نتایج جستجو برای: human prion protein
تعداد نتایج: 2481093 فیلتر نتایج به سال:
Inherited prion diseases are neurodegenerative disorders caused by autosomal dominant mutations in the human prion protein gene (PRNP). Kindred with inherited prion disease can show remarkable phenotypic variability that has yet to be explained. Here we report analysis of protease resistant disease-related prion protein (PrP(Sc)) isoforms from a range of inherited prion disease cases (point mut...
Mutation in the prion gene, PRNP, accounts for approx. 10-15% of human prion diseases. However, little is known about the mechanisms by which a mutant prion protein (PrP) causes disease. We compared the biochemical properties of a wild-type human prion protein, rPrP(C) (recombinant wild-type PrP), which has five octapeptide-repeats, with two recombinant human prion proteins with insertion mutat...
Prion propagation in transmissible spongiform encephalopathies involves the conversion of cellular prion protein, PrP(C), into a pathogenic conformer, PrP(Sc). Hereditary forms of the disease are linked to specific mutations in the gene coding for the prion protein. To gain insight into the molecular basis of these disorders, the solution structure of the familial Creutzfeldt-Jakob disease-rela...
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are infectious fatal neurodegenerative disorders that include a variety of human diseases, such as CreutzfeldtJacob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), kuru and fatal familial insomnia [1, 2]. Mammalian prion protein (PrP) in an abnormal aggregation-prone selfperpetuating (prion) conformation has been...
Prion diseases are fatal neurodegenerative that affect mammals, including humans. The hallmark of prion is the protein: misfolded and aggregated form protein PrPSc binds to cellular PrPC induces conformational conversion. Although gene polymorphisms correlate with varying degrees susceptibility host develop diseases, how residue substitutions modulate structural dynamics towards pathological mi...
Significance We present evidence that alleviating nitrergic stress during early phases of neurodegeneration reduces neuroinflammatory posttranslational nitric oxide signaling and glycation-assisted dysfunction in the hippocampus prion-diseased mice, a mechanism which might be applicable to other protein-misfolding neurodegenerative conditions. confirmed pharmacological suppression activity form...
Misfolding and subsequent aggregation of endogenous proteins constitute essential steps in many human disorders, including Alzheimer and prion diseases. In most prion protein-folding studies, the posttranslational modifications, the lipid anchor in particular, were lacking. Here, we studied a fully posttranslationally modified cellular prion protein, carrying two N-glycosylations and the natura...
Transgenic (Tg) mice expressing human (Hu) and chimeric prion protein (PrP) genes were inoculated with brain extracts from humans with inherited or sporadic prion disease to investigate the mechanism by which PrPC is transformed into PrPSc. Although Tg(HuPrP) mice expressed high levels of HuPrPC, they were resistant to human prions. They became susceptible to human prions upon ablation of the m...
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