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 …

Cellular redox homeostasis is precisely balanced by generation and elimination of reactive
oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and …

Hsp70 proteins are central components of the cellular network of molecular chaperones and
folding catalysts. They assist a large variety of protein folding processes in the cell by …

An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

▪ Abstract Recent years have witnessed dramatic advances in our understanding of how
newly translated proteins fold in the cell and the contribution of molecular chaperones to this …

The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

▪ Abstract Proteolysis in Escherichia coli serves to rid the cell of abnormal and misfolded
proteins and to limit the time and amounts of availability of critical regulatory proteins. Most …

The rapid yet transient transcriptional activation of heat shock genes is mediated by the
reversible conversion of HSF1 from an inert negatively regulated monomer to a …

It is a general feature of molecular chaperones that they are highly conserved throughout
evolution. Prokaryotic and eukaryotic Hsp70 proteins, for example, are over 50% identical at …

Hsp70 chaperones assist a large variety of protein folding processes within the entire
lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ …