Cargando…
The role of mutations at codons 32, 47, 54, and 90 in HIV-1 protease flap dynamics
Treatment of Human Immunodeficiency Virus remains challenging due to the emergence of drug resistant strains under the selective pressure produced by standard anti-retroviral therapy. To explore the structural mechanisms of drug resistance, we performed 40 ns molecular dynamics simulations on three...
Autores principales: | Chordia, Poorvi, Dewdney, Tamaria G., Keusch, Bradley, Kuiper, Benjamin D., Ross, Kyla, Kovari, Iulia A., MacArthur, Rodger, Salimnia, Hossein, Kovari, Ladislau C. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Applied Systems srl
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6941557/ https://www.ncbi.nlm.nih.gov/pubmed/32309558 http://dx.doi.org/10.15190/d.2014.19 |
Ejemplares similares
-
The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops
por: Kuiper, Benjamin D., et al.
Publicado: (2015) -
Higher Desolvation Energy Reduces Molecular Recognition in Multi-Drug Resistant HIV-1 Protease
por: Wang, Yong, et al.
Publicado: (2012) -
Status Epilepticus due to Severe HHV-6 Encephalitis in an Allogeneic Stem Cell Transplant Recipient
por: Chordia, Poorvi, et al.
Publicado: (2014) -
GitLab use at CERN: keeping the illusion of a monorepo
por: Kovari, Zsolt
Publicado: (2018) -
New Timing Sequencer Application in Python with Qt - Development Workflow and Lessons Learnt
por: Kovari, Zsolt, et al.
Publicado: (2022)