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

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 …

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 …

Apoptosis is the programmed cell death which maintains the healthy survival/death balance
in metazoan cells. Defect in apoptosis can cause cancer or autoimmunity, while enhanced …

Over the last few decades, computer-aided drug design has emerged as a powerful
technique playing a crucial role in the development of new drug molecules. Structure-based …

Over the past decade, whole genome sequencing and other'omics' technologies have
defined pathogenic driver mutations to which tumor cells are addicted. Such addictions …

Due to its relatively easy synthesis, isoxazole ring has been as an object of interest for
chemists and pharmacologists from research groups all over the world. Its chemical …

Heat shock protein (Hsp) 90 is an ATP-dependent molecular chaperone that is exploited by
malignant cells to support activated oncoproteins, including many cancer-associated …

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