메뉴 건너뛰기




Volumn 54, Issue 6, 2011, Pages 1812-1824

Magnesium chelating 2-hydroxyisoquinoline-1,3(2H, 4H)-diones, as inhibitors of HIV-1 integrase and/or the HIV-1 reverse transcriptase ribonuclease H domain: Discovery of a novel selective inhibitor of the ribonuclease H function

Author keywords

[No Author keywords available]

Indexed keywords

1 HYDROXY 1,8 NAPHTHYRIDIN 2 (1H) ONE DERIVATIVE; 2 HYDROXY 4 METHOXYCARBONYLISOQUINOLINE 1,3 (2H,4H)DIONE; 2 HYDROXY 4 METHYLISOQUINOLINE 1,3 (2H,4H)DIONE; 2 HYDROXYISOQUINOLINE 1,3 (2H,4H)DIONE; ANTI HUMAN IMMUNODEFICIENCY VIRUS AGENT; DNA POLYMERASE; EFAVIRENZ; INTEGRASE; ISOQUINOLINE DERIVATIVE; MAGNESIUM DERIVATIVE; MANGANESE; METHYL 2 HYDROXY 1,3 DIOXO 1,2,3,4 TETRAHYDROISOQUINOLINE 4 CARBOXYLATE; RALTEGRAVIR; RIBONUCLEASE H; RNA DIRECTED DNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 79952789620     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm1014692     Document Type: Article
Times cited : (124)

References (61)
  • 1
    • 36749073433 scopus 로고    scopus 로고
    • The design of drugs for HIV and HCV
    • DOI 10.1038/nrd2424, PII NRD2424
    • De Clercq, E. The design of drugs for HIV and HCV Nat. Rev. Drug Discovery 2007, 6, 1001-1018 (Pubitemid 350213865)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.12 , pp. 1001-1018
    • De Clercq, E.1
  • 2
    • 6944235757 scopus 로고    scopus 로고
    • Closely related antiretroviral agents as inhibitors of two HIV-1 enzymes, ribonuclease H and integrase: Killing two birds with one stone
    • Andréola, M. L. Closely related antiretroviral agents as inhibitors of two HIV-1 enzymes, ribonuclease H and integrase: "illing two birds with one stone Curr. Pharm. Des. 2004, 10, 3713-3723
    • (2004) Curr. Pharm. Des. , vol.10 , pp. 3713-3723
    • Andréola, M.L.1
  • 3
    • 43049125772 scopus 로고    scopus 로고
    • RNase H activity: Structure and function in reverse transcription
    • Schultz, S. J.; Champoux, J. J. RNase H activity: Structure and function in reverse transcription Virus Res. 2008, 134, 86-103
    • (2008) Virus Res. , vol.134 , pp. 86-103
    • Schultz, S.J.1    Champoux, J.J.2
  • 4
    • 2942553781 scopus 로고    scopus 로고
    • Structure and function of HIV-1 integrase
    • Chiu, T. K.; Davies, D. R. Structure and function of HIV-1 integrase Curr. Top. Med. Chem. 2004, 4, 965-977
    • (2004) Curr. Top. Med. Chem. , vol.4 , pp. 965-977
    • Chiu, T.K.1    Davies, D.R.2
  • 10
    • 0030566832 scopus 로고    scopus 로고
    • The catalytic domain of human immunodeficiency virus integrase: Ordered active site in the F185H mutant
    • DOI 10.1016/S0014-5793(96)01236-7, PII S0014579396012367
    • Bujacz, G.; Alexandratos, J.; ZhouLiu, Q.; ClementMella, C.; Wlodawer, A. The catalytic domain of human immunodeificiency virus integrase: ordered active site in the F185H mutant FEBS Lett. 1996, 398, 175-178 (Pubitemid 26414304)
    • (1996) FEBS Letters , vol.398 , Issue.2-3 , pp. 175-178
    • Bujacz, G.1    Alexandratos, J.2    Zhou-Liu, Q.3    Clement-Mella, C.4    Wlodawer, A.5
  • 11
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, F.; Hickman, A. B.; Jenkins, T. M.; Engelman, A.; Craigie, R.; Davies, D. R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases Science 1994, 266, 1981-1986
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 12
    • 0033551443 scopus 로고    scopus 로고
    • The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity
    • Greenwald, J.; Le, V.; Butler, S. L.; Bushman, F. D.; Choe, S. The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity Biochemistry 1999, 38, 8892-8898
    • (1999) Biochemistry , vol.38 , pp. 8892-8898
    • Greenwald, J.1    Le, V.2    Butler, S.L.3    Bushman, F.D.4    Choe, S.5
  • 13
    • 0032544311 scopus 로고    scopus 로고
    • Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: High level of similarity of the active site with other viral integrases
    • DOI 10.1006/jmbi.1998.2002
    • Maignan, S.; Guilloteau, J. P.; Zhou-Liu, Q.; Clément-Mella, C.; Mikol, V. Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases J. Mol. Biol. 1998, 282, 359-368 (Pubitemid 28418789)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.2 , pp. 359-368
    • Maignan, S.1    Guilloteau, J.-P.2    Zhou-Liu, Q.3    Clement-Mella, C.4    Mikol, V.5
  • 14
    • 0030746054 scopus 로고    scopus 로고
    • Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity
    • DOI 10.1074/jbc.272.29.18161
    • Bujacz, G.; Alexandratos, J.; Wlodawer, A.; Merkel, G.; Andrake, M.; Katz, R. A.; Skalka, A. M. Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity J. Biol. Chem. 1997, 272, 18161-18168 (Pubitemid 27306402)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18161-18168
    • Bujacz, G.1    Alexandratos, J.2    Wlodawer, A.3    Merkel, G.4    Andrake, M.5    Katz, R.A.6    Skalka, A.M.7
  • 15
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare, S.; Gupta, S. S.; Volkov, E.; Engelman, A.; Cherepanov, P. Retroviral intasome assembly and inhibition of DNA strand transfer Nature 2010, 464, 232-236
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Volkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 16
    • 0025908083 scopus 로고
    • Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase
    • Davies, J. F., II; Hostomska, Z.; Hostomsky, Z.; Jordan, S. R.; Matthews, D. A. Crystal structure of the ribonuclease H domain of HIV-1 reverse transcriptase Science 1991, 252, 88-95 (Pubitemid 21916941)
    • (1991) Science , vol.252 , Issue.5002 , pp. 88-95
    • Davies III, J.F.1    Hostomska, Z.2    Hostomsky, Z.3    Jordan, S.R.4    Matthews, D.A.5
  • 18
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 - Resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt, L. A.; Wang, J.; Friedman, J. M.; Rice, P. A.; Steizt, T. A. Crystal structure at 3.5 - resolution of HIV-1 reverse transcriptase complexed with an inhibitor Science 1992, 256, 1783-1790
    • (1992) Science , vol.56 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steizt, T.A.5
  • 20
    • 0032573488 scopus 로고    scopus 로고
    • Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: Implications for drug resistance
    • Huang, H.; Chopra, R.; Verdine, G. L.; Harrison, S. C. Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance Science 1998, 282, 1669-1675 (Pubitemid 28549275)
    • (1998) Science , vol.282 , Issue.5394 , pp. 1669-1675
    • Huang, H.1    Chopra, R.2    Verdine, G.L.3    Harrison, S.C.4
  • 21
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: Substrate specificity and metal-dependent catalysis
    • DOI 10.1016/j.cell.2005.04.024, PII S0092867405004046
    • Nowotny, M.; Gaidarnakov, S. A.; Crouch, R. J.; Yang, W. Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis Cell 2005, 121, 1005-1016 (Pubitemid 40884393)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 22
    • 35348978302 scopus 로고    scopus 로고
    • Structure of Human RNase H1 Complexed with an RNA/DNA Hybrid: Insight into HIV Reverse Transcription
    • DOI 10.1016/j.molcel.2007.08.015, PII S1097276507005588
    • Nowotny, M.; Gaidarnakov, S. A.; Ghirlando, R.; Cerritelli, S. M.; Crouch, R. J.; Yang, W. Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription Mol. Cell 2007, 28, 264-276 (Pubitemid 47599996)
    • (2007) Molecular Cell , vol.28 , Issue.2 , pp. 264-276
    • Nowotny, M.1    Gaidamakov, S.A.2    Ghirlando, R.3    Cerritelli, S.M.4    Crouch, R.J.5    Yang, W.6
  • 23
    • 0037469137 scopus 로고    scopus 로고
    • Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium
    • DOI 10.1021/bi0204894
    • Pari, K.; Mueller, G. A.; DeRose, E. F.; Kirby, T. W.; London, R. E. Solution structure of the RNase H domain of the HIV-1 reverse transcriptase in the presence of magnesium Biochemistry 2003, 42, 639-650 (Pubitemid 36133288)
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 639-650
    • Pari, K.1    Mueller, G.A.2    DeRose, E.F.3    Kirby, T.W.4    London, R.E.5
  • 26
    • 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
    • DOI 10.1016/j.antiviral.2004.11.002
    • Tramontano, E.; Esposito, F.; Badas, R.; Di Santo, R.; Costi, R.; La Colla, P. 6-[1-(4-Fluorophenyl)methyl-1 H -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 Antiviral Res. 2005, 65, 117-124 (Pubitemid 40222288)
    • (2005) Antiviral Research , 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
  • 33
    • 6044232037 scopus 로고    scopus 로고
    • Spectroscopic studies of diketoacids-metal interactions. A probing tool for the pharmacophoric intermetallic distance in the HIV-1 integrase active site
    • DOI 10.1021/jm0408464
    • Maurin, C.; Bailly, F.; Buisine, E.; Vezin, H.; Mbemba, G.; Mouscadet, J. F.; Cotelle, P. Spectroscopic studies of diketoacids-metal interactions. A probing tool for the pharmacophoric intermetallic distance in the HIV-1 integrase active site J. Med. Chem. 2004, 47, 5583-5586 (Pubitemid 39382805)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.22 , pp. 5583-5586
    • Maurin, C.1    Bailly, F.2    Buisine, E.3    Vezin, H.4    Mbemba, G.5    Mouscadet, J.F.6    Cotelle, P.7
  • 36
    • 33646497669 scopus 로고    scopus 로고
    • Recent progress in the design of small molecule inhibitors of HIV RNase H
    • Klumpp, K.; Mirzdegan, T. Recent progress in the design of small molecule inhibitors of HIV RNase H Curr. Pharm. Des. 2006, 12, 1909-1922
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 1909-1922
    • Klumpp, K.1    Mirzdegan, T.2
  • 37
    • 58149083480 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of a series of 2-hydroxyisoquinoline-1,3(2 H,4 H)-diones as dual inhibitors of human immunodeficiency virus type 1 integrase and reverse transcriptase RNase H domain
    • Billamboz, M.; Bailly, F.; Barreca, M. L.; De Luca, L.; Mouscadet, J. F.; Calmels, C.; Andreola, M. L.; Christ, F.; Debyser, Z.; Witvrouw, M.; Cotelle, P. Design, synthesis and biological evaluation of a series of 2-hydroxyisoquinoline-1,3(2 H,4 H)-diones as dual inhibitors of human immunodeficiency virus type 1 integrase and reverse transcriptase RNase H domain J. Med. Chem. 2008, 51, 7717-7730
    • (2008) J. Med. Chem. , vol.51 , pp. 7717-7730
    • Billamboz, M.1    Bailly, F.2    Barreca, M.L.3    De Luca, L.4    Mouscadet, J.F.5    Calmels, C.6    Andreola, M.L.7    Christ, F.8    Debyser, Z.9    Witvrouw, M.10    Cotelle, P.11
  • 39
    • 11744305193 scopus 로고
    • Efficient implementation of the gauge-independent atomic orbital method for NMR chemical shift calculations
    • Wolinski, K.; Hinton, J. F.; Pulay, P. Efficient implementation of the gauge-independent atomic orbital method for NMR chemical shift calculations J. Am. Chem. Soc. 1990, 112, 8251-8260
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 8251-8260
    • Wolinski, K.1    Hinton, J.F.2    Pulay, P.3
  • 40
    • 1242268874 scopus 로고    scopus 로고
    • A comparison of models for calculating nuclear magnetic resonance shielding tensors
    • Cheeseman, J. R.; Trucks, G. W.; Keith, T. A.; Frish, M. J. A comparison of models for calculating nuclear magnetic resonance shielding tensors J. Chem. Phys. 1996, 104, 5497-5509 (Pubitemid 126715510)
    • (1996) Journal of Chemical Physics , vol.104 , Issue.14 , pp. 5497-5509
    • Cheeseman, J.R.1
  • 41
    • 9644286821 scopus 로고    scopus 로고
    • Comparison of different theory models and basis sets in the calculation of 13C NMR chemical shifts of natural products
    • Cimino, P.; Gomez-Paloma, L.; Duca, D.; Riccio, R.; Bifulco, G. Comparison of different theory models and basis sets in the calculation of 13C NMR chemical shifts of natural products Magn. Reson. Chem. 2004, 42, S26-S33
    • (2004) Magn. Reson. Chem. , vol.42
    • Cimino, P.1    Gomez-Paloma, L.2    Duca, D.3    Riccio, R.4    Bifulco, G.5
  • 42
    • 33746274916 scopus 로고    scopus 로고
    • 13C NMR spectra of complex organic molecules by DFT methods: Application to natural substances
    • DOI 10.1002/chem.200501583
    • 13C NMR spectra of complex organic molecules by DFT methods: application to natural substances Chem.a - Eur. J. 2006, 12, 5514-5525 (Pubitemid 44106360)
    • (2006) Chemistry - A European Journal , vol.12 , Issue.21 , pp. 5514-5525
    • Bagno, A.1    Rastrelli, F.2    Saielli, G.3
  • 44
    • 0037137647 scopus 로고    scopus 로고
    • aOH radicals to the ipso positions of alkyl-substituted aromatics: Production of 4-hydroxy-4-methyl-2,5-cyclohexadien- 1-one in the radiolytic oxidation of p -cresol
    • aOH radicals to the ipso positions of alkyl-substituted aromatics: production of 4-hydroxy-4-methyl-2,5- cyclohexadien-1-one in the radiolytic oxidation of p -cresol J. Phys. Chem. A 2002, 106, 12178-12183
    • (2002) J. Phys. Chem. A , vol.106 , pp. 12178-12183
    • Schuler, R.H.1    Albarran, G.2    Zajicek, J.3    George, M.V.4    Fessenden, R.W.5    Carmichael, I.6
  • 45
    • 0038527254 scopus 로고    scopus 로고
    • Structure reassignment of the fungal metabolite TAEMC161 as the phytotoxin viridiol
    • DOI 10.1021/np0300277
    • Wipf, P.; Kerekes, A. Structure reassignment of the fungal metabolite TAEMC161 as the phytotoxin viridiol J. Nat. Prod. 2003, 66, 716-718 (Pubitemid 36617906)
    • (2003) Journal of Natural Products , vol.66 , Issue.5 , pp. 716-718
    • Wipf, P.1    Kerekes, A.D.2
  • 46
    • 56449084281 scopus 로고    scopus 로고
    • 13C NMR shifts of diazaphenanthrene alkaloids: Reinvestigation of the structure of samoquasine A
    • 13C NMR shifts of diazaphenanthrene alkaloids: reinvestigation of the structure of samoquasine A J. Org. Chem. 2008, 73, 9168-9170
    • (2008) J. Org. Chem. , vol.73 , pp. 9168-9170
    • Timmons, C.1    Wipf, P.2
  • 49
    • 62149093020 scopus 로고    scopus 로고
    • The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation
    • Delelis, O.; Malet, I.; Na, L.; Tchertanov, L.; Calvez, V.; Marcelin, A. G.; Subra, F.; Deprez, E.; Mouscadet, J. F. The G140S mutation in HIV integrases from raltegravir-resistant patients rescues catalytic defect due to the resistance Q148H mutation Nucleic Acids Res. 2009, 37, 1193-1201
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1193-1201
    • Delelis, O.1    Malet, I.2    Na, L.3    Tchertanov, L.4    Calvez, V.5    Marcelin, A.G.6    Subra, F.7    Deprez, E.8    Mouscadet, J.F.9
  • 51
    • 0345314349 scopus 로고
    • 3-Hydroxyimides. II. Derivatives of homophthalic and phthalic acids
    • Ames, D. E.; Grey, T. F. 3-Hydroxyimides. II. Derivatives of homophthalic and phthalic acids J. Chem. Soc. 1955, 3518-3521
    • (1955) J. Chem. Soc. , pp. 3518-3521
    • Ames, D.E.1    Grey, T.F.2
  • 52
    • 53149114851 scopus 로고    scopus 로고
    • Complexation of 2,3-dihydroxyquinoline with some bivalent d metals. Crystal and molecular structures of 2,3-dihydroxyquinoline
    • Strashnova, S. B.; Kovalchukova, O. V.; Zaitsev, B. E.; Stash, A. Complexation of 2,3-dihydroxyquinoline with some bivalent d metals. Crystal and molecular structures of 2,3-dihydroxyquinoline Russ. J. Coord. Chem. 2008, 34, 775-779
    • (2008) Russ. J. Coord. Chem. , vol.34 , pp. 775-779
    • Strashnova, S.B.1    Kovalchukova, O.V.2    Zaitsev, B.E.3    Stash, A.4
  • 55
    • 66349087352 scopus 로고    scopus 로고
    • Facile synthesis of 4-alkoxycarbonylisoquinoline-1,3-diones and 5-alkoxycarbonyl-2-benzazepine-1,3-diones via a mild alkaline cyclization
    • Billamboz, M.; Bailly, F.; Cotelle, P. Facile synthesis of 4-alkoxycarbonylisoquinoline-1,3-diones and 5-alkoxycarbonyl-2-benzazepine-1,3- diones via a mild alkaline cyclization J. Heterocycl. Chem. 2009, 46, 392-398
    • (2009) J. Heterocycl. Chem. , vol.46 , pp. 392-398
    • Billamboz, M.1    Bailly, F.2    Cotelle, P.3
  • 57
    • 0034672040 scopus 로고    scopus 로고
    • Rapid microtiter assays for poxvirus topoisomerase, mammalian type IB topoisomerase and HIV-1 integrase: Application to inhibitor isolation
    • Hwang, Y.; Rhodes, D.; Bushman, F. Rapid microtiter assays for poxvirus topoisomerase, mammalian type IB topoisomerase and HIV-1 integrase: application to inhibitor isolation Nucleic Acids Res. 2000, 28, 4884-4892 (Pubitemid 32014258)
    • (2000) Nucleic Acids Research , vol.28 , Issue.24 , pp. 4884-4892
    • Hwang, Y.1    Rhodes, D.2    Bushman, F.3
  • 59
    • 0024416124 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 RNase H by sulfated polyanions
    • Moelling, K.; Schulze, T.; Diringer, H. Inhibition of human immunodeficiency virus type 1 RNase H by polysulfated polyanions J. Virol. 1989, 63, 5489-5491 (Pubitemid 19278795)
    • (1989) Journal of Virology , vol.63 , Issue.12 , pp. 5489-5491
    • Moelling, K.1    Schulze, T.2    Diringer, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.