about
Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion proteinConservation of a glycine-rich region in the prion protein is required for uptake of prion infectivityViral phenotypes and antibody responses in long-term survivors infected with attenuated human immunodeficiency virus type 1 containing deletions in the nef and long terminal repeat regions.Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPres level disparity.Near-infrared fluorescence imaging of apoptotic neuronal cell death in a live animal model of prion diseasePrion protein glycosylation.Prion infection impairs cholesterol metabolism in neuronal cells.Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.PrPC-related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site.Packaging of prions into exosomes is associated with a novel pathway of PrP processing.Residues surrounding the glycosylphosphatidylinositol anchor attachment site of PrP modulate prion infection: insight from the resistance of rabbits to prion disease.Increased proportions of C1 truncated prion protein protect against cellular M1000 prion infection.Optical imaging detects apoptosis in the brain and peripheral organs of prion-infected mice.Dominant roles of the polybasic proline motif and copper in the PrP23-89-mediated stress protection response.Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro.Extended period of asymptomatic prion disease after low dose inoculation: assessment of detection methods and implications for infection control.Gene knockout of tau expression does not contribute to the pathogenesis of prion disease.Blood vessel cell death during prion disease: implications for disease management and infection control.Enzymatic detergent treatment protocol that reduces protease-resistant prion protein load and infectivity from surgical-steel monofilaments contaminated with a human-derived prion strain.Evidence for prion protein expression in enteroglial cells of the myenteric plexus of mouse intestineCorrelative studies support lipid peroxidation is linked to PrPres propagation as an early primary pathogenic event in prion diseasePrion acute synaptotoxicity is largely driven by protease-resistant PrPSc speciesEarly existence and biochemical evolution characterise acutely synaptotoxic PrPScThe role of lipids in α-synuclein misfolding and neurotoxicity.
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description
hulumtuese
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researcher
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ricercatrice
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wetenschapper
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հետազոտող
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name
Victoria A Lawson
@nl
Victoria A Lawson
@sl
Victoria A. Lawson
@de
Victoria A. Lawson
@en
Victoria A. Lawson
@es
type
label
Victoria A Lawson
@nl
Victoria A Lawson
@sl
Victoria A. Lawson
@de
Victoria A. Lawson
@en
Victoria A. Lawson
@es
prefLabel
Victoria A Lawson
@nl
Victoria A Lawson
@sl
Victoria A. Lawson
@de
Victoria A. Lawson
@en
Victoria A. Lawson
@es
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