Hsp90 is a conserved and essential molecular chaperone responsible for the folding and
activation of hundreds of 'client'proteins,–. The glucocorticoid receptor (GR) is a model client …

Mitochondrial complex II is traditionally studied for its participation in two key respiratory
processes: the electron transport chain and the Krebs cycle. There is now a rich body of …

The major classes of molecular chaperones have highly variable sequences, sizes, and
shapes, yet they all bind to unfolded proteins, limit their aggregation, and assist in their …

Mitochondrial function is dependent on molecular chaperones, primarily due to their
necessity in the formation of respiratory complexes and clearance of misfolded proteins …

Hsp90 isoform-selective inhibitors represent a new paradigm for novel anti-cancer drugs as
each of the four isoforms have specific cellular localization, function, and client proteins. The …

TRAP1, the mitochondrial component of the Hsp90 family of molecular chaperones, displays
important bioenergetic and proteostatic functions. In tumor cells, TRAP1 contributes to shape …

Protein-assembly defects due to an enrichment of aberrant conformational protein variants
are emerging as a new frontier in therapeutics design. Understanding the structural …

The Hsp90 chaperone machinery plays a crucial role in maintaining cellular homeostasis.
Beyond its traditional role in protein folding, Hsp90 is integral to key pathways influencing …

Fluctuations in nutrient and biomass availability, often as a result of disease, impart
metabolic challenges that must be overcome in order to sustain cell survival and promote …

Tumor necrosis factor receptor-associated protein 1 (TRAP1) is a mitochondrial molecular
chaperone modulating cellular metabolism and signaling pathways by altering the …