Probing copper/tau protein interactions electrochemically

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Characterisation of gold electrodes modified with self-assembled monolayers of l-cysteine for the adsorptive stripping analysis of copper

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Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State

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Copper and Zinc Binding Modulates the Aggregation and Neurotoxic Properties of the Prion Peptide PrP106−126

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Raman Spectroscopic Study on the Copper(II) Binding Mode of Prion Octapeptide and Its pH Dependence

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Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer?s A? peptides

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A Rapid Label-Free Electrochemical Detection and Kinetic Study of Alzheimer's Amyloid Beta Aggregation

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Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide

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Redox Reactions of Copper Complexes Formed with Different β-Amyloid Peptides and Their Neuropathalogical Relevance

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Low Micromolar Zinc Accelerates the Fibrillization of Human Tau via Bridging of Cys-291 and Cys-322

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Acceleration of Amyloid β-Peptide Aggregation by Physiological Concentrations of Calcium

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Amyloid-β detection with saccharide immobilized gold nanoparticle on carbon electrode

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Electrochemical and homogeneous electron transfers to the Alzheimer amyloid-β copper complex follow a preorganization mechanism

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Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS

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Binding of α-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes

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Structural Characterization of Binding of Cu(II) to Tau Protein

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Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI‐TOF MS, CD, and NMR

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The tangled tale of tau

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Copper Redox Cycling in the Prion Protein Depends Critically on Binding Mode

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Direct electrochemistry of the photosynthetic blue copper protein plastocyanin. Electrostatic promotion of rapid charge transfer at an edge-oriented pyrolytic graphite electrode

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Copper (II) modulates in vitro aggregation of a tau peptide

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Reaction Rates and Mechanism of the Ascorbic Acid Oxidation by Molecular Oxygen Facilitated by Cu(II)-Containing Amyloid-β Complexes and Aggregates

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Hydrogen peroxide can be generated by tau in the presence of Cu(II)

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pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

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Zn2+’s Ability to Alter the Distribution of Cu2+ among the Available Binding Sites of Aβ(1–16)-Polyethylenglycol-ylated Peptide: Implications in Alzheimer’s Disease

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Study of formation of Cu- and Zn-containing tau protein using isotopically-enriched tracers by LA-ICP-MS and MALDI-FTICR-MS

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Insight into Potential Cu(II)-Binding Motifs in the Four Pseudorepeats of Tau Protein

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Rapid label-free detection of metal-induced Alzheimer’s amyloid β peptide aggregation by electrochemical method

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Modeling Copper Binding to the Amyloid-β Peptide at Different pH: Toward a Molecular Mechanism for Cu Reduction

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Electrochemical Oxidation of Benzothiazole Dyes for Monitoring Amyloid Formation Related to the Alzheimer’s Disease

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Electrochemical and Conformational Consequences of Copper (CuI and CuII) Binding to β‐Amyloid(1–40)

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Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: Separation of synthetic prion peptides

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Electrochemical Investigations of Tau Protein Phosphorylations and Interactions with Pin1

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Copper proteins immobilised on gold electrodes for (bio)analytical studies

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Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

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The metal ion hypothesis of Alzheimer’s disease and the anti-neuroinflammatory effect of metal chelators

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Modulation of tau phosphorylation by environmental copper

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tau protein hyperphosphorylation and Alzheimer’s disease

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Hyperphosphorylation of tau and protein phosphatases in Alzheimer disease.

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FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

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Lead exposure and tau hyperphosphorylation: An in vitro study

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