The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …

Stress proteins (SPs) including heat-shock proteins (HSPs), RNA chaperones, and ER
associated stress proteins are molecular chaperones essential for cellular homeostasis. The …

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

Aging is the leading risk factor for several age-associated diseases such as
neurodegenerative diseases. Understanding the biology of aging mechanisms is essential …

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 …

Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis)
and prevent the accumulation of potentially toxic protein aggregates. This proteostasis …

Abiotic stresses usually cause protein dysfunction. Maintaining proteins in their functional
conformations and preventing the aggregation of non-native proteins are particularly …

Efficient folding of many newly synthesized proteins depends on assistance from molecular
chaperones, which serve to prevent protein misfolding and aggregation in the crowded …