has been cited by the following article(s):
[1]
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Natural Polymorphisms D60E and I62V Stabilize a Closed Conformation in HIV-1 Protease in the Absence of an Inhibitor or Substrate
Viruses,
2024
DOI:10.3390/v16020236
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[2]
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Realtime, continuous assessment of complex-mixture protease and protease inhibitor activity
4open,
2022
DOI:10.1051/fopen/2022010
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[3]
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Darunavir-Resistant HIV-1 Protease Constructs Uphold a Conformational Selection Hypothesis for Drug Resistance
Viruses,
2020
DOI:10.3390/v12111275
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[4]
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Pulsed EPR characterization of HIV-1 protease conformational sampling and inhibitor-induced population shifts
Phys. Chem. Chem. Phys.,
2016
DOI:10.1039/C5CP04556H
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[5]
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The Role of Select Subtype Polymorphisms on HIV-1 Protease Conformational Sampling and Dynamics
Journal of Biological Chemistry,
2014
DOI:10.1074/jbc.M114.571836
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[6]
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Inhibitor-Induced Conformational Shifts and Ligand-Exchange Dynamics for HIV-1 Protease Measured by Pulsed EPR and NMR Spectroscopy
The Journal of Physical Chemistry B,
2012
DOI:10.1021/jp308207h
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[7]
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Inhibitor-Induced Conformational Shifts and Ligand-Exchange Dynamics for HIV-1 Protease Measured by Pulsed EPR and NMR Spectroscopy
The Journal of Physical Chemistry B,
2012
DOI:10.1021/jp308207h
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