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• W2018428043 abstract "Prion diseases are a heterogeneous group of disorders with an invariably fatal disease course. Although various etiologies have been proposed it is apparent that at least a subset of these diseases are of infectious nature. An essential part of the infectious agent, termed the prion, is mainly composed of an abnormal isoform (PrPSc) of a host-encoded normal cellular protein (PrPC). The molecular details of the pathophysiology of this group of diseases are unclear but the conversion of PrPC to PrPSc plays a fundamental role. In all human prion diseases, PrPSc is deposited in the central nervous system. These disorders include sporadic, genetic and acquired Creutzfeldt-Jakob disease. The molecular classification of human prion diseases is important in order to understand underlying disease mechanisms and for the development of novel therapy protocols. Current classification systems are based on the assessment of clinical presentation, genetic investigations, neuropathological findings and biochemical analysis of PrPSc." @default.
• W2018428043 created "2016-06-24" @default.
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• W2018428043 date "2007-07-01" @default.
• W2018428043 modified "2023-10-11" @default.
• W2018428043 title "Understanding the natural variability of prion diseases" @default.
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• W2018428043 doi "https://doi.org/10.1016/j.vaccine.2007.02.041" @default.
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