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• W2962977998 endingPage "3606" @default.
• W2962977998 startingPage "3606" @default.
• W2962977998 abstract "Inherited mutations in the Prion protein (PrP), encoded by the PRNP gene, have been associated with autosomal dominant neurodegenerative disorders, such as Creutzfeldt-Jacob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), and Fatal Familial Insomnia (FFI). Notably, PRNP mutations have also been described in clinical pictures resembling other neurodegenerative diseases, such as frontotemporal dementia. Regarding the pathogenesis, it has been observed that these point mutations are located in the C-terminal region of the PRNP gene and, currently, the potential significance of the N-terminal domain has largely been underestimated. The purpose of this report is to review and provide current insights into the pathogenic mechanisms of PRNP mutations, emphasizing the differences between the C- and N-terminal regions and focusing, in particular, on the lesser-known flexible N-terminal, for which recent biophysical evidence has revealed a physical interaction with the globular C-terminal domain of the cellular prion protein (PrPC)." @default.
• W2962977998 created "2019-07-30" @default.
• W2962977998 creator A5016120298 @default.
• W2962977998 creator A5059411860 @default.
• W2962977998 date "2019-07-23" @default.
• W2962977998 modified "2023-10-14" @default.
• W2962977998 title "Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review" @default.
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• W2962977998 doi "https://doi.org/10.3390/ijms20143606" @default.
• W2962977998 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6678283" @default.
• W2962977998 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31340582" @default.
• W2962977998 hasPublicationYear "2019" @default.
• W2962977998 type Work @default.

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