Prion protein interconversions and the transmissible spongiform encephalopathies.
Autocatalytic changes in the conformation and aggregation state of prion protein appear to be fundamental to transmissible spongiform encephalopathies or prion diseases. Here we review the considerable progress that has been made in describing the normal properties of prion protein and the changes that occur during these devastating neurodegenerative diseases.
Horiuchi
M
M
Rocky Mountain Laboratories, NIAID, NIH Hamilton, Montana 59840, USA.
Caughey
B
B
D000818:Animals; D019281:Dimerization; D006801:Humans; D046911:Macromolecular Substances; D008958:Models, Molecular; D009154:Mutation; D018620:PrPSc Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism*; D011328:Prions / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D020836:Protein Structure, Quaternary
D046911:Macromolecular Substances; D018620:PrPSc Proteins; D011328:Prions