Abstract Heat shock protein 90 (HSP90) is a chaperone with vital roles in regulating
proteostasis, long recognized for its function in protein folding and maturation. A view is …

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 …

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 …

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 …

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 …

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of
disparate client proteins. This implicates Hsp90 in diverse biological processes that require …

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 …

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 …

Hsp90 (heat shock protein of 90 kDa) is a ubiquitous molecular chaperone responsible for
the assembly and regulation of many eukaryotic signalling systems and is an emerging …