Response to Ji et al.: why priori diseases are precluded by non-mammals

摘要

Our review article entitled 'Delineating common molecular mechanisms in Alzheimer's and prion diseases' [1] implicated the role of certain conserved residues in both Ap and the prion protein (PrP) that could participate in redox-mediated toxicity by these two proteins. We proposed that, in the case of PrP, the methionine residue at codon 129 of the human sequence could interact with tyrosine residues at position 163 and participate, with the aid of the nearby copper-binding domain, in mediating redox reactions leading to oxidative modification of the protein.