Gag-protease coevolution analyses define novel structural surfaces in the HIV-1 matrix and capsid involved in resistance to Protease Inhibitors-Reference-Cited by-同舟云学术

Gag-protease coevolution analyses define novel structural surfaces in the HIV-1 matrix and capsid involved in resistance to Protease Inhibitors

Published:2017-06-16 Issue:1 Volume:7 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Codoñer Francisco M,Peña Ruth,Blanch-Lombarte Oscar,Jimenez-Moyano Esther,Pino Maria,Vollbrecht Thomas,Clotet Bonaventura,Martinez-Picado Javier,Draenert Rika,Prado Julia G.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-017-03260-4.pdf

Reference43 articles.

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2. Santos, J. R. et al. Monotherapy with boosted PIs as an ART simplification strategy in clinical practice. J Antimicrob Chemother 70, 1124–1129 (2015).

3. Pulido, F. et al. Long-term (4 years) efficacy of lopinavir/ritonavir monotherapy for maintenance of HIV suppression. J Antimicrob Chemother 61, 1359–1361 (2008).

4. Fun, A., Wensing, A. M., Verheyen, J. & Nijhuis, M. Human Immunodeficiency Virus Gag and protease: partners in resistance. Retrovirology 9, 63 (2012).

5. van Maarseveen et al. Modulation of HIV-1 Gag NC/p1 cleavage efficiency affects protease inhibitor resistance and viral replicative capacity. Retrovirology 9, 29 (2012).

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