The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

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 …

Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

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

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 …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …

The 70-kDa heat shock protein (HSP70) family of molecular chaperones represents one of
the most ubiquitous classes of chaperones and is highly conserved in all organisms …

The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …