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Journal Abstract Search


84 related items for PubMed ID: 8333844

  • 21. A folding inhibitor of the HIV-1 protease.
    Broglia RA, Provasi D, Vasile F, Ottolina G, Longhi R, Tiana G.
    Proteins; 2006 Mar 01; 62(4):928-33. PubMed ID: 16385559
    [Abstract] [Full Text] [Related]

  • 22. The structural stability of the HIV-1 protease.
    Todd MJ, Semo N, Freire E.
    J Mol Biol; 1998 Oct 23; 283(2):475-88. PubMed ID: 9769219
    [Abstract] [Full Text] [Related]

  • 23. 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 23; 9(9):1631-41. PubMed ID: 11045610
    [Abstract] [Full Text] [Related]

  • 24. The pH-dependent subunit dissociation and catalytic activity of bovine dopamine beta-hydroxylase.
    Saxena A, Hensley P, Osborne JC, Fleming PJ.
    J Biol Chem; 1985 Mar 25; 260(6):3386-92. PubMed ID: 3972830
    [Abstract] [Full Text] [Related]

  • 25. Mechanical effects on the kinetics of the HIV proteinase deactivation.
    Kuzmic P, Peranteau AG, García-Echeverría G, Rich DH.
    Biochem Biophys Res Commun; 1996 Apr 16; 221(2):313-7. PubMed ID: 8619852
    [Abstract] [Full Text] [Related]

  • 26. Activity of linked HIV-1 proteinase dimers containing mutations in the active site region.
    Bagossi P, Cheng YS, Oroszlan S, Tözsér J.
    Protein Eng; 1996 Nov 16; 9(11):997-1003. PubMed ID: 8961352
    [Abstract] [Full Text] [Related]

  • 27. HIV-1 protease substrate-groove: Role in substrate recognition and inhibitor resistance.
    Laco GS.
    Biochimie; 2015 Nov 16; 118():90-103. PubMed ID: 26300060
    [Abstract] [Full Text] [Related]

  • 28. Analysis of the pH-dependencies of the association and dissociation kinetics of HIV-1 protease inhibitors.
    Gossas T, Danielson UH.
    J Mol Recognit; 2003 Nov 16; 16(4):203-12. PubMed ID: 12898670
    [Abstract] [Full Text] [Related]

  • 29. The inhibition of HIV-1 protease by interface peptides.
    Schramm HJ, Billich A, Jaeger E, Rücknagel KP, Arnold G, Schramm W.
    Biochem Biophys Res Commun; 1993 Jul 30; 194(2):595-600. PubMed ID: 8343146
    [Abstract] [Full Text] [Related]

  • 30. Active human cytomegalovirus protease is a dimer.
    Darke PL, Cole JL, Waxman L, Hall DL, Sardana MK, Kuo LC.
    J Biol Chem; 1996 Mar 29; 271(13):7445-9. PubMed ID: 8631772
    [Abstract] [Full Text] [Related]

  • 31. [Specific ligand induced dimerization of allosteric enzymes].
    Kurganov BI.
    Mol Biol (Mosk); 1982 Mar 29; 16(2):424-33. PubMed ID: 7073865
    [Abstract] [Full Text] [Related]

  • 32. Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected].
    Milton RC, Milton SC, Kent SB.
    Science; 1992 Jun 05; 256(5062):1445-8. PubMed ID: 1604320
    [Abstract] [Full Text] [Related]

  • 33. Comparison of the specificity of homo- and heterodimeric linked HIV-1 and HIV-2 proteinase dimers.
    Bagossi P, Cheng YS, Oroszlan S, Tözsér J.
    Protein Eng; 1998 Jun 05; 11(6):439-45. PubMed ID: 9725622
    [Abstract] [Full Text] [Related]

  • 34. Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.
    Louis JM, Nashed NT, Parris KD, Kimmel AR, Jerina DM.
    Proc Natl Acad Sci U S A; 1994 Aug 16; 91(17):7970-4. PubMed ID: 8058744
    [Abstract] [Full Text] [Related]

  • 35. An engineered retroviral proteinase from myeloblastosis associated virus acquires pH dependence and substrate specificity of the HIV-1 proteinase.
    Konvalinka J, Horejsí M, Andreánsky M, Novek P, Pichová I, Bláha I, Fábry M, Sedlácek J, Foundling S, Strop P.
    EMBO J; 1992 Mar 16; 11(3):1141-4. PubMed ID: 1547777
    [Abstract] [Full Text] [Related]

  • 36. Functional characterization of the protease of human endogenous retrovirus, K10: can it complement HIV-1 protease?
    Towler EM, Gulnik SV, Bhat TN, Xie D, Gustschina E, Sumpter TR, Robertson N, Jones C, Sauter M, Mueller-Lantzsch N, Debouck C, Erickson JW.
    Biochemistry; 1998 Dec 08; 37(49):17137-44. PubMed ID: 9860826
    [Abstract] [Full Text] [Related]

  • 37. 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]

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