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Evolution of inhibitor-resistant natural mutant forms of HIV-1 protease probed by pre-steady state kinetic analysis

Research output: Contribution to journal › Article › peer-review

DOI

https://doi.org/10.1016/j.biochi.2017.08.014
Final published version

Maria Yu Zakharova
Alexandra A. Kuznetsova
Elena N. Kaliberda
Maria A. Dronina
Alexander V. Kolesnikov
Arina V. Kozyr
Ivan V. Smirnov
Lev D. Rumsh
Olga S. Fedorova
Dmitry G. Knorre
Alexander G. Gabibov
Nikita A. Kuznetsov

Original language	English
Pages (from-to)	125-134
Number of pages	10
Journal	Biochimie
Volume	142
DOIs	https://doi.org/10.1016/j.biochi.2017.08.014
Publication status	Published - 1 Nov 2017

OECD FOS+WOS

Research areas

Active site evolution, Enzyme-substrate interaction, FRET, HIV-1 protease, Mechanism of protease action, Multidrug-resistant mutant, Pre-steady state kinetics, Stopped-flow analysis, RECOGNITION, MECHANISM, DRUG-RESISTANCE, CONFORMATION, SITES, MUTATIONS, BINDING, REVEALS

ID: 8681233