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 …

The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

Safety and efficacy constitute the major criteria governing regulatory approval of any new
drug. The best method to maximize safety and efficacy is to deliver a proven therapeutic …

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

The oncogenic effects of long non-coding RNA (lncRNA) Nicotinamide Nucleotide
Transhydrogenase-antisense RNA1 (NNT-AS1) role in colorectal cancer (CRC) hasn't been …

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 …

The epidermal growth factor family of receptor tyrosine kinases (ErbBs) plays essential roles
in regulating cell proliferation, survival, differentiation and migration. The ErbB receptors …

Summary Heat shock protein 90 (HSP90) is a molecular chaperone that is crucial for the
stability and function of many proteins essential for cell survival. Many oncogenes, including …

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are powerful chaperones. Their
expression is induced in response to a wide variety of physiological and environmental …