Protein–protein interactions (PPIs) have pivotal roles in life processes. The studies showed
that aberrant PPIs are associated with various diseases, including cancer, infectious …

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 …

A fundamental assumption in statistical physics is that generic closed quantum many-body
systems thermalize under their own dynamics. Recently, the emergence of many-body …

The Hsp90 molecular chaperone and its Cdc37 cochaperone help stabilize and activate
more than half of the human kinome. However, both the mechanism by which these …

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 …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

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 …

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 …