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Journal Abstract Search

298 related items for PubMed ID: 11054292

  • 1. Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model.
    Wang W, Kollman PA.
    J Mol Biol; 2000 Nov 03; 303(4):567-82. PubMed ID: 11054292
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  • 2. Autoprocessing of HIV-1 protease is tightly coupled to protein folding.
    Louis JM, Clore GM, Gronenborn AM.
    Nat Struct Biol; 1999 Sep 03; 6(9):868-75. PubMed ID: 10467100
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  • 3. Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants.
    Kozísek M, Bray J, Rezácová P, Sasková K, Brynda J, Pokorná J, Mammano F, Rulísek L, Konvalinka J.
    J Mol Biol; 2007 Dec 07; 374(4):1005-16. PubMed ID: 17977555
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  • 4. Some insights into mechanism for binding and drug resistance of wild type and I50V V82A and I84V mutations in HIV-1 protease with GRL-98065 inhibitor from molecular dynamic simulations.
    Hu GD, Zhu T, Zhang SL, Wang D, Zhang QG.
    Eur J Med Chem; 2010 Jan 07; 45(1):227-35. PubMed ID: 19910081
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  • 5. Disruption of the HIV-1 protease dimer with interface peptides: structural studies using NMR spectroscopy combined with [2-(13)C]-Trp selective labeling.
    Frutos S, Rodriguez-Mias RA, Madurga S, Collinet B, Reboud-Ravaux M, Ludevid D, Giralt E.
    Biopolymers; 2007 Jan 07; 88(2):164-73. PubMed ID: 17236209
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  • 7. The folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations.
    Levy Y, Caflisch A, Onuchic JN, Wolynes PG.
    J Mol Biol; 2004 Jun 25; 340(1):67-79. PubMed ID: 15184023
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  • 8. 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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  • 9. Structure, dynamics and solvation of HIV-1 protease/saquinavir complex in aqueous solution and their contributions to drug resistance: molecular dynamic simulations.
    Wittayanarakul K, Aruksakunwong O, Sompornpisut P, Sanghiran-Lee V, Parasuk V, Pinitglang S, Hannongbua S.
    J Chem Inf Model; 2005 Mar 22; 45(2):300-8. PubMed ID: 15807491
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  • 10. An alternative strategy for inhibiting multidrug-resistant mutants of the dimeric HIV-1 protease by targeting the subunit interface.
    Bannwarth L, Reboud-Ravaux M.
    Biochem Soc Trans; 2007 Jun 22; 35(Pt 3):551-4. PubMed ID: 17511649
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  • 11. A molecular dynamics study comparing a wild-type with a multiple drug resistant HIV protease: differences in flap and aspartate 25 cavity dimensions.
    Seibold SA, Cukier RI.
    Proteins; 2007 Nov 15; 69(3):551-65. PubMed ID: 17623840
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  • 13. Systematic mutational analysis of the active-site threonine of HIV-1 proteinase: rethinking the "fireman's grip" hypothesis.
    Strisovsky K, Tessmer U, Langner J, Konvalinka J, Kräusslich HG.
    Protein Sci; 2000 Sep 15; 9(9):1631-41. PubMed ID: 11045610
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  • 15. Efficiency of a second-generation HIV-1 protease inhibitor studied by molecular dynamics and absolute binding free energy calculations.
    Lepsík M, Kríz Z, Havlas Z.
    Proteins; 2004 Nov 01; 57(2):279-93. PubMed ID: 15340915
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  • 20. Effect of mutations on the dimer stability and the pH optimum of the human foamy virus protease.
    Sperka T, Boross P, Eizert H, Tözsér J, Bagossi P.
    Protein Eng Des Sel; 2006 Aug 01; 19(8):369-75. PubMed ID: 16799151
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