Numerous ATPases associated with diverse cellular activities (AAA+) proteins form
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …

There is a growing body of evidence that prionoid protein behaviors are a core element of
neurodegenerative diseases (NDs) that afflict humans. Common elements in pathogenesis …

FUS and EWSR1 are RNA-binding proteins with prion-like domains (PrLDs) that aggregate
in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). The FUS and …

Amyloid appearance is a rare event that is promoted in the presence of other aggregated
proteins. These aggregates were thought to act by templating the formation of an assembly …

Hsp104 is a hexameric AAA+ ATPase and protein disaggregase found in yeast, which can
be potentiated via mutations in its middle domain (MD) to counter toxic phase separation by …

Prion variants are self-perpetuating conformers of a single protein that assemble into
amyloid fibers and confer unique phenotypic states. Multiple prion variants can arise …

The formation of amyloid fibers is associated with a diverse range of disease and phenotypic
states. These amyloid fibers often assemble into multi-protofibril, high-order architectures in …

Prions are conformationally flexible proteins capable of adopting a native state and a
spectrum of alternative states associated with a change in the function of the protein. These …

Prions of lower eukaryotes are transmissible protein particles that propagate by converting
homotypic soluble proteins into growing protein assemblies. Prion activity is conferred by so …

A number of [PSI+]-no-more (PNM) mutations, eliminating [PSI+] prion, were previously
described in SUP35. In this study, we designed and analyzed a new PNM mutation based …