HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …

The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are
involved in myriad cellular processes. Their distribution in various cellular compartments …

Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and
bacteria. They are responsible for the correct protein folding, protection of the cell against …

The glucose-regulated proteins (GRPs) are stress-inducible chaperones that mostly reside
in the endoplasmic reticulum or the mitochondria. Recent advances show that the GRPs …

In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

Proteins that permanently reside in the lumen of the endoplasmic reticulum (ER) must
somehow be distinguished from newly synthesized secretory proteins, which pass through …

The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-
kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major …

Glucose-regulated protein 94 is the HSP90-like protein in the lumen of the endoplasmic
reticulum and therefore it chaperones secreted and membrane proteins. It has essential …

Scanning confocal microscopes offer improved rejection of out-of-focus noise and greater
resolution than conventional imaging. In such a microscope, the imaging and condenser …

The heat shock protein 90 (Hsp90) is a molecular chaperone and a key regulator of
proteostasis under both physiological and stress conditions. In mammals, there are two …