## Abstract __The molecular chaperone Hsp90 is responsible for activation and stabilization of several oncoproteins in cancer cells, and has emerged as an important target in cancer treatment because of this pivotal role. In recent years, interests have arisen around structureβbased design of small
Discovery and Design of Novel HSP90 Inhibitors Using Multiple Fragment-based Design Strategies
β Scribed by Jeffrey R. Huth; Chang Park; Andrew M. Petros; Aaron R. Kunzer; Michael D. Wendt; Xilu Wang; Christopher L. Lynch; Jamey C. Mack; Kerry M. Swift; Russell A. Judge; Jun Chen; Paul L. Richardson; Sha Jin; Stephen K. Tahir; Edward D. Matayoshi; Sarah A. Dorwin; Uri S. Ladror; Jean M. Severin; Karl A. Walter; Diane M. Bartley; Stephen W. Fesik; Steven W. Elmore; Philip J. Hajduk
- Book ID
- 111368439
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 671 KB
- Volume
- 70
- Category
- Article
- ISSN
- 1747-0277
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## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a βFull Textβ option. The original article is trackable v
## Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
A series of novel pyrazole-based lipoprotein-associated phospholipase A 2 (Lp-PLA 2 ) inhibitors have been designed and synthetized by a variety of acetophenones via a 10-step convergent approach. The synthetic approach is carefully optimized, and an unsuccessful alternative route is also discussed.