Susan Lindquist

TL;DR: It is confirmed that ER stress is induced and that caspase-12 is proteolytically processed in a murine model of infectious prion disease, and the survival, behavior, pathology and accumulation of proteinase K-resistant PrP are indistinguishable between casp enzyme-12 knockout and control mice, suggesting that cospase- 12 is not necessary for mediating the neurotoxic effects of prion protein misfolding.

TL;DR: Ste24, an evolutionarily conserved protease that was recently reported to degrade peptides stuck within the translocon between the cytoplasm and the endoplasmic reticulum, was the strongest suppressor of IAPP toxicity.

TL;DR: The ability to correlate multiple alternate b-structures to experiment opens the possibility of computational investigation of prion strains and structural heterogeneity of amyloid, and a new strategy for b-structure prediction is developed.

TL;DR: It is concluded that single codon differences in a single gene in an otherwise normal genome can cause remarkably different neurodegenerative diseases and are sufficient to create distinct protein-based infectious elements.

TL;DR: Yeast [PSI+] prions in the native, hydrated state in situ are examined to suggest these structures constitute a self-organizing mechanism that coordinates fiber deposition and the regulation of prion inheritance.