Michael R. Scott

TL;DR: This research was supported by grants from the National Institute of Aging and the National institute of Neurologic Diseases and Stroke of the National Institutes of Health, International Human Frontiers of Science Program, and American Health Assistance Foundation, as well as by gifts from the Sherman Fairchild Foundation, Keck Foundation, G. Mathers Foundation, Bernard Osher Foundation, and Centeon.

TL;DR: The results argue that species specificity of scrapie prions resides in the PrP sequence and prion synthesis is initiated by a species-specific interaction between PrPSc in the inoculum and homologous PrPC.

TL;DR: The results demonstrate that PrPSc binds to PrPC in a region delimited by codons 96 to 167, and suggest that PrPC binds protein X through residues near the C-terminus, and argue that a species-specific macromolecule, provisionally designated protein X, participates in prion formation.

TL;DR: The primary structure of PrP encoded by the gene of a healthy animal does not differ from that encoded by a cDNA from a scrapie-infected animal, suggesting that the different properties ofPrP from normal and scrapie -infected brains are due to post-translational events.

TL;DR: Aberrant regulation of protein biogenesis and topology at the endoplasmic reticulum can result in neurodegeneration.