NR AUTX
AU Harris,D.A.; True,H.L.
TI New insights into prion structure and toxicity
QU Neuron 2006 May 4; 50(3): 353-7
PT journal article; review
AB Prion diseases in humans and animals are due to conformational conversion of PrPc, a cellular glycoprotein of unknown function, into PrPsc, an isoform that appears to be infectious in the absence of nucleic acids. Proteins that behave as prions are also found in yeast and filamentous fungi. Although there is now strong experimental support for the hypothesis that prions are infectious proteins, two subjects have remained poorly understood: the structure of prions, and the mechanisms by which they kill neurons. In this review, we will highlight recent studies that shed new light on these important issues.
ZR 32
MH Animals; Disease Transmission; Humans; Models, Molecular; PrPc Proteins/chemistry/metabolism; PrPsc Proteins/chemistry/metabolism/toxicity; Prion Diseases/*metabolism/physiopathology; Prions/*chemistry/*metabolism/toxicity; Protein Folding; Protein Structure, Tertiary/physiology; Yeasts/genetics/metabolism
AD Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA
SP englisch
PO USA