A conformational change of the prion protein is responsible for a class of neurodegenerative
diseases called the transmissible spongiform encephalopathies that include mad cow …

The transmissible spongiform encephalopathies (TSEs) arise from conversion of the
membrane-bound prion protein from PrPC to PrPSc. Examples of the TSEs include mad cow …

Recent evidence suggests that the prion protein (PrP) is a copper binding protein. The N-
terminal region of human PrP contains four sequential copies of the highly conserved …

The prion protein (PrP) binds divalent copper at physiologically relevant conditions and is
believed to participate in copper regulation or act as a copper-dependent enzyme. Ongoing …

A change of the prion protein conformation results in a class of neurodegenerative diseases
called the transmissible spongiform encephalopathies (like mad cow and Creutzfeld–Jakob …

The prion protein (PrP) binds Cu2+ in its N-terminal octarepeat domain. This unusual
domain is comprised of four or more tandem repeats of the fundamental sequence …

The binding stoichiometry between Cu (II) and the full-length β-amyloid Aβ (1− 42) and the
oxidation state of copper in the resultant complex were determined by electrospray …

An oxygen-rich atmosphere obligated living organisms to cope with reactive oxygen species
(O2−, H2O2, OH·) that were the unavoidable by-products of cellular metabolism. As a redox …

The prion protein (PrP) is a Cu 2+ binding cell surface glycoprotein. There is increasing
evidence that PrP functions as a copper transporter. In addition, strains of prion disease …

The coordination ability of histidine containing peptides towards Cu2+ ion is discussed. The
binding ability of the peptide strongly depends on the position and number of histidine …