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- W2016351953 endingPage "155" @default.
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- W2016351953 abstract "Misfolded aggregates present in amyloid fibrils are associated with various diseases known as protein misfolding disorders. Among them, prion diseases are unique in that the pathology can be transmitted by an infectious process involving an unprecedented agent known as a prion. Prions are infectious proteins that can transmit biological information by propagating protein misfolding and aggregation. The molecular mechanism of prion conversion has a striking resemblance to the process of amyloid formation, suggesting that misfolded aggregates have an inherent ability to be transmissible. Intriguing recent data suggest that other protein misfolding disorders might also be transmitted by a prion-like infectious process." @default.
- W2016351953 created "2016-06-24" @default.
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- W2016351953 date "2006-03-01" @default.
- W2016351953 modified "2023-10-10" @default.
- W2016351953 title "Amyloids, prions and the inherent infectious nature of misfolded protein aggregates" @default.
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- W2016351953 doi "https://doi.org/10.1016/j.tibs.2006.01.002" @default.
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