The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Small-molecule drug discovery has traditionally focused on occupancy of a binding site that
directly affects protein function, and this approach typically precludes targeting proteins that …

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 …

Stress proteins (SPs) including heat-shock proteins (HSPs), RNA chaperones, and ER
associated stress proteins are molecular chaperones essential for cellular homeostasis. The …

The advent of HER2-directed therapies has significantly improved the outlook for patients
with HER2-positive early stage breast cancer. However, a significant proportion of these …

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 …

VCP (also known as p97 or Cdc48p in yeast) is an AAA+ ATPase regulating endoplasmic
reticulum–associated degradation. After high-throughput screening, we developed …

Hsp90 is an ATP dependent molecular chaperone protein which integrates multiple
oncogenic pathways. As such, Hsp90 inhibition is a promising anti-cancer strategy. Several …

Photodynamic therapy (PDT) has emerged as a promising alternative to conventional
cancer therapies such as surgery, chemotherapy, and radiotherapy. PDT comprises the …

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 …