757976-25-3Relevant articles and documents
Arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 2: Optimization of P1 and N-aryl
Alper, Phillip B.,Liu, Hong,Chatterjee, Arnab K.,Nguyen, Khanhlinh T.,Tully, David C.,Tumanut, Christine,Li, Jun,Harris, Jennifer L.,Tuntland, Tove,Chang, Jonathan,Gordon, Perry,Hollenbeck, Thomas,Karanewsky, Donald S.
, p. 1486 - 1490 (2007/10/03)
A systematic study of anilines led to the discovery of a metabolically robust fluoroindoline replacement for the alkoxy aniline toxicophore in 1. Investigations of the P1 pocket resulted in the discovery of a wide tolerance of functionality leading to the discovery of 11 as a potent and selective inhibitor of cathepsin S.
Potent and selective cathepsin K inhibitors
Shinozuka, Tsuyoshi,Shimada, Kousei,Matsui, Satoshi,Yamane, Takahiro,Ama, Mayumi,Fukuda, Takeshi,Taki, Motohiko,Takeda, Yuko,Otsuka, Eri,Yamato, Michiko,Mochizuki, Shin-ichi,Ohhata, Keiko,Naito, Satoru
, p. 6789 - 6806 (2007/10/03)
A novel series of cathepsin K inhibitors derived from Novartis compound I is described. Optimization of the P1, P3, and P1′ units led to the identification of 4-aminophenoxyacetic acid 24b with an IC50 value of 4.8 nM, which possessed an excell