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Journal Abstract Search


268 related items for PubMed ID: 8841113

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  • 6. Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272.
    Wang YX, Freedberg DI, Yamazaki T, Wingfield PT, Stahl SJ, Kaufman JD, Kiso Y, Torchia DA.
    Biochemistry; 1996 Aug 06; 35(31):9945-50. PubMed ID: 8756455
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  • 9. Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex.
    Brynda J, Rezácová P, Fábry M, Horejsí M, Stouracová R, Soucek M, Hradílek M, Konvalinka J, Sedlácek J.
    Acta Crystallogr D Biol Crystallogr; 2004 Nov 06; 60(Pt 11):1943-8. PubMed ID: 15502300
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  • 10. Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy.
    Yamazaki T, Hinck AP, Wang YX, Nicholson LK, Torchia DA, Wingfield P, Stahl SJ, Kaufman JD, Chang CH, Domaille PJ, Lam PY.
    Protein Sci; 1996 Mar 06; 5(3):495-506. PubMed ID: 8868486
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  • 12. 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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  • 17. Structural and dynamical properties of different protonated states of mutant HIV-1 protease complexed with the saquinavir inhibitor studied by molecular dynamics simulations.
    Aruksakunwong O, Wittayanarakul K, Sompornpisut P, Sanghiran V, Parasuk V, Hannongbua S.
    J Mol Graph Model; 2006 Nov 15; 25(3):324-32. PubMed ID: 16504560
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  • 19. Comparative studies on inhibitors of HIV protease: a target for drug design.
    Jayaraman S, Shah K.
    In Silico Biol; 2008 Nov 15; 8(5-6):427-47. PubMed ID: 19374129
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