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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 [Abstract] [Full Text] [Related]
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 [Abstract] [Full Text] [Related]
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 [Abstract] [Full Text] [Related]
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