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 …

A system of endoplasmic reticulum (ER) chaperones has evolved to optimize the output of
properly folded secretory and membrane proteins. An important player in this network is …

The Hsp40, Hsp70, and Hsp90 chaperone families are ancient, highly conserved, and
critical to cellular protein homeostasis. Hsp40 chaperones can transfer their protein clients to …

The polarity of biological mediums controls a host of physiological processes such as
digestion, signaling, transportation, metabolism, and excretion. With the recent widespread …

Heat shock proteins (HSPs) have been implicated in the stimulation and generation of both
innate and adaptive immunity. The ability of HSPs to bind antigenic peptides and deliver …

Heat shock protein gp96 is an endoplasmic reticulum chaperone, belonging to the HSP90
family. The function of gp96 as a molecular chaperone was discovered more than 10 years …

The unique properties of fullerenes have raised the interest of using them for biomedical
applications. Within this framework, the interactions of fullerenes with proteins have been an …

Grp94, the Hsp90 paralog of the endoplasmic reticulum, plays a crucial role in protein
secretion. Like cytoplasmic Hsp90, Grp94 is regulated by nucleotide binding to its N-terminal …

Heat shock proteins (HSPs) are primordial and abundant molecules expressed in all cells.
Publications starting in 1984 have shown that immunization of mice, rats, and frogs with …

Hsp90 and Hsp70 are highly conserved molecular chaperones that promote the proper
folding and activation of substrate proteins that are often referred to as clients. The two …