitro and in vivo therefore acting as chaperones. Since calbindin-D28K is co-localized with Ca2+ neuronal membrane pumps, and since α-synuclein is also found in the membrane proximity, these two proteins can potentially interact in vivo. Here we show that calbindin-D28K interacts with α-synuclein and inhibits its fibrillation in a calcium-dependent manner, therefore potentially acting as a calcium-dependent chaperone." @default.
- W2037794385 created "2016-06-24" @default.
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- W2037794385 date "2010-02-01" @default.
- W2037794385 modified "2023-09-26" @default.
- W2037794385 title "Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro" @default.
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- W2037794385 doi "https://doi.org/10.2478/s11535-009-0071-8" @default.
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