The α-crystallin-related, small heat shock proteins (smHSPs) are ubiquitous in nature, but
are unusually abundant and diverse in higher plants as opposed to other eukaryotes. The …

Protein folding in vivo is mediated by an array of proteins that act either as 'foldases' or
'molecular chaperones'. Foldases include protein disulfide isomerase and peptidyl prolyl …

DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote
protein folding, interaction, and translocation, both constitutively and in response to stress …

Many bacteria live only within animal cells and infect hosts through cytoplasmic inheritance.
These endosymbiotic lineages show distinctive population structure, with small population …

Insoluble, inactive inclusion bodies are frequently formed upon recombinant protein
production in transformed microorganisms. These inclusion bodies, which contain the …

Most major systems that transport proteins across a membrane share the following features:
an amino-terminal transient signal sequence on the transported protein, a targeting system …

The properties of molecular chaperones in protein‐assisted refolding were examined in vitro
using recombinant human cytosolic chaperones hsp90, hsc70, hsp70 and hdj‐1, and …

It has recently been recognized that cellular stresses activate certain members of the
mitogen-activated protein kinase (MAPK) superfamily. One role of these “stress-activated” …

Molecular chaperones are a set of conserved protein families that share the remarkable
ability to recognize and selectively bind nonnative proteins under physiological and stress …

The effects of the human DnaJ homolog, Hsp40, on the ATPase and chaperone functions of
the constitutively expressed Hsp70 homolog, Hsc70, were analyzed. Hsp40 stimulates the …