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        Characterization of Prion Proteins

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        Prion disease represents a group of transmissible neurodegenerative disorders that include scrapie in sheep and goats, bovine spongiform encephalopathy (BSE), and Creutzfeldt-Jakob disease (CJD), Gerstmann-Str�ussler-Scheinker syndrome, fatal familial insomnia, and kuru in humans. The disease is characterized clinically by ataxia, dementia, and myoclonus as well as pathologically by spongiosis, astrocytic gliosis, and neuronal loss (reviewed in refs. 1 and 2 ). CJD occurs mostly (about 85% of all cases) as sporadic cases (unknown etiology), with the rest of the cases being familial (owing to inheritance of mutations in the prion protein gene) or iatrogenic (due to accidental transmission during medical procedure). Recently, a new variant form of CJD (vCJD) has emerged in the United Kingdom that may originate from the BSE epidemic (3 ).
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