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- Publisher
- Springer Journals
- Copyright
- Copyright © 2015 by The Pharmaceutical Society of Korea
- Subject
- Pharmacy; Pharmacy; Pharmacology/Toxicology
- ISSN
- 0253-6269
- eISSN
- 1976-3786
- DOI
- 10.1007/s12272-015-0595-6
- pmid
- 25855012
- Publisher site
- See Article on Publisher Site
Abstract
Heat shock protein 90 (Hsp90) is a ATP dependent molecular chaperone and has emerged as an attractive therapeutic target in the war on cancer due to its role in regulating maturation and stabilization of numerous oncogenic proteins. In this study, we discovered that 2′,4′-dimethoxychalcone ( 1b ) disrupted Hsp90 chaperoning function and inhibited the growth of iressa-resistant non-small cell lung cancer (NSCLC, H1975). The result suggested that 2′,4′-dimethoxychalcone ( 1b ) could serve as a potential therapeutic lead to circumvent the drug resistance acquired by EGFR mutation and Met amplification.
Journal
Archives of Pharmacal Research – Springer Journals
Published: Oct 1, 2015