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Resistance of cell lines to prion toxicity aided by phospho-ERK expression
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Elevated manganese levels in blood and CNS in human prion disease
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Copper(II) inhibits in vitro conformational conversion of ovine prion protein triggered by low pH
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Exposure to low dietary copper or low copper coupled with high dietary manganese for one year does not alter brain prion protein characteristics in the mature cow
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Oral transmissibility of prion disease is enhanced by binding to soil particles
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Elevated manganese levels in blood and central nervous system occur before onset of clinical signs in scrapie and bovine spongiform encephalopathy
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Copper is required for prion protein-associated superoxide dismutase-I activity in Pichia pastoris
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Soluble protein oligomers in neurodegeneration:: lessons from the Alzheimer's amyloid β-peptide
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Real-time kinetics of discontinuous and highly conformational metal-ion binding sites of prion protein
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Effect of copper and manganese on the de novo generation of protease-resistant prion protein in yeast cells
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Copper(II) ions potently inhibit purified PrPres amplification
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Urine from scrapie-infected hamsters comprises low levels of prion infectivity
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Hydrogen peroxide cleavage of the prion protein generates a fragment able to initiate polymerisation of full length prion protein
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Recombinant prion protein does not possess SOD-1 activity
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Copper binding is the governing determinant of prion protein turnover
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Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities
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In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrPSc
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Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(11): NMR and EPR studies
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Role of the prion protein in copper turnover in astrocytes
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Effect of metal ions on de novo aggregation of full-length prion protein
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Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases
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Evidence for assembly of prions with left-handed β3-helices into trimers
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Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein
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Prion protein expression modulates neuronal copper content
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Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein
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No superoxide dismutase activity of cellular prion protein in vivo
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Copper coordination in the full-length, recombinant prion protein
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Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
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Pathway complexity of prion protein assembly into amyloid
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Metal imbalance and compromised antioxidant function are early changes in prion disease
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Antioxidant activity related to copper binding of native prion protein
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Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities
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Aberrant metal binding by prion protein in human prion disease
BS Wong et al.
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Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion
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Location and properties of metal-binding sites on the human prion protein
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Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein
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On the mechanism of α-helix to β-sheet transition in the recombinant prion protein
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Folding of prion protein to its native α-helical conformation is under kinetic control
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Prion protein binds copper within the physiological concentration range
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Hyaluronic acid induces survival and proliferation of human myeloma cells through an interleukin-6-mediated pathway involving the phosphorylation of retinoblastoma protein
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Prion infection impairs the cellular response to oxidative stress
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Copper refolding of prion protein
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Differential contribution of superoxide dismutase activity by prion protein in vivo
BS Wong et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2000)
Brain copper content and cuproenzyme activity do not vary with prion protein expression level
DJ Waggoner et al.
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Consequences of manganese replacement of copper for prion protein function and proteinase resistance
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Ecosystems supporting clusters of sporadic TSEs demonstrate excesses of the radical-generating divalent cation manganese and deficiencies of antioxidant co factors Co, Se, Fe, Zn - Does a foreign cation substitution at prion protein's Cu domain initiate TSE?
M Purdey
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