NR ARTS
AU Tatzelt,J.; Winklhofer,K.F.
TI Folding and misfolding of the prion protein in the secretory pathway
QU Amyloid 2004 Sep; 11(3): 162-72
PT journal article; review; review, tutorial
AB A hallmark of prion diseases in humans and animals is the conversion of the cellular prion protein PrPc to a pathogenic isoform, denoted PrPsc. PrPsc is characterized by distinct biochemical and biophysical properties; in addition, it is the major component of infectious prions. All available data indicate that the only difference between PrPc and PrPsc resides in their conformation, emphasizing a critical role of protein folding in the pathogenesis of prion diseases.
ZR 113
MH Animals; Humans; PrPc Proteins/genetics/*secretion; PrPsc Proteins/genetics/*secretion; Prion Diseases/genetics/metabolism/pathology; *Protein Folding; Protein Transport/genetics/physiology; Research Support, Non-U.S. Gov't
AD Department of Cellular Biochemistry, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany. tatzelt@biochem.mpg.de
SP englisch
PO USA