A naturally occurring variant of the human prion protein completely prevents prion disease
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چکیده
منابع مشابه
Human Prion Protein V129 Prevents Expression of Variant CJD Phenotype
Materials and Methods Transgenic mice. Transgenic mice homozygous for a human PrP 129V transgene array and murine PrP null alleles (Prnp) designated Tg(HuPrP129V Prnp)-152 mice (129VV Tg152 mice) and transgenic mice homozygous for a human PrP 129M transgene array and murine PrP null alleles (Prnp) designated Tg(HuPrP129M Prnp)-35 mice (129MM Tg35 mice) have been described previously (S1-S4). In...
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In prion disease, a profound microglial activation that precedes neurodegeneration has been observed in the CNS. It is still not fully elucidated whether microglial activation has beneficial effects in terms of prion clearance or whether microglial cells have a mainly detrimental function through the release of pro-inflammatory cytokines. To date, no disease-modifying therapy exists. Several im...
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Prion protein (PrP) is a required factor for susceptibility to transmissible spongiform encephalopathy or prion diseases. In transgenic mice, expression of prion protein (PrP) from another species often confers susceptibility to prion disease from that donor species. For example, expression of deer or elk PrP in transgenic mice has induced susceptibility to chronic wasting disease (CWD), the pr...
متن کاملA Study on The Effect of Temperature on Human Prion Protein Structure through Molecular Dynamic Simulation
Background & Aims: The normal form of the prion protein is called PrPC and its infectious form is called PrPSc. This protein functions like a crystallized core for the transformation of PrPc into an abnormal PrPSc. The aim of the present study was to investigate the effect of temperature on human prion protein structure through molecular dynamic simulation. Methods: In this research, the GROMAC...
متن کاملAberrant metal binding by prion protein in human prion disease.
Human prion diseases are characterized by the conversion of the normal prion protein (PrP(C)) into a pathogenic isomer (PrP(Sc)). Distinct PrP(Sc) conformers are associated with different subtypes of prion diseases. PrP(C) binds copper and has antioxidation activity. Changes in metal-ion occupancy can lead to significant decline of the antioxidation activity and changes in conformation of the p...
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ژورنال
عنوان ژورنال: Nature
سال: 2015
ISSN: 0028-0836,1476-4687
DOI: 10.1038/nature14510