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Volumn 56, Issue 7, 2012, Pages 3620-3628

Activity of human immunodeficiency virus type 1 protease inhibitors against the initial autocleavage in Gag-Pol polyprotein processing

Author keywords

[No Author keywords available]

Indexed keywords

DARUNAVIR; GAG PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE 1 INHIBITOR; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; INDINAVIR; NELFINAVIR; RITONAVIR; SAQUINAVIR; TIPRANAVIR; UNCLASSIFIED DRUG;

EID: 84862551062     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.00055-12     Document Type: Article
Times cited : (33)

References (26)
  • 1
    • 76249090052 scopus 로고    scopus 로고
    • Once-daily treatment with saquinavir mesylate (2000 mg) and ritonavir (100 mg) together with a fixed-dose combination of abacavir/lamivudine (600/300 mg) or tenofovir/emtricitabine (245/200 mg) in HIV-1-infected patients
    • Bickel M, et al. 2009. Once-daily treatment with saquinavir mesylate (2000 mg) and ritonavir (100 mg) together with a fixed-dose combination of abacavir/lamivudine (600/300 mg) or tenofovir/emtricitabine (245/200 mg) in HIV-1-infected patients. J. Antimicrob. Chemother. 64: 1260-1264.
    • (2009) J. Antimicrob. Chemother. , vol.64 , pp. 1260-1264
    • Bickel, M.1
  • 2
    • 0029916638 scopus 로고    scopus 로고
    • Saquinavir: An HIV proteinase inhibitor
    • Bragman K. 1996. Saquinavir: an HIV proteinase inhibitor. Adv. Exp. Med. Biol. 394:305-317.
    • (1996) Adv. Exp. Med. Biol. , vol.394 , pp. 305-317
    • Bragman, K.1
  • 3
    • 23844551491 scopus 로고    scopus 로고
    • Prospects for the resistance to HIV protease inhibitors: Current drug design approaches and perspectives
    • Burlet S, et al. 2005. Prospects for the resistance to HIV protease inhibitors: current drug design approaches and perspectives. Curr. Pharm. Des. 11:3077-3090.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 3077-3090
    • Burlet, S.1
  • 4
    • 21244495659 scopus 로고    scopus 로고
    • Low-doses of indinavir boosted with ritonavir in HIV-infected Thai patients: Pharmacokinetics, efficacy and tolerability
    • Cressey TR, et al. 2005. Low-doses of indinavir boosted with ritonavir in HIV-infected Thai patients: pharmacokinetics, efficacy and tolerability. J. Antimicrob. Chemother. 55:1041-1044.
    • (2005) J. Antimicrob. Chemother. , vol.55 , pp. 1041-1044
    • Cressey, T.R.1
  • 5
    • 23744461868 scopus 로고    scopus 로고
    • Tipranavir: A ritonavir-boosted protease inhibitor
    • 1669-1677; discussion, 1678-1679
    • Croom, K. F., and Keam. S. J. 2005. Tipranavir: a ritonavir-boosted protease inhibitor. Drugs 65:1669-1677; discussion, 1678-1679.
    • (2005) Drugs , vol.65
    • Croom, K.F.1    Keam, S.J.2
  • 6
    • 78149463288 scopus 로고    scopus 로고
    • The initial step in human immunodeficiency virus type 1 GagProPol processing can be regulated by reversible oxidation
    • Daniels SI, et al. 2010. The initial step in human immunodeficiency virus type 1 GagProPol processing can be regulated by reversible oxidation. PLoS One 5:e13595.
    • (2010) PLoS One , vol.5
    • Daniels, S.I.1
  • 7
    • 33748457900 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by a peptide dimerization inhibitor of HIV-1 protease
    • Davis DA, et al. 2006. Inhibition of HIV-1 replication by a peptide dimerization inhibitor of HIV-1 protease. Antiviral Res. 72:89-99.
    • (2006) Antiviral Res. , vol.72 , pp. 89-99
    • Davis, D.A.1
  • 8
    • 8644220502 scopus 로고    scopus 로고
    • Stereoselective photochemical 1,3-dioxolane addition to 5-alkoxymethyl-2(5H)-furanone: Synthesis of bis-tetrahydrofuranyl ligand for HIV protease inhibitor UIC-94017 (TMC-114)
    • Ghosh AK, Leshchenko S, Noetzel M. 2004. Stereoselective photochemical 1,3-dioxolane addition to 5-alkoxymethyl-2(5H)-furanone: synthesis of bis-tetrahydrofuranyl ligand for HIV protease inhibitor UIC-94017 (TMC-114). J. Org. Chem. 69:7822-7829.
    • (2004) J. Org. Chem. , vol.69 , pp. 7822-7829
    • Ghosh, A.K.1    Leshchenko, S.2    Noetzel, M.3
  • 9
    • 35348960903 scopus 로고    scopus 로고
    • Potent inhibition of HIV-1 replication by novel nonpeptidyl small molecule inhibitors of protease dimerization
    • Koh Y, et al. 2007. Potent inhibition of HIV-1 replication by novel nonpeptidyl small molecule inhibitors of protease dimerization. J. Biol. Chem. 282:28709-28720.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28709-28720
    • Koh, Y.1
  • 10
    • 22844441964 scopus 로고    scopus 로고
    • The steady-state pharmacokinetics of nelfinavir in combination with tenofovir in HIV-infected patients
    • Kruse G, et al. 2005. The steady-state pharmacokinetics of nelfinavir in combination with tenofovir in HIV-infected patients. Antivir. Ther. 10:349-355.
    • (2005) Antivir. Ther. , vol.10 , pp. 349-355
    • Kruse, G.1
  • 11
    • 55049134097 scopus 로고    scopus 로고
    • Resilience to resistance of HIV-1 protease inhibitors: Profile of darunavir
    • Lefebvre E, Schiffer CA. 2008. Resilience to resistance of HIV-1 protease inhibitors: profile of darunavir. AIDS Rev. 10:131-142.
    • (2008) AIDS Rev. , vol.10 , pp. 131-142
    • Lefebvre, E.1    Schiffer, C.A.2
  • 12
    • 74249094258 scopus 로고    scopus 로고
    • First-line boosted protease inhibitor-based regimens in treatment-naive HIV-1-infected patients-making a good thing better
    • Llibre JM. 2009. First-line boosted protease inhibitor-based regimens in treatment-naive HIV-1-infected patients-making a good thing better. AIDS Rev. 11:215-222.
    • (2009) AIDS Rev. , vol.11 , pp. 215-222
    • Llibre, J.M.1
  • 13
    • 79959371401 scopus 로고    scopus 로고
    • Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors
    • Louis JM, Aniana A, Weber IT, Sayer JM. 2011. Inhibition of autoprocessing of natural variants and multidrug resistant mutant precursors of HIV-1 protease by clinical inhibitors. Proc. Natl. Acad. Sci. U. S. A. 108:9072-9077.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9072-9077
    • Louis, J.M.1    Aniana, A.2    Weber, I.T.3    Sayer, J.M.4
  • 14
    • 17444392445 scopus 로고    scopus 로고
    • Autoprocessing of HIV-1 protease is tightly coupled to protein folding
    • Louis JM, Clore GM, Gronenborn AM. 1999. Autoprocessing of HIV-1 protease is tightly coupled to protein folding. Nat. Struct. Biol. 6:868-875.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 868-875
    • Louis, J.M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 15
    • 35348860148 scopus 로고    scopus 로고
    • Prevalence of darunavir resistance-associated mutations: Patterns of occurrence and association with past treatment
    • Mitsuya Y, Liu TF, Rhee SY, Fessel WJ, Shafer RW. 2007. Prevalence of darunavir resistance-associated mutations: patterns of occurrence and association with past treatment. J. Infect. Dis. 196:1177-1179.
    • (2007) J. Infect. Dis. , vol.196 , pp. 1177-1179
    • Mitsuya, Y.1    Liu, T.F.2    Rhee, S.Y.3    Fessel, W.J.4    Shafer, R.W.5
  • 16
    • 77953509953 scopus 로고    scopus 로고
    • Protease inhibitor-based antiretroviral therapy in treatment-naive HIV-1-infected patients: The evidence behind the options
    • Naggie S, Hicks C. 2010. Protease inhibitor-based antiretroviral therapy in treatment-naive HIV-1-infected patients: the evidence behind the options. J. Antimicrob. Chemother. 65:1094-1099.
    • (2010) J. Antimicrob. Chemother. , vol.65 , pp. 1094-1099
    • Naggie, S.1    Hicks, C.2
  • 17
    • 23244441900 scopus 로고    scopus 로고
    • Ordered processing of the human immunodeficiency virus type 1 GagPol precursor is influenced by the context of the embedded viral protease
    • Pettit SC, Clemente JC, Jeung JA, Dunn BM, Kaplan AH. 2005. Ordered processing of the human immunodeficiency virus type 1 GagPol precursor is influenced by the context of the embedded viral protease. J. Virol. 79:10601-10607.
    • (2005) J. Virol. , vol.79 , pp. 10601-10607
    • Pettit, S.C.1    Clemente, J.C.2    Jeung, J.A.3    Dunn, B.M.4    Kaplan, A.H.5
  • 18
    • 3543142335 scopus 로고    scopus 로고
    • Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism
    • Pettit SC, Everitt LE, Choudhury S, Dunn BM, Kaplan AH. 2004. Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism. J. Virol. 78:8477-8485.
    • (2004) J. Virol. , vol.78 , pp. 8477-8485
    • Pettit, S.C.1    Everitt, L.E.2    Choudhury, S.3    Dunn, B.M.4    Kaplan, A.H.5
  • 19
    • 0037213627 scopus 로고    scopus 로고
    • The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage
    • Pettit SC, Gulnik S, Everitt L, Kaplan AH. 2003. The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage. J. Virol. 77:366-374.
    • (2003) J. Virol. , vol.77 , pp. 366-374
    • Pettit, S.C.1    Gulnik, S.2    Everitt, L.3    Kaplan, A.H.4
  • 20
    • 0029563229 scopus 로고
    • Development of drug resistance to HIV-1 protease inhibitors
    • Ridky T, Leis J. 1995. Development of drug resistance to HIV-1 protease inhibitors. J. Biol. Chem. 270:29621-29623.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29621-29623
    • Ridky, T.1    Leis, J.2
  • 21
    • 0029614884 scopus 로고
    • Drug-resistance patterns of saquinavir and other HIV proteinase inhibitors
    • Roberts NA. 1995. Drug-resistance patterns of saquinavir and other HIV proteinase inhibitors. AIDS 9(Suppl. 2):S27-S32.
    • (1995) AIDS , vol.9 , Issue.SUPPL. 2
    • Roberts, N.A.1
  • 22
    • 0141672041 scopus 로고    scopus 로고
    • The binding of HIV-1 protease inhibitors to human serum proteins
    • Schon A, del Mar Ingaramo M, Freire E. 2003. The binding of HIV-1 protease inhibitors to human serum proteins. Biophys. Chem. 105:221-230.
    • (2003) Biophys. Chem. , vol.105 , pp. 221-230
    • Schon, A.1    Del Mar Ingaramo, M.2    Freire, E.3
  • 23
    • 77957341230 scopus 로고    scopus 로고
    • Pharmacokinetics of darunavir/ritonavir and rifabutin coadministered in HIV-negative healthy volunteers
    • Sekar V, et al. 2010. Pharmacokinetics of darunavir/ritonavir and rifabutin coadministered in HIV-negative healthy volunteers. Antimicrob. Agents Chemother. 54:4440-4445.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 4440-4445
    • Sekar, V.1
  • 24
    • 20944431808 scopus 로고    scopus 로고
    • Novel human immunodeficiency virus type 1 protease mutations potentially involved in resistance to protease inhibitors
    • Svicher V, et al. 2005. Novel human immunodeficiency virus type 1 protease mutations potentially involved in resistance to protease inhibitors. Antimicrob. Agents Chemother. 49:2015-2025.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2015-2025
    • Svicher, V.1
  • 25
    • 10644266087 scopus 로고    scopus 로고
    • Acquisition of multi-PI (protease inhibitor) resistance in HIV-1 in vivo and in vitro
    • Yusa K, Harada S. 2004. Acquisition of multi-PI (protease inhibitor) resistance in HIV-1 in vivo and in vitro. Curr. Pharm. Des. 10:4055-4064.
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 4055-4064
    • Yusa, K.1    Harada, S.2
  • 26
    • 0030769354 scopus 로고    scopus 로고
    • Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites
    • Zhang YM, et al. 1997. Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites. J. Virol. 71:6662-6670.
    • (1997) J. Virol. , vol.71 , pp. 6662-6670
    • Zhang, Y.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.