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The amyloidogenic region of the human prion protein contains a high affinity (Met)2(His)2 Cu(I) binding site
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Functional implications of multistage copper binding to the prion protein
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Early Onset Prion Disease from Octarepeat Expansion Correlates with Copper Binding Properties
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Copper binding sites in the C-terminal domain of mouse prion protein: A hybrid (QM/MM) molecular dynamics study
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Pau Bernado et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2007)
Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage
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Structural characterization of β-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro
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Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: Speciation, stability constants and binding details
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Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy
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Rare large scale subdomain motions in prion protein can initiate aggregation
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Aggregation/fibrillogenesis of recombinant human prion protein and Gerstmann-Straussler-Scheinker disease peptides in the presence of metal ions
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BIOCHEMISTRY (2006)
Putative aggregation initiation sites in prion protein
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FEBS LETTERS (2006)
Copper(II) ions potently inhibit purified PrPres amplification
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JOURNAL OF NEUROCHEMISTRY (2006)
High affinity binding between copper and full-length prion protein identified by two different techniques
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Copper(II) interaction with unstructured prion domain outside the octarepeat region:: Speciation, stability, and binding details of copper(II) complexes with PrP106-126 peptides
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INORGANIC CHEMISTRY (2005)
Interfaces and the driving force of hydrophobic assembly
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NATURE (2005)
The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4
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Copper(II) inhibits in vitro conversion of prion protein into amyloid fibrils
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PrPc capping in T cells promotes its association with the lipid raft proteins reggie-1 and reggie-2 and leads to signal transduction
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Copper chelation delays the onset of prion disease
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Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases
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Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy
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Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP - Effect of protein age and deamidation
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JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
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Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
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