The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

The prion protein, PrPC, is a small, cell-surface glycoprotein notable primarily for its critical
role in pathogenesis of the neurodegenerative disorders known as prion diseases. A …

The prion glycoprotein (PrPC) is mostly located at the cell surface, tethered to the plasma
membrane through a glycosyl-phosphatydil inositol (GPI) anchor. Misfolding of PrPC is …

Soluble oligomers of the amyloid-β (Aβ) peptide cause neurotoxicity, synaptic dysfunction,
and memory impairments that underlie Alzheimer disease (AD). The cellular prion protein …

Cellular prion protein (PrP c) undergoes a disintegrin-mediated physiological cleavage,
generating a soluble amino-terminal fragment (N1), the function of which remained …

The prion protein (PrP< sup> C) is highly expressed in the nervous system, and its abnormal
conformer is associated with prion diseases. PrP< sup> C is anchored to cell membranes by …

More than thirty years elapsed since a protein, not yet called p53 at the time, was detected to
bind SV40 during viral infection. Thousands of papers later, p53 evolved as the main tumor …

Ovarian cancers are frequently not diagnosed until advanced stages, resulting in a high
case fatality rate. Because of this, more tumor markers, in addition to CA125, for detecting …

Prion protein (PrPc) was originally viewed solely as being involved in prion disease, but now
several intriguing lines of evidence have emerged indicating that it plays a fundamental role …

The prion protein (PrP C) is a conserved glycosylphosphatidylinositol-anchored cell surface
protein expressed by neurons and other cells. Stress-inducible protein 1 (STI1) binds PrP C …