메뉴 건너뛰기




Volumn 1, Issue 3, 2009, Pages 1209-1239

Current and novel inhibitors of HIV protease

Author keywords

Alternative inhibitors; HAART; HIV protease; Pharmacokinetic boosting; Protease dimerization; Protease inhibitors; Resistance development

Indexed keywords


EID: 84868216387     PISSN: 19994915     EISSN: None     Source Type: Journal    
DOI: 10.3390/v1031209     Document Type: Review
Times cited : (98)

References (150)
  • 2
    • 21444441862 scopus 로고    scopus 로고
    • Insertions in the human immunodeficiency virus type 1 protease and reverse transcriptase genes: Clinical impact and molecular mechanisms
    • Winters, M.A.; Merigan, T.C. Insertions in the human immunodeficiency virus type 1 protease and reverse transcriptase genes: clinical impact and molecular mechanisms. Antimicrob. Agents Chemother. 2005, 49, 2575-2582.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2575-2582
    • Winters, M.A.1    Merigan, T.C.2
  • 3
    • 44949137457 scopus 로고    scopus 로고
    • Ninety-nine is not enough: Molecular characterization of inhibitor-resistant human immunodeficiency virus type 1 protease mutants with insertions in the flap region
    • Kozisek, M.; Saskova, K.G.; Rezacova, P.; Brynda, J.; van Maarseveen, N.M.; de Jong, D.; Boucher, C.A.; Kagan, R.M.; Nijhuis, M.; Konvalinka, J. Ninety-nine is not enough: molecular characterization of inhibitor-resistant human immunodeficiency virus type 1 protease mutants with insertions in the flap region. J. Virol. 2008, 82, 5869-5878.
    • (2008) J. Virol. , vol.82 , pp. 5869-5878
    • Kozisek, M.1    Saskova, K.G.2    Rezacova, P.3    Brynda, J.4    van Maarseveen, N.M.5    de Jong, D.6    Boucher, C.A.7    Kagan, R.M.8    Nijhuis, M.9    Konvalinka, J.10
  • 4
    • 0029899093 scopus 로고    scopus 로고
    • Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors
    • Doyon, L.; Croteau, G.; Thibeault, D.; Poulin, F.; Pilote, L.; Lamarre, D. Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitors. J. Virol. 1996, 70, 3763-3769.
    • (1996) J. Virol. , vol.70 , pp. 3763-3769
    • Doyon, L.1    Croteau, G.2    Thibeault, D.3    Poulin, F.4    Pilote, L.5    Lamarre, D.6
  • 5
    • 0031846317 scopus 로고    scopus 로고
    • Resistance-associated loss of viral fitness in human immunodeficiency virus type 1: Phenotypic analysis of protease and gag coevolution in protease inhibitor-treated patients
    • Mammano, F.; Petit, C.; Clavel, F. Resistance-associated loss of viral fitness in human immunodeficiency virus type 1: phenotypic analysis of protease and gag coevolution in protease inhibitor-treated patients. J. Virol. 1998, 72, 7632-7637.
    • (1998) J. Virol. , vol.72 , pp. 7632-7637
    • Mammano, F.1    Petit, C.2    Clavel, F.3
  • 8
    • 69249215358 scopus 로고    scopus 로고
    • Molecular characterization of clinical isolates of human immunodeficiency virus resistant to the protease inhibitor darunavir
    • Saskova, K.G.; Kozisek, M.; Rezacova, P.; Brynda, J.; Yashina, T.; Kagan, R.M.; Konvalinka, J. Molecular characterization of clinical isolates of human immunodeficiency virus resistant to the protease inhibitor darunavir. J. Virol. 2009, 83, 8810-8818.
    • (2009) J. Virol. , vol.83 , pp. 8810-8818
    • Saskova, K.G.1    Kozisek, M.2    Rezacova, P.3    Brynda, J.4    Yashina, T.5    Kagan, R.M.6    Konvalinka, J.7
  • 10
    • 20944438569 scopus 로고    scopus 로고
    • Adverse effects of antiretroviral therapy for HIV infection: A review of selected topics
    • Nolan, D.; Reiss, P.; Mallal, S. Adverse effects of antiretroviral therapy for HIV infection: a review of selected topics. Expert Opin. Drug Saf. 2005, 4, 201-218.
    • (2005) Expert Opin. Drug Saf. , vol.4 , pp. 201-218
    • Nolan, D.1    Reiss, P.2    Mallal, S.3
  • 13
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: A major success of structure-assisted drug design
    • Wlodawer, A.; Vondrasek, J. Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu. Rev. Biophys. Biomol. Struct. 1998, 27, 249-284.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 14
    • 0036176766 scopus 로고    scopus 로고
    • Rational approach to AIDS drug design through structural biology
    • Wlodawer, A. Rational approach to AIDS drug design through structural biology. Annu. Rev. Med. 2002, 53, 595-614.
    • (2002) Annu. Rev. Med. , vol.53 , pp. 595-614
    • Wlodawer, A.1
  • 16
    • 14944344464 scopus 로고    scopus 로고
    • New approaches toward anti-HIV chemotherapy
    • de Clercq, E. New approaches toward anti-HIV chemotherapy. J. Med. Chem. 2005, 48, 1297-1313.
    • (2005) J. Med. Chem. , vol.48 , pp. 1297-1313
    • de Clercq, E.1
  • 17
    • 33747099931 scopus 로고    scopus 로고
    • Overcoming HIV drug resistance through rational drug design based on molecular, biochemical, and structural profiles of HIV resistance
    • Yin, P.D.; Das, D.; Mitsuya, H. Overcoming HIV drug resistance through rational drug design based on molecular, biochemical, and structural profiles of HIV resistance. Cell Mol. Life Sci. 2006, 63, 1706-1724.
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 1706-1724
    • Yin, P.D.1    Das, D.2    Mitsuya, H.3
  • 18
    • 36248969694 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: Current state of the art 10 years after their introduction. From antiretroviral drugs to antifungal, antibacterial and antitumor agents based on aspartic protease inhibitors
    • Mastrolorenzo, A.; Rusconi, S.; Scozzafava, A.; Barbaro, G.; Supuran, C.T. Inhibitors of HIV-1 protease: current state of the art 10 years after their introduction. From antiretroviral drugs to antifungal, antibacterial and antitumor agents based on aspartic protease inhibitors. Curr. Med. Chem. 2007, 14, 2734-2748.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 2734-2748
    • Mastrolorenzo, A.1    Rusconi, S.2    Scozzafava, A.3    Barbaro, G.4    Supuran, C.T.5
  • 19
    • 70350708165 scopus 로고    scopus 로고
    • The history of antiretrovirals: Key discoveries over the past 25 years
    • de Clercq, E. The history of antiretrovirals: key discoveries over the past 25 years. Rev. Med. Virol. 2009, 19, 287-299.
    • (2009) Rev. Med. Virol. , vol.19 , pp. 287-299
    • de Clercq, E.1
  • 20
    • 61549084714 scopus 로고    scopus 로고
    • Viral protease inhibitors
    • In, Kräusslich, H.G., Bartenschlager, R., Eds.; Springer: Berlin, Heidelberg, Germany
    • Anderson, J.; Schiffer, C.A.; Lee, S.K.; Swanstrom, R. Viral protease inhibitors. In Handbook of Experimental Pharmacology; Kräusslich, H.G., Bartenschlager, R., Eds.; Springer: Berlin, Heidelberg, Germany, 2009; Volume 189, pp. 85-110.
    • (2009) Handbook of Experimental Pharmacology , vol.189 , pp. 85-110
    • Anderson, J.1    Schiffer, C.A.2    Lee, S.K.3    Swanstrom, R.4
  • 22
    • 1542319002 scopus 로고    scopus 로고
    • Susceptibility of HIV-2, SIV and SHIV to various anti-HIV-1 compounds: Implications for treatment and postexposure prophylaxis
    • Witvrouw, M.; Pannecouque, C.; Switzer, W.M.; Folks, T.M.; de Clercq, E.; Heneine, W. Susceptibility of HIV-2, SIV and SHIV to various anti-HIV-1 compounds: implications for treatment and postexposure prophylaxis. Antivir. Ther. 2004, 9, 57-65.
    • (2004) Antivir. Ther. , vol.9 , pp. 57-65
    • Witvrouw, M.1    Pannecouque, C.2    Switzer, W.M.3    Folks, T.M.4    de Clercq, E.5    Heneine, W.6
  • 24
    • 59849124169 scopus 로고    scopus 로고
    • Metabolic syndrome associated with HIV and highly active antiretroviral therapy
    • Barbaro, G.; Iacobellis, G. Metabolic syndrome associated with HIV and highly active antiretroviral therapy. Curr. Diab. Rep. 2009, 9, 37-42.
    • (2009) Curr. Diab. Rep. , vol.9 , pp. 37-42
    • Barbaro, G.1    Iacobellis, G.2
  • 25
    • 62749096647 scopus 로고    scopus 로고
    • The role of protease inhibitors in the pathogenesis of HIV-associated lipodystrophy: Cellular mechanisms and clinical implications
    • Flint, O.P.; Noor, M.A.; Hruz, P.W.; Hylemon, P.B.; Yarasheski, K.; Kotler, D.P.; Parker, R.A.; Bellamine, A. The role of protease inhibitors in the pathogenesis of HIV-associated lipodystrophy: cellular mechanisms and clinical implications. Toxicol. Pathol. 2009, 37, 65-77.
    • (2009) Toxicol. Pathol. , vol.37 , pp. 65-77
    • Flint, O.P.1    Noor, M.A.2    Hruz, P.W.3    Hylemon, P.B.4    Yarasheski, K.5    Kotler, D.P.6    Parker, R.A.7    Bellamine, A.8
  • 26
    • 67649639637 scopus 로고    scopus 로고
    • Greater decrease in bone mineral density with protease inhibitor regimens compared with nonnucleoside reverse transcriptase inhibitor regimens in HIV-1 infected naive patients
    • Duvivier, C.; Kolta, S.; Assoumou, L.; Ghosn, J.; Rozenberg, S.; Murphy, R.L.; Katlama, C.; Costagliola, D. Greater decrease in bone mineral density with protease inhibitor regimens compared with nonnucleoside reverse transcriptase inhibitor regimens in HIV-1 infected naive patients. AIDS 2009, 27, 817-824.
    • (2009) AIDS , vol.27 , pp. 817-824
    • Duvivier, C.1    Kolta, S.2    Assoumou, L.3    Ghosn, J.4    Rozenberg, S.5    Murphy, R.L.6    Katlama, C.7    Costagliola, D.8
  • 28
    • 33747335917 scopus 로고    scopus 로고
    • Influence of highly active antiretroviral therapy on persistence of HIV in the central nervous system
    • Nath, A.; Sacktor, N. Influence of highly active antiretroviral therapy on persistence of HIV in the central nervous system. Curr. Opin. Neurol. 2006, 19, 358-361.
    • (2006) Curr. Opin. Neurol. , vol.19 , pp. 358-361
    • Nath, A.1    Sacktor, N.2
  • 31
    • 13644249455 scopus 로고    scopus 로고
    • Protease-inhibitor boosting in the treatment-experienced patient
    • Gallant, J.E. Protease-inhibitor boosting in the treatment-experienced patient. AIDS Rev. 2004, 6, 226-233.
    • (2004) AIDS Rev. , vol.6 , pp. 226-233
    • Gallant, J.E.1
  • 32
    • 68649113534 scopus 로고    scopus 로고
    • Pharmacokinetic enhancers for HIV drugs
    • Xu, L.; Desai, M.C. Pharmacokinetic enhancers for HIV drugs. Curr. Opin. Investig. Drugs 2009, 10, 775-786.
    • (2009) Curr. Opin. Investig. Drugs , vol.10 , pp. 775-786
    • Xu, L.1    Desai, M.C.2
  • 33
    • 36549014231 scopus 로고    scopus 로고
    • Overview of boosted protease inhibitors in treatment-experienced HIV-infected patients
    • Youle, M. Overview of boosted protease inhibitors in treatment-experienced HIV-infected patients. J. Antimicrob. Chemother. 2007, 60, 1195-1205.
    • (2007) J. Antimicrob. Chemother. , vol.60 , pp. 1195-1205
    • Youle, M.1
  • 34
    • 24044474081 scopus 로고    scopus 로고
    • The management of HIV-1 protease inhibitor pharmacokinetic interactions
    • Winston, A.; Boffito, M. The management of HIV-1 protease inhibitor pharmacokinetic interactions. J. Antimicrob. Chemother. 2005, 56, 1-5.
    • (2005) J. Antimicrob. Chemother. , vol.56 , pp. 1-5
    • Winston, A.1    Boffito, M.2
  • 36
    • 0033802649 scopus 로고    scopus 로고
    • Safety and pharmacokinetics of once-daily regimens of soft-gel capsule saquinavir plus minidose ritonavir in human immunodeficiency virus-negative adults
    • Kilby, J.M.; Sfakianos, G.; Gizzi, N.; Siemon-Hryczyk, P.; Ehrensing, E.; Oo, C.; Buss, N.; Saag, M. S. Safety and pharmacokinetics of once-daily regimens of soft-gel capsule saquinavir plus minidose ritonavir in human immunodeficiency virus-negative adults. Antimicrob. Agents Chemother. 2000, 44, 2672-2678.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2672-2678
    • Kilby, J.M.1    Sfakianos, G.2    Gizzi, N.3    Siemon-Hryczyk, P.4    Ehrensing, E.5    Oo, C.6    Buss, N.7    Saag, M.S.8
  • 37
    • 0031914446 scopus 로고    scopus 로고
    • Saquinavir soft-gel capsule formulation. A review of its use in patients with HIV infection
    • Perry, C.M.; Noble, S. Saquinavir soft-gel capsule formulation. A review of its use in patients with HIV infection. Drugs 1998, 55, 461-486.
    • (1998) Drugs , vol.55 , pp. 461-486
    • Perry, C.M.1    Noble, S.2
  • 39
    • 0035198762 scopus 로고    scopus 로고
    • Principles and practice of HIV-protease inhibitor pharmacoenhancement
    • Moyle, G.J.; Back, D. Principles and practice of HIV-protease inhibitor pharmacoenhancement. HIV Med. 2001, 2, 105-113.
    • (2001) HIV Med. , vol.2 , pp. 105-113
    • Moyle, G.J.1    Back, D.2
  • 42
    • 0031571306 scopus 로고    scopus 로고
    • Protease inhibitors' metabolic side effects: Cholesterol, triglycerides, blood sugar, and "Crix belly. " Interview with Lisa Capaldini, Interview by John S. James
    • Capaldini, L. Protease inhibitors' metabolic side effects: cholesterol, triglycerides, blood sugar, and "Crix belly. " Interview with Lisa Capaldini, Interview by John S. James. AIDS Treat. News 1997, (No 277), 1-4.
    • (1997) AIDS Treat. News , Issue.277 , pp. 1-4
    • Capaldini, L.1
  • 44
    • 35748950982 scopus 로고    scopus 로고
    • Molecular analysis of the HIV-1 resistance development: Enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants
    • Kozisek, M.; Bray, J.; Rezacova, P.; Saskova, K.; Brynda, J.; Pokorna, J.; Mammano, F.; Rulisek, L.; Konvalinka, J. Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants. J. Mol. Biol. 2007, 374, 1005-1016.
    • (2007) J. Mol. Biol. , vol.374 , pp. 1005-1016
    • Kozisek, M.1    Bray, J.2    Rezacova, P.3    Saskova, K.4    Brynda, J.5    Pokorna, J.6    Mammano, F.7    Rulisek, L.8    Konvalinka, J.9
  • 45
    • 0034104217 scopus 로고    scopus 로고
    • Nelfinavir: An update on its use in HIV infection
    • Bardsley-Elliot, A.; Plosker, G.L. Nelfinavir: an update on its use in HIV infection. Drugs 2000, 59, 581-620.
    • (2000) Drugs , vol.59 , pp. 581-620
    • Bardsley-Elliot, A.1    Plosker, G.L.2
  • 46
    • 0028846226 scopus 로고
    • Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme
    • Kim, E.E.; Baker, C.T.; Dwyer, M.D.; Murcko, M.A.; Rao, B.G.; Tung, R.D.; Navia, M.A. Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme. J. Am. Chem. Soc. 1995, 117, 1181-1182.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1181-1182
    • Kim, E.E.1    Baker, C.T.2    Dwyer, M.D.3    Murcko, M.A.4    Rao, B.G.5    Tung, R.D.6    Navia, M.A.7
  • 49
    • 0031804689 scopus 로고    scopus 로고
    • Amprenavir
    • discussion 843-844
    • Adkins, J.C.; Faulds, D. Amprenavir. Drugs 1998, 55, 837-842; discussion 843-844.
    • (1998) Drugs , vol.55 , pp. 837-842
    • Adkins, J.C.1    Faulds, D.2
  • 50
    • 10744220505 scopus 로고    scopus 로고
    • Risk factors and occurrence of rash in HIVpositive patients not receiving nonnucleoside reverse transcriptase inhibitor: Data from a randomized study evaluating use of protease inhibitors in nucleoside-experienced patients with very low CD4 levels (<50 cells/microL)
    • Floridia, M.; Bucciardini, R.; Fragola, V.; Galluzzo, C.M.; Giannini, G.; Pirillo, M.F.; Amici, R.; Andreotti, M.; Ricciardulli, D.; Tomino, C.; Vella, S. Risk factors and occurrence of rash in HIVpositive patients not receiving nonnucleoside reverse transcriptase inhibitor: data from a randomized study evaluating use of protease inhibitors in nucleoside-experienced patients with very low CD4 levels (<50 cells/microL). HIV Med. 2004, 5, 1-10.
    • (2004) HIV Med. , vol.5 , pp. 1-10
    • Floridia, M.1    Bucciardini, R.2    Fragola, V.3    Galluzzo, C.M.4    Giannini, G.5    Pirillo, M.F.6    Amici, R.7    Andreotti, M.8    Ricciardulli, D.9    Tomino, C.10    Vella, S.11
  • 51
    • 0042991375 scopus 로고    scopus 로고
    • Prodrugs of HIV protease inhibitors
    • Vierling, P.; Greiner, J. Prodrugs of HIV protease inhibitors. Curr. Pharm. Des. 2003, 9, 1755-1770.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1755-1770
    • Vierling, P.1    Greiner, J.2
  • 52
    • 34447250071 scopus 로고    scopus 로고
    • Fosamprenavir calcium plus ritonavir for HIV infection
    • Torres, H.A.; Arduino, R.C. Fosamprenavir calcium plus ritonavir for HIV infection. Expert Rev. Anti Infect. Ther. 2007, 5, 349-363.
    • (2007) Expert Rev. Anti Infect. Ther. , vol.5 , pp. 349-363
    • Torres, H.A.1    Arduino, R.C.2
  • 54
    • 0034909925 scopus 로고    scopus 로고
    • Identification of genotypic changes in human immunodeficiency virus protease that correlate with reduced susceptibility to the protease inhibitor lopinavir among viral isolates from protease inhibitor-experienced patients
    • Kempf, D.J.; Isaacson, J.D.; King, M.S.; Brun, S.C.; Xu, Y.; Real, K.; Bernstein, B.M.; Japour, A.J.; Sun, E.; Rode, R.A. Identification of genotypic changes in human immunodeficiency virus protease that correlate with reduced susceptibility to the protease inhibitor lopinavir among viral isolates from protease inhibitor-experienced patients. J. Virol. 2001, 75, 7462-7469.
    • (2001) J. Virol. , vol.75 , pp. 7462-7469
    • Kempf, D.J.1    Isaacson, J.D.2    King, M.S.3    Brun, S.C.4    Xu, Y.5    Real, K.6    Bernstein, B.M.7    Japour, A.J.8    Sun, E.9    Rode, R.A.10
  • 55
    • 0031849665 scopus 로고    scopus 로고
    • In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor
    • Carrillo, A.; Stewart, K.D.; Sham, H.L.; Norbeck, D.W.; Kohlbrenner, W.E.; Leonard, J.M.; Kempf, D.J.; Molla, A. In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor. J. Virol. 1998, 72, 7532-7541.
    • (1998) J. Virol. , vol.72 , pp. 7532-7541
    • Carrillo, A.1    Stewart, K.D.2    Sham, H.L.3    Norbeck, D.W.4    Kohlbrenner, W.E.5    Leonard, J.M.6    Kempf, D.J.7    Molla, A.8
  • 56
    • 33646381660 scopus 로고    scopus 로고
    • Prevalence of the HIV-1 protease mutation I47A in clinical practice and association with lopinavir resistance
    • de Mendoza, C.; Valer, L.; Bacheler, L.; Pattery, T.; Corral, A.; Soriano, V. Prevalence of the HIV-1 protease mutation I47A in clinical practice and association with lopinavir resistance. AIDS 2006, 20, 1071-1074.
    • (2006) AIDS , vol.20 , pp. 1071-1074
    • de Mendoza, C.1    Valer, L.2    Bacheler, L.3    Pattery, T.4    Corral, A.5    Soriano, V.6
  • 57
    • 50049088535 scopus 로고    scopus 로고
    • Enzymatic and structural analysis of the I47A mutation contributing to the reduced susceptibility to HIV protease inhibitor lopinavir
    • Saskova, K.G.; Kozisek, M.; Lepsik, M.; Brynda, J.; Rezacova, P.; Vaclavikova, J.; Kagan, R.M.; Machala, L.; Konvalinka, J. Enzymatic and structural analysis of the I47A mutation contributing to the reduced susceptibility to HIV protease inhibitor lopinavir. Protein Sci. 2008, 17, 1555-1564.
    • (2008) Protein Sci. , vol.17 , pp. 1555-1564
    • Saskova, K.G.1    Kozisek, M.2    Lepsik, M.3    Brynda, J.4    Rezacova, P.5    Vaclavikova, J.6    Kagan, R.M.7    McHala, L.8    Konvalinka, J.9
  • 59
    • 22244462118 scopus 로고    scopus 로고
    • Structural analysis of an HIV-1 protease I47A mutant resistant to the protease inhibitor lopinavir
    • Kagan, R.M.; Shenderovich, M.D.; Heseltine, P.N.; Ramnarayan, K. Structural analysis of an HIV-1 protease I47A mutant resistant to the protease inhibitor lopinavir. Protein Sci. 2005, 14, 1870-1878.
    • (2005) Protein Sci. , vol.14 , pp. 1870-1878
    • Kagan, R.M.1    Shenderovich, M.D.2    Heseltine, P.N.3    Ramnarayan, K.4
  • 60
    • 0037251643 scopus 로고    scopus 로고
    • Lopinavir/ritonavir: A review of its use in the management of HIV infection
    • Cvetkovic, R.S.; Goa, K.L. Lopinavir/ritonavir: a review of its use in the management of HIV infection. Drugs 2003, 63, 769-802.
    • (2003) Drugs , vol.63 , pp. 769-802
    • Cvetkovic, R.S.1    Goa, K.L.2
  • 62
    • 25144448034 scopus 로고    scopus 로고
    • Clinical pharmacokinetics and summary of efficacy and tolerability of atazanavir
    • Le Tiec, C.; Barrail, A.; Goujard, C.; Taburet, A.M. Clinical pharmacokinetics and summary of efficacy and tolerability of atazanavir. Clin. Pharmacokinet. 2005, 44, 1035-1050.
    • (2005) Clin. Pharmacokinet. , vol.44 , pp. 1035-1050
    • Le Tiec, C.1    Barrail, A.2    Goujard, C.3    Taburet, A.M.4
  • 64
    • 34248336220 scopus 로고    scopus 로고
    • Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations
    • Muzammil, S.; Armstrong, A.A.; Kang, L.W.; Jakalian, A.; Bonneau, P.R.; Schmelmer, V.; Amzel, L.M.; Freire, E. Unique thermodynamic response of tipranavir to human immunodeficiency virus type 1 protease drug resistance mutations. J. Virol. 2007, 81, 5144-5154.
    • (2007) J. Virol. , vol.81 , pp. 5144-5154
    • Muzammil, S.1    Armstrong, A.A.2    Kang, L.W.3    Jakalian, A.4    Bonneau, P.R.5    Schmelmer, V.6    Amzel, L.M.7    Freire, E.8
  • 68
    • 37749039471 scopus 로고    scopus 로고
    • Increased risk of bleeding with the use of tipranavir boosted with ritonavir in haemophilic patients
    • Arbuthnot, C.; Wilde, J.T. Increased risk of bleeding with the use of tipranavir boosted with ritonavir in haemophilic patients. Haemophilia 2008, 14, 140-141.
    • (2008) Haemophilia , vol.14 , pp. 140-141
    • Arbuthnot, C.1    Wilde, J.T.2
  • 69
    • 33745603209 scopus 로고    scopus 로고
    • Tipranavir: A novel nonpeptidic protease inhibitor of HIV
    • King, J.R.; Acosta, E.P. Tipranavir: a novel nonpeptidic protease inhibitor of HIV. Clin. Pharmacokinet. 2006, 45, 665-682.
    • (2006) Clin. Pharmacokinet. , vol.45 , pp. 665-682
    • King, J.R.1    Acosta, E.P.2
  • 71
    • 0034283345 scopus 로고    scopus 로고
    • How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease
    • Prabu-Jeyabalan, M.; Nalivaika, E.; Schiffer, C.A. How does a symmetric dimer recognize an asymmetric substrate? A substrate complex of HIV-1 protease. J. Mol. Biol. 2000, 301, 1207-1220.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1207-1220
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 73
    • 55049134097 scopus 로고    scopus 로고
    • Resilience to resistance of HIV-1 protease inhibitors: Profile of darunavir
    • Lefebvre, E.; Schiffer, C.A. Resilience to resistance of HIV-1 protease inhibitors: profile of darunavir. AIDS Rev 2008, 10, 131-142.
    • (2008) AIDS Rev , vol.10 , pp. 131-142
    • Lefebvre, E.1    Schiffer, C.A.2
  • 74
    • 33748955158 scopus 로고    scopus 로고
    • Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114
    • Kovalevsky, A.Y.; Liu, F.; Leshchenko, S.; Ghosh, A.K.; Louis, J.M.; Harrison, R.W.; Weber, I.T. Ultra-high resolution crystal structure of HIV-1 protease mutant reveals two binding sites for clinical inhibitor TMC114. J. Mol. Biol. 2006, 363, 161-173.
    • (2006) J. Mol. Biol. , vol.363 , pp. 161-173
    • Kovalevsky, A.Y.1    Liu, F.2    Leshchenko, S.3    Ghosh, A.K.4    Louis, J.M.5    Harrison, R.W.6    Weber, I.T.7
  • 75
    • 54549105456 scopus 로고    scopus 로고
    • Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir
    • Kovalevsky, A.Y.; Ghosh, A.K.; Weber, I.T. Solution kinetics measurements suggest HIV-1 protease has two binding sites for darunavir and amprenavir. J. Med. Chem. 2008, 51, 6599-6603.
    • (2008) J. Med. Chem. , vol.51 , pp. 6599-6603
    • Kovalevsky, A.Y.1    Ghosh, A.K.2    Weber, I.T.3
  • 77
    • 6344231715 scopus 로고    scopus 로고
    • Structural and thermodynamic basis for the binding of TMC114, a next-generation human immunodeficiency virus type 1 protease inhibitor
    • King, N.M.; Prabu-Jeyabalan, M.; Nalivaika, E.A.; Wigerinck, P.; de Bethune, M.P.; Schiffer, C.A. Structural and thermodynamic basis for the binding of TMC114, a next-generation human immunodeficiency virus type 1 protease inhibitor. J. Virol. 2004, 78, 12012-12021.
    • (2004) J. Virol. , vol.78 , pp. 12012-12021
    • King, N.M.1    Prabu-Jeyabalan, M.2    Nalivaika, E.A.3    Wigerinck, P.4    de Bethune, M.P.5    Schiffer, C.A.6
  • 82
    • 64649102226 scopus 로고    scopus 로고
    • Darunavir: A review of its use in the management of HIV infection in adults
    • McKeage, K.; Perry, C.M.; Keam, S.J. Darunavir: a review of its use in the management of HIV infection in adults. Drugs 2009, 69, 477-503.
    • (2009) Drugs , vol.69 , pp. 477-503
    • McKeage, K.1    Perry, C.M.2    Keam, S.J.3
  • 83
  • 84
    • 34548154182 scopus 로고    scopus 로고
    • Crystal structure of lysine sulfonamide inhibitor reveals the displacement of the conserved flap water molecule in human immunodeficiency virus type 1 protease
    • Nalam, M.N.; Peeters, A.; Jonckers, T.H.; Dierynck, I.; Schiffer, C.A. Crystal structure of lysine sulfonamide inhibitor reveals the displacement of the conserved flap water molecule in human immunodeficiency virus type 1 protease. J. Virol. 2007, 81, 9512-9518.
    • (2007) J. Virol. , vol.81 , pp. 9512-9518
    • Nalam, M.N.1    Peeters, A.2    Jonckers, T.H.3    Dierynck, I.4    Schiffer, C.A.5
  • 86
    • 84894631317 scopus 로고    scopus 로고
    • A First-in-Human Study Evaluating the Safety, Tolerability, and Pharmacokinetics (PK) of SPI-256, a Novel HIV Protease Inhibitor (PI), Administered Alone and in Combination with Ritonavir (RTV) in Healthy Adult Subjects
    • Washington, DC, USA
    • Wynne, B.; Holland, A.; Ruff, D.; Guttendorf, R. A First-in-Human Study Evaluating the Safety, Tolerability, and Pharmacokinetics (PK) of SPI-256, a Novel HIV Protease Inhibitor (PI), Administered Alone and in Combination with Ritonavir (RTV) in Healthy Adult Subjects. Presented at the ICAAC®/IDSA Annual Meeting, Washington, DC, USA, 2008.
    • (2008) Presented at the ICAAC®/IDSA Annual Meeting
    • Wynne, B.1    Holland, A.2    Ruff, D.3    Guttendorf, R.4
  • 89
    • 67649631240 scopus 로고    scopus 로고
    • Approaches to the design of HIV protease inhibitors with improved resistance profiles
    • Gulnik, S.V.; Eissenstat, M. Approaches to the design of HIV protease inhibitors with improved resistance profiles. Curr. Opin. HIV AIDS 2008, 3, 633-641.
    • (2008) Curr. Opin. HIV AIDS , vol.3 , pp. 633-641
    • Gulnik, S.V.1    Eissenstat, M.2
  • 91
    • 67649946397 scopus 로고    scopus 로고
    • Design of HIV-1 protease inhibitors with pyrrolidinones and oxazolidinones as novel P1'-ligands to enhance backbone-binding interactions with protease: Synthesis, biological evaluation, and protein-ligand X-ray studies
    • Ghosh, A.K.; Leshchenko-Yashchuk, S.; Anderson, D.D.; Baldridge, A.; Noetzel, M.; Miller, H. B.; Tie, Y.; Wang, Y.F.; Koh, Y.; Weber, I.T.; Mitsuya, H. Design of HIV-1 protease inhibitors with pyrrolidinones and oxazolidinones as novel P1'-ligands to enhance backbone-binding interactions with protease: synthesis, biological evaluation, and protein-ligand X-ray studies. J. Med. Chem. 2009, 52, 3902-3914.
    • (2009) J. Med. Chem. , vol.52 , pp. 3902-3914
    • Ghosh, A.K.1    Leshchenko-Yashchuk, S.2    Anderson, D.D.3    Baldridge, A.4    Noetzel, M.5    Miller, H.B.6    Tie, Y.7    Wang, Y.F.8    Koh, Y.9    Weber, I.T.10    Mitsuya, H.11
  • 93
    • 0028260973 scopus 로고
    • Potency and selectivity of inhibition of human immunodeficiency virus protease by a small nonpeptide cyclic urea, DMP 323
    • Erickson-Viitanen, S.; Klabe, R.M.; Cawood, P.G.; O'Neal, P.L.; Meek, J.L. Potency and selectivity of inhibition of human immunodeficiency virus protease by a small nonpeptide cyclic urea, DMP 323. Antimicrob. Agents Chemother. 1994, 38, 1628-1634.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 1628-1634
    • Erickson-Viitanen, S.1    Klabe, R.M.2    Cawood, P.G.3    O'Neal, P.L.4    Meek, J.L.5
  • 98
    • 0345257786 scopus 로고    scopus 로고
    • Fullerene derivatives: An attractive tool for biological applications
    • Bosi, S.; Da Ros, T.; Spalluto, G.; Prato, M. Fullerene derivatives: an attractive tool for biological applications. Eur. J. Med. Chem. 2003, 38, 913-923.
    • (2003) Eur. J. Med. Chem. , vol.38 , pp. 913-923
    • Bosi, S.1    Da Ros, T.2    Spalluto, G.3    Prato, M.4
  • 99
    • 0027244713 scopus 로고
    • Inhibition of the HIV-1 protease by fullerene derivatives: Model building studies and experimental verification
    • Friedman, S.H.; DeCamp, D.L.; Sijbesma, R.P.; Srdanov, G.; Wudl, F.; Kenyon, G.L. Inhibition of the HIV-1 protease by fullerene derivatives: model building studies and experimental verification. J. Am. Chem. Soc. 1993, 115, 6506-6509.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6506-6509
    • Friedman, S.H.1    DeCamp, D.L.2    Sijbesma, R.P.3    Srdanov, G.4    Wudl, F.5    Kenyon, G.L.6
  • 102
    • 40749094740 scopus 로고    scopus 로고
    • Boron Units as Pharmacophores-New Applications and Opportunities of Boron Cluster Chemistry
    • Lesnikowski, Z.J. Boron Units as Pharmacophores-New Applications and Opportunities of Boron Cluster Chemistry. Coll. Czech CC. 2007, 72, 1646-1658.
    • (2007) Coll. Czech CC. , vol.72 , pp. 1646-1658
    • Lesnikowski, Z.J.1
  • 103
    • 34748850708 scopus 로고    scopus 로고
    • The bioinorganic and medicinal chemistry of carboranes: From new drug discovery to molecular imaging and therapy
    • Armstrong, A.F.; Valliant, J.F. The bioinorganic and medicinal chemistry of carboranes: from new drug discovery to molecular imaging and therapy. Dalton Trans. 2007, 4240-4251.
    • (2007) Dalton Trans. , pp. 4240-4251
    • Armstrong, A.F.1    Valliant, J.F.2
  • 106
    • 68949201698 scopus 로고    scopus 로고
    • Toward the design of mutation-resistant enzyme inhibitors: Further evaluation of the substrate envelope hypothesis
    • Kairys, V.; Gilson, M.K.; Lather, V.; Schiffer, C.A.; Fernandes, M.X. Toward the design of mutation-resistant enzyme inhibitors: further evaluation of the substrate envelope hypothesis. Chem. Biol. Drug Des. 2009, 74, 234-245.
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 234-245
    • Kairys, V.1    Gilson, M.K.2    Lather, V.3    Schiffer, C.A.4    Fernandes, M.X.5
  • 107
    • 0036121219 scopus 로고    scopus 로고
    • Substrate shape determines specificity of recognition for HIV-1 protease: Analysis of crystal structures of six substrate complexes
    • Prabu-Jeyabalan, M.; Nalivaika, E.; Schiffer, C.A. Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes. Structure 2002, 10, 369-381.
    • (2002) Structure , vol.10 , pp. 369-381
    • Prabu-Jeyabalan, M.1    Nalivaika, E.2    Schiffer, C.A.3
  • 109
    • 0026803394 scopus 로고
    • PCR amplification of HIV-1 proteinase sequences directly from lab isolates allows determination of five conserved domains
    • Fontenot, G.; Johnston, K.; Cohen, J.C.; Gallaher, W.R.; Robinson, J.; Luftig, R.B. PCR amplification of HIV-1 proteinase sequences directly from lab isolates allows determination of five conserved domains. Virology 1992, 190, 1-10.
    • (1992) Virology , vol.190 , pp. 1-10
    • Fontenot, G.1    Johnston, K.2    Cohen, J.C.3    Gallaher, W.R.4    Robinson, J.5    Luftig, R.B.6
  • 110
    • 0141720374 scopus 로고    scopus 로고
    • Kinetics of the dimerization of retroviral proteases: The "fireman's grip" and dimerization
    • Ingr, M.; Uhlikova, T.; Strisovsky, K.; Majerova, E.; Konvalinka, J. Kinetics of the dimerization of retroviral proteases: the "fireman's grip" and dimerization. Protein Sci. 2003, 12, 2173-2182.
    • (2003) Protein Sci. , vol.12 , pp. 2173-2182
    • Ingr, M.1    Uhlikova, T.2    Strisovsky, K.3    Majerova, E.4    Konvalinka, J.5
  • 111
    • 0025641617 scopus 로고
    • Stability and activity of human immunodeficiency virus protease: Comparison of the natural dimer with a homologous, single-chain tethered dimer
    • Cheng, Y.S.; Yin, F.H.; Foundling, S.; Blomstrom, D.; Kettner, C.A. Stability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer. Proc. Natl. Acad. Sci. U S A 1990, 87, 9660-9664.
    • (1990) Proc. Natl. Acad. Sci. U S A , vol.87 , pp. 9660-9664
    • Cheng, Y.S.1    Yin, F.H.2    Foundling, S.3    Blomstrom, D.4    Kettner, C.A.5
  • 112
    • 0025986843 scopus 로고
    • Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide
    • Zhang, Z.Y.; Poorman, R.A.; Maggiora, L.L.; Heinrikson, R.L.; Kezdy, F.J. Dissociative inhibition of dimeric enzymes. Kinetic characterization of the inhibition of HIV-1 protease by its COOH-terminal tetrapeptide. J. Biol. Chem. 1991, 266, 15591-15594.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15591-15594
    • Zhang, Z.Y.1    Poorman, R.A.2    Maggiora, L.L.3    Heinrikson, R.L.4    Kezdy, F.J.5
  • 113
    • 0026640529 scopus 로고
    • Activity and dimerization of human immunodeficiency virus protease as a function of solvent composition and enzyme concentration
    • Jordan, S.P.; Zugay, J.; Darke, P.L.; Kuo, L.C. Activity and dimerization of human immunodeficiency virus protease as a function of solvent composition and enzyme concentration. J. Biol. Chem. 1992, 267, 20028-20032.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20028-20032
    • Jordan, S.P.1    Zugay, J.2    Darke, P.L.3    Kuo, L.C.4
  • 114
    • 0027240443 scopus 로고
    • Kinetic assay for HIV proteinase subunit dissociation
    • Kuzmic, P. Kinetic assay for HIV proteinase subunit dissociation. Biochem. Biophys. Res. Commun. 1993, 191, 998-1003.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 998-1003
    • Kuzmic, P.1
  • 115
    • 0027957967 scopus 로고
    • Dissociation and association of the HIV-1 protease dimer subunits: Equilibria and rates
    • Darke, P.L.; Jordan, S.P.; Hall, D.L.; Zugay, J.A.; Shafer, J.A.; Kuo, L.C. Dissociation and association of the HIV-1 protease dimer subunits: equilibria and rates. Biochemistry 1994, 33, 98-105.
    • (1994) Biochemistry , vol.33 , pp. 98-105
    • Darke, P.L.1    Jordan, S.P.2    Hall, D.L.3    Zugay, J.A.4    Shafer, J.A.5    Kuo, L.C.6
  • 116
    • 0028046926 scopus 로고
    • Determination of kinetic rate constants for the binding of inhibitors to HIV-1 protease and for the association and dissociation of active homodimer
    • Pargellis, C.A.; Morelock, M.M.; Graham, E.T.; Kinkade, P.; Pav, S.; Lubbe, K.; Lamarre, D.; Anderson, P.C. Determination of kinetic rate constants for the binding of inhibitors to HIV-1 protease and for the association and dissociation of active homodimer. Biochemistry 1994, 33, 12527-12534.
    • (1994) Biochemistry , vol.33 , pp. 12527-12534
    • Pargellis, C.A.1    Morelock, M.M.2    Graham, E.T.3    Kinkade, P.4    Pav, S.5    Lubbe, K.6    Lamarre, D.7    Anderson, P.C.8
  • 118
    • 0025336093 scopus 로고
    • Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases
    • Weber, I.T. Comparison of the crystal structures and intersubunit interactions of human immunodeficiency and Rous sarcoma virus proteases. J. Biol. Chem. 1990, 265, 10492-10496.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10492-10496
    • Weber, I.T.1
  • 120
    • 0032561137 scopus 로고    scopus 로고
    • The structural stability of the HIV-1 protease
    • Todd, M.J.; Semo, N.; Freire, E. The structural stability of the HIV-1 protease. J. Mol. Biol. 1998, 283, 475-488.
    • (1998) J. Mol. Biol. , vol.283 , pp. 475-488
    • Todd, M.J.1    Semo, N.2    Freire, E.3
  • 121
    • 0027087479 scopus 로고
    • Synthetic "interface" peptides alter dimeric assembly of the HIV 1 and 2 proteases
    • Babe, L.M.; Rose, J.; Craik, C.S. Synthetic "interface" peptides alter dimeric assembly of the HIV 1 and 2 proteases. Protein Sci. 1992, 1, 1244-1253.
    • (1992) Protein Sci. , vol.1 , pp. 1244-1253
    • Babe, L.M.1    Rose, J.2    Craik, C.S.3
  • 124
    • 0033575743 scopus 로고    scopus 로고
    • Probing the role of interfacial residues in a dimerization inhibitor of HIV-1 protease
    • Shultz, M.D.; Chmielewski, J. Probing the role of interfacial residues in a dimerization inhibitor of HIV-1 protease. Bioorg. Med. Chem. Lett. 1999, 9, 2431-2436.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2431-2436
    • Shultz, M.D.1    Chmielewski, J.2
  • 125
    • 0033602546 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of conformationally constrained tongs, new inhibitors of HIV-1 protease dimerization
    • Bouras, A.; Boggetto, N.; Benatalah, Z.; de Rosny, E.; Sicsic, S.; Reboud-Ravaux, M. Design, synthesis, and evaluation of conformationally constrained tongs, new inhibitors of HIV-1 protease dimerization. J. Med. Chem. 1999, 42, 957-962.
    • (1999) J. Med. Chem. , vol.42 , pp. 957-962
    • Bouras, A.1    Boggetto, N.2    Benatalah, Z.3    de Rosny, E.4    Sicsic, S.5    Reboud-Ravaux, M.6
  • 127
    • 58949087899 scopus 로고    scopus 로고
    • Sidechain-linked inhibitors of HIV-1 protease dimerization
    • Bowman, M.J.; Chmielewski, J. Sidechain-linked inhibitors of HIV-1 protease dimerization. Bioorg. Med. Chem. 2009, 17, 967-976.
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 967-976
    • Bowman, M.J.1    Chmielewski, J.2
  • 129
    • 0037378406 scopus 로고    scopus 로고
    • Thyroxine-derivatives of lipopeptides: Bifunctional dimerization inhibitors of human immunodeficiency virus-1 protease
    • Dumond, J.; Boggetto, N.; Schramm, H.J.; Schramm, W.; Takahashi, M.; Reboud-Ravaux, M. Thyroxine-derivatives of lipopeptides: bifunctional dimerization inhibitors of human immunodeficiency virus-1 protease. Biochem. Pharmacol. 2003, 65, 1097-1102.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1097-1102
    • Dumond, J.1    Boggetto, N.2    Schramm, H.J.3    Schramm, W.4    Takahashi, M.5    Reboud-Ravaux, M.6
  • 130
    • 59849109511 scopus 로고    scopus 로고
    • Dimer disruption and monomer sequestration by alkyl tripeptides are successful strategies for inhibiting wild-type and multidrugresistant mutated HIV-1 proteases
    • Bannwarth, L.; Rose, T.; Dufau, L.; Vanderesse, R.; Dumond, J.; Jamart-Gregoire, B.; Pannecouque, C.; de Clercq, E.; Reboud-Ravaux, M. Dimer disruption and monomer sequestration by alkyl tripeptides are successful strategies for inhibiting wild-type and multidrugresistant mutated HIV-1 proteases. Biochemistry 2009, 48, 379-387.
    • (2009) Biochemistry , vol.48 , pp. 379-387
    • Bannwarth, L.1    Rose, T.2    Dufau, L.3    Vanderesse, R.4    Dumond, J.5    Jamart-Gregoire, B.6    Pannecouque, C.7    de Clercq, E.8    Reboud-Ravaux, M.9
  • 131
    • 0034605187 scopus 로고    scopus 로고
    • Targeting the dimerization interface for irreversible inhibition of HIV-1 protease
    • Zutshi, R.; Chmielewski, J. Targeting the dimerization interface for irreversible inhibition of HIV-1 protease. Bioorg. Med. Chem. Lett. 2000, 10, 1901-1903.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 1901-1903
    • Zutshi, R.1    Chmielewski, J.2
  • 133
    • 64249150747 scopus 로고    scopus 로고
    • Analysis and characterization of dimerization inhibition of a multidrug-resistant human immunodeficiency virus type 1 protease using a novel size-exclusion chromatographic approach
    • Davis, D.A.; Tebbs, I.R.; Daniels, S.I.; Stahl, S.J.; Kaufman, J.D.; Wingfield, P.; Bowman, M.J.; Chmielewski, J.; Yarchoan, R. Analysis and characterization of dimerization inhibition of a multidrug-resistant human immunodeficiency virus type 1 protease using a novel size-exclusion chromatographic approach. Biochem. J. 2009, 419, 497-506.
    • (2009) Biochem. J. , vol.419 , pp. 497-506
    • Davis, D.A.1    Tebbs, I.R.2    Daniels, S.I.3    Stahl, S.J.4    Kaufman, J.D.5    Wingfield, P.6    Bowman, M.J.7    Chmielewski, J.8    Yarchoan, R.9
  • 137
    • 13844250583 scopus 로고    scopus 로고
    • Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide
    • Rezacova, P.; Brynda, J.; Lescar, J.; Fabry, M.; Horejsi, M.; Sieglova, I.; Sedlacek, J.; Bentley, G.A. Crystal structure of a cross-reaction complex between an anti-HIV-1 protease antibody and an HIV-2 protease peptide. J. Struct. Biol. 2005, 149, 332-337.
    • (2005) J. Struct. Biol. , vol.149 , pp. 332-337
    • Rezacova, P.1    Brynda, J.2    Lescar, J.3    Fabry, M.4    Horejsi, M.5    Sieglova, I.6    Sedlacek, J.7    Bentley, G.A.8
  • 138
    • 34247525134 scopus 로고    scopus 로고
    • 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, R.A.; Madurga, S.; Collinet, B.; Reboud-Ravaux, M.; Ludevid, D.; Giralt, E. Disruption of the HIV-1 protease dimer with interface peptides: structural studies using NMR spectroscopy combined with [2-(13)C]-Trp selective labeling. Biopolymers 2007, 88, 164-173.
    • (2007) Biopolymers , vol.88 , pp. 164-173
    • Frutos, S.1    Rodriguez-Mias, R.A.2    Madurga, S.3    Collinet, B.4    Reboud-Ravaux, M.5    Ludevid, D.6    Giralt, E.7
  • 139
    • 57449117704 scopus 로고    scopus 로고
    • In search of small molecules blocking interactions between HIV proteins and intracellular cofactors
    • Busschots, K.; De Rijck, J.; Christ, F.; Debyser, Z. In search of small molecules blocking interactions between HIV proteins and intracellular cofactors. Mol. Biosyst. 2009, 5, 21-31.
    • (2009) Mol. Biosyst. , vol.5 , pp. 21-31
    • Busschots, K.1    De Rijck, J.2    Christ, F.3    Debyser, Z.4
  • 141
    • 2642581493 scopus 로고    scopus 로고
    • Herpesvirus protease inhibition by dimer disruption
    • Shimba, N.; Nomura, A.M.; Marnett, A.B.; Craik, C.S. Herpesvirus protease inhibition by dimer disruption. J. Virol. 2004, 78, 6657-6665.
    • (2004) J. Virol. , vol.78 , pp. 6657-6665
    • Shimba, N.1    Nomura, A.M.2    Marnett, A.B.3    Craik, C.S.4
  • 142
    • 33747116051 scopus 로고    scopus 로고
    • Dimerization inhibitors of HIV-1 reverse transcriptase, protease and integrase: A single mode of inhibition for the three HIV enzymes?
    • Camarasa, M.J.; Velazquez, S.; San-Felix, A.; Perez-Perez, M.J.; Gago, F. Dimerization inhibitors of HIV-1 reverse transcriptase, protease and integrase: a single mode of inhibition for the three HIV enzymes? Antiviral Res. 2006, 71, 260-267.
    • (2006) Antiviral Res. , vol.71 , pp. 260-267
    • Camarasa, M.J.1    Velazquez, S.2    San-Felix, A.3    Perez-Perez, M.J.4    Gago, F.5
  • 143
    • 33846635484 scopus 로고    scopus 로고
    • Targeting structural flexibility in HIV-1 protease inhibitor binding
    • Hornak, V.; Simmerling, C. Targeting structural flexibility in HIV-1 protease inhibitor binding. Drug Discov. Today 2007, 12, 132-138.
    • (2007) Drug Discov. Today , vol.12 , pp. 132-138
    • Hornak, V.1    Simmerling, C.2
  • 144
    • 0033200247 scopus 로고    scopus 로고
    • Flap opening and dimerinterface flexibility in the free and inhibitor-bound HIV protease, and their implications for function
    • Ishima, R.; Freedberg, D.I.; Wang, Y.X.; Louis, J.M.; Torchia, D.A. Flap opening and dimerinterface flexibility in the free and inhibitor-bound HIV protease, and their implications for function. Structure 1999, 7, 1047-1055.
    • (1999) Structure , vol.7 , pp. 1047-1055
    • Ishima, R.1    Freedberg, D.I.2    Wang, Y.X.3    Louis, J.M.4    Torchia, D.A.5
  • 145
    • 0026344399 scopus 로고
    • The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU
    • Spinelli, S.; Liu, Q.Z.; Alzari, P.M.; Hirel, P.H.; Poljak, R.J. The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU. Biochimie 1991, 73, 1391-1396.
    • (1991) Biochimie , vol.73 , pp. 1391-1396
    • Spinelli, S.1    Liu, Q.Z.2    Alzari, P.M.3    Hirel, P.H.4    Poljak, R.J.5
  • 146
    • 54849414837 scopus 로고    scopus 로고
    • Targeting the open-flap conformation of HIV-1 protease with pyrrolidine-based inhibitors
    • Bottcher, J.; Blum, A.; Dorr, S.; Heine, A.; Diederich, W.E.; Klebe, G. Targeting the open-flap conformation of HIV-1 protease with pyrrolidine-based inhibitors. Chem. Med. Chem. 2008, 3, 1337-1344.
    • (2008) Chem. Med. Chem. , vol.3 , pp. 1337-1344
    • Bottcher, J.1    Blum, A.2    Dorr, S.3    Heine, A.4    Diederich, W.E.5    Klebe, G.6
  • 148
  • 149
    • 67650511438 scopus 로고    scopus 로고
    • HIV protease inhibitors: Recent clinical trials and recommendations on use
    • Fernández-Montero, J.V.; Barreiro, P.; Soriano, V. HIV protease inhibitors: recent clinical trials and recommendations on use. Expert Opin. Pharmacother. 2009, 10, 1615-1629.
    • (2009) Expert Opin. Pharmacother. , vol.10 , pp. 1615-1629
    • Fernández-Montero, J.V.1    Barreiro, P.2    Soriano, V.3
  • 150
    • 67649586350 scopus 로고    scopus 로고
    • Protease inhibitor therapy in resource-limited settings
    • Elliott, J.H.; Pujari, S. Protease inhibitor therapy in resource-limited settings. Curr. Opin. HIV 2008, 3, 612-619.
    • (2008) Curr. Opin. HIV , vol.3 , pp. 612-619
    • Elliott, J.H.1    Pujari, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.