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 …

Nearly two decades ago, Xenopus oocytes were found to contain mRNAs harboring a small
sequence in their 3′ untranslated regions that control cytoplasmic polyadenylation and …

Pathogens and cellular danger signals activate sensors such as RIG-I and NLRP3 to
produce robust immune and inflammatory responses through respective adaptor proteins …

Prions are proteins that convert between structurally and functionally distinct states, one or
more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian …

Protein aggregation results in β-sheet–like assemblies that adopt either a variety of
amorphous morphologies or ordered amyloid-like structures. These differences in structure …

Abstract Changes in protein conformation drive most biological processes, but none have
seized the imagination of scientists and the public alike as have the self-replicating …

Prions are proteins that can assume at least two distinct conformational states, one of which
is dominant and self-perpetuating. Previously we found that a translation regulator CPEB …

Abundant nonfibrillar oligomeric intermediates are a common feature of amyloid formation,
and these oligomers, rather than the final fibers, have been suggested to be the toxic …

Self-perpetuating changes in the conformations of amyloidogenic proteins play vital roles in
normal biology and disease. Despite intense research, the architecture and conformational …

Prion conversion from a soluble protein to an aggregated state may be involved in the
cellular adaptation of yeast to the environment. However, it remains unclear whether and …