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• W3137508727 abstract "Significance The misfolding and aggregation into amyloid fibrils of the prion protein (PrP) have been strongly linked with a group of neurodegenerative disorders that include the mad cow disease. Currently, the molecular origins of the prion diseases are unknown, including the underlying mechanisms of PrP misfolding and the regions promoting its aggregation. Here, we identified the structural basis by which the folded domain of the human PrP converts into amyloids. We showed that this process is promoted by intermediate species forming as a result of the pathological mutation T183A, and that POM antibodies are able to suppress completely the aggregation process by blocking the misfolding mechanism. This study thereby suggests possible molecular strategies to inhibit PrP aggregation into amyloids." @default.
• W3137508727 created "2021-03-29" @default.
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• W3137508727 date "2021-03-17" @default.
• W3137508727 modified "2023-10-18" @default.
• W3137508727 title "Mechanism of misfolding of the human prion protein revealed by a pathological mutation" @default.
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• W3137508727 doi "https://doi.org/10.1073/pnas.2019631118" @default.
• W3137508727 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7999870" @default.
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