Abstract
Prion diseases are neurodegenerative disorders that result from changes in the conformation of a single, highly unusual membrane glycoprotein called PrP (prion protein). This molecular transition converts a normal version of the protein (PrPC) into a pathogenic form (PrPSc) that constitutes the major component of an unprecedented type of infectious particle (prion) devoid of nucleic acid. Although there is a wealth of information now available about the role of PrPSc in the disease process, relatively little is known about the normal physiological function of PrPC. Aside from its intrinsic biological interest, identifying the function of PrPC is likely to be important in understanding the pathogenesis of prion diseases, as it has been suggested that impairment of this function as a result of conversion to PrPSc may explain some features of the disease phenotype.
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Brown, L.R., Harris, D.A. (2002). The Prion Protein and Copper. In: Massaro, E.J. (eds) Handbook of Copper Pharmacology and Toxicology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-288-3_5
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