Despite a large number of antiretroviral drugs targeting HIV-1 protease for inhibition,
mutations in this protein during the course of patient treatment can render them inefficient …

Drug resistance of mutations in HIV-1 protease (PR) badly reduce the efficiency of the
current inhibitors in clinical treatments of AIDS. In this work, molecular dynamics (MD) …

A major problem in the antiretroviral treatment of HIV-infections with protease-inhibitors is
the emergence of resistance, resulting from the occurrence of distinct mutations within the …

Molecular recognition is a highly interdependent process. Subsite couplings within the
active site of proteases are most often revealed through conditional amino acid preferences …

Darunavir (DRV) is a high affinity (4.5× 10− 12 M, Δ G=− 15.2 kcal/mol) HIV-1 protease
inhibitor. Two drug-resistant protease variants FLAP+ (L10I, G48V, I54V, V82A) and ACT …

HIV‐1 protease has been an important drug target for the antiretroviral treatment of HIV
infection. The efficacy of protease drugs is impaired by the rapid emergence of resistant …

Under the selective pressure of therapy, HIV-1 protease mutants resistant to inhibitors
evolve to confer drug resistance. Such mutations can impact both the dynamics and …

Drug resistance is a very important factor contributing to the failure of current HIV therapies.
The ability to understand the resistance mechanism of HIV-protease mutants may be useful …

Drug resistance of mutations in HIV-1 protease (PR) is the most severe challenge to the long-
term efficacy of HIV-1 PR inhibitor in highly active antiretroviral therapy. To elucidate the …

Fully quantum mechanical studies of detailed binding interactions between HIV‐1 protease
and six FDA (Food and Drug Administration)‐approved drugs (saquinavir, indinavir …