NR ACJJ
AU Caughey,B.W.
TI Prion protein interconversions
QU Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 2001 Feb 28; 356(1406): 197-200; discussion 200-2
IA http://www.journals.royalsoc.ac.uk/media/64cr5hurmp7xn2gu8g8h/contributions/k/q/h/a/kqharvxbm4penwgd.pdf
PT journal article; review; review, tutorial
AB The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use of in vitro models to describe how PrP is converted to the disease-associated, protease-resistant form. These models reflect many important biological parameters of TSE diseases and have been used to identify inhibitors of the PrP conversion as lead compounds in the development of anti-TSE drugs.
ZR 42
MH Animal; Cattle; Drug Design; Human; Prion Diseases/*metabolism/transmission; Prions/*chemistry/*metabolism/pathogenicity
AD Laboratory of Persistent Viral Diseases, NIAID/NIH, Rocky Mountain Laboratories, Hamilton, MT 59840, USA. bcaughey@nih.gov
SP englisch
PO England