The number of yeast prions and prion-like proteins described since 1994 has grown from
two to nearly twenty. If in the early years most scientists working with the classic mammalian …

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 …

Protein self-assemblies modulate protein activities over biological timescales that can
exceed the lifetimes of the proteins or even the cells that harbor them. We hypothesized that …

Structural differences of lysozyme amyloid fibrils prepared under different conditions were
examined with the use of electron microscopy, CD spectroscopy together with a specially …

Motivation Numerous experimental studies have suggested that polypeptide chains of large
amyloidogenic regions zig-zag in β-serpentine arrangements. These β-serpentines are …

Multiple yeast prions have been identified that result from the structural conversion of
proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires …

Yeast [PSI+] prion is one of the most suitable and well characterized system for the
investigation of the prion phenomenon. However, until recently, the lack of data on the 3D …

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 …

Prions are a group of proteins that can adopt a spectrum of metastable conformations in
vivo. These alternative states change protein function and are self-replicating and …

The yeast Sup35 protein is a subunit of the translation termination factor, and its conversion
to the [PSI+] prion state leads to more translational read-through. Although extensive studies …