The misfolding of the cellular prion protein (PrP C) causes fatal neurodegenerative
diseases. Yet PrP C is highly conserved in mammals, suggesting that it exerts beneficial …

Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to
conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer …

Prion diseases are caused by conversion of a normal cell-surface glycoprotein (PrPC) into a
conformationally altered isoform (PrPSc) that is infectious in the absence of nucleic acid …

The protein-only hypothesis posits that the infectious agent causing transmissible
spongiform encephalopathies consists of protein and lacks any informational nucleic acids …

Iron has emerged as a significant cause of neurotoxicity in several neurodegenerative
conditions, including Alzheimer's disease (AD), Parkinson's disease (PD), sporadic …

Reactive oxygen species (ROS) constitute a group of highly reactive molecules that have
evolved as regulators of important signaling pathways. In this context, tumor cells have an …

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

HIV virus particles interact with several receptors on cell surfaces. Two receptors, CD4 and a
co-receptor act sequentially to trigger fusion of viral and cellular membranes and confer …

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 …