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Volumn 7, Issue 7, 2012, Pages

Unprocessed viral DNA could be the primary target of the HIV-1 integrase inhibitor Raltegravir

Author keywords

[No Author keywords available]

Indexed keywords

RALTEGRAVIR; VIRUS DNA; 2 PYRROLIDONE DERIVATIVE; INTEGRASE; INTEGRASE INHIBITOR;

EID: 84863623171     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040223     Document Type: Article
Times cited : (8)

References (73)
  • 1
    • 0027102597 scopus 로고
    • Genetics of Retroviral Integration
    • Goff SP, (1992) Genetics of Retroviral Integration. Annual Review of Genetics 26: 527-544.
    • (1992) Annual Review of Genetics , vol.26 , pp. 527-544
    • Goff, S.P.1
  • 2
    • 0028264163 scopus 로고
    • The retroviral enzymes
    • 10.1146/annurev.bi.63.070194.001025 [doi]
    • Katz RA, Skalka AM, (1994) The retroviral enzymes. Annu Rev Biochem 63: 133-173 10.1146/annurev.bi.63.070194.001025 [doi].
    • (1994) Annu Rev Biochem , vol.63 , pp. 133-173
    • Katz, R.A.1    Skalka, A.M.2
  • 3
    • 14944374558 scopus 로고    scopus 로고
    • Integrase inhibitors to treat HIV/AIDS
    • nrd1660 [pii];10.1038/nrd1660 [doi]
    • Pommier Y, Johnson AA, Marchand C, (2005) Integrase inhibitors to treat HIV/AIDS. Nat Rev Drug Discov 4: 236-248 nrd1660 [pii];10.1038/nrd1660 [doi].
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 236-248
    • Pommier, Y.1    Johnson, A.A.2    Marchand, C.3
  • 4
    • 79952070221 scopus 로고    scopus 로고
    • Structural biology of retroviral DNA integration
    • S0042-6822(10)00752-X [pii];10.1016/j.virol.2010.12.008 [doi]
    • Li X, Krishnan L, Cherepanov P, Engelman A, (2011) Structural biology of retroviral DNA integration. Virology 411: 194-205 S0042-6822(10)00752-X [pii];10.1016/j.virol.2010.12.008 [doi].
    • (2011) Virology , vol.411 , pp. 194-205
    • Li, X.1    Krishnan, L.2    Cherepanov, P.3    Engelman, A.4
  • 5
    • 0037076324 scopus 로고    scopus 로고
    • Diketo acid inhibitor mechanism and HIV-1 integrase: implications for metal binding in the active site of phosphotransferase enzymes
    • 10.1073/pnas.092056199 [doi];092056199 [pii]
    • Grobler JA, Stillmock K, Hu B, Witmer M, Felock P, et al. (2002) Diketo acid inhibitor mechanism and HIV-1 integrase: implications for metal binding in the active site of phosphotransferase enzymes. Proc Natl Acad Sci U S A 99: 6661-6666 10.1073/pnas.092056199 [doi];092056199 [pii].
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6661-6666
    • Grobler, J.A.1    Stillmock, K.2    Hu, B.3    Witmer, M.4    Felock, P.5
  • 6
    • 74049103073 scopus 로고    scopus 로고
    • HIV-1 IN inhibitors: 2010 update and perspectives
    • Abs-010-9-11 [pii]
    • Marchand C, Maddali K, Metifiot M, Pommier Y, (2009) HIV-1 IN inhibitors: 2010 update and perspectives. Curr Top Med Chem 9: 1016-1037 Abs-010-9-11 [pii].
    • (2009) Curr Top Med Chem , vol.9 , pp. 1016-1037
    • Marchand, C.1    Maddali, K.2    Metifiot, M.3    Pommier, Y.4
  • 7
    • 73549123203 scopus 로고    scopus 로고
    • Strand transfer inhibitors of HIV-1 integrase: bringing IN a new era of antiretroviral therapy
    • S0166-3542(09)00533-6 [pii];10.1016/j.antiviral.2009.11.004 [doi]
    • McColl DJ, Chen X, (2010) Strand transfer inhibitors of HIV-1 integrase: bringing IN a new era of antiretroviral therapy. Antiviral Res 85: 101-118 S0166-3542(09)00533-6 [pii];10.1016/j.antiviral.2009.11.004 [doi].
    • (2010) Antiviral Res , vol.85 , pp. 101-118
    • McColl, D.J.1    Chen, X.2
  • 8
    • 34147136222 scopus 로고    scopus 로고
    • Safety and efficacy of the HIV-1 integrase inhibitor raltegravir (MK-0518) in treatment-experienced patients with multidrug-resistant virus: a phase II randomised controlled trial
    • S0140-6736(07)60597-2 [pii];10.1016/S0140-6736(07)60597-2 [doi]
    • Grinsztejn B, Nguyen BY, Katlama C, Gatell JM, Lazzarin A, et al. (2007) Safety and efficacy of the HIV-1 integrase inhibitor raltegravir (MK-0518) in treatment-experienced patients with multidrug-resistant virus: a phase II randomised controlled trial. Lancet 369: 1261-1269 S0140-6736(07)60597-2 [pii];10.1016/S0140-6736(07)60597-2 [doi].
    • (2007) Lancet , vol.369 , pp. 1261-1269
    • Grinsztejn, B.1    Nguyen, B.Y.2    Katlama, C.3    Gatell, J.M.4    Lazzarin, A.5
  • 9
    • 70350154011 scopus 로고    scopus 로고
    • Integrase inhibitors in salvage therapy regimens for HIV-1 infection
    • 10.1097/COH.0b013e328331b526 [doi];01222929-200911000-00011 [pii]
    • Koelsch KK, Cooper DA, (2009) Integrase inhibitors in salvage therapy regimens for HIV-1 infection. Curr Opin HIV AIDS 4: 518-523 10.1097/COH.0b013e328331b526 [doi];01222929-200911000-00011 [pii].
    • (2009) Curr Opin HIV AIDS , vol.4 , pp. 518-523
    • Koelsch, K.K.1    Cooper, D.A.2
  • 10
    • 51549116289 scopus 로고    scopus 로고
    • Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants
    • 10.1021/bi800791q [doi]
    • Marinello J, Marchand C, Mott BT, Bain A, Thomas CJ, et al. (2008) Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants. Biochemistry 47: 9345-9354 10.1021/bi800791q [doi].
    • (2008) Biochemistry , vol.47 , pp. 9345-9354
    • Marinello, J.1    Marchand, C.2    Mott, B.T.3    Bain, A.4    Thomas, C.J.5
  • 12
    • 77956412031 scopus 로고    scopus 로고
    • The HIV-1 integrase mutations Y143C/R are an alternative pathway for resistance to Raltegravir and impact the enzyme functions
    • 10.1371/journal.pone.0010311 [doi]
    • Reigadas S, Anies G, Masquelier B, Calmels C, Stuyver LJ, et al. (2010) The HIV-1 integrase mutations Y143C/R are an alternative pathway for resistance to Raltegravir and impact the enzyme functions. PLoS One 5: e10311 10.1371/journal.pone.0010311 [doi].
    • (2010) PLoS One , vol.5
    • Reigadas, S.1    Anies, G.2    Masquelier, B.3    Calmels, C.4    Stuyver, L.J.5
  • 13
    • 0037827778 scopus 로고    scopus 로고
    • Strategy to discriminate between high and low affinity bindings of human immunodeficiency virus, type 1 integrase to viral DNA
    • Zargarian L, Benleumi MS, Renisio JG, Merad H, Maroun RG, et al. (2003) Strategy to discriminate between high and low affinity bindings of human immunodeficiency virus, type 1 integrase to viral DNA. J Biol Chem 278: 19966-19973.
    • (2003) J Biol Chem , vol.278 , pp. 19966-19973
    • Zargarian, L.1    Benleumi, M.S.2    Renisio, J.G.3    Merad, H.4    Maroun, R.G.5
  • 14
    • 77953230564 scopus 로고    scopus 로고
    • HIV-1 integrase and virus and cell DNAs: complex formation and perturbation by inhibitors of integration
    • 10.1007/s11064-009-0098-2 [doi]
    • Hobaika Z, Zargarian L, Maroun RG, Mauffret O, Burke TR, et al. (2010) HIV-1 integrase and virus and cell DNAs: complex formation and perturbation by inhibitors of integration. Neurochem Res 35: 888-893 10.1007/s11064-009-0098-2 [doi].
    • (2010) Neurochem Res , vol.35 , pp. 888-893
    • Hobaika, Z.1    Zargarian, L.2    Maroun, R.G.3    Mauffret, O.4    Burke, T.R.5
  • 15
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • nature08784 [pii];10.1038/nature08784 [doi]
    • Hare S, Gupta SS, Valkov E, Engelman A, Cherepanov P, (2010) Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 464: 232-236 nature08784 [pii];10.1038/nature08784 [doi].
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 16
    • 13044295993 scopus 로고    scopus 로고
    • Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design
    • Goldgur Y, Craigie R, Cohen GH, Fujiwara T, Yoshinaga T, et al. (1999) Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design. Proc Natl Acad Sci U S A 96: 13040-13043.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13040-13043
    • Goldgur, Y.1    Craigie, R.2    Cohen, G.H.3    Fujiwara, T.4    Yoshinaga, T.5
  • 17
    • 77957670046 scopus 로고    scopus 로고
    • Structure-based modeling of the functional HIV-1 intasome and its inhibition
    • 1002346107 [pii];10.1073/pnas.1002346107 [doi]
    • Krishnan L, Li X, Naraharisetty HL, Hare S, Cherepanov P, et al. (2010) Structure-based modeling of the functional HIV-1 intasome and its inhibition. Proc Natl Acad Sci U S A 107: 15910-15915 1002346107 [pii];10.1073/pnas.1002346107 [doi].
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 15910-15915
    • Krishnan, L.1    Li, X.2    Naraharisetty, H.L.3    Hare, S.4    Cherepanov, P.5
  • 18
    • 78650533230 scopus 로고    scopus 로고
    • Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance
    • 1010246107 [pii];10.1073/pnas.1010246107 [doi]
    • Hare S, Vos AM, Clayton RF, Thuring JW, Cummings MD, et al. (2010) Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Proc Natl Acad Sci U S A 107: 20057-20062 1010246107 [pii];10.1073/pnas.1010246107 [doi].
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20057-20062
    • Hare, S.1    Vos, A.M.2    Clayton, R.F.3    Thuring, J.W.4    Cummings, M.D.5
  • 19
    • 33644863638 scopus 로고    scopus 로고
    • Novel HIV-1 integrase inhibitors derived from quinolone antibiotics
    • 10.1021/jm0600139 [doi]
    • Sato M, Motomura T, Aramaki H, Matsuda T, Yamashita M, et al. (2006) Novel HIV-1 integrase inhibitors derived from quinolone antibiotics. J Med Chem 49: 1506-1508 10.1021/jm0600139 [doi].
    • (2006) J Med Chem , vol.49 , pp. 1506-1508
    • Sato, M.1    Motomura, T.2    Aramaki, H.3    Matsuda, T.4    Yamashita, M.5
  • 20
    • 77953587761 scopus 로고    scopus 로고
    • HIV-1 resistance patterns to integrase inhibitors in antiretroviral-experienced patients with virological failure on raltegravir-containing regimens
    • dkq099 [pii];10.1093/jac/dkq099 [doi]
    • Da Silva D, Van WL, Breilh D, Reigadas S, Anies G, et al. (2010) HIV-1 resistance patterns to integrase inhibitors in antiretroviral-experienced patients with virological failure on raltegravir-containing regimens. J Antimicrob Chemother 65: 1262-1269 dkq099 [pii];10.1093/jac/dkq099 [doi].
    • (2010) J Antimicrob Chemother , vol.65 , pp. 1262-1269
    • Da Silva, D.1    Van, W.L.2    Breilh, D.3    Reigadas, S.4    Anies, G.5
  • 21
    • 80054678089 scopus 로고    scopus 로고
    • MK-0536 inhibits HIV-1 integrases resistant to raltegravir
    • AAC.05288-11 [pii];10.1128/AAC.05288-11 [doi]
    • Metifiot M, Johnson B, Smith S, Zhao XZ, Marchand C, et al. (2011) MK-0536 inhibits HIV-1 integrases resistant to raltegravir. Antimicrob Agents Chemother 55: 5127-5133 AAC.05288-11 [pii];10.1128/AAC.05288-11 [doi].
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 5127-5133
    • Metifiot, M.1    Johnson, B.2    Smith, S.3    Zhao, X.Z.4    Marchand, C.5
  • 22
    • 80054851811 scopus 로고    scopus 로고
    • Discovery of MK-2048 - subtle changes confer unique resistance properties to a series of tricyclic hydroxypyrrole integrase strand transfer inhibitors
    • Poster discussion: 4th IAS Conference on HIV Pathogenesis, Treatment and Prevention: Abstract no WEPEA088
    • Vacca J, Wai J, Fisher T, Embrey M, Hazuda D, et al. (2007) Discovery of MK-2048 - subtle changes confer unique resistance properties to a series of tricyclic hydroxypyrrole integrase strand transfer inhibitors. Poster discussion: 4th IAS Conference on HIV Pathogenesis, Treatment and Prevention: Abstract no WEPEA088.
    • (2007)
    • Vacca, J.1    Wai, J.2    Fisher, T.3    Embrey, M.4    Hazuda, D.5
  • 23
    • 84874325826 scopus 로고    scopus 로고
    • The discovery of S/GSK1349572: a once-daily next generation integrase inhibitor with a superior resistance profile
    • in 17th Conference on Retroviruses and Opportunistic Infections, SanFrancisco, CA
    • Johns B, Kawasuiji T, Taishi T, Yoshida H, Garvey E, et al. (2010) The discovery of S/GSK1349572: a once-daily next generation integrase inhibitor with a superior resistance profile. in 17th Conference on Retroviruses and Opportunistic Infections, SanFrancisco, CA.
    • (2010)
    • Johns, B.1    Kawasuiji, T.2    Taishi, T.3    Yoshida, H.4    Garvey, E.5
  • 24
    • 80052847538 scopus 로고    scopus 로고
    • Structural and functional analyses of the second-generation integrase strand transfer inhibitor dolutegravir (S/GSK1349572)
    • mol.111.073189 [pii];10.1124/mol.111.073189 [doi]
    • Hare S, Smith SJ, Metifiot M, Jaxa-Chamiec A, Pommier Y, et al. (2011) Structural and functional analyses of the second-generation integrase strand transfer inhibitor dolutegravir (S/GSK1349572). Mol Pharmacol 80: 565-572 mol.111.073189 [pii];10.1124/mol.111.073189 [doi].
    • (2011) Mol Pharmacol , vol.80 , pp. 565-572
    • Hare, S.1    Smith, S.J.2    Metifiot, M.3    Jaxa-Chamiec, A.4    Pommier, Y.5
  • 25
    • 12944270496 scopus 로고    scopus 로고
    • HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase
    • 10.1073/pnas.200139397 [doi];200139397 [pii]
    • Espeseth AS, Felock P, Wolfe A, Witmer M, Grobler J, et al. (2000) HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase. Proc Natl Acad Sci U S A 97: 11244-11249 10.1073/pnas.200139397 [doi];200139397 [pii].
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11244-11249
    • Espeseth, A.S.1    Felock, P.2    Wolfe, A.3    Witmer, M.4    Grobler, J.5
  • 26
    • 77952930950 scopus 로고    scopus 로고
    • Solution conformation and dynamics of the HIV-1 integrase core domain
    • M110.113407 [pii];10.1074/jbc.M110.113407 [doi]
    • Fitzkee NC, Masse JE, Shen Y, Davies DR, Bax A, (2010) Solution conformation and dynamics of the HIV-1 integrase core domain. J Biol Chem 285: 18072-18084 M110.113407 [pii];10.1074/jbc.M110.113407 [doi].
    • (2010) J Biol Chem , vol.285 , pp. 18072-18084
    • Fitzkee, N.C.1    Masse, J.E.2    Shen, Y.3    Davies, D.R.4    Bax, A.5
  • 27
    • 0026011643 scopus 로고
    • DNA-drug recognition and effects on topoisomerase II-mediated cytotoxicity. A three-mode binding model for ellipticine derivatives
    • Monnot M, Mauffret O, Simon V, Lescot E, Psaume B, et al. (1991) DNA-drug recognition and effects on topoisomerase II-mediated cytotoxicity. A three-mode binding model for ellipticine derivatives. J Biol Chem 266: 1820-1829.
    • (1991) J Biol Chem , vol.266 , pp. 1820-1829
    • Monnot, M.1    Mauffret, O.2    Simon, V.3    Lescot, E.4    Psaume, B.5
  • 28
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, Van Der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 29
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • 10.1002/prot.22711 [doi]
    • Lindorff-Larsen K, Piana S, Palmo K, Maragakis P, Klepeis JL, et al. (2010) Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78: 1950-1958 10.1002/prot.22711 [doi].
    • (2010) Proteins , vol.78 , pp. 1950-1958
    • Lindorff-Larsen, K.1    Piana, S.2    Palmo, K.3    Maragakis, P.4    Klepeis, J.L.5
  • 30
    • 0032560959 scopus 로고    scopus 로고
    • Continuum Solvent Studies of the Stability of DNA, RNA, and Phosphoramidate-DNA Helices
    • Srinivasan J, Cheatham TE, Cieplak P, Kollman PA, Case DA, (1998) Continuum Solvent Studies of the Stability of DNA, RNA, and Phosphoramidate-DNA Helices. J Am Chem Soc 120: 9401-9409.
    • (1998) J Am Chem Soc , vol.120 , pp. 9401-9409
    • Srinivasan, J.1    Cheatham, T.E.2    Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 31
    • 0042710087 scopus 로고    scopus 로고
    • Computational Alanine Scanning To Probe Protein-Protein Interactions: A Novel Approach To Evaluate Binding Free Energies
    • Massova I, Kollman PA, (1999) Computational Alanine Scanning To Probe Protein-Protein Interactions: A Novel Approach To Evaluate Binding Free Energies. J Am Chem Soc 121: 8133-8143.
    • (1999) J Am Chem Soc , vol.121 , pp. 8133-8143
    • Massova, I.1    Kollman, P.A.2
  • 32
    • 79952588669 scopus 로고    scopus 로고
    • Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations
    • Hou T, Wang J, Li Y, Wang W, (2011) Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations. J Chem Inf Model 51: 69-82.
    • (2011) J Chem Inf Model , vol.51 , pp. 69-82
    • Hou, T.1    Wang, J.2    Li, Y.3    Wang, W.4
  • 33
    • 84856226122 scopus 로고    scopus 로고
    • Molecular mechanism of HIV-1 integrase-vDNA interactions and strand transfer inhibitor action: A molecular modeling perspective
    • 10.1002/jcc.22887 [doi]
    • Xue W, Liu H, Yao X, (2012) Molecular mechanism of HIV-1 integrase-vDNA interactions and strand transfer inhibitor action: A molecular modeling perspective. J Comput Chem 33: 527-536 10.1002/jcc.22887 [doi].
    • (2012) J Comput Chem , vol.33 , pp. 527-536
    • Xue, W.1    Liu, H.2    Yao, X.3
  • 34
    • 35748930263 scopus 로고    scopus 로고
    • Changes to the HIV long terminal repeat and to HIV integrase differentially impact HIV integrase assembly, activity, and the binding of strand transfer inhibitors
    • M704935200 [pii];10.1074/jbc.M704935200 [doi]
    • Dicker IB, Samanta HK, Li Z, Hong Y, Tian Y, et al. (2007) Changes to the HIV long terminal repeat and to HIV integrase differentially impact HIV integrase assembly, activity, and the binding of strand transfer inhibitors. J Biol Chem 282: 31186-31196 M704935200 [pii];10.1074/jbc.M704935200 [doi].
    • (2007) J Biol Chem , vol.282 , pp. 31186-31196
    • Dicker, I.B.1    Samanta, H.K.2    Li, Z.3    Hong, Y.4    Tian, Y.5
  • 35
    • 0031050297 scopus 로고    scopus 로고
    • Disruption of the terminal base pairs of retroviral DNA during integration
    • Scottoline BP, Chow S, Ellison V, Brown PO, (1997) Disruption of the terminal base pairs of retroviral DNA during integration. Genes Dev 11: 371-382.
    • (1997) Genes Dev , vol.11 , pp. 371-382
    • Scottoline, B.P.1    Chow, S.2    Ellison, V.3    Brown, P.O.4
  • 36
    • 79960403326 scopus 로고    scopus 로고
    • Retroviral integrases promote fraying of viral DNA ends
    • M111.229179 [pii];10.1074/jbc.M111.229179 [doi]
    • Katz RA, Merkel G, Andrake MD, Roder H, Skalka AM, (2011) Retroviral integrases promote fraying of viral DNA ends. J Biol Chem 286: 25710-25718 M111.229179 [pii];10.1074/jbc.M111.229179 [doi].
    • (2011) J Biol Chem , vol.286 , pp. 25710-25718
    • Katz, R.A.1    Merkel, G.2    Andrake, M.D.3    Roder, H.4    Skalka, A.M.5
  • 37
    • 0029643858 scopus 로고    scopus 로고
    • The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations
    • Bujacz G, Jaskolski M, Alexandratos J, Wlodawer A, Merkel G, et al. (1996) The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure 4: 89-96.
    • (1996) Structure , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5
  • 38
    • 0024316466 scopus 로고
    • DNA topoisomerase poisons as antitumor drugs
    • 10.1146/annurev.bi.58.070189.002031 [doi]
    • Liu LF, (1989) DNA topoisomerase poisons as antitumor drugs. Annu Rev Biochem 58: 351-375 10.1146/annurev.bi.58.070189.002031 [doi].
    • (1989) Annu Rev Biochem , vol.58 , pp. 351-375
    • Liu, L.F.1
  • 39
    • 77954187741 scopus 로고    scopus 로고
    • DNA topoisomerases and their poisoning by anticancer and antibacterial drugs
    • S1074-5521(10)00161-4 [pii];10.1016/j.chembiol.2010.04.012 [doi]
    • Pommier Y, Leo E, Zhang H, Marchand C, (2010) DNA topoisomerases and their poisoning by anticancer and antibacterial drugs. Chem Biol 17: 421-433 S1074-5521(10)00161-4 [pii];10.1016/j.chembiol.2010.04.012 [doi].
    • (2010) Chem Biol , vol.17 , pp. 421-433
    • Pommier, Y.1    Leo, E.2    Zhang, H.3    Marchand, C.4
  • 40
    • 0023229226 scopus 로고
    • A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions
    • Bujalowski W, Lohman TM, (1987) A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions. Biochemistry 26: 3099-3106.
    • (1987) Biochemistry , vol.26 , pp. 3099-3106
    • Bujalowski, W.1    Lohman, T.M.2
  • 41
    • 2942532422 scopus 로고    scopus 로고
    • Development and testing of a general amber force field
    • 10.1002/jcc.20035 [doi]
    • Wang J, Wolf RM, Caldwell JW, Kollman PA, Case DA, (2004) Development and testing of a general amber force field. J Comput Chem 25: 1157-1174 10.1002/jcc.20035 [doi].
    • (2004) J Comput Chem , vol.25 , pp. 1157-1174
    • Wang, J.1    Wolf, R.M.2    Caldwell, J.W.3    Kollman, P.A.4    Case, D.A.5
  • 42
    • 33748538349 scopus 로고    scopus 로고
    • Automatic atom type and bond type perception in molecular mechanical calculations
    • S1093-3263(05)00173-7 [pii];10.1016/j.jmgm.2005.12.005 [doi]
    • Wang J, Wang W, Kollman PA, Case DA, (2006) Automatic atom type and bond type perception in molecular mechanical calculations. J Mol Graph Model 25: 247-260 S1093-3263(05)00173-7 [pii];10.1016/j.jmgm.2005.12.005 [doi].
    • (2006) J Mol Graph Model , vol.25 , pp. 247-260
    • Wang, J.1    Wang, W.2    Kollman, P.A.3    Case, D.A.4
  • 43
    • 2342430094 scopus 로고
    • New Developments in Molecular Orbital Theory
    • Roothaan CCJ, (1951) New Developments in Molecular Orbital Theory. Rev Mod Phys 23: 69-89.
    • (1951) Rev Mod Phys , vol.23 , pp. 69-89
    • Roothaan, C.C.J.1
  • 45
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • 0263785596000185 [pii]
    • Humphrey W, Dalke A, Schulten K, (1996) VMD: visual molecular dynamics. J Mol Graph 14: 33-38 0263785596000185 [pii].
    • (1996) J Mol Graph , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 47
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N. log(N) method for Ewald sums in large systems
    • Darden T, Darrin Y, Pedersen L, (1993) Particle mesh Ewald: An N. log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    Darrin, Y.2    Pedersen, L.3
  • 48
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJ, Fraaije JG, (1997) LINCS: A linear constraint solver for molecular simulations. J Comput Chem 18: 1463-1472.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.3    Fraaije, J.G.4
  • 49
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • 10.1063/1.2408420 [doi]
    • Bussi G, Donadio D, Parrinello M, (2007) Canonical sampling through velocity rescaling. J Chem Phys 126: 014101-014107 10.1063/1.2408420 [doi].
    • (2007) J Chem Phys , vol.126 , pp. 014101-014107
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 50
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello M, Rahman A, (1981) Polymorphic transitions in single crystals: A new molecular dynamics method. J App Phys 52: 7182-7190.
    • (1981) J App Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 51
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models
    • ar000033j [pii]
    • Kollman PA, Massova I, Reyes C, Kuhn B, Huo S, et al. (2000) Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Acc Chem Res 33: 889-897 ar000033j [pii].
    • (2000) Acc Chem Res , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5
  • 52
    • 0036519363 scopus 로고    scopus 로고
    • DNA and its associated processes as targets for cancer therapy
    • 10.1038/nrc749 [doi]
    • Hurley LH, (2002) DNA and its associated processes as targets for cancer therapy. Nat Rev Cancer 2: 188-200 10.1038/nrc749 [doi].
    • (2002) Nat Rev Cancer , vol.2 , pp. 188-200
    • Hurley, L.H.1
  • 53
    • 0020095856 scopus 로고
    • Spectroscopic analysis of drug-nucleic acid interactions
    • Dougherty G, Pigram WJ, (1982) Spectroscopic analysis of drug-nucleic acid interactions. CRC Crit Rev Biochem 12: 103-132.
    • (1982) CRC Crit Rev Biochem , vol.12 , pp. 103-132
    • Dougherty, G.1    Pigram, W.J.2
  • 54
    • 0025353018 scopus 로고
    • The interaction of unfused polyaromatic heterocycles with DNA: intercalation, groove-binding and bleomycin amplification
    • Wilson WD, Tanious FA, Barton HJ, Wydra RL, Jones RL, et al. (1990) The interaction of unfused polyaromatic heterocycles with DNA: intercalation, groove-binding and bleomycin amplification. Anticancer Drug Des 5: 31-42.
    • (1990) Anticancer Drug Des , vol.5 , pp. 31-42
    • Wilson, W.D.1    Tanious, F.A.2    Barton, H.J.3    Wydra, R.L.4    Jones, R.L.5
  • 55
    • 0024324205 scopus 로고
    • On the mechanism of topoisomerase I inhibition by camptothecin: evidence for binding to an enzyme-DNA complex
    • Hertzberg RP, Caranfa MJ, Hecht SM, (1989) On the mechanism of topoisomerase I inhibition by camptothecin: evidence for binding to an enzyme-DNA complex. Biochemistry 28: 4629-4638.
    • (1989) Biochemistry , vol.28 , pp. 4629-4638
    • Hertzberg, R.P.1    Caranfa, M.J.2    Hecht, S.M.3
  • 57
    • 0003546549 scopus 로고    scopus 로고
    • Circular dichroism: principles and applications
    • Wiley-VCH, New York
    • Berova N, Nakanishi K, Woody RW, (2000) Circular dichroism: principles and applications. Wiley-VCH, New York.
    • (2000)
    • Berova, N.1    Nakanishi, K.2    Woody, R.W.3
  • 58
    • 0026523525 scopus 로고
    • Probing intercalation and conformational effects of the anticancer drug 2-methyl-9-hydroxyellipticinium acetate in DNA fragments with circular dichroism
    • Monnot M, Mauffret O, Lescot E, Fermandjian S, (1992) Probing intercalation and conformational effects of the anticancer drug 2-methyl-9-hydroxyellipticinium acetate in DNA fragments with circular dichroism. Eur J Biochem 204: 1035-1039.
    • (1992) Eur J Biochem , vol.204 , pp. 1035-1039
    • Monnot, M.1    Mauffret, O.2    Lescot, E.3    Fermandjian, S.4
  • 59
    • 0025261344 scopus 로고
    • Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction
    • Heyduk T, Lee JC, (1990) Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction. Proc Natl Acad Sci U S A 87: 1744-1748.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 1744-1748
    • Heyduk, T.1    Lee, J.C.2
  • 60
    • 0030919292 scopus 로고    scopus 로고
    • Fluorescence approaches to study of protein-nucleic acid complexation
    • Hill JJ, Royer CA, (1997) Fluorescence approaches to study of protein-nucleic acid complexation. Methods Enzymol 278: 390-416.
    • (1997) Methods Enzymol , vol.278 , pp. 390-416
    • Hill, J.J.1    Royer, C.A.2
  • 61
    • 58149154667 scopus 로고    scopus 로고
    • The terminal (catalytic) adenosine of the HIV LTR controls the kinetics of binding and dissociation of HIV integrase strand transfer inhibitors
    • 10.1021/bi801372d [doi]
    • Langley DR, Samanta HK, Lin Z, Walker MA, Krystal MR, et al. (2008) The terminal (catalytic) adenosine of the HIV LTR controls the kinetics of binding and dissociation of HIV integrase strand transfer inhibitors. Biochemistry 47: 13481-13488 10.1021/bi801372d [doi].
    • (2008) Biochemistry , vol.47 , pp. 13481-13488
    • Langley, D.R.1    Samanta, H.K.2    Lin, Z.3    Walker, M.A.4    Krystal, M.R.5
  • 62
    • 17144425757 scopus 로고    scopus 로고
    • Pre-organized structure of viral DNA at the binding-processing site of HIV-1 integrase
    • 33/6/1970 [pii];10.1093/nar/gki346 [doi]
    • Renisio JG, Cosquer S, Cherrak I, El AS, Mauffret O, et al. (2005) Pre-organized structure of viral DNA at the binding-processing site of HIV-1 integrase. Nucleic Acids Res 33: 1970-1981 33/6/1970 [pii];10.1093/nar/gki346 [doi].
    • (2005) Nucleic Acids Res , vol.33 , pp. 1970-1981
    • Renisio, J.G.1    Cosquer, S.2    Cherrak, I.3    El, A.S.4    Mauffret, O.5
  • 63
    • 0003896404 scopus 로고
    • Understanding DNA: The Molecule and How It Works
    • Academic Press, London
    • Calladine CR, Drew HR, (1992) Understanding DNA: The Molecule and How It Works. Academic Press, London.
    • (1992)
    • Calladine, C.R.1    Drew, H.R.2
  • 64
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison V, Brown PO, (1994) A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc Natl Acad Sci U S A 91: 7316-7320.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 65
    • 0035915354 scopus 로고    scopus 로고
    • Cooperativity in drug-DNA recognition: a molecular dynamics study
    • ja016233n [pii]
    • Harris SA, Gavathiotis E, Searle MS, Orozco M, Laughton CA, (2001) Cooperativity in drug-DNA recognition: a molecular dynamics study. J Am Chem Soc 123: 12658-12663 ja016233n [pii].
    • (2001) J Am Chem Soc , vol.123 , pp. 12658-12663
    • Harris, S.A.1    Gavathiotis, E.2    Searle, M.S.3    Orozco, M.4    Laughton, C.A.5
  • 66
    • 70450257688 scopus 로고    scopus 로고
    • A detailed binding free energy study of 2:1 ligand-DNA complex formation by experiment and simulation
    • 10.1039/b910574c [doi]
    • Treesuwan W, Wittayanarakul K, Anthony NG, Huchet G, Alniss H, et al. (2009) A detailed binding free energy study of 2:1 ligand-DNA complex formation by experiment and simulation. Phys Chem Chem Phys 11: 10682-10693 10.1039/b910574c [doi].
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 10682-10693
    • Treesuwan, W.1    Wittayanarakul, K.2    Anthony, N.G.3    Huchet, G.4    Alniss, H.5
  • 67
    • 77956186444 scopus 로고    scopus 로고
    • Medicinal chemistry by the numbers: the physicochemistry, thermodynamics and kinetics of modern drug design
    • Smith GF, (2009) Medicinal chemistry by the numbers: the physicochemistry, thermodynamics and kinetics of modern drug design. Prog Med Chem 48: 1-29.
    • (2009) Prog Med Chem , vol.48 , pp. 1-29
    • Smith, G.F.1
  • 68
    • 33747802145 scopus 로고    scopus 로고
    • A thermodynamic signature for drug-DNA binding mode
    • S0003-9861(06)00132-9 [pii];10.1016/j.abb.2006.03.027 [doi]
    • Chaires JB, (2006) A thermodynamic signature for drug-DNA binding mode. Arch Biochem Biophys 453: 26-31 S0003-9861(06)00132-9 [pii];10.1016/j.abb.2006.03.027 [doi].
    • (2006) Arch Biochem Biophys , vol.453 , pp. 26-31
    • Chaires, J.B.1
  • 69
    • 84455192537 scopus 로고    scopus 로고
    • Molecular dynamics approaches estimate the binding energy of HIV-1 integrase inhibitors and correlate with in vitro activity
    • AAC.05292-11 [pii];10.1128/AAC.05292-11 [doi]
    • Johnson BC, Metifiot M, Pommier Y, Hughes SH, (2012) Molecular dynamics approaches estimate the binding energy of HIV-1 integrase inhibitors and correlate with in vitro activity. Antimicrob Agents Chemother 56: 411-419 AAC.05292-11 [pii];10.1128/AAC.05292-11 [doi].
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 411-419
    • Johnson, B.C.1    Metifiot, M.2    Pommier, Y.3    Hughes, S.H.4
  • 70
    • 0026095906 scopus 로고
    • Human immunodeficiency virus integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage
    • Vink C, van Gent DC, Elgersma Y, Plasterk RH, (1991) Human immunodeficiency virus integrase protein requires a subterminal position of its viral DNA recognition sequence for efficient cleavage. J Virol 65: 4636-4644.
    • (1991) J Virol , vol.65 , pp. 4636-4644
    • Vink, C.1    van Gent, D.C.2    Elgersma, Y.3    Plasterk, R.H.4
  • 71
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: mechanism of viral DNA cleavage and DNA strand transfer
    • 0092-8674(91)90297-C [pii]
    • Engelman A, Mizuuchi K, Craigie R, (1991) HIV-1 DNA integration: mechanism of viral DNA cleavage and DNA strand transfer. Cell 67: 1211-1221 0092-8674(91)90297-C [pii].
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 72
    • 0026348879 scopus 로고
    • Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein
    • Vink C, Yeheskiely E, van der Marel GA, van Boom JH, Plasterk RH, (1991) Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein. Nucleic Acids Res 19: 6691-6698.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6691-6698
    • Vink, C.1    Yeheskiely, E.2    van der Marel, G.A.3    van Boom, J.H.4    Plasterk, R.H.5


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