NR AIWK
AU Nicotera,P.
TI A route for prion neuroinvasion
QU Neuron 2001 Aug 16; 31(3): 345-8
PT journal article; review; review, tutorial
AB The astonishing recognition that self-propagating changes in protein structure may be at the basis of spongiform encephalopathies is changing our views of transmissible diseases. Infectious agents consisting of abnormally folded proteins (i.e., the prion) can propagate in host organisms using previously unrecognized routes and invade the brain after a dangerous liaison with the immune system. The identification of the nodal points of neuroinvasion and new techniques to amplify minute amounts of misfolded proteins may open the possibility for post exposure prophylaxis.
ZR 22
MH Animal; Blood-Brain Barrier; Brain/pathology/*physiology/physiopathology; Human; Prion Diseases/pathology/*physiopathology; Prions/*pathogenicity/physiology; Protein Folding
AD MRC Toxicology Unit, Hodgkin Building, University of Leicester, Lancaster Road, LE1 9HN, Leicester, United Kingdom. pn10@le.ac.uk
SP englisch
PO USA