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Arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 2: Optimization of P1 and N-aryl

โœ Scribed by Phillip B. Alper; Hong Liu; Arnab K. Chatterjee; KhanhLinh T. Nguyen; David C. Tully; Christine Tumanut; Jun Li; Jennifer L. Harris; Tove Tuntland; Jonathan Chang; Perry Gordon; Thomas Hollenbeck; Donald S. Karanewsky


Book ID
108073910
Publisher
Elsevier Science
Year
2006
Tongue
English
Weight
148 KB
Volume
16
Category
Article
ISSN
0960-894X

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โœ B.J. Goursalin; P. Lachance; P.R. Bonneau; A.C. Storer; H. Kirschke; D. Broemme ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 749 KB

A number of epoxysuccinyl amino acid benzyl esters (HO-Eps-AA-OBzl, 1) in which the amino acid (AA) had been systematically varied were tested as inhibitors of cathepsins \(\mathrm{L}\) and S. These E-64 analogs were designed to investigate whether selectivity for cathepsin \(\mathbf{L}\) or catheps