NR ARAA
AU Deignan,M.E.; Prior,M.; Stuart,L.E.; Comerford,E.J.; McMahon,H.E.
TI The structure function relationship for the Prion protein
QU Journal of Alzheimer's Disease : JAD 2004 Jun; 6(3): 283-9
PT journal article; review; review, academic
AB Central to Prion diseases is the normal endogenous Prion protein, PrPc. In spite of years of research the exact function of this protein remains enigmatic. Numerous binding partners have been identified for PrPc and due to the presence of a repeated sequence of PHGGGWGQ in the proteins amino-terminus it can bind metal ions. The protein is a complex molecule and each portion of PrPc possesses different roles for function and/ or trafficking. As understanding the role of PrPc is central to these disorders the structure/function relationship will be reviewed here.
ZR 68
MH Biological Transport/physiology; Carrier Proteins/metabolism; Copper/metabolism; Glycosylation; Heat-Shock Proteins/metabolism; Human; Laminin/metabolism; Prion Diseases/*metabolism/physiopathology; Prions/*metabolism; Signal Transduction/physiology; Support, Non-U.S. Gov't
AD Department of Industrial Microbiology, Ardmore House, University College Dublin, Belfield, Dublin 4, Ireland.
SP englisch
PO Niederlande