The accumulation of misfolded proteins in the endoplasmic reticulum (ER) leads to ER
stress, resulting in activation of the unfolded protein response (UPR) that aims to restore …

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 …

The heat shock protein 90 (Hsp90) family consists of four highly conserved isoforms: the
mitochondrial TRAP-1, the endoplasmic reticulum-localised Grp94, and the cytoplasmic …

In the past few decades, the development of heat shock protein 90 (Hsp90) inhibitors for
cancer treatment has not stopped. About twenty compounds have been evaluated in the …

The endoplasmic reticulum (ER) is an essential organelle in eukaryotic cells, responsible for
protein synthesis, folding, sorting, and transportation. ER stress is initiated when the …

As a molecular chaperone, heat shock protein 90 (HSP90) plays important roles in the
folding, stabilization, activation, and degradation of over 500 client proteins, and is …

During tumor development and progression, intrinsic and extrinsic factors trigger
endoplasmic reticulum (ER) stress and the unfolded protein response, resulting in the …

Aging is characterized by progressive decay of biological systems and although it is not
considered a disease, it is one of the main risk factors for chronic diseases and many types …

Heat shock protein 90 (HSP90), a highly conserved member of the heat shock protein family,
regulates various proteins and signaling pathways involved in cancer, making it a promising …

Abstract The Suzuki-Miyaura coupling is a widely used CC bond forming reaction.
Numerous mechanistic studies have enabled the use of low catalyst loadings and broad …