The concept of a prion as an infectious self-propagating protein isoform was initially
proposed to explain certain mammalian diseases. It is now clear that yeast also has …

[Het-s] is a prion from the filamentous fungus Podospora anserina and corresponds to a self-
perpetuating amyloid aggregate of the HET-s protein. This prion protein is involved in a …

Hsp100 and Hsp70 chaperones in bacteria, yeast, and plants cooperate to reactivate
aggregated proteins. Disaggregation relies on Hsp70 function and on ATP-dependent …

Prions containing misfolded prion protein (PrPSc) can be formed with cofactor molecules
using the technique of serial protein misfolding cyclic amplification. However, it remains …

The mouse cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is a
translational regulator implicated in long-term memory maintenance. Invertebrate orthologs …

Yeast prions are self-perpetuating, QN-rich amyloids that control heritable traits and serve as
a model for mammalian amyloidoses. De novo prion formation by overproduced prion …

Amyloids are fibrous cross-β protein aggregates that are capable of proliferation via
nucleated polymerization. Amyloid conformation likely represents an ancient protein fold …

Tia1/Pub1 is a stress granule component carrying a Q/N-rich prion domain. We provide
direct evidence that Tia1 forms a prion in yeast. Moreover, Tia1/Pub1 acts cooperatively with …

Many neurodegenerative diseases including amyotrophic lateral sclerosis (ALS) are linked
to the accumulation of specific protein aggregates in affected regions of the nervous system …

Prions are self-perpetuating protein isoforms that cause fatal and incurable
neurodegenerative disease in mammals. Recent evidence indicates that a majority of …