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Volumn 11, Issue 24, 2005, Pages 3077-3090

Prospects for the resistance to HIV protease inhibitors: Current drug design approaches and prespectives

Author keywords

[No Author keywords available]

Indexed keywords

4,7 DIBENZYL 2,3,4,5,6,7 HEXAHYDRO 5,6 DIHYDROXY 1,3 BIS[4 (HYDROXYMETHYL)BENZYL] 2H 1,3 DIAZEPIN 2 ONE; 6 [2 (4 AMINOPHENYL)ETHYL] 3 (2 TERT BUTYL 4 HYDROXY 5 METHYLPHENYLTHIO) 5,6 DIHYDRO 4 HYDROXY 6 ISOPROPYL 2 PYRANONE; A 70450; ALUVIRAN; AMPRENAVIR; AMPRENAVIR PHOSPHATE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; ASPARTIC PROTEINASE INHIBITOR; ATAZANAVIR; BMS 234475; BRECANAVIR; DARUNAVIR; DPC 681; DPC 684; INDINAVIR; JE 2147; KNI 529; KNI 764; LASINAVIR; LIMONOID; LOPINAVIR; LOPINAVIR PLUS RITONAVIR; LYCERNUIC ACID C; MOZENAVIR; NELFINAVIR; NOMILIN; PNU 140690E; PROTEINASE INHIBITOR; RITONAVIR; RNA DIRECTED DNA POLYMERASE INHIBITOR; SAQUINAVIR; SM 319377; TIPRANAVIR; TMC 126; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 23844551491     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612054864939     Document Type: Review
Times cited : (16)

References (59)
  • 1
    • 0037936537 scopus 로고    scopus 로고
    • Aspartic proteases involved in Alzheimer's disease
    • Schmidt B. Aspartic proteases involved in Alzheimer's disease. Chembiochem 2003; 4: 366-378.
    • (2003) Chembiochem. , vol.4 , pp. 366-378
    • Schmidt, B.1
  • 2
    • 0037385686 scopus 로고    scopus 로고
    • A novel antiviral intervention results in more accurate assessment of human immunodeficiency virus type 1 replication dynamics and T-Cell decay in vivo
    • Markowitz M, Louie M, Hurley A, Sun E, Di Mascio M. A novel antiviral intervention results in more accurate assessment of human immunodeficiency virus type 1 replication dynamics and T-Cell decay in vivo. J Virol 2003; 77: 5037-5038.
    • (2003) J. Virol. , vol.77 , pp. 5037-5038
    • Markowitz, M.1    Louie, M.2    Hurley, A.3    Sun, E.4    Di Mascio, M.5
  • 4
    • 0000380425 scopus 로고
    • Recent Advances in Antiretroviral Chemotherapy for Aids
    • Norbeck DW. Recent Advances in Antiretroviral Chemotherapy for Aids. Annu Rep Med Chem 1990; 25: 149-158.
    • (1990) Annu. Rep. Med. Chem. , vol.25 , pp. 149-158
    • Norbeck, D.W.1
  • 5
    • 0027524696 scopus 로고
    • Human-Immunodeficiency-Virus Type-1 Reverse-Transcriptase and Ribonuclease-H as Substrates of the Viral Protease
    • Tomasselli AG, Sarcich JL, Barrett LJ, Reardon IM, Howe WJ, Evans DB, et al. Human-Immunodeficiency-Virus Type-1 Reverse-Transcriptase and Ribonuclease-H as Substrates of the Viral Protease. Protein Sci 1993; 2: 2167-2176.
    • (1993) Protein Sci. , vol.2 , pp. 2167-2176
    • Tomasselli, A.G.1    Sarcich, J.L.2    Barrett, L.J.3    Reardon, I.M.4    Howe, W.J.5    Evans, D.B.6
  • 6
    • 0029052114 scopus 로고
    • Specificity of Retroviral Proteases - An Analysis of Viral and Nonviral Protein Substrates. Retroviral Proteases
    • Tomasselli AG, Heinrikson RL. Specificity of Retroviral Proteases - an Analysis of Viral and Nonviral Protein Substrates. Retroviral Proteases. Methods Enzymol 1994; 241: 279-301.
    • (1994) Methods Enzymol. , vol.241 , pp. 279-301
    • Tomasselli, A.G.1    Heinrikson, R.L.2
  • 9
    • 0034011309 scopus 로고    scopus 로고
    • Human immunodeficiency virus type-1 protease inhibitors: Therapeutic successes and failures, suppression and resistance
    • Swanstrom R, Eron J. Human immunodeficiency virus type-1 protease inhibitors: therapeutic successes and failures, suppression and resistance. Pharmacol Therapeut 2000; 86: 145-170.
    • (2000) Pharmacol. Therapeut. , vol.86 , pp. 145-170
    • Swanstrom, R.1    Eron, J.2
  • 11
    • 0033940444 scopus 로고    scopus 로고
    • Incidence and impact of resistance against approved antiretroviral drugs
    • Pillay D, Taylor S, Richman DD. Incidence and impact of resistance against approved antiretroviral drugs. Rev Med Virol 2000; 10: 231-253.
    • (2000) Rev. Med. Virol. , vol.10 , pp. 231-253
    • Pillay, D.1    Taylor, S.2    Richman, D.D.3
  • 13
    • 0032850984 scopus 로고    scopus 로고
    • Evolution of genotypic resistance to nucleoside analogues in patients receiving protease inhibitor-containing regimens
    • Perez-Olmeda M, Rubio A, Puig T, Gomez-Cano M, Ruiz L, Leal M, et al. Evolution of genotypic resistance to nucleoside analogues in patients receiving protease inhibitor-containing regimens. Antivir Ther 1999; 4: 179-181.
    • (1999) Antivir. Ther. , vol.4 , pp. 179-181
    • Perez-Olmeda, M.1    Rubio, A.2    Puig, T.3    Gomez-Cano, M.4    Ruiz, L.5    Leal, M.6
  • 14
    • 0042658343 scopus 로고    scopus 로고
    • Long-cycle structured intermittent versus continuous highly active antiretroviral therapy for the treatment of chronic infection with human immunodeficiency virus: Effects on drug toxicity and on immunologic and virologic parameters
    • Dybul M, Nies-Kraske E, Daucher M, Hertogs K, Hallahan CW, Csako G, et al. Long-cycle structured intermittent versus continuous highly active antiretroviral therapy for the treatment of chronic infection with human immunodeficiency virus: Effects on drug toxicity and on immunologic and virologic parameters. J Infect Dis 2003; 188: 388-396.
    • (2003) J. Infect. Dis. , vol.188 , pp. 388-396
    • Dybul, M.1    Nies-Kraske, E.2    Daucher, M.3    Hertogs, K.4    Hallahan, C.W.5    Csako, G.6
  • 15
    • 0037415030 scopus 로고    scopus 로고
    • Immunological changes during treatment interruptions: Risk factors and clinical sequelae
    • Poulton MB, Sabin CA, Fisher M. Immunological changes during treatment interruptions: risk factors and clinical sequelae. Aids 2003; 17: 126-128.
    • (2003) Aids , vol.17 , pp. 126-128
    • Poulton, M.B.1    Sabin, C.A.2    Fisher, M.3
  • 16
    • 1942502407 scopus 로고    scopus 로고
    • Novel lopinavir analogues incorporating heterocyclic replacements of six-member cyclic urea synthesis and structure-activity relationships
    • in press
    • Sham HL, Betebenner DA, Herrin T, Kumar G, Saldivar A, Vasavanonda S, et al. Novel lopinavir analogues incorporating heterocyclic replacements of six-member cyclic urea synthesis and structure-activity relationships. Bioorg Med Chem Lett 2004; in press.
    • (2004) Bioorg. Med. Chem. Lett.
    • Sham, H.L.1    Betebenner, D.A.2    Herrin, T.3    Kumar, G.4    Saldivar, A.5    Vasavanonda, S.6
  • 17
  • 19
    • 0033931167 scopus 로고    scopus 로고
    • BMS-232632; a highly potent human immunodeficiency virus protease inhibitor that can be used in combination with other available antiretroviral agents
    • Robinson BS, Riccardi KA, Gong YF, Guo Q, Stock DA, Blair WS, et al. BMS-232632; a highly potent human immunodeficiency virus protease inhibitor that can be used in combination with other available antiretroviral agents. Antimicrob Agents Ch 2000; 44: 2093-2099.
    • (2000) Antimicrob. Agents Ch. , vol.44 , pp. 2093-2099
    • Robinson, B.S.1    Riccardi, K.A.2    Gong, Y.F.3    Guo, Q.4    Stock, D.A.5    Blair, W.S.6
  • 20
    • 0030610689 scopus 로고    scopus 로고
    • In vitro effect of alpha(1)-acid glycoprotein on the anti-human immunodeficiency virus (HIV) activity of the protease inhibitor CGP 61755: A comparative study with other relevant HIV protease inhibitors
    • Lazdins JK, Mestan J, Goutte G, Walker MR, Bold G, Capraro HG, et al. In vitro effect of alpha(1)-acid glycoprotein on the anti-human immunodeficiency virus (HIV) activity of the protease inhibitor CGP 61755: A comparative study with other relevant HIV protease inhibitors. J Infect Dis 1997; 175: 1063-1070.
    • (1997) J. Infect. Dis. , vol.175 , pp. 1063-1070
    • Lazdins, J.K.1    Mestan, J.2    Goutte, G.3    Walker, M.R.4    Bold, G.5    Capraro, H.G.6
  • 21
    • 0036229961 scopus 로고    scopus 로고
    • Fosamprenavir. Vertex Pharmaceuticals/GlaxoSmithKline
    • Corbett AH, Kashuba AD. Fosamprenavir. Vertex Pharmaceuticals/GlaxoSmithKline. Curr Opin Investig Drugs 2002; 3: 384-390
    • (2002) Curr. Opin. Investig. Drugs , vol.3 , pp. 384-390
    • Corbett, A.H.1    Kashuba, A.D.2
  • 23
    • 0842281261 scopus 로고    scopus 로고
    • Novel arylsulfonamides possessing sub-picomolar HIV protease activities and potent anti-HIV activity against wild-type and drug-resistant viral strains
    • Miller JF, Furfine ES, Hanlon MH, Hazen RJ, Ray JA, Robinson L, et al. Novel arylsulfonamides possessing sub-picomolar HIV protease activities and potent anti-HIV activity against wild-type and drug-resistant viral strains. Bioorg Med Chem Lett 2004; 14: 959-963.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 959-963
    • Miller, J.F.1    Furfine, E.S.2    Hanlon, M.H.3    Hazen, R.J.4    Ray, J.A.5    Robinson, L.6
  • 24
    • 0028846226 scopus 로고
    • Crystal-Structure of HIV-1 Protease in Complex with Vx-478: A Potent and Orally Bioavailable Inhibitor of the Enzyme
    • Kim EE, Baker CT, Dwyer MD, Murcko MA, Rao BG, Tung RD, et al. 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
  • 25
    • 0033862253 scopus 로고    scopus 로고
    • Structural and kinetic analyses of the protease from an amprenavir-resistant human immunodeficiency virus type 1 mutant rendered resistant to saquinavir and resensitized to amprenavir
    • Markland W, Rao BG, Parsons JD, Black J, Zuchowski L, Tisdale M, et al. Structural and kinetic analyses of the protease from an amprenavir-resistant human immunodeficiency virus type 1 mutant rendered resistant to saquinavir and resensitized to amprenavir. J Virol 2000; 74: 7636-7641.
    • (2000) J. Virol. , vol.74 , pp. 7636-7641
    • Markland, W.1    Rao, B.G.2    Parsons, J.D.3    Black, J.4    Zuchowski, L.5    Tisdale, M.6
  • 27
    • 0036145503 scopus 로고    scopus 로고
    • A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site
    • Yoshimura K, Kato R, Kavlick MF, Nguyen A, Maroun V, Maeda K, et al. A potent human immunodeficiency virus type 1 protease inhibitor, UIC-94003 (TMC-126), and selection of a novel (A28S) mutation in the protease active site. J Virol 2002; 76: 1349-1358.
    • (2002) J. Virol. , vol.76 , pp. 1349-1358
    • Yoshimura, K.1    Kato, R.2    Kavlick, M.F.3    Nguyen, A.4    Maroun, V.5    Maeda, K.6
  • 28
    • 10744226241 scopus 로고    scopus 로고
    • Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro
    • Koh Y, Nakata H, Maeda K, Ogata H, Bilcer G, Devasamudram, T, et al. Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro. Antimicrob Agents Chemother 2003; 47: 3123-3129.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3123-3129
    • Koh, Y.1    Nakata, H.2    Maeda, K.3    Ogata, H.4    Bilcer, G.5    Devasamudram, T.6
  • 29
    • 33645204477 scopus 로고    scopus 로고
    • Antiretroviral Activity, Resistance and Safety of TMC 114: A next generation HIV-protease inhibitor, in multiple PI-experienced patients Abstract LB 16
    • Abstracts of the 2nd IAS Conference on HIV Pathogenesis and Treatment July 13-16: Paris, France
    • Arasteh K, Clumeck N, Pozniak A, Jaeger H, De Pauw M, Muller H, et al. Antiretroviral Activity, Resistance and Safety of TMC 114: a next generation HIV-protease inhibitor, in multiple PI-experienced patients. Abstract LB 16. Abstracts of the 2nd IAS Conference on HIV Pathogenesis and Treatment. July 13-16: 2003; Paris, France.
    • (2003)
    • Arasteh, K.1    Clumeck, N.2    Pozniak, A.3    Jaeger, H.4    De Pauw, M.5    Muller, H.6
  • 30
    • 33645203315 scopus 로고    scopus 로고
    • TMC114: A next generation HIV protease inhibitor: Pharmacokinetics and safety following oral administration of multiple doses with and without low doses of Ritonavir in healthy volunteers
    • Abstract 549: 10th Conference on Retroviruses and Opportunistic Infections. February 10-14: Boston, MA, USA
    • Hoetelmans R, Van der Sandt I, De Pauw M, Struble K, Peeters M, Van der Geest R. TMC114: a next generation HIV protease inhibitor: pharmacokinetics and safety following oral administration of multiple doses with and without low doses of Ritonavir in healthy volunteers. Abstract 549: 10th Conference on Retroviruses and Opportunistic Infections. February 10-14: 2003. Boston, MA, USA.
    • (2003)
    • Hoetelmans, R.1    Van der Sandt, I.2    De Pauw, M.3    Struble, K.4    Peeters, M.5    Van der Geest, R.6
  • 32
    • 0036137494 scopus 로고    scopus 로고
    • Designing drugs against heterogeneous targets
    • Freire E. Designing drugs against heterogeneous targets. Nat Biotechnol 2002; 20: 15-16.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 15-16
    • Freire, E.1
  • 33
    • 0036078615 scopus 로고    scopus 로고
    • Overcoming drug resistance in HIV-1 chemotherapy: The binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug-resistant mutants ofthe HIV-1 protease
    • Ohtaka H, Velaquez-Campoy A, Xie D, Freire E. Overcoming drug resistance in HIV-1 chemotherapy: The binding thermodynamics of Amprenavir and TMC-126 to wild-type and drug-resistant mutants ofthe HIV-1 protease. Protein Sci 2002; 11: 1908-1916.
    • (2002) Protein Sci. , vol.11 , pp. 1908-1916
    • Ohtaka, H.1    Velaquez-Campoy, A.2    Xie, D.3    Freire, E.4
  • 34
    • 0347931880 scopus 로고    scopus 로고
    • Structure-activity and structure-metabolism relationships of HIV protease inhibitors containing the 3-hydroxy-2-methylbenzoyl-allophenylnorstatine structure
    • Mimoto T, Terashima K, Nojima S, Takaku H, Nakayama M, Shintani M, et al. Structure-activity and structure-metabolism relationships of HIV protease inhibitors containing the 3-hydroxy-2-methylbenzoyl-allophenylnorstatine structure. Bioorg Med Chem 2004; 12: 281-293.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 281-293
    • Mimoto, T.1    Terashima, K.2    Nojima, S.3    Takaku, H.4    Nakayama, M.5    Shintani, M.6
  • 35
    • 0037122707 scopus 로고    scopus 로고
    • Beta-strand mimicking macrocyclic amino acids: Templates for protease inhibitors with antiviral activity
    • Glenn MP, Pattenden LK, Reid RC, Tyssen DP, Tyndall JDA, Birch CJ, et al. beta-strand mimicking macrocyclic amino acids: Templates for protease inhibitors with antiviral activity. J Med Chem 2002; 45: 371-381.
    • (2002) J. Med. Chem. , vol.45 , pp. 371-381
    • Glenn, M.P.1    Pattenden, L.K.2    Reid, R.C.3    Tyssen, D.P.4    Tyndall, J.D.A.5    Birch, C.J.6
  • 36
    • 0029926111 scopus 로고    scopus 로고
    • Substrate-based cyclic peptidomimetics of Phe-Ile-Val that inhibit HIV-1 protease using a novel enzyme-binding mode
    • March DR, Abbenante G, Bergman DA, Brinkworth RI, Wickramasinghe W, Begun J, et al. Substrate-based cyclic peptidomimetics of Phe-Ile-Val that inhibit HIV-1 protease using a novel enzyme-binding mode. J Am Chem Soc 1996; 118: 3375-3379.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3375-3379
    • March, D.R.1    Abbenante, G.2    Bergman, D.A.3    Brinkworth, R.I.4    Wickramasinghe, W.5    Begun, J.6
  • 37
    • 0034699496 scopus 로고    scopus 로고
    • Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease
    • Tyndall JDA, Reid RC, Tyssen DP, Jardine DK, Todd B, Passmore M, et al. Synthesis, stability, antiviral activity, and protease-bound structures of substrate-mimicking constrained macrocyclic inhibitors of HIV-1 protease. J Med Chem 2000; 43: 3495-3504.
    • (2000) J. Med. Chem. , vol.43 , pp. 3495-3504
    • Tyndall, J.D.A.1    Reid, R.C.2    Tyssen, D.P.3    Jardine, D.K.4    Todd, B.5    Passmore, M.6
  • 38
    • 0034611591 scopus 로고    scopus 로고
    • Conformational selection of inhibitors and substrates by proteolytic enzymes: Implications for drug design and polypeptide processing
    • Fairlie DP, Tyndall JDA, Reid RC, Wong AK, Abbenante G, Scanlon MJ, et al. Conformational selection of inhibitors and substrates by proteolytic enzymes: Implications for drug design and polypeptide processing. J Med Chem 2000; 43: 1271-1281.
    • (2000) J. Med. Chem. , vol.43 , pp. 1271-1281
    • Fairlie, D.P.1    Tyndall, J.D.A.2    Reid, R.C.3    Wong, A.K.4    Abbenante, G.5    Scanlon, M.J.6
  • 40
    • 0027450602 scopus 로고
    • Effect of the oral anticoagulant, warfarin, on HIV-1 replication and spread
    • Bourinbaiar AS, Tan X, Nagorny R. Effect of the oral anticoagulant, warfarin, on HIV-1 replication and spread. Aids 1993; 7: 129-130.
    • (1993) Aids , vol.7 , pp. 129-130
    • Bourinbaiar, A.S.1    Tan, X.2    Nagorny, R.3
  • 41
    • 0033047131 scopus 로고    scopus 로고
    • Structure-based discovery of tipranavir disodium (PNU-140690E): A potent, orally bioavailable, nonpeptidic HIV protease inhibitor
    • Thaisrivongs S, Strohbach JW. Structure-based discovery of tipranavir disodium (PNU-140690E): A potent, orally bioavailable, nonpeptidic HIV protease inhibitor. Biopolymers 1999; 51: 51-58.
    • (1999) Biopolymers , vol.51 , pp. 51-58
    • Thaisrivongs, S.1    Strohbach, J.W.2
  • 42
    • 0030895692 scopus 로고    scopus 로고
    • Antiviral activity of the dihydro-pyrone PNU-140690; A new nonpeptidic human immunodeficiency virus protease inhibitor
    • Poppe SM, Slade DE, Chong KT, Hinshaw RR, Pagano PJ, Markowitz M, et al. Antiviral activity of the dihydro-pyrone PNU-140690; a new nonpeptidic human immunodeficiency virus protease inhibitor. Antimicrob Agents Chemother 1997; 41: 1058-1063.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1058-1063
    • Poppe, S.M.1    Slade, D.E.2    Chong, K.T.3    Hinshaw, R.R.4    Pagano, P.J.5    Markowitz, M.6
  • 43
    • 0035811452 scopus 로고    scopus 로고
    • 4-hydroxy-5, 6-dihydropyrones as inhibitors of HIV protease: The effect of heterocyclic substituents at C-6 on antiviral potency and pharmacokinetic parameters
    • Hagen SE, Domagala J, Gajda C, Lovdahl M, Tait BD, Wise E, et al. 4-hydroxy-5, 6-dihydropyrones as inhibitors of HIV protease: The effect of heterocyclic substituents at C-6 on antiviral potency and pharmacokinetic parameters. J Med Chem 2001; 44: 2319-2332.
    • (2001) J. Med. Chem. , vol.44 , pp. 2319-2332
    • Hagen, S.E.1    Domagala, J.2    Gajda, C.3    Lovdahl, M.4    Tait, B.D.5    Wise, E.6
  • 44
    • 33645206364 scopus 로고
    • IX International Conference on AIDS, June 7-11: Berlin, Germany
    • Wild H, Hansen J, Lautz J.: IX International Conference on AIDS, June 7-11: 1993; Berlin, Germany.
    • (1993)
    • Wild, H.1    Hansen, J.2    Lautz, J.3
  • 45
    • 0028057975 scopus 로고
    • Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors
    • Lam PYS, Jadhav PK, Eyermann CJ, Hodge CN, Ru Y, Bacheler LT, et al. Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors. Science 1994; 263: 380-384.
    • (1994) Science , vol.263 , pp. 380-384
    • Lam, P.Y.S.1    Jadhav, P.K.2    Eyermann, C.J.3    Hodge, C.N.4    Ru, Y.5    Bacheler, L.T.6
  • 46
    • 33645196308 scopus 로고
    • Reduced sensitivity to HIV PR inhibitors is associated with single amino acid substitutions in HIV-1 PR
    • Second International Workshop on HIV Drug Resistance. June 3-5: Noordwijk, Netherlands
    • Otto MJ, Garber S, Stack S, Winslow D. Reduced sensitivity to HIV PR inhibitors is associated with single amino acid substitutions in HIV-1 PR. Second International Workshop on HIV Drug Resistance. June 3-5: 1993; Noordwijk, Netherlands.
    • (1993)
    • Otto, M.J.1    Garber, S.2    Stack, S.3    Winslow, D.4
  • 47
    • 0030113025 scopus 로고    scopus 로고
    • Improved cyclic urea inhibitors of the HIV-I protease: Synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450
    • Hodge CN, Aldrich PE, Bacheler LT, Chang CH, Eyermann CJ, Garber S, et al. Improved cyclic urea inhibitors of the HIV-I protease: Synthesis, potency, resistance profile, human pharmacokinetics and X-ray crystal structure of DMP 450. Chem Biol 1996; 3: 301-314.
    • (1996) Chem. Biol. , vol.3 , pp. 301-314
    • Hodge, C.N.1    Aldrich, P.E.2    Bacheler, L.T.3    Chang, C.H.4    Eyermann, C.J.5    Garber, S.6
  • 48
    • 33645189971 scopus 로고
    • 33rd Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC). October 17-20: New-Orleans, LA, USA
    • Appelt K. 33rd Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC). October 17-20: 1993; New-Orleans, LA, USA.
    • (1993)
    • Appelt, K.1
  • 49
    • 16044375105 scopus 로고
    • Crystal structures of HIV-1 protease inhibitor complexes
    • Appelt K. Crystal structures of HIV-1 protease inhibitor complexes. Perspect Drug Discov Des 1993; 1: 23-48.
    • (1993) Perspect. Drug Discov. Des. , vol.1 , pp. 23-48
    • Appelt, K.1
  • 50
    • 0023477907 scopus 로고
    • Human immunodeficiency virus protease expressed in escherichia-coli exhibits autoprocessing and specific maturation of the Gag precursor
    • Debouck C, Gorniak JG, Strickler JE, Meek TD, Metcalf BW, Rosenberg M. Human immunodeficiency virus protease expressed in escherichia-coli exhibits autoprocessing and specific maturation of the Gag precursor. Proc Natl Acad Sci USA 1987; 84: 8903-8906.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8903-8906
    • Debouck, C.1    Gorniak, J.G.2    Strickler, J.E.3    Meek, T.D.4    Metcalf, B.W.5    Rosenberg, M.6
  • 51
    • 0034615536 scopus 로고    scopus 로고
    • Synthesis and chemical reactivity of thiophenoxyphenylalanine bioisosteres, suitable synthons for the design of HIV protease inhibitors
    • Priem G, Rocheblave L, De Michelis C, Courcambeck J, Kraus JL. Synthesis and chemical reactivity of thiophenoxyphenylalanine bioisosteres, suitable synthons for the design of HIV protease inhibitors. J Chem Soc Perkin Trans 1 2000; 819-824.
    • (2000) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 819-824
    • Priem, G.1    Rocheblave, L.2    De Michelis, C.3    Courcambeck, J.4    Kraus, J.L.5
  • 52
    • 0035974621 scopus 로고    scopus 로고
    • New 3′-azido-3′-deoxythymidin-5′-yl O-(4-hydroxyalkyl or -alkenyl or -alkylepoxide) carbonate prodrugs: Synthesis and anti-HIV evaluation
    • Vlieghe P, Clerc T, Pannecouque C, Witvrouw M, De Clercq E, Salles JP, et al. New 3′-azido-3′-deoxythymidin-5′-yl O-(4-hydroxyalkyl or -alkenyl or -alkylepoxide) carbonate prodrugs: Synthesis and anti-HIV evaluation. J Med Chem 2001; 44: 3014-3021.
    • (2001) J. Med. Chem. , vol.44 , pp. 3014-3021
    • Vlieghe, P.1    Clerc, T.2    Pannecouque, C.3    Witvrouw, M.4    De Clercq, E.5    Salles, J.P.6
  • 53
    • 0038309240 scopus 로고    scopus 로고
    • Novel prodrug approach to amprenavir-based HIV-1 protease inhibitors via O -> N Acyloxy migration of P1 moiety
    • Kazmierski WM, Bevans P, Furfine E, Spaltenstein A. Yang HB. Novel prodrug approach to amprenavir-based HIV-1 protease inhibitors via O -> N Acyloxy migration of P1 moiety. Bioorg Med Chem Lett 2003; 13: 2523-2526.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2523-2526
    • Kazmierski, W.M.1    Bevans, P.2    Furfine, E.3    Spaltenstein, A.4    Yang, H.B.5
  • 56
    • 0037310296 scopus 로고    scopus 로고
    • Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors
    • Watkins T, Resch W, Irlbeck D, Swanstrom R. Selection of high-level resistance to human immunodeficiency virus type 1 protease inhibitors. Antimicrob Agents Chemother 2003; 47: 759-769.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 759-769
    • Watkins, T.1    Resch, W.2    Irlbeck, D.3    Swanstrom, R.4
  • 57
    • 0344276472 scopus 로고    scopus 로고
    • Novel inhibitors of HIV integrase: The discovery of potential anti-HIV therapeutic agents
    • Nair V. Novel inhibitors of HIV integrase: the discovery of potential anti-HIV therapeutic agents. Curr Pharm Design 2003; 9(31): 2553-65.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.31 , pp. 2553-2565
    • Nair, V.1
  • 58
    • 0041488689 scopus 로고    scopus 로고
    • Proteolytic events of HIV-1 replication as targets for therapeutic intervention
    • Tozser J, Oroszlan S. Proteolytic events of HIV-1 replication as targets for therapeutic intervention. Curr Pharm Design 2003; 9(22): 1803-15.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.22 , pp. 1803-1815
    • Tozser, J.1    Oroszlan, S.2
  • 59
    • 0042991375 scopus 로고    scopus 로고
    • Prodrugs of HIV protease inhibitors
    • Vierling P, Greiner J. Prodrugs of HIV protease inhibitors. Curr Pharm Design 2003; 9(22): 1755-70.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.22 , pp. 1755-1770
    • Vierling, P.1    Greiner, J.2


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