Conformational variations in an infectious protein determine prion strain differences

By Motomasa Tanaka, Peter Chien, N. Naber, R. Cooke, Jonathan S. Weissman. Nature, 2004

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Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs (2004, background): “Moreover, the altered phenotypes are transferable from mother to daughter cell without any underlying nucleic acid change and, similar to the animal models of prion diseases, the abnormal protein can be isolated and generated in vitro”
In vitro generation of infectious scrapie prions. (2005, background): “Recent studies showed that bacterially produced N-terminal fragments of Sup35p, when transformed into amyloid fibrils, were able to propagate the prion phenotype to yeast cells (King and Diaz-Avalos, 2004; Tanaka et al., 2004).”
What is the role of protein aggregation in neurodegeneration? (2005, background): “For example, in prion disease, different conformations of the abnormally folded monomeric prion protei”
Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis (2019, background): “Several of the fungal prions have been vividly shown to infect in a “protein only” fashion (King and Diaz-Avalos, 2004; Tanaka et al., 2004; Patel and Liebman, 2007).”