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Volumn 19, Issue 10, 2013, Pages 1850-1859

Molecular aspects of the RT/drug interactions. Perspective of dual inhibitors

Author keywords

HIV; RT binding pockets and novel inhibitors

Indexed keywords

ABACAVIR; ADEFOVIR; CP 94707; DAPIVIRINE; DELAVIRDINE; DIDANOSINE; EFAVIRENZ; EMTRICITABINE; ETRAVIRINE; LAMIVUDINE; NEVIRAPINE; NONNUCLEOSIDE REVERSE TRANSCRIPTASE INHIBITOR; RIBONUCLEASE H; RILPIVIRINE; RNA DIRECTED DNA POLYMERASE INHIBITOR; STAVUDINE; TENOFOVIR; UNCLASSIFIED DRUG; ZALCITABINE; ZIDOVUDINE;

EID: 84876709287     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319100009     Document Type: Review
Times cited : (40)

References (73)
  • 1
    • 0020596551 scopus 로고
    • Isolation of a Tlymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS)
    • Barre-Sinoussi F, Chermann JC, Rey F, et al. Isolation of a Tlymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science 1983; 220(4599): 868-71.
    • (1983) Science , vol.220 , Issue.4599 , pp. 868-871
    • Barre-Sinoussi, F.1    Chermann, J.C.2    Rey, F.3
  • 2
    • 0021281132 scopus 로고
    • Serological analysis of a subgroup of human Tlymphotropic retroviruses (HTLV-III) associated with AIDS
    • Schupbach J, Popovic M, Gilden RV, Gonda MA, Sarngadharan MG, Gallo RC. Serological analysis of a subgroup of human Tlymphotropic retroviruses (HTLV-III) associated with AIDS. Science 1984; 224(4648): 503-5.
    • (1984) Science , vol.224 , Issue.4648 , pp. 503-505
    • Schupbach, J.1    Popovic, M.2    Gilden, R.V.3    Gonda, M.A.4    Sarngadharan, M.G.5    Gallo, R.C.6
  • 3
    • 84876701087 scopus 로고    scopus 로고
    • www.unaids.org/en/media/unaids/contentassets/documents/ unaidspublication/ 2011/JC2216_WorldAIDSday_report_2011_en.pdf.
  • 4
    • 77249134151 scopus 로고    scopus 로고
    • Twenty-six years of anti-HIV drug discovery: Where do we stand and where do we go?
    • Mehellou Y, De Clercq E. Twenty-six years of anti-HIV drug discovery: Where do we stand and where do we go? J Med Chem 2009; 53(2): 521-38.
    • (2009) J Med Chem , vol.53 , Issue.2 , pp. 521-538
    • Mehellou, Y.1    de Clercq, E.2
  • 5
    • 33847414203 scopus 로고    scopus 로고
    • Ten years of highly active antiretroviral therapy for HIV infection
    • Chen LF, Hoy J, Lewin SR. Ten years of highly active antiretroviral therapy for HIV infection. Med J Aust 2007; 186(3): 146-51.
    • (2007) Med J Aust , vol.186 , Issue.3 , pp. 146-151
    • Chen, L.F.1    Hoy, J.2    Lewin, S.R.3
  • 6
    • 0021912920 scopus 로고
    • Complete nucleotide sequence of the AIDS virus, HTLV-III
    • Ratner L, Haseltine W, Patarca R, et al. Complete nucleotide sequence of the AIDS virus, HTLV-III. Nature 1985; 313(6000): 277-84.
    • (1985) Nature , vol.313 , Issue.6000 , pp. 277-284
    • Ratner, L.1    Haseltine, W.2    Patarca, R.3
  • 7
    • 0002615512 scopus 로고    scopus 로고
    • RNase H of retroviral reverse transcriptases
    • In: H CR, Toulmé JJ., Eds, Les Editions Inserm: Paris
    • Hughes S, Arnold E, Hostomsky Z. RNase H of retroviral reverse transcriptases. In: H CR, Toulmé JJ., Eds. Ribonucleases. Les Editions Inserm: Paris; 1998; pp. 195-224.
    • (1998) Ribonucleases , pp. 195-224
    • Hughes, S.1    Arnold, E.2    Hostomsky, Z.3
  • 8
    • 0025314263 scopus 로고
    • Processing of the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase
    • Huber HE, Richardson CC. Processing of the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase. J Biol Chem 1990; 265(18): 10565-73.
    • (1990) J Biol Chem , vol.265 , Issue.18 , pp. 10565-10573
    • Huber, H.E.1    Richardson, C.C.2
  • 9
    • 2942525660 scopus 로고    scopus 로고
    • 'Binding, bending and bonding': Polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus
    • Rausch JW, Le Grice SFJ. 'Binding, bending and bonding': polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus. Int J Biochem Cell Biol 2004; 36(9): 1752-66.
    • (2004) Int J Biochem Cell Biol , vol.36 , Issue.9 , pp. 1752-1766
    • Rausch, J.W.1    Le Grice, S.F.J.2
  • 11
    • 0028964233 scopus 로고
    • Dimerization kinetics of HIV-1 and HIV-2 Reverse Transcriptase: A two step process
    • Divita G, Rittinger K, Geourjon C, Deléage G, Goody RS. Dimerization kinetics of HIV-1 and HIV-2 Reverse Transcriptase: A two step process. J Mol Biol 1995; 245(5): 508-21.
    • (1995) J Mol Biol , vol.245 , Issue.5 , pp. 508-521
    • Divita, G.1    Rittinger, K.2    Geourjon, C.3    Deléage, G.4    Goody, R.S.5
  • 12
    • 0027318776 scopus 로고
    • Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA
    • Jacobo-Molina A, Ding J, Nanni RG, et al. Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA. Proc Natl Acad Sci USA 1993; 90(13): 6320-4.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.13 , pp. 6320-6324
    • Jacobo-Molina, A.1    Ding, J.2    Nanni, R.G.3
  • 13
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt L, Wang J, Friedman J, Rice P, Steitz T. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 1992; 256(5065): 1783-90.
    • (1992) Science , vol.256 , Issue.5065 , pp. 1783-1790
    • Kohlstaedt, L.1    Wang, J.2    Friedman, J.3    Rice, P.4    Steitz, T.5
  • 14
    • 56449114709 scopus 로고    scopus 로고
    • Slide into action: Dynamic shuttling of HIV Reverse Transcriptase on nucleic acid substrates
    • Liu S, Abbondanzieri EA, Rausch JW, Grice SFJL, Zhuang X. Slide into action: Dynamic shuttling of HIV Reverse Transcriptase on nucleic acid substrates. Science 2008; 322(5904): 1092-7.
    • (2008) Science , vol.322 , Issue.5904 , pp. 1092-1097
    • Liu, S.1    Abbondanzieri, E.A.2    Rausch, J.W.3    Grice, S.F.J.L.4    Zhuang, X.5
  • 15
    • 0032518374 scopus 로고    scopus 로고
    • Structural biology: A mechanism for all polymerases
    • Steitz TA. Structural biology: A mechanism for all polymerases. Nature 1998; 391(6664): 231-2.
    • (1998) Nature , vol.391 , Issue.6664 , pp. 231-232
    • Steitz, T.A.1
  • 16
    • 56649096052 scopus 로고    scopus 로고
    • Examining the ribonuclease H primer grip of HIV-1 reverse transcriptase by charge neutralization of RNA/DNA hybrids
    • Dash C, Scarth BJ, Badorrek C, Götte M, Le Grice SFJ. Examining the ribonuclease H primer grip of HIV-1 reverse transcriptase by charge neutralization of RNA/DNA hybrids. Nucleic Acids Res 2008; 36(20): 6363-71.
    • (2008) Nucleic Acids Res , vol.36 , Issue.20 , pp. 6363-6371
    • Dash, C.1    Scarth, B.J.2    Badorrek, C.3    Götte, M.4    Le Grice, S.F.J.5
  • 17
    • 58149133507 scopus 로고    scopus 로고
    • Structure and function of HIV-1 Reverse Transcriptase: Molecular mechanisms of polymerization and Inhibition
    • Sarafianos SG, Marchand B, Das K, et al. Structure and function of HIV-1 Reverse Transcriptase: Molecular mechanisms of polymerization and Inhibition. J Mol Biol 2009; 385(3): 693-713.
    • (2009) J Mol Biol , vol.385 , Issue.3 , pp. 693-713
    • Sarafianos, S.G.1    Marchand, B.2    Das, K.3
  • 18
    • 77952388742 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational change governs specificity and analog discrimination by HIV reverse transcriptase
    • Kellinger MW, Johnson KA. Nucleotide-dependent conformational change governs specificity and analog discrimination by HIV reverse transcriptase. Proc Natl Acad Sci USA 2010; 107(17): 7734-9.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.17 , pp. 7734-7739
    • Kellinger, M.W.1    Johnson, K.A.2
  • 19
    • 77955648999 scopus 로고    scopus 로고
    • HIV-1 RT-associated RNase H function inhibitors: Recent advances in drug development
    • Tramontano E, Di Santo R. HIV-1 RT-associated RNase H function inhibitors: Recent advances in drug development. Curr Med Chem 2010; 17(26): 2837-53.
    • (2010) Curr Med Chem , vol.17 , Issue.26 , pp. 2837-2853
    • Tramontano, E.1    Di Santo, R.2
  • 20
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: Substrate specificity and metal-dependent catalysis
    • Nowotny M, Gaidamakov SA, Crouch RJ, Yang W. Crystal structures of RNase H bound to an RNA/DNA hybrid: Substrate specificity and metal-dependent catalysis. Cell 2005; 121(7): 1005-16.
    • (2005) Cell , vol.121 , Issue.7 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 22
    • 56249142738 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid traps Reverse Transcriptase on nucleic acid substrates
    • Grohmann D, Godet J, Mély Y, Darlix J-L, Restle T. HIV-1 nucleocapsid traps Reverse Transcriptase on nucleic acid substrates. Biochemistry 2008; 47(46): 12230-40.
    • (2008) Biochemistry , vol.47 , Issue.46 , pp. 12230-12240
    • Grohmann, D.1    Godet, J.2    Mély, Y.3    Darlix, J.-L.4    Restle, T.5
  • 23
    • 0030067973 scopus 로고    scopus 로고
    • Effect of Human Immunodeficiency Virus Type 1 (HIV-1) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro
    • Ji X, Klarmann GJ, Preston BD. Effect of Human Immunodeficiency Virus Type 1 (HIV-1) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro. Biochemistry 1996; 35(1): 132-43.
    • (1996) Biochemistry , vol.35 , Issue.1 , pp. 132-143
    • Ji, X.1    Klarmann, G.J.2    Preston, B.D.3
  • 24
    • 0032506228 scopus 로고    scopus 로고
    • Unblocking of chainterminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism
    • Meyer PR, Matsuura SE, So AG, Scott WA. Unblocking of chainterminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism. Proc Natl Acad Sci USA 1998; 95(23): 13471-6.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.23 , pp. 13471-13476
    • Meyer, P.R.1    Matsuura, S.E.2    So, A.G.3    Scott, W.A.4
  • 25
    • 0032506055 scopus 로고    scopus 로고
    • Phenotypic mechanism of HIV-1 resistance to 3'-Azido-3'-deoxythymidine (AZT):β increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral Reverse Transcriptase
    • Arion D, Kaushik N, McCormick S, Borkow G, Parniak MA. Phenotypic mechanism of HIV-1 resistance to 3'-Azido-3'-deoxythymidine (AZT):β increased polymerization processivity and enhanced sensitivity to pyrophosphate of the mutant viral Reverse Transcriptase. Biochemistry 1998; 37(45): 15908-17.
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15908-15917
    • Arion, D.1    Kaushik, N.2    McCormick, S.3    Borkow, G.4    Parniak, M.A.5
  • 26
    • 43049113468 scopus 로고    scopus 로고
    • APOBEC3 proteins and reverse transcription
    • Aguiar RS, Peterlin BM. APOBEC3 proteins and reverse transcription. Virus Res 2008; 134(1-2): 74-85.
    • (2008) Virus Res , vol.134 , Issue.1-2 , pp. 74-85
    • Aguiar, R.S.1    Peterlin, B.M.2
  • 27
    • 0030969223 scopus 로고    scopus 로고
    • Incorporation of selected nucleoside phosphonates and anti-human immunodeficiency virus nucleotide analogues into DNA by human DNA polymerases β, α and ć
    • Cihlar T, Chen MS. Incorporation of selected nucleoside phosphonates and anti-human immunodeficiency virus nucleotide analogues into DNA by human DNA polymerases β, α and ć. Antivir Chem Chemother 1997; 8(3): 187-95.
    • (1997) Antivir Chem Chemother , vol.8 , Issue.3 , pp. 187-195
    • Cihlar, T.1    Chen, M.S.2
  • 28
    • 84856711380 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase complex with DNA and nevirapine reveals nonnucleoside inhibition mechanism
    • Das K, Martinez SE, Bauman JD, Arnold E. HIV-1 reverse transcriptase complex with DNA and nevirapine reveals nonnucleoside inhibition mechanism. Nat Struct Mol Biol 2012; 19(2): 253-9.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.2 , pp. 253-259
    • Das, K.1    Martinez, S.E.2    Bauman, J.D.3    Arnold, E.4
  • 29
    • 41149145592 scopus 로고    scopus 로고
    • Amino acid mutation N348I in the connection subdomain of human immunodeficiency virus type 1 reverse transcriptase confers multiclass resistance to nucleoside and nonnucleoside reverse transcriptase inhibitors
    • Hachiya A, Kodama EN, Sarafianos SG, et al. Amino acid mutation N348I in the connection subdomain of human immunodeficiency virus type 1 reverse transcriptase confers multiclass resistance to nucleoside and nonnucleoside reverse transcriptase inhibitors. J Virol 2008; 82(7): 3261-70.
    • (2008) J Virol , vol.82 , Issue.7 , pp. 3261-3270
    • Hachiya, A.1    Kodama, E.N.2    Sarafianos, S.G.3
  • 30
    • 34547105526 scopus 로고    scopus 로고
    • Selection of mutations in the connection and RNase H domains of human immunodeficiency virus type 1 reverse transcriptase that increase resistance to 3 '-azido-3 '-dideoxythymidine
    • Brehm JH, Koontz D, Meteer JD, Pathak V, Sluis-Cremer N, Mellors JW. Selection of mutations in the connection and RNase H domains of human immunodeficiency virus type 1 reverse transcriptase that increase resistance to 3 '-azido-3 '-dideoxythymidine. J Virol 2007; 81(15): 7852-9.
    • (2007) J Virol , vol.81 , Issue.15 , pp. 7852-7859
    • Brehm, J.H.1    Koontz, D.2    Meteer, J.D.3    Pathak, V.4    Sluis-Cremer, N.5    Mellors, J.W.6
  • 31
    • 34250811908 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3-Azido-3'-deoxythymidine resistance
    • Delviks-Frankenberry KA, Nikolenko GN, Barr R, Pathak VK. Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3-Azido-3'-deoxythymidine resistance. J Virol 2007; 81(13): 6837-45.
    • (2007) J Virol , vol.81 , Issue.13 , pp. 6837-6845
    • Delviks-Frankenberry, K.A.1    Nikolenko, G.N.2    Barr, R.3    Pathak, V.K.4
  • 32
    • 38049028352 scopus 로고    scopus 로고
    • N348I in the connection domain of HIV-1 Reverse Transcriptase confers Zidovudine and Nevirapine resistance
    • Yap SH, Sheen CW, Fahey J, et al. N348I in the connection domain of HIV-1 Reverse Transcriptase confers Zidovudine and Nevirapine resistance. PLoS Med 2007; 4(12): e335.
    • (2007) PLoS Med , vol.4 , Issue.12
    • Yap, S.H.1    Sheen, C.W.2    Fahey, J.3
  • 33
    • 33846063300 scopus 로고    scopus 로고
    • Mutations in the connection domain of HIV-1 reverse transcriptase increase 3 '-azido-3 '-deoxythymidine resistance
    • Nikolenko GN, Delviks-Frankenberry KA, Palmer S, et al. Mutations in the connection domain of HIV-1 reverse transcriptase increase 3 '-azido-3 '-deoxythymidine resistance. Proc Natl Acad Sci USA 2007; 104(1): 317-22.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.1 , pp. 317-322
    • Nikolenko, G.N.1    Delviks-Frankenberry, K.A.2    Palmer, S.3
  • 34
    • 0032731244 scopus 로고    scopus 로고
    • Intracellular metabolism of CycloSaligenyl 3 '-azido-2 ',3 '-dideoxythymidine monophosphate, a prodrug of 3 '-azido-2 ',3 '-dideoxythymidine (zidovudine)
    • Balzarini J, Naesens L, Aquaro S, et al. Intracellular metabolism of CycloSaligenyl 3 '-azido-2 ',3 '-dideoxythymidine monophosphate, a prodrug of 3 '-azido-2 ',3 '-dideoxythymidine (zidovudine). Mol Pharmacol 1999; 56(6): 1354-61.
    • (1999) Mol Pharmacol , vol.56 , Issue.6 , pp. 1354-1361
    • Balzarini, J.1    Naesens, L.2    Aquaro, S.3
  • 35
    • 73549088038 scopus 로고    scopus 로고
    • Nucleoside and nucleotide HIV reverse transcriptase inhibitors: 25 years after zidovudine
    • Cihlar T, Ray AS. Nucleoside and nucleotide HIV reverse transcriptase inhibitors: 25 years after zidovudine. Antivir Res 2010; 85(1): 39-58.
    • (2010) Antivir Res , vol.85 , Issue.1 , pp. 39-58
    • Cihlar, T.1    Ray, A.S.2
  • 36
    • 57649233039 scopus 로고    scopus 로고
    • Mutations M184V and Y115F in HIV-1 Reverse Transcriptase discriminate against "Nucleotide-competing Reverse Transcriptase inhibitors"
    • Ehteshami M, Scarth BJ, Tchesnokov EP, et al. Mutations M184V and Y115F in HIV-1 Reverse Transcriptase discriminate against "Nucleotide-competing Reverse Transcriptase inhibitors". J Biol Chem 2008; 283(44): 29904-11.
    • (2008) J Biol Chem , vol.283 , Issue.44 , pp. 29904-29911
    • Ehteshami, M.1    Scarth, B.J.2    Tchesnokov, E.P.3
  • 37
    • 33845410116 scopus 로고    scopus 로고
    • Indolopyridones inhibit Human Immunodeficiency Virus Reverse Transcriptase with a novel mechanism of action
    • Jochmans D, Deval J, Kesteleyn B, et al. Indolopyridones inhibit Human Immunodeficiency Virus Reverse Transcriptase with a novel mechanism of action. J Virol 2006; 80(24): 12283-92.
    • (2006) J Virol , vol.80 , Issue.24 , pp. 12283-12292
    • Jochmans, D.1    Deval, J.2    Kesteleyn, B.3
  • 38
    • 77749264656 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 Reverse Transcriptase bound to a non-nucleoside inhibitor with a novel mechanism of action
    • Freisz S, Bec G, Radi M, et al. Crystal structure of HIV-1 Reverse Transcriptase bound to a non-nucleoside inhibitor with a novel mechanism of action. Angew Chem, Int Ed 2010; 49(10): 1805-8.
    • (2010) Angew Chem, Int Ed , vol.49 , Issue.10 , pp. 1805-1808
    • Freisz, S.1    Bec, G.2    Radi, M.3
  • 39
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-I reverse transcriptase: Implications for drug resistance
    • Huang HF, Chopra R, Verdine GL, Harrison SC. Structure of a covalently trapped catalytic complex of HIV-I reverse transcriptase: Implications for drug resistance. Science 1998; 282(5394): 1669-75.
    • (1998) Science , vol.282 , Issue.5394 , pp. 1669-1675
    • Huang, H.F.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 40
    • 43049148447 scopus 로고    scopus 로고
    • Mechanisms of inhibition of HIV replication by non-nucleoside reverse transcriptase inhibitors
    • Sluis-Cremer N, Tachedjian G. Mechanisms of inhibition of HIV replication by non-nucleoside reverse transcriptase inhibitors. Virus Res 2008; 134(1-2): 147-56.
    • (2008) Virus Res , vol.134 , Issue.1-2 , pp. 147-156
    • Sluis-Cremer, N.1    Tachedjian, G.2
  • 42
    • 9744258219 scopus 로고    scopus 로고
    • Crystallography and the design of anti-AIDS drugs: Conformational flexibility and positional adaptability are important in the design of nonnucleoside HIV-1 reverse transcriptase inhibitors
    • Das K, Lewi PJ, Hughes SH, Arnold E. Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of nonnucleoside HIV-1 reverse transcriptase inhibitors. Prog Biophys Mol Biol 2005; 88(2): 209-31.
    • (2005) Prog Biophys Mol Biol , vol.88 , Issue.2 , pp. 209-231
    • Das, K.1    Lewi, P.J.2    Hughes, S.H.3    Arnold, E.4
  • 43
    • 70450184400 scopus 로고    scopus 로고
    • Design strategies of novel NNRTIs to overcome drug resistance
    • Zhan P, Liu X, Li Z, Pannecouque C, De Clercq E. Design strategies of novel NNRTIs to overcome drug resistance. Curr Med Chem 2009; 16(29): 3903-17.
    • (2009) Curr Med Chem , vol.16 , Issue.29 , pp. 3903-3917
    • Zhan, P.1    Liu, X.2    Li, Z.3    Pannecouque, C.4    de Clercq, E.5
  • 44
    • 44449115313 scopus 로고    scopus 로고
    • Development of non-nucleoside Reverse Transcriptase inhibitors for anti-HIV therapy
    • Sahlberg C, Zhou X-X. Development of non-nucleoside Reverse Transcriptase inhibitors for anti-HIV therapy. Anti-Infect Agents Med Chem 2008; 7(2): 101-17.
    • (2008) Anti-Infect Agents Med Chem , vol.7 , Issue.2 , pp. 101-117
    • Sahlberg, C.1    Zhou, X.-X.2
  • 45
    • 0029075207 scopus 로고
    • Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors
    • Ding JP, Das K, Moereels H, et al. Structure of HIV-1 RT/TIBO R 86183 complex reveals similarity in the binding of diverse nonnucleoside inhibitors. Nat Struct Biol 1995; 2(5): 407-15.
    • (1995) Nat Struct Biol , vol.2 , Issue.5 , pp. 407-415
    • Ding, J.P.1    Das, K.2    Moereels, H.3
  • 46
    • 79955434216 scopus 로고    scopus 로고
    • Crystal structure of tert-Butyldimethylsilyl-spiroaminooxathioledioxide-thymine (TSAO-T) in Complex with HIV-1 Reverse Transcriptase (RT) redefines the elastic limits of the non-nucleoside inhibitor-binding pocket
    • Das K, Bauman JD, Rim AS, et al. Crystal structure of tert-Butyldimethylsilyl-spiroaminooxathioledioxide-thymine (TSAO-T) in Complex with HIV-1 Reverse Transcriptase (RT) redefines the elastic limits of the non-nucleoside inhibitor-binding pocket. J Med Chem 2011; 54(8): 2727-37.
    • (2011) J Med Chem , vol.54 , Issue.8 , pp. 2727-2737
    • Das, K.1    Bauman, J.D.2    Rim, A.S.3
  • 47
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and characterizing binding sites and assessing druggability
    • Halgren TA. Identifying and characterizing binding sites and assessing druggability. J Chem Inf Model 2009; 49(2): 377-89.
    • (2009) J Chem Inf Model , vol.49 , Issue.2 , pp. 377-389
    • Halgren, T.A.1
  • 48
    • 0036229823 scopus 로고    scopus 로고
    • Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant
    • Lindberg J, Sigursson S, Löwgren S, et al. Structural basis for the inhibitory efficacy of efavirenz (DMP-266), MSC194 and PNU142721 towards the HIV-1 RT K103N mutant. Eur J Biochem 2002; 269(6): 1670-7.
    • (2002) Eur J Biochem , vol.269 , Issue.6 , pp. 1670-1677
    • Lindberg, J.1    Sigursson, S.2    Löwgren, S.3
  • 49
    • 2342620790 scopus 로고    scopus 로고
    • Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (Etravirine) and related non-nucleoside Reverse Transcriptase inhibitors that are highly potent and effective against wild-type and drug-resistant HIV-1 variants
    • Das K, Clark AD, Lewi PJ, et al. Roles of conformational and positional adaptability in structure-based design of TMC125-R165335 (Etravirine) and related non-nucleoside Reverse Transcriptase inhibitors that are highly potent and effective against wild-type and drug-resistant HIV-1 variants. J Med Chem 2004; 47(10): 2550-60.
    • (2004) J Med Chem , vol.47 , Issue.10 , pp. 2550-2560
    • Das, K.1    Clark, A.D.2    Lewi, P.J.3
  • 50
    • 3242657912 scopus 로고    scopus 로고
    • Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors
    • Pata JD, Stirtan WG, Goldstein SW, Steitz TA. Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors. Proc Natl Acad Sci USA 2004; 101(29): 10548-53.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.29 , pp. 10548-10553
    • Pata, J.D.1    Stirtan, W.G.2    Goldstein, S.W.3    Steitz, T.A.4
  • 51
    • 0030596068 scopus 로고    scopus 로고
    • Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant
    • Das K, Ding J, Hsiou Y, et al. Crystal structures of 8-Cl and 9-Cl TIBO complexed with wild-type HIV-1 RT and 8-Cl TIBO complexed with the Tyr181Cys HIV-1 RT drug-resistant mutant. J Mol Biol 1996; 264(5): 1085-100.
    • (1996) J Mol Biol , vol.264 , Issue.5 , pp. 1085-1100
    • Das, K.1    Ding, J.2    Hsiou, Y.3
  • 53
    • 0030586090 scopus 로고    scopus 로고
    • Structure of unliganded HIV-1 reverse transcriptase at 2.7 å resolution: Implications of conformational changes for polymerization and inhibition mechanisms
    • Hsiou Y, Ding J, Das K, Clark JAD, Hughes SH, Arnold E. Structure of unliganded HIV-1 reverse transcriptase at 2.7 å resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure 1996; 4(7): 853-60.
    • (1996) Structure , vol.4 , Issue.7 , pp. 853-860
    • Hsiou, Y.1    Ding, J.2    Das, K.3    Clark, J.A.D.4    Hughes, S.H.5    Arnold, E.6
  • 54
    • 0034094041 scopus 로고    scopus 로고
    • Mutational analysis of Trp-229 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase (RT) identifies this amino acid residue as a prime target for the rational design of new non-nucleoside RT inhibitors
    • Pelemans H, Esnouf R, De Clercq E, Balzarini J. Mutational analysis of Trp-229 of Human Immunodeficiency Virus Type 1 Reverse Transcriptase (RT) identifies this amino acid residue as a prime target for the rational design of new non-nucleoside RT inhibitors. Mol Pharmacol 2000; 57(5): 954-60.
    • (2000) Mol Pharmacol , vol.57 , Issue.5 , pp. 954-960
    • Pelemans, H.1    Esnouf, R.2    de Clercq, E.3    Balzarini, J.4
  • 55
    • 84455161713 scopus 로고    scopus 로고
    • F18, a novel small-molecule nonnucleoside Reverse Transcriptase inhibitor, inhibits HIV-1 replication using distinct binding motifs as demonstrated by resistance selection and docking analysis
    • Lu X, Liu L, Zhang X, et al. F18, a novel small-molecule nonnucleoside Reverse Transcriptase inhibitor, inhibits HIV-1 replication using distinct binding motifs as demonstrated by resistance selection and docking analysis. Antimicrob Agents Chemother 2012; 56(1): 341-51.
    • (2012) Antimicrob Agents Chemother , vol.56 , Issue.1 , pp. 341-351
    • Lu, X.1    Liu, L.2    Zhang, X.3
  • 56
    • 33745107517 scopus 로고    scopus 로고
    • HIV-1 RNase H: Recent progress in an exciting, yet little explored, drug target
    • Tramontano E. HIV-1 RNase H: Recent progress in an exciting, yet little explored, drug target. Mini-Rev Med Chem 2006; 6(6): 727-37.
    • (2006) Mini-Rev Med Chem , vol.6 , Issue.6 , pp. 727-737
    • Tramontano, E.1
  • 57
    • 33646497669 scopus 로고    scopus 로고
    • Recent progress in the design of small molecule inhibitors of HIV RNase H
    • Klumpp K, Mirzadegan T. Recent progress in the design of small molecule inhibitors of HIV RNase H. Curr Pharm Des 2006; 12(15): 1909-22.
    • (2006) Curr Pharm Des , vol.12 , Issue.15 , pp. 1909-1922
    • Klumpp, K.1    Mirzadegan, T.2
  • 58
    • 71049185147 scopus 로고    scopus 로고
    • Structure of HIV-1 Reverse Transcriptase with the inhibitor β-Thujaplicinol bound at the RNase H active site
    • Himmel DM, Maegley KA, Pauly TA, et al. Structure of HIV-1 Reverse Transcriptase with the inhibitor β-Thujaplicinol bound at the RNase H active site. Structure 2009; 17(12): 1625-35.
    • (2009) Structure , vol.17 , Issue.12 , pp. 1625-1635
    • Himmel, D.M.1    Maegley, K.A.2    Pauly, T.A.3
  • 59
    • 79960189034 scopus 로고    scopus 로고
    • Synthesis, activity, and structural analysis of novel α-Hydroxytropolone inhibitors of Human Immunodeficiency Virus Reverse Transcriptase-associated Ribonuclease H
    • Chung S, Himmel DM, Jiang J-K, et al. Synthesis, activity, and structural analysis of novel α-Hydroxytropolone inhibitors of Human Immunodeficiency Virus Reverse Transcriptase-associated Ribonuclease H. J Med Chem 2011; 54(13): 4462-73.
    • (2011) J Med Chem , vol.54 , Issue.13 , pp. 4462-4473
    • Chung, S.1    Himmel, D.M.2    Jiang, J.-K.3
  • 60
    • 70349638920 scopus 로고    scopus 로고
    • RNase H active site inhibitors of Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Design, biochemical activity, and structural information
    • Kirschberg TA, Balakrishnan M, Squires NH, et al. RNase H active site inhibitors of Human Immunodeficiency Virus Type 1 Reverse Transcriptase: Design, biochemical activity, and structural information. J Med Chem 2009; 52(19): 5781-4.
    • (2009) J Med Chem , vol.52 , Issue.19 , pp. 5781-5784
    • Kirschberg, T.A.1    Balakrishnan, M.2    Squires, N.H.3
  • 61
    • 79956334444 scopus 로고    scopus 로고
    • Structural and binding analysis of pyrimidinol carboxylic acid and N-hydroxy quinazolinedione HIV-1 RNase H inhibitors
    • Lansdon EB, Liu Q, Leavitt SA, et al. Structural and binding analysis of pyrimidinol carboxylic acid and N-hydroxy quinazolinedione HIV-1 RNase H inhibitors. Antimicrob Agents Chemother 2011; 55(6): 2905-15.
    • (2011) Antimicrob Agents Chemother , vol.55 , Issue.6 , pp. 2905-2915
    • Lansdon, E.B.1    Liu, Q.2    Leavitt, S.A.3
  • 62
    • 11144355815 scopus 로고    scopus 로고
    • Activity of the isolated HIV RNase H domain and specific inhibition by N-hydroxyimides
    • Hang JQ, Rajendran S, Yang Y, et al. Activity of the isolated HIV RNase H domain and specific inhibition by N-hydroxyimides. Biochem Biophys Res Commun 2004; 317(2): 321-9.
    • (2004) Biochem Biophys Res Commun , vol.317 , Issue.2 , pp. 321-329
    • Hang, J.Q.1    Rajendran, S.2    Yang, Y.3
  • 63
    • 13544276913 scopus 로고    scopus 로고
    • 6-[1-(4-Fluorophenyl)methyl-1H-pyrrol-2-yl)]-2,4-dioxo-5-hexenoic acid ethyl ester a novel diketo acid derivative which selectively inhibits the HIV-1 viral replication in cell culture and the ribonuclease H activity in vitro
    • Tramontano E, Esposito F, Badas R, Di Santo R, Costi R, La Colla P. 6-[1-(4-Fluorophenyl)methyl-1H-pyrrol-2-yl)]-2,4-dioxo-5-hexenoic acid ethyl ester a novel diketo acid derivative which selectively inhibits the HIV-1 viral replication in cell culture and the ribonuclease H activity in vitro. Antivir Res 2005; 65(2): 117-24.
    • (2005) Antivir Res , vol.65 , Issue.2 , pp. 117-124
    • Tramontano, E.1    Esposito, F.2    Badas, R.3    Di Santo, R.4    Costi, R.5    la Colla, P.6
  • 64
    • 0027521797 scopus 로고
    • 3,4-Dihydro-2-Alkoxy-6-Benzyl-4-Oxopyrimidines (DABOs)-A new class of specific inhibitors of Human-Immunodeficiency-Virus type-1
    • Artico M, Massa S, Mai A, Marongiu ME, Piras G, Tramontano E, Lacolla P. 3,4-Dihydro-2-Alkoxy-6-Benzyl-4-Oxopyrimidines (DABOs)-A new class of specific inhibitors of Human-Immunodeficiency-Virus type-1. Antivir Chem Chemother 1993; 4(6): 361-8.
    • (1993) Antivir Chem Chemother , vol.4 , Issue.6 , pp. 361-368
    • Artico, M.1    Massa, S.2    Mai, A.3    Marongiu, M.E.4    Piras, G.5    Tramontano, E.6    Lacolla, P.7
  • 65
    • 37249062449 scopus 로고    scopus 로고
    • HIV-1 Reverse Transcriptase structure with RNase H inhibitor dihydroxy benzoyl naphthyl hydrazone Bound at a novel site
    • Himmel DM, Sarafianos SG, Dharmasena S, et al. HIV-1 Reverse Transcriptase structure with RNase H inhibitor dihydroxy benzoyl naphthyl hydrazone Bound at a novel site. ACS Chem Biol 2006; 1(11): 702-12.
    • (2006) ACS Chem Biol , vol.1 , Issue.11 , pp. 702-712
    • Himmel, D.M.1    Sarafianos, S.G.2    Dharmasena, S.3
  • 66
    • 77954521861 scopus 로고    scopus 로고
    • Structural basis for the inhibition of RNase H activity of HIV-1 Reverse Transcriptase by RNase H active site-directed inhibitors
    • Su H-P, Yan Y, Prasad GS, et al. Structural basis for the inhibition of RNase H activity of HIV-1 Reverse Transcriptase by RNase H active site-directed inhibitors. J Virol 2010; 84(15): 7625-33.
    • (2010) J Virol , vol.84 , Issue.15 , pp. 7625-7633
    • Su, H.-P.1    Yan, Y.2    Prasad, G.S.3
  • 67
    • 58149160464 scopus 로고    scopus 로고
    • Vinylogous ureas as a novel class of inhibitors of Reverse Transcriptase-associated ribonuclease H activity
    • Wendeler M, Lee H-F, Bermingham A, et al. Vinylogous ureas as a novel class of inhibitors of Reverse Transcriptase-associated ribonuclease H activity. ACS Chem Biol 2008; 3(10): 635-44.
    • (2008) ACS Chem Biol , vol.3 , Issue.10 , pp. 635-644
    • Wendeler, M.1    Lee, H.-F.2    Bermingham, A.3
  • 68
    • 80051975966 scopus 로고    scopus 로고
    • Identification of alternative binding sites for inhibitors of HIV-1 Ribonuclease H through comparative analysis of virtual enrichment studies
    • Felts AK, LaBarge K, Bauman JD, et al. Identification of alternative binding sites for inhibitors of HIV-1 Ribonuclease H through comparative analysis of virtual enrichment studies. J Chem Inf Model 2011; 51(8): 1986-98.
    • (2011) J Chem Inf Model , vol.51 , Issue.8 , pp. 1986-1998
    • Felts, A.K.1    LaBarge, K.2    Bauman, J.D.3
  • 69
    • 0036076157 scopus 로고    scopus 로고
    • Destabilization of the HIV-1 Reverse Transcriptase dimer upon interaction with N-acyl hydrazone inhibitors
    • Sluis-Cremer N, Arion D, Parniak MA. Destabilization of the HIV-1 Reverse Transcriptase dimer upon interaction with N-acyl hydrazone inhibitors. Mol Pharmacol 2002; 62(2): 398-405.
    • (2002) Mol Pharmacol , vol.62 , Issue.2 , pp. 398-405
    • Sluis-Cremer, N.1    Arion, D.2    Parniak, M.A.3
  • 70
    • 79955072485 scopus 로고    scopus 로고
    • Alizarine derivatives as new dual inhibitors of the HIV-1 reverse transcriptase-associated DNA polymerase and RNase H activities effective also on the RNase H activity of non-nucleoside resistant reverse transcriptases
    • Esposito F, Kharlamova T, Distinto S, et al. Alizarine derivatives as new dual inhibitors of the HIV-1 reverse transcriptase-associated DNA polymerase and RNase H activities effective also on the RNase H activity of non-nucleoside resistant reverse transcriptases. FEBS J 2011; 278(9): 1444-57.
    • (2011) FEBS J , vol.278 , Issue.9 , pp. 1444-1457
    • Esposito, F.1    Kharlamova, T.2    Distinto, S.3
  • 71
    • 84858440068 scopus 로고    scopus 로고
    • Identification of HIV-1 reverse transcriptase dual inhibitors by a combined shape-, 2Dfingerprint-and pharmacophore-based virtual screening approach
    • Distinto S, Esposito F, Kirchmair J, et al. Identification of HIV-1 reverse transcriptase dual inhibitors by a combined shape-, 2Dfingerprint-and pharmacophore-based virtual screening approach. Eur J Med Chem 2012; 50(0): 216-29.
    • (2012) Eur J Med Chem , vol.50 , Issue.0 , pp. 216-229
    • Distinto, S.1    Esposito, F.2    Kirchmair, J.3
  • 72
    • 33745584385 scopus 로고    scopus 로고
    • GBPM: GRID-based pharmacophore model: Concept and application studies to protein-protein recognition
    • Ortuso F, Langer T, Alcaro S. GBPM: GRID-based pharmacophore model: concept and application studies to protein-protein recognition. Bioinformatics 2006; 22(12): 1449-55.
    • (2006) Bioinformatics , vol.22 , Issue.12 , pp. 1449-1455
    • Ortuso, F.1    Langer, T.2    Alcaro, S.3
  • 73
    • 84876720458 scopus 로고    scopus 로고
    • SiteMap. Schrodinger Suite, 2010, Portland, OR
    • SiteMap. Schrodinger Suite, 2010, Portland, OR.


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