Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation. It also stabilizes a …

HSP90 proteins take part in essential cellular processes and regulatory pathways like apoptosis, cell cycle control, cell viability, protein folding and degradation, and signalling events. In …

Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling …

Apr 21, 2017 · The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells.

Aug 29, 2018 · 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 …

Jul 31, 2023 · We describe how these variations influence context-dependent functions of HSP90 as well as its interaction with other chaperones, co-chaperones and proteins, and how this …

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 ubiquitin …

Heat shock protein 90 (Hsp90) is a predominant member among Heat shock proteins (HSPs), playing a central role in cellular protection and maintenance by aiding in the folding, …

Jun 15, 2023 · The central eukaryotic molecular chaperone Hsp90 physically interacts with a large fraction of the yeast proteome by targeting select intrinsically disordered regions (IDRs) on …

Feb 23, 2017 · HSP90 acts as a protein-folding buffer that shapes the manifestations of genetic variation in model organisms. Whether HSP90 influences the consequences of mutations in …