The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

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 …

Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily
conserved class of proteins that guide the normal folding, intracellular disposition and …

Molecular chaperones are diverse families of multidomain proteins that have evolved to
assist nascent proteins to reach their native fold, protect subunits from heat shock during the …

Nearly 100 proteins are known to be regulated by hsp90. Most of these substrates or “client
proteins” are involved in signal transduction, and they are brought into complex with hsp90 …

The adaptor protein Hop mediates the association of the molecular chaperones Hsp70 and
Hsp90. The TPR1 domain of Hop specifically recognizes the C-terminal heptapeptide of …

Chaperones are central to the proteostasis network (PN) and safeguard the proteome from
misfolding, aggregation, and proteotoxicity. We categorized the human chaperome of 332 …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating
many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 …

Cells are faced with the task of folding thousands of different polypeptides into a wide range
of conformations. For many proteins, the folding process requires the action of molecular …