title: Hsp104 and prion propagation.
abstract: High-ordered aggregates (amyloids) may disrupt cell functions, cause toxicity at certain conditions and provide a basis for self-perpetuated, protein-based infectious heritable agents (prions). Heat shock proteins acting as molecular chaperones counteract protein aggregation and influence amyloid propagation. The yeast Hsp104/Hsp70/Hsp40 chaperone complex plays a crucial role in interactions with both ordered and unordered aggregates. The main focus of this review will be on the Hsp104 chaperone, a molecular "disaggregase".
authors.affiliation: School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA, USA.
authors.forename: Nina V
authors.initials: NV
authors.lastname: Romanova
authors.forename: Yury O
authors.initials: YO
authors.lastname: Chernoff
mesh_terms: D000682:Amyloid; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000502:physiology*; D011328:Prions / Q000737:chemistry* / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000502:physiology*
chemical_list: D000682:Amyloid; D006360:Heat-Shock Proteins; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae