The new and less toxic protease inhibitor saquinavir-NO maintains anti-HIV-1 properties in vitro indistinguishable from those of the parental compound saquinavir.
Abstract: Mutations resulting in enzymatic inactivation (D25N) and resistance to standard antiretroviral drugs (V82F/I84V) were introduced in order to examine the impact of the enzymatic activity on immunogenicity and the possibility to induce immune responses against drug resistant protease, respectively.
Gender differences in HIV drug resistance mutations and virological outcome.
PMID: 21190485
2011
Journal of women's health (2002)
Abstract: There were no major statistically significant differences in the baseline demographic, clinical, or genotypic characteristics between males and females before GRT except for race, presence of coexisting hepatitis B and C infection, prior diagnosis of tuberculosis, presence of thymidine analogue mutations (TAMs), and protease inhibitor (PI) mutations L90M and I84V (p < 0.05).
The L76V mutation in HIV-1 protease is potentially associated with hypersusceptibility to protease inhibitors Atazanavir and Saquinavir: is there a clinical advantage?
Abstract: During the further development of symmetrically disubstituted 3,4-amino-pyrrolidines as human immunodeficiency virus type 1 protease inhibitors, we discovered that, by modification of the P1/P1' moieties of our lead structure, the activity of the inhibitors towards the active-site mutation Ile84Val was altered, however, not being explainable with the initial underlying structure-activity relationship.
G140S/Q148R and N155H mutations render HIV-2 Integrase resistant to raltegravir whereas Y143C does not.
Result: The two B viruses differed from the EHO reference sequence by identical variations at the following residues: N17G, R34K, S56A, V72I, I84V, A129V, I133V, E146Q, T180V, I201L, L213F, T215A, R224Q, D240E and N270H.
Can linear regression modeling help clinicians in the interpretation of genotypic resistance data? An application to derive a lopinavir-score.
Abstract: A highly DRV-resistant in vitro-selected HIV variant and clinical HIV strains isolated from AIDS patients failing to respond to DRV-containing antiviral regimens typically had the V32I, L33F, I54M, and I84V substitutions in common in protease.
The L76V drug resistance mutation decreases the dimer stability and rate of autoprocessing of HIV-1 protease by reducing internal hydrophobic contacts.
Result: For example, Tm values for ATV resistant mutant I50L/A71V and multi-drug resistant mutant V82F/I84V were both higher than the values observed for PR by 2.2 and 4 C, respectively.
Accurate ensemble molecular dynamics binding free energy ranking of multidrug-resistant HIV-1 proteases.
PMID: 20384328
2010
Journal of chemical information and modeling
Abstract: Multidrug resistance to lopinavir is enthalpically driven and increases through a decrease in the protein-ligand van der Waals interaction, principally due to the V82A/I84V mutation, and an increase in net electrostatic repulsion due to water-mediated disruption of protein-ligand interactions in the catalytic region.
HIV mutation literature information.
PMID: 
2011
Antiviral research
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