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Prion diseases are fatal neurodegenerative disorders with unique transmissible properties. The infectious and pathological agent is thought to be a misfolded conformer of the prion protein. Little is known about the initial events in prion infection because the infecting prion source has been immunologically indistinguishable from normal cellular prion(More)
Prion diseases are associated with the conversion of cellular prion protein (PrP(C)) to toxic β-sheet isoforms (PrP(Sc)), which are reported to inhibit the ubiquitin-proteasome system (UPS). Accordingly, UPS substrates accumulate in prion-infected mouse brains, suggesting impairment of the 26S proteasome. A direct interaction between its 20S core particle(More)
Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of misfolded prion protein (PrP(Sc)) in the brain. They are caused by the templated misfolding of normal cellular protein, PrP(C), by PrP(Sc). We have recently generated a unique cell system in which epitope-tagged PrP(C) competent to produce bona fide PrP(Sc) is expressed(More)
Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be developed, strategies aimed at stimulating the degradation of PrP(Sc) have shown efficacy in(More)
Prion diseases are a group of fatal neurodegenerative disorders characterised by the accumulation of misfolded prion protein (PrPSc) in the brain. The critical relationship between aberrant protein misfolding and neurotoxicity currently remains unclear. The accumulation of aggregation-prone proteins has been linked to impairment of the ubiquitin–proteasome(More)
Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of misfolded prion protein (PrP Sc) in the brain. They are caused by the templated misfolding of normal cellular protein, PrP C , by PrP Sc. We have recently generated a unique cell system in which epitope-tagged PrP C competent to produce bona fide PrP Sc is expressed in(More)
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Prion diseases are fatal neurodegenerative diseases characterised by the accumulation of misfolded prion protein (PrP Sc) in the brain. They are caused by the templated misfolding of normal cellular protein, PrP C , by PrP Sc. We have recently generated a unique cell system in which epitope-tagged PrP C competent to produce bona fide PrP Sc is expressed in(More)
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