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• W2139023437 abstract "Prion diseases are fatal transmissible neurological disorders afflicting a range of mammalian species. Although still controversial, a large body of data suggests that the causative agent may be composed entirely of a small glycoprotein. The brains of infected animals have accumulations of a pathogenic protease-resistant isoform (PrPsc) of a normal host-encoded glycoprotein, PrPc or prion protein. A number of lines of biochemical evidence implicate the disease-specific isoform, PrPsc, as the transmissible agent and genetic analysis has shown tight linkage between PrP gene mutations and polymorphisms and differential susceptibility to prion diseases, Perhaps the strongest evidence for a protein-only model of the agent is that PrP gene-ablated mice are resistant to scrapie and that mice with PrP mutation, corresponding to those found in a human familial prion disease, spontaneously develop a transmissible prion disease. This review describes the critical role that transgenic technology has played in the study of the biology of prion diseases and considers the issues raised by this work." @default.
• W2139023437 created "2016-06-24" @default.
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• W2139023437 date "1997-06-01" @default.
• W2139023437 modified "2023-10-13" @default.
• W2139023437 title "Transgenic analysis of prion diseases" @default.
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• W2139023437 doi "https://doi.org/10.1093/molehr/3.6.529" @default.
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