Discovery of novel celastrol-triazole derivatives with Hsp90-Cdc37 disruption to induce tumor cell apoptosis.
Sign Up to like & getrecommendations! Published in 2021 at "Bioorganic chemistry"
DOI: 10.1016/j.bioorg.2021.104867
Abstract: To enhance the disruption of Hsp90-Cdc37, we designed and synthesized a series (27) of CEL-triazole derivatives. Most of the target compounds showed enhanced anti-proliferative activity on four cancer cell lines (MDA-MB-231, MCF-7, HepG2 and A459).… read more here.
Keywords: triazole derivatives; cell apoptosis; tumor cell; compound ... See more keywords
Discovery of Novel Celastrol-Imidazole Derivatives with Anticancer Activity In Vitro and In Vivo.
Sign Up to like & getrecommendations! Published in 2022 at "Journal of medicinal chemistry"
DOI: 10.1021/acs.jmedchem.1c01293
Abstract: To discover celastrol (CEL) derivatives with enhanced Hsp90-Cdc37 inhibition, C-20-COOH was introduced with various substituted imidazoles, which might affect the Michael addition of CEL by nucleophilic attack. The most potent compound 9, which showed higher… read more here.
Keywords: vivo; hsp90 cdc37; activity; celastrol ... See more keywords
Okicamelliaside targets the N-terminal chaperone pocket of HSP90 disrupts the chaperone protein interaction of HSP90-CDC37 and exerts antitumor activity.
Sign Up to like & getrecommendations! Published in 2021 at "Acta pharmacologica Sinica"
DOI: 10.1038/s41401-021-00737-x
Abstract: Heat shock protein 90 (HSP90) has been recognized as a crucial target in cancer cells. However, various toxic reactions targeting the ATP binding site of HSP90 may not be the best choice for HSP90 inhibitors.… read more here.
Keywords: protein; hsp90; antitumor; chaperone ... See more keywords
Small-molecule inhibitor targeting the Hsp90-Cdc37 protein-protein interaction in colorectal cancer
Sign Up to like & getrecommendations! Published in 2019 at "Science Advances"
DOI: 10.1126/sciadv.aax2277
Abstract: Directly disrupting the Hsp90-Cdc37 complex can selectively down-regulate kinase clients of Hsp90 and achieve cell cycle arrest. Disrupting the interactions between Hsp90 and Cdc37 is emerging as an alternative and specific way to regulate the… read more here.
Keywords: cdc37; small molecule; molecule inhibitor; hsp90 cdc37 ... See more keywords
Medium-Throughput Detection of Hsp90/Cdc37 Protein–Protein Interaction Inhibitors Using a Split Renilla Luciferase-Based Assay
Sign Up to like & getrecommendations! Published in 2019 at "SLAS Discovery"
DOI: 10.1177/2472555219884033
Abstract: The protein-folding chaperone Hsp90 enables the maturation and stability of various oncogenic signaling proteins and is thus pursued as a cancer drug target. Folding in particular of protein kinases is assisted by the co-chaperone Cdc37.… read more here.
Keywords: protein; hsp90; cdc37; renilla luciferase ... See more keywords
Targeting Hsp90-Cdc37: A Promising Therapeutic Strategy by Inhibiting Hsp90 Chaperone Function.
Sign Up to like & getrecommendations! Published in 2017 at "Current drug targets"
DOI: 10.2174/1389450117666160527125522
Abstract: BACKGROUND & OBJECTIVE The Hsp90 chaperone protein regulates the folding, maturation and stability of a wide variety of oncoproteins. In recent years, many Hsp90 inhibitors have entered into the clinical trials while all of them… read more here.
Keywords: hsp90 chaperone; hsp90; targeting hsp90; hsp90 cdc37 ... See more keywords
Elaiophylin Is a Potent Hsp90/ Cdc37 Protein Interface Inhibitor with K-Ras Nanocluster Selectivity
Sign Up to like & getrecommendations! Published in 2021 at "Biomolecules"
DOI: 10.3390/biom11060836
Abstract: The natural product elaiophylin is a macrodiolide with a broad range of biological activities. However, no direct target of elaiophylin in eukaryotes has been described so far, which hinders a systematic explanation of its astonishing… read more here.
Keywords: interface inhibitor; protein interface; hsp90; hsp90 cdc37 ... See more keywords
Novel Small Molecule Hsp90/Cdc37 Interface Inhibitors Indirectly Target K-Ras-Signaling
Sign Up to like & getrecommendations! Published in 2021 at "Cancers"
DOI: 10.3390/cancers13040927
Abstract: Simple Summary The correct folding of proteins is essential for their activity. Therefore, cells have evolved protein-folding chaperones, such as Hsp90. Interestingly, in several cancer cells, Hsp90 appears to have a role that is more… read more here.
Keywords: cancer; hsp90; cdc37 interface; hsp90 cdc37 ... See more keywords