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

摘要：

Our review article entitled Delineating common molecular mechanisms in Alzheimers 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.

作者: Andrew F.Hill Kevin J.Barnham

作者单位: Department of Biochemistry and Molecular Biology, and Bio21 Molecular Science and Biotechnology Inst Department of Pathology, and Bio21 Molecular Science and Biotechnology Institute, The University of

会议类型: 国际会议

会议名称: 第四届国际分子模拟与信息技术应用学术会议(The 4th International Conference of Molecular Simulations and Applied Informatics Technologies)

会议地点: 广州

会议语种:英文

页码: 576-576

在线出版日期: 2008-11-01（万方平台首次上网日期，不代表论文的发表时间）