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 …

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 …

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 …

Heat shock protein 90 (Hsp90), one of the most abundant and conserved molecular
chaperones, is essential in eukaryotic cells.[1, 2] Different from other well‑known mo‑lecular …

Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of
numerous client proteins many of which are involved in essential cellular processes like …

The heat shock protein (Hsp) 90 chaperone machinery regulates the activity of hundreds of
client proteins in the eukaryotic cytosol. It undergoes large conformational changes between …

FKBP51 and FKBP52 are diverse regulators of steroid hormone receptor signaling,
including receptor maturation, hormone binding and nuclear translocation. Although …

Among the chaperones and co-chaperones regulating the glucocorticoid receptor (GR),
FK506 binding protein (FKBP) 51 is the most intensely investigated across different …

Hsp90 is an essential molecular chaperone responsible for the folding and activation of
hundreds of 'client'proteins, including the glucocorticoid receptor (GR). Previously, we …

The tetratricopeptide repeat (TPR) motif is one of many repeat motifs that form structural
domains in proteins that can act as interaction scaffolds in the formation of multi-protein …