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Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.
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Kinetic intermediate in the folding of human prion protein.
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Cellular cholesterol enrichment prevents prion peptide-induced neuron cell damages.
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Reactive Sterol Electrophiles: Mechanisms of Formation and Reactions with Proteins and Amino Acid Nucleophiles.
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Biochemical properties of cholesterol aldehyde secosterol and its derivatives.
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New views on cellular uptake and trafficking of manufactured nanoparticles.
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Cholesterol secosterol aldehydes induce amyloidogenesis and dysfunction of wild-type tumor protein p53.
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Adduction of cholesterol 5,6-secosterol aldehyde to membrane-bound myelin basic protein exposes an immunodominant epitope.
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Lipid-derived aldehydes accelerate light chain amyloid and amorphous aggregation.
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Small molecule oxidation products trigger disease-associated protein misfolding.
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The role of rafts in the fibrillization and aggregation of prions.
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Chronic lymphocytic inflammation specifies the organ tropism of prions.
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Metabolite-initiated protein misfolding may trigger Alzheimer's disease.
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Evidence for ozone formation in human atherosclerotic arteries.
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Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.
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