Design of potent and selective human cathepsin K inhibitors that span the active site

Potent and selective active-site-spanning inhibitors have been designed for cathepsin K, a cysteine protease unique to osteoclasts. They act by mechanisms that involve tight binding intermediates, potentially on a hydrolytic pathway. X-ray crystallographic, MS, NMR spectroscopic, and kinetic studies...

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Главные авторы: Thompson, Scott K., Halbert, Stacie M., Bossard, Mary J., Tomaszek, Thaddeus A., Levy, Mark A., Zhao, Baoguang, Smith, Ward W., Abdel-Meguid, Sherin S., Janson, Cheryl A., D’Alessio, Karla J., McQueney, Michael S., Amegadzie, Bernard Y., Hanning, Charles R., DesJarlais, Renee L., Briand, Jacques, Sarkar, Susanta K., Huddleston, Michael J., Ijames, Carl F., Carr, Steven A., Garnes, Keith T., Shu, Art, Heys, J. Richard, Bradbeer, Jeremy, Zembryki, Denise, Lee-Rykaczewski, Liz, James, Ian E., Lark, Michael W., Drake, Fred H., Gowen, Maxine, Gleason, John G., Veber, Daniel F.
Формат: Artigo
Язык:Inglês
Опубликовано: The National Academy of Sciences of the USA 1997
Предметы:
Physical Sciences
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC24926/
https://ncbi.nlm.nih.gov/pubmed/9405598
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