Heat shock protein 90 (HSP90) is a vital chaperone protein, regulating signaling pathways
and correcting misfolded proteins in cancer cells by interacting with oncogenic client …

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 …

Cancer cells continuously rewire their metabolism to fulfill their need for rapid growth and
survival while subject to changes in environmental cues. Thus, a vital component of a cancer …

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 …

Mitochondrial metabolism must constantly adapt to stress conditions in order to maintain
bioenergetic levels related to cellular functions. This absence of proper adaptation can be …

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 …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that ensures cellular
proteostasis by maintaining the folding, stabilization, activation, and degradation of over 400 …

Heat shock proteins (HSPs) are a large family of molecular chaperones aberrantly
expressed in cancer. The expression of HSPs in tumor cells has been shown to be …

Cancer metabolism is an essential aspect of tumorigenesis, as cancer cells have increased
energy requirements in comparison to normal cells. Thus, an enhanced metabolism is …