Metal ions, especially redox active copper, are thought to play critical roles in
neurodegenerative disorders. As a matter of fact, metal binding may result into severe …

The review describes the stability and the coordination modes of Cu2+ complexes with
different regions of N-terminus prion proteins. The structural features of the different metal …

X-ray absorption spectroscopy data show different metal binding site structures in β-amyloid
peptides according to whether they are complexed with Cu 2+ or Zn 2+ ions. While the …

There has been an enormous body of literature published in the last 10 years concerning
copper and PrP (prion protein). Despite this, there is still no generally accepted role for …

Abnormal structural changes of the prion protein (PrP) are the cause of prion disease in a
wide range of mammals. However, spontaneous infected cases have not been reported in …

The aim of this review is to show how the challenging problem of understanding the physico-
chemical basis of protein misfolding and aggregation which are at the origin of plaque …

Background Prion diseases are zoonotic diseases with a broad infection spectrum among
mammalian hosts and are caused by the misfolded prion protein (PrP Sc) derived from the …

Prion protein (PrP) misfolding is one of the pivotal issues in understanding the rudiments of
neurodegenerative disorders. The conformational change of mammalian cellular PrP to …

Background Prion diseases have been extensively reported in various mammalian species
and are caused by a pathogenic prion protein (PrPSc), which is a misfolded version of …

The cellular prion protein (PrP C) is a Cu 2+ binding protein connected to the outer cell
membrane. The molecular features of the Cu 2+ binding sites have been investigated and …