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126 related items for PubMed ID: 26317593

  • 1. A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.
    Chen J, Wang X, Zhu T, Zhang Q, Zhang JZ.
    J Chem Inf Model; 2015 Sep 28; 55(9):1903-13. PubMed ID: 26317593
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  • 2. A contribution to the drug resistance mechanism of darunavir, amprenavir, indinavir, and saquinavir complexes with HIV-1 protease due to flap mutation I50V: a systematic MM-PBSA and thermodynamic integration study.
    Leonis G, Steinbrecher T, Papadopoulos MG.
    J Chem Inf Model; 2013 Aug 26; 53(8):2141-53. PubMed ID: 23834142
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  • 3. Decoding drug resistant mechanism of V32I, I50V and I84V mutations of HIV-1 protease on amprenavir binding by using molecular dynamics simulations and MM-GBSA calculations.
    Yu YX, Wang W, Sun HB, Zhang LL, Wang LF, Yin YY.
    SAR QSAR Environ Res; 2022 Oct 26; 33(10):805-831. PubMed ID: 36322686
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  • 4. Systematic molecular dynamics, MM-PBSA, and ab initio approaches to the saquinavir resistance mechanism in HIV-1 PR due to 11 double and multiple mutations.
    Tzoupis H, Leonis G, Avramopoulos A, Mavromoustakos T, Papadopoulos MG.
    J Phys Chem B; 2014 Aug 14; 118(32):9538-52. PubMed ID: 25036111
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  • 5. Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir.
    Kar P, Knecht V.
    J Comput Aided Mol Des; 2012 Feb 14; 26(2):215-32. PubMed ID: 22350569
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  • 9. Overcoming drug resistance in HIV-1 chemotherapy: the binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug-resistant mutants of the HIV-1 protease.
    Ohtaka H, Velázquez-Campoy A, Xie D, Freire E.
    Protein Sci; 2002 Aug 14; 11(8):1908-16. PubMed ID: 12142445
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  • 10. Structural and thermodynamic basis of amprenavir/darunavir and atazanavir resistance in HIV-1 protease with mutations at residue 50.
    Mittal S, Bandaranayake RM, King NM, Prabu-Jeyabalan M, Nalam MN, Nalivaika EA, Yilmaz NK, Schiffer CA.
    J Virol; 2013 Apr 14; 87(8):4176-84. PubMed ID: 23365446
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  • 12. Molecular dynamics and free energy studies on the wild-type and double mutant HIV-1 protease complexed with amprenavir and two amprenavir-related inhibitors: mechanism for binding and drug resistance.
    Hou T, Yu R.
    J Med Chem; 2007 Mar 22; 50(6):1177-88. PubMed ID: 17300185
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  • 13. Importance of polar solvation and configurational entropy for design of antiretroviral drugs targeting HIV-1 protease.
    Kar P, Lipowsky R, Knecht V.
    J Phys Chem B; 2013 May 16; 117(19):5793-805. PubMed ID: 23614718
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  • 14. Insights into drug resistance of mutations D30N and I50V to HIV-1 protease inhibitor TMC-114: free energy calculation and molecular dynamic simulation.
    Chen J, Zhang S, Liu X, Zhang Q.
    J Mol Model; 2010 Mar 16; 16(3):459-68. PubMed ID: 19629548
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  • 19. Structural and kinetic analyses of the protease from an amprenavir-resistant human immunodeficiency virus type 1 mutant rendered resistant to saquinavir and resensitized to amprenavir.
    Markland W, Rao BG, Parsons JD, Black J, Zuchowski L, Tisdale M, Tung R.
    J Virol; 2000 Aug 16; 74(16):7636-41. PubMed ID: 10906218
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  • 20. Genotypic and phenotypic cross-resistance patterns to lopinavir and amprenavir in protease inhibitor-experienced patients with HIV viremia.
    Paulsen D, Liao Q, Fusco G, St Clair M, Shaefer M, Ross L.
    AIDS Res Hum Retroviruses; 2002 Sep 20; 18(14):1011-9. PubMed ID: 12396453
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