Prions are self-templating protein conformers that are naturally transmitted between
individuals and promote phenotypic change. In yeast, prion-encoded phenotypes can be …

Key challenges faced by all cells include how to spatiotemporally organize complex
biochemistry and how to respond to environmental fluctuations. The budding yeast …

Cytoplasmic TDP-43 mislocalization and aggregation is a pathological hallmark of
amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 is an RNA …

Protein amplification techniques exploit the ability of PrP TSE to induce a conformational
change in prion protein (PrP) in a continuous fashion, so that the small amount of PrP TSE …

Exosomes are nanovesicles, generally 50 to 90 nm in diameter, that correspond to the
intraluminal vesicles of the endosomal multivesicular bodies and are secreted upon fusion …

The prion hypothesis is strongly supported by the fact that prion infectivity and the
pathogenic conformer of prion protein (PrP) are simultaneously propagated in vitro by the …

Prions, characterized by self-propagating protease-resistant prion protein (PrP)
conformations, are agents causing prion disease. Recent studies generated several such …

The AAA+ protein disaggregase, Hsp104, increases fitness under stress by reversing stress-
induced protein aggregation. Natural Hsp104 variants might exist with enhanced, selective …

During prion infection, the normal, protease-sensitive conformation of prion protein (PrPC) is
converted via seeded polymerization to an abnormal, infectious conformation with greatly …

The existence of more than 30 strains of transmissible spongiform encephalopathy (TSE)
and the paucity of infectivity of purified PrP Sc, as well as considerations of PrP structure, are …