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• W2111048594 abstract "Inherited prion diseases are neurodegenerative disorders caused by autosomal dominant mutations in the human prion protein gene (PRNP). Kindred with inherited prion disease can show remarkable phenotypic variability that has yet to be explained. Here we report analysis of protease resistant disease-related prion protein (PrP(Sc)) isoforms from a range of inherited prion disease cases (point mutations P102L, D178N, E200K and 2-, 4- and 6-octapeptide repeat insertions) and show that the glycoform ratios of PrP(Sc) associated with PRNP point mutations are distinct from those observed in sporadic, iatrogenic and variant Creutzfeldt-Jakob disease. Patients with the same PRNP mutation can also propagate PrP(Sc) with distinct conformations. These data extend the spectrum of recognized PrP(Sc) types seen in human prion diseases and provide further insight into the generation of diverse clinicopathological phenotypes associated with inherited prion disease." @default.
• W2111048594 created "2016-06-24" @default.
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• W2111048594 date "2006-01-16" @default.
• W2111048594 modified "2023-10-18" @default.
• W2111048594 title "Distinct glycoform ratios of protease resistant prion protein associated with PRNP point mutations" @default.
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• W2111048594 doi "https://doi.org/10.1093/brain/awl013" @default.
• W2111048594 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16415305" @default.
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