𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Difluoroethylamines as an amide isostere in inhibitors of cathepsin K

✍ Scribed by Elise Isabel; Christophe Mellon; Michael J. Boyd; Nathalie Chauret; Denis Deschênes; Sylvie Desmarais; Jean-Pierre Falgueyret; Jacques Yves Gauthier; Karine Khougaz; Cheuk K. Lau; Serge Léger; Dorothy A. Levorse; Chun Sing Li; Frédéric Massé; M. David Percival; Bruno Roy; John Scheigetz; Michel Thérien; Vouy Linh Truong; Gregg Wesolowski; Robert N. Young; Robert Zamboni; W. Cameron Black

Book ID
104005246
Publisher
Elsevier Science
Year
2011
Tongue
English
Weight
888 KB
Volume
21
Category
Article
ISSN
0960-894X

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Peptide mimetics as enzyme inhibitors: U
Peptide mimetics as enzyme inhibitors: Use of free energy perturbation calculations to evaluate isosteric replacement for amide bonds in a potent HIV protease inhibitor
✍ Piotr Cieplak; Peter A. Kollman 📂 Article 📅 1993 🏛 Springer Netherlands 🌐 English ⚖ 935 KB

We present the application of free energy perturbation theory/molecular dynamics to predict the consequence of replacing each of the seven peptide bonds in the potent HIV protease inhibitor JG365: ACE (acetyl)-Ser-Leu-Asn-HEA (hydroxyethylamine analog of Phe-Pro)-Ile-Val-NME (N-methyl) by ethylene o

Expression of human cathepsin K in Pichi
Expression of human cathepsin K in Pichia pastoris and preliminary crystallographic studies of an inhibitor complex
✍ Christopher J. Linnevers; Mary E. Mcgrath; Andy Armstrong; Firoz R. Mistry; Mich 📂 Article 📅 2008 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 322 KB

## Abstract Cathepsin K is a cysteine protease of the papain family, which is predominantly expressed in osteoclasts, and is regarded as a key protease in bone remodeling. To facilitate structural studies of the protein, the wild‐type sequence of the protease has been mutated so as to replace a pot