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

Amyloidogenesis is a characteristic feature of the 40 or so known protein deposition
diseases, and accumulating evidence strongly suggests that self-association of misfolded …

The pathogenesis of transmissible encephalopathies is associated with the conversion of
the cellular prion protein, PrP C, into a conformationally altered oligomeric form, PrP Sc …

Soluble oligomers of Aβ42 peptide are believed to play a major role in the pathogenesis of
Alzheimer disease (AD). It was recently found that at least some of the neurotoxic effects of …

The prion (infectious protein) concept has evolved with the discovery of new self-
propagating protein states in organisms as diverse as mammals and fungi. The infectious …

The mode of internalization of glycosylphosphatidylinositol‐anchored proteins, lacking any
cytoplasmic domain by which to engage adaptors to recruit them into coated pits, is …

Structural transition of polypeptide chains into the β-sheet state followed by amyloid fibril
formation is the key characteristic of a number of the so-called conformational diseases. The …

▪ Abstract Medical genetics so far has identified∼ 16,000 missense mutations leading to
single amino acid changes in protein sequences that are linked to human disease. A …

Transmissible spongiform encephalopathies (TSEs) are a group of neurodegenerative
diseases that are associated with the conformational conversion of a normal prion protein …

Spongiform encephalopathies are believed to be transmitted by self-perpetuating
conformational conversion of the prion protein. It was shown recently that fundamental …