Copper is too redox active to exist in an unbound form in the cell without causing oxidative
damage: an upper limit of 10-18 M for the free concentration of Cu (II) in unstressed cells has …

The variety of factors and events involved in neurodegeneration renders the subject a major
challenge. Neurodegenerative disorders include a number of different pathological …

In the 20 years, since the introduction of electrospray mass spectrometry (ESI‐MS), the use
of this technique in various fields of inorganic, organometallic, and analytical chemistry has …

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 …

Protein misfolding and conformational changes are a cornerstone of neurodegenerative
diseases involving formation and deposition of toxic protein oligomers. Although mutations …

The prion protein (PrP) is a Cu 2+ binding cell surface glycoprotein that can misfold into a β-
sheet-rich conformation to cause prion diseases. The majority of copper binding studies …

Prion, or PrPSc, is the pathological isoform of the cellular prion protein (PrPC) and it is the
etiological agent of transmissible spongiform encephalopathies (TSE) affecting humans and …

Protein and peptide assembly into amyloid has been implicated in functions that range from
beneficial epigenetic controls to pathological etiologies. However, the exact structures of the …

Amyloids are protein aggregates bearing a highly ordered cross β structural motif, which
may be functional but are mostly pathogenic. Their formation, deposition in tissues and …

The cellular prion protein is known to be a copper-binding protein. Despite the wide range of
studies on the copper binding of PrP, there have been no studies to determine the affinity of …