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 …

In the last decade, the molecular chaperone HSP90 has emerged as an important target in
cancer therapeutics and has subsequently become the focus of several drug discovery and …

Exercise benefits the human body in many ways. Irisin is secreted by muscle, increased with
exercise, and conveys physiological benefits, including improved cognition and resistance …

Background Metastasis is a multi-step process that is responsible for the majority of deaths
in cancer patients. Current treatments are not effective in targeting metastasis. The …

Heat shock protein 90-α (Hsp90α) is an intracellular molecular chaperone. However, it can
also be secreted with the underlying regulatory mechanism remaining far from clear. Here …

Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is required for
the stability and function of multiple mutated, chimeric and over‐expressed signaling …

In addition to exerting several essential house-keeping activities in the cell, heat shock
proteins (HSPs) are crucial players in a well-structured molecular program activated in …

The molecular chaperone Hsp90 (heat shock protein 90) is a promising target in cancer
therapy. Preclinical and clinical evaluations of a variety of Hsp90 inhibitors have shown anti …

Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone that maintains function of
numerous intracellular signaling nodes utilized by cancer cells for proliferation and survival …

HSP90 is a ubiquitously expressed molecular chaperone that controls the folding, assembly,
intracellular disposition, and proteolytic turnover of many proteins, most of which are …