Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

Conspectus Metal ions have been identified as key factors modulating the aggregation of
amyloid-β peptide (Aβ) implicated in Alzheimer's disease (AD). The presence of elevated …

Metal ions, such as copper and zinc ions, have been shown to strongly modulate the self-
assembly of the amyloid-β (Aβ) peptide into insoluble fibrils, and elevated concentrations of …

We report on a concept that some of us first described a decade ago for pure electron
transfer [V. Balland, C. Hureau and J.-M. Savéant, Proc. Natl. Acad. Sci. USA, 2010, 107 …

Metal chelation can provide structural stability and form reactive centers in metalloproteins.
Approximately one third of known protein structures are metalloproteins, and metal binding …

The process of aggregation of proteins and peptides is dependent on the concentration of
proteins, and the rate of aggregation can be altered by the presence of metal ions, but this …

Metal ions are fundamental to guarantee the regular physiological activity of the human
organism. Similarly, vitamins play a key role in many biological functions of the metabolism …

Tau protein is present in significant amounts in neurons, where it contributes to the
stabilization of microtubules. Insoluble neurofibrillary tangles of tau are associated with …

Amyloid fibrils are insoluble, fibrous nanostructures that accumulate extracellularly in
biological tissue during the progression of several human disorders, including Alzheimer's …

In vitro Cu (Aβ1–x)‐induced ROS production has been extensively studied. Conversely, the
ability of N‐truncated isoforms of Aβ to alter the Cu‐induced ROS production has been …