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 …

Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

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 …

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 …

Central to the chaperone function of Hsp70s is the transition between open and closed
conformations of their polypeptide substrate binding domain (SBD), which is regulated …

Cellular novelty can emerge when non-functional loci become functional genes in a process
termed de novo gene birth. But how proteins with random amino acid sequences …

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 …

Molecular chaperones assist folding processes and conformational changes in many
proteins. In order to do so, they progress through complex conformational cycles …

The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in
cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE …

SUMMARY α-Crystallins were originally recognized as proteins contributing to the
transparency of the mammalian eye lens. Subsequently, they have been found in many, but …