Key steps in the structure-based optimization of the hepatitis C virus NS3/4A protease inhibitor SCH503034

The structures of both native and S139A holo-HCV NS3/4A protease domain were solved to high resolution. Subsequently, structures were determined for a series of ketoamide inhibitors in complex with the protease. The changes in the inhibitor potency were correlated with changes in the buried surface...

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Detalhes bibliográficos
Main Authors: Madison, Vincent, Prongay, Andrew J., Guo, Zhuyan, Yao, Nanhua, Pichardo, John, Fischmann, Thierry, Strickland, Corey, Myers Jr, Joseph, Weber, Patricia C., Beyer, Brian M., Ingram, Richard, Hong, Zhi, Prosise, Winifred W., Ramanathan, Lata, Taremi, S. Shane, Yarosh-Tomaine, Taisa, Zhang, Rumin, Senior, Mary, Yang, Rong-Sheng, Malcolm, Bruce, Arasappan, Ashok, Bennett, Frank, Bogen, Stephane L., Chen, Kevin, Jao, Edwin, Liu, Yi-Tsung, Lovey, Raymond G., Saksena, Anil K., Venkatraman, Srikanth, Girijavallabhan, Viyyoor, Njoroge, F. George
Formato: Artigo
Idioma:Inglês
Publicado em: International Union of Crystallography 2008
Assuntos:
Diffraction Structural Biology
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2394794/
https://ncbi.nlm.nih.gov/pubmed/18421139
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0909049507064229
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