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lüll New insights into prion structure and toxicity Harris DA; True HLNeuron 2006[May]; 50 (3): 353-7Prion diseases in humans and animals are due to conformational conversion of PrP(C), a cellular glycoprotein of unknown function, into PrP(Sc), 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.|Animals[MESH]|Disease Transmission, Infectious[MESH]|Humans[MESH]|Models, Molecular[MESH]|PrPC Proteins/chemistry/metabolism[MESH]|PrPSc Proteins/chemistry/metabolism/toxicity[MESH]|Prion Diseases/*metabolism/physiopathology[MESH]|Prions/*chemistry/*metabolism/toxicity[MESH]|Protein Folding[MESH]|Protein Structure, Tertiary/physiology[MESH]|Yeasts/genetics/metabolism[MESH] |