Cargando…
Drug Resistance Conferred by Mutations Outside the Active Site through Alterations in the Dynamic and Structural Ensemble of HIV-1 Protease
[Image: see text] HIV-1 protease inhibitors are part of the highly active antiretroviral therapy effectively used in the treatment of HIV infection and AIDS. Darunavir (DRV) is the most potent of these inhibitors, soliciting drug resistance only when a complex combination of mutations occur both ins...
Autores principales: | Ragland, Debra A., Nalivaika, Ellen A., Nalam, Madhavi N. L., Prachanronarong, Kristina L., Cao, Hong, Bandaranayake, Rajintha M., Cai, Yufeng, Kurt-Yilmaz, Nese, Schiffer, Celia A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4151706/ https://www.ncbi.nlm.nih.gov/pubmed/25091085 http://dx.doi.org/10.1021/ja504096m |
Ejemplares similares
-
Molecular Basis for Drug Resistance in HIV-1 Protease
por: Ali, Akbar, et al.
Publicado: (2010) -
Interdependence of Inhibitor Recognition in HIV-1
Protease
por: Paulsen, Janet L., et al.
Publicado: (2017) -
Crystal Structure of SARS-CoV-2 Main Protease in Complex with the Non-Covalent Inhibitor ML188
por: Lockbaum, Gordon J., et al.
Publicado: (2021) -
Viral proteases: Structure, mechanism and inhibition
por: Zephyr, Jacqueto, et al.
Publicado: (2021) -
Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 Protease
por: Cai, Yufeng, et al.
Publicado: (2014)