The molecular chaperone Hsp90 is highly conserved from bacteria to mammals. In fission
yeast, Hsp90 is essential in many cellular processes and its expression is known to be …

The yeast Hsp26 protein, a conserved a-crystallin small heatshock chaperone, is assembled
in to oligomeric complexes, microscopically visible as distinct cytoplasmic foci. We studied at …

The 70-kDa heat shock proteins, hsp70, are highly conserved among both prokaryotes and
eukaryotes, and function as chaperones in diverse cellular processes. To elucidate the …

TPN (tetrachloroisophthalonitrile) affected the growth in yeastSaccharomyces cerevisiaeand
enhanced the superoxide dismutase and glutathione reductase activity under sublethal …

At the primary structure level, the 90-kDa heat shock protein (HSP90) is composed of three
regions: the N-terminal (Met 1–Arg 400), middle (Glu 401–Lys 615), and C-terminal (Asp …

In the highly concentrated environment of the cell, polypeptide chains are prone to
aggregation during synthesis (as nascent chains await the emergence of the remainder of …

Heat shock protein (Hsp 90) is a highly abundant and critical molecular chaperone that
plays key roles in cellular quality control systems. The Hsp90 mechanism of function has …

To reveal the intracellular localization of Hsp104 in the yeastSaccharomyces
cerevisiaebefore and after heat-shock, we performed immunoelectron microscopy after …

The molecular chaperone Hsp90 (Heat shock protein, 90 kDa) is an abundant and essential
cytosolic protein required for the stability and/or folding of hundreds of client proteins …

Enhanced phenotypic diversity increases a population's likelihood of surviving catastrophic
conditions. Hsp90, an essential molecular chaperone and a central network hub in …