Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

Increasing evidence indicates that reactive oxygen species (ROS), consisting of superoxide,
hydrogen peroxide, and multiple others, do not only cause oxidative stress, but rather may …

Heat shock factors (HSFs) are essential for all organisms to survive exposures to acute
stress. They are best known as inducible transcriptional regulators of genes encoding …

A common need for microbial cells is the ability to respond to potentially toxic environmental
insults. Here we review the progress in understanding the response of the yeast …

The protein components of eukaryotic cells face acute and chronic challenges to their
integrity. Eukaryotic protein homeostasis, or proteostasis, enables healthy cell and …

With the release of the landmark report Toxicity Testing in the 21st Century: A Vision and a
Strategy, the US National Academy of Sciences, in 2007, precipitated a major change in the …

A number of stresses, including nutrient stress, temperature shock, DNA damage, and
hypoxia, can lead to changes in gene expression patterns caused by a general shutdown …

Many diseases appear to be caused by the misregulation of protein maintenance. Such
diseases of protein homeostasis, or “proteostasis,” include loss-of-function diseases (cystic …

Proteins generally must fold into precise three-dimensional conformations to fulfill their
biological functions. In the cell, this fundamental process is aided by molecular chaperones …