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

With the contribution from more than one hundred CNS neurotrauma experts, this book
provides a comprehensive and up-to-date account on the latest developments in the area of …

Calpain is a ubiquitous calcium-sensitive protease that is essential for normal physiologic
neuronal function. However, alterations in calcium homeostasis lead to persistent …

Similar to neurodegenerative diseases, the concept that tumors are prion like diseases has
been proposed in recent years. p53, the most well-known tumor suppressor, has been …

The molecular basis for neuronal death in prion disease is not established, but putative
pathogenic roles for both disease-related prion protein (PrP Sc) and accumulated cytosolic …

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 …

The conversion of the properly folded prion protein, PrPc, to its misfolded amyloid form,
PrPsc, occurs as the two proteins traffic along the endocytic pathway and PrPc is exposed to …

After signal sequence-dependent targeting to the endoplasmic reticulum (ER), prion protein
(PrP) undergoes several post-translational modifications, including glycosylation, disulfide …

A peptide derived from the N-terminus of the unprocessed bovine prion protein (bPrPp),
incorporating the hydrophobic signal sequence (residues 1–24) and a basic domain …

Inherited prion diseases are linked to mutations in the prion protein (PrP) gene, which favor
conversion of PrP into a conformationally altered, pathogenic isoform. The cellular …