ArticleBiophysical journal2005
Comparison of multiple molecular dynamics trajectories calculated for the drug-resistant HIV-1 integrase T66I/M154I catalytic domain.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 46 citations in OpenAlex.
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- In Silico Study Identified Methotrexate Analog as Potential Inhibitor of Drug Resistant Human Dihydrofolate Reductase for Cancer Therapeutics.Molecules (Basel, Switzerland) · 2020Article
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- Binding modes of diketo-acid inhibitors of HIV-1 integrase: a comparative molecular dynamics simulation study.Journal of molecular graphics & modelling · 2011Article
- Effect of raltegravir resistance mutations in HIV-1 integrase on viral fitness.Journal of acquired immune deficiency syndromes (1999) · 2010Article
- Molecular modeling study for interaction between Bacillus subtilis Obg and Nucleotides.PloS one · 2010Article
- Raltegravir: molecular basis of its mechanism of action.European journal of medical research · 2009Review
- Characterizing rare-event property distributions via replicate molecular dynamics simulations of proteins.Journal of molecular modeling · 2009Article
- Exploring the binding of HIV-1 integrase inhibitors by comparative residue interaction analysis (CoRIA).Journal of molecular modeling · 2009Article
- A quantum mechanic/molecular mechanic study of the wild-type and N155S mutant HIV-1 integrase complexed with diketo acid.Biophysical journal · 2008Article
- Hybrid quantum mechanical/molecular mechanical molecular dynamics simulations of HIV-1 integrase/inhibitor complexes.Biophysical journal · 2007Article
- Modeling and simulation of chemomechanics at the cell-matrix interface.Cell adhesion & migrationArticle
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
HIV-1 integrase (IN) is an essential enzyme for the viral replication and an interesting target for the design of new pharmaceuticals for multidrug therapy of AIDS. Single and multiple mutations of IN at residues T66, S153, or M154 confer degrees of resistance to several inhibitors that prevent the enzyme from performing its normal strand transfer activity. Four different conformations of IN were chosen from a prior molecular dynamics (MD) simulation on the modeled IN T66I/M154I catalytic core domain as starting points for additional MD studies. The aim of this article is to understand the dynamic features that may play roles in the catalytic activity of the double mutant enzyme in the absence of any inhibitor. Moreover, we want to verify the influence of using different starting points on the MD trajectories and associated dynamical properties. By comparison of the trajectories obtained from these MD simulations we have demonstrated that the starting point does not affect the conformational space explored by this protein and that the time of the simulation is long enough to achieve convergence for this system.
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