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Volumn 3, Issue 10, 2008, Pages 635-644

Vinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activity

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 5,6,7,8 TETRAHYDRO 4H CYCLOHEPTA[B]THIOPHENE 3 CARBOXAMIDE; CYSTEINE; LYSINE; N [3 (AMINOCARBONYL) 4,5 DIMETHYL 2 THIENYL] 2 FURANCARBOXAMIDE; NSC 727447; NSC 727448; PROTEIN P51; PROTEIN P66; PROTEIN SUBUNIT; RIBONUCLEASE H; RIBONUCLEASE INHIBITOR; RNA DIRECTED DNA POLYMERASE; RNA DIRECTED DNA POLYMERASE INHIBITOR; THUJAPLICIN; UNCLASSIFIED DRUG; VINYLOGOUS UREA DERIVATIVE;

EID: 58149160464     PISSN: 15548929     EISSN: None     Source Type: Journal    
DOI: 10.1021/cb8001039     Document Type: Article
Times cited : (58)

References (34)
  • 1
    • 0024847468 scopus 로고
    • Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function
    • Schatz, O., Cromme, F. V., Gruninger-Leitch, F., and Le Grice, S. F. (1989) Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function, FEBS Lett. 257, 311-314.
    • (1989) FEBS Lett , vol.257 , pp. 311-314
    • Schatz, O.1    Cromme, F.V.2    Gruninger-Leitch, F.3    Le Grice, S.F.4
  • 2
    • 0001851755 scopus 로고
    • Inactivation of the RNase H domain of HIV-1 reverse transcriptase blocks viral infectivity
    • Papas, T, Ed, pp, Portfolio Publishing, Houston, TX
    • Schatz, O., Mous, J., and Le Grice, S. F. J. (1990) Inactivation of the RNase H domain of HIV-1 reverse transcriptase blocks viral infectivity, in Oncogenesis and AIDS (Papas, T., Ed.) pp 293-303, Portfolio Publishing, Houston, TX.
    • (1990) Oncogenesis and AIDS , pp. 293-303
    • Schatz, O.1    Mous, J.2    Le Grice, S.F.J.3
  • 4
    • 33646497669 scopus 로고    scopus 로고
    • Recent progress in the design of small molecule inhibitors of HIV RNase H
    • Klumpp, K., and Mirzadegan, T. (2006) Recent progress in the design of small molecule inhibitors of HIV RNase H, Curr. Pharm. Des. 12, 1909-1922.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 1909-1922
    • Klumpp, K.1    Mirzadegan, T.2
  • 5
    • 13444257639 scopus 로고    scopus 로고
    • Dissecting the effects of DNA polymerase and ribonuclease H inhibitor combinations on HIV-1 reverse-transcriptase activities
    • Shaw-Reid, C. A., Feuston, B., Munshi, V., Getty, K., Krueger, J., Hazuda, D. J., Parniak, M. A., Miller, M. D., and Lewis, D. (2005) Dissecting the effects of DNA polymerase and ribonuclease H inhibitor combinations on HIV-1 reverse-transcriptase activities, Biochemistry 44, 1595-1606.
    • (2005) Biochemistry , vol.44 , pp. 1595-1606
    • Shaw-Reid, C.A.1    Feuston, B.2    Munshi, V.3    Getty, K.4    Krueger, J.5    Hazuda, D.J.6    Parniak, M.A.7    Miller, M.D.8    Lewis, D.9
  • 8
    • 0037058982 scopus 로고    scopus 로고
    • Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent
    • Kvaratskhelia, M., Miller, J. T., Budihas, S. R., Pannell, L. K., and Le Grice, S. F. (2002) Identification of specific HIV-1 reverse transcriptase contacts to the viral RNA:tRNA complex by mass spectrometry and a primary amine selective reagent, Proc. Natl. Acad. Sci. U.S.A. 99, 15988-15993.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 15988-15993
    • Kvaratskhelia, M.1    Miller, J.T.2    Budihas, S.R.3    Pannell, L.K.4    Le Grice, S.F.5
  • 12
    • 0037117744 scopus 로고    scopus 로고
    • Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity
    • Rausch, J. W., Lener, D., Miller, J. T., Julias, J. G., Hughes, S. H., and Le Grice, S. F. (2002) Altering the RNase H primer grip of human immunodeficiency virus reverse transcriptase modifies cleavage specificity, Biochemistry 41, 4856-4865.
    • (2002) Biochemistry , vol.41 , pp. 4856-4865
    • Rausch, J.W.1    Lener, D.2    Miller, J.T.3    Julias, J.G.4    Hughes, S.H.5    Le Grice, S.F.6
  • 13
    • 0038107748 scopus 로고    scopus 로고
    • Mutation of amino acids in the connection domain of human immunodeficiency virus type 1 reverse transcriptase that contact the template-primer affects RNase H activity
    • Julias, J. G., McWilliams, M. J., Sarafianos, S. G., Alvord, W. G., Arnold, E., and Hughes, S. H. (2003) Mutation of amino acids in the connection domain of human immunodeficiency virus type 1 reverse transcriptase that contact the template-primer affects RNase H activity, J. Virol. 77, 8548-8554.
    • (2003) J. Virol , vol.77 , pp. 8548-8554
    • Julias, J.G.1    McWilliams, M.J.2    Sarafianos, S.G.3    Alvord, W.G.4    Arnold, E.5    Hughes, S.H.6
  • 14
    • 33645325418 scopus 로고    scopus 로고
    • Efficient incorporation of unnatural amino acids into proteins in Escherichia coli
    • Ryu, Y., and Schultz, P. G. (2006) Efficient incorporation of unnatural amino acids into proteins in Escherichia coli, Nat. Methods 3, 263-265.
    • (2006) Nat. Methods , vol.3 , pp. 263-265
    • Ryu, Y.1    Schultz, P.G.2
  • 16
    • 0141758137 scopus 로고    scopus 로고
    • A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity
    • Parniak, M. A., Min, K. L., Budihas, S. R., Le Grice, S. F., and Beutler, J. A. (2003) A fluorescence-based high-throughput screening assay for inhibitors of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H activity, Anal. Biochem. 322, 33-39.
    • (2003) Anal. Biochem , vol.322 , pp. 33-39
    • Parniak, M.A.1    Min, K.L.2    Budihas, S.R.3    Le Grice, S.F.4    Beutler, J.A.5
  • 17
    • 9744258219 scopus 로고    scopus 로고
    • Crystallography and the design of anti-AIDS drugs: Conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors
    • Das, K., Lewi, P. J., Hughes, S. H., and Arnold, E. (2005) Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors, Prog. Biophys. Mol. Biol. 88, 209-231.
    • (2005) Prog. Biophys. Mol. Biol , vol.88 , pp. 209-231
    • Das, K.1    Lewi, P.J.2    Hughes, S.H.3    Arnold, E.4
  • 18
    • 0020346411 scopus 로고
    • The Yonetani-Theorell graphical method for examining overlapping subsites of enzyme active centers
    • Yonetani, T. (1982) The Yonetani-Theorell graphical method for examining overlapping subsites of enzyme active centers, Methods Enzymol. 87, 500-9.
    • (1982) Methods Enzymol , vol.87 , pp. 500-509
    • Yonetani, T.1
  • 19
    • 0015495920 scopus 로고
    • Adsorbents for affinity chromatography. Use of N-hydroxysuccinimide esters of agarose
    • Cuatrecasas, P., and Parikh, I. (1972) Adsorbents for affinity chromatography. Use of N-hydroxysuccinimide esters of agarose, Biochemisry 11, 2291-2299.
    • (1972) Biochemisry , vol.11 , pp. 2291-2299
    • Cuatrecasas, P.1    Parikh, I.2
  • 20
    • 0034111063 scopus 로고    scopus 로고
    • Trapping of a catalytic HIV reverse transcriptase*template:primer complex through a disulfide bond
    • Huang, H., Harrison, S. C., and Verdine, G. L. (2000) Trapping of a catalytic HIV reverse transcriptase*template:primer complex through a disulfide bond, Chem. Biol. 7, 355-364.
    • (2000) Chem. Biol , vol.7 , pp. 355-364
    • Huang, H.1    Harrison, S.C.2    Verdine, G.L.3
  • 22
    • 0032478535 scopus 로고    scopus 로고
    • Effects of mutations in the polymerase domain on the polymerase, RNase H and strand transfer activities of human immunodeficiency virus type 1 reverse transcriptase
    • Gao, H. Q., Boyer, P. L., Arnold, E., and Hughes, S. H. (1998) Effects of mutations in the polymerase domain on the polymerase, RNase H and strand transfer activities of human immunodeficiency virus type 1 reverse transcriptase, J. Mol. Biol. 277, 559-572.
    • (1998) J. Mol. Biol , vol.277 , pp. 559-572
    • Gao, H.Q.1    Boyer, P.L.2    Arnold, E.3    Hughes, S.H.4
  • 23
    • 0028096227 scopus 로고
    • Modulation of HIV-1 reverse transcriptase function in "selectively deleted" p66/p51 heterodimers
    • Jacques, P. S., Wohrl, B. M., Howard, K. J., and Le Grice, S. F. (1994) Modulation of HIV-1 reverse transcriptase function in "selectively deleted" p66/p51 heterodimers, J. Biol. Chem. 269, 1388-1393.
    • (1994) J. Biol. Chem , vol.269 , pp. 1388-1393
    • Jacques, P.S.1    Wohrl, B.M.2    Howard, K.J.3    Le Grice, S.F.4
  • 24
    • 34250811908 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3′-azido-3′-deoxythymidine resistance
    • Delviks-Frankenberry, K. A., Nikolenko, G. N., Barr, R., and Pathak, V. K. (2007) Mutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3′-azido-3′-deoxythymidine resistance, J. Virol. 81, 6837-6845.
    • (2007) J. Virol , vol.81 , pp. 6837-6845
    • Delviks-Frankenberry, K.A.1    Nikolenko, G.N.2    Barr, R.3    Pathak, V.K.4
  • 27
    • 33749019097 scopus 로고    scopus 로고
    • A chemical toolkit for proteins-an expanded genetic code
    • Xie, J., and Schultz, P. G. (2006) A chemical toolkit for proteins-an expanded genetic code, Nat. Rev. Mol. Cell Biol. 7, 775-782.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 775-782
    • Xie, J.1    Schultz, P.G.2
  • 29
    • 0026070438 scopus 로고
    • Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase
    • Le Grice, S. F., Naas, T., Wohlgensinger, B., and Schatz, O. (1991) Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase, EMBO J. 10, 3905-3911.
    • (1991) EMBO J , vol.10 , pp. 3905-3911
    • Le Grice, S.F.1    Naas, T.2    Wohlgensinger, B.3    Schatz, O.4
  • 30
    • 0026633994 scopus 로고
    • Specificity of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H in removal of the minus-strand primer, tRNA(Lys3)
    • Smith, J. S., and Roth, M. J. (1992) Specificity of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H in removal of the minus-strand primer, tRNA(Lys3), J. Biol. Chem. 267, 15071-15079.
    • (1992) J. Biol. Chem , vol.267 , pp. 15071-15079
    • Smith, J.S.1    Roth, M.J.2
  • 31
    • 33845462923 scopus 로고    scopus 로고
    • HIV-1 RT nonnucleoside inhibitors and their interaction with RT for antiviral drug development
    • Zhou, Z., Lin, X., and Madura, J. D. (2006) HIV-1 RT nonnucleoside inhibitors and their interaction with RT for antiviral drug development, Infect. Disord. Drug Targets 6, 391-413.
    • (2006) Infect. Disord. Drug Targets , vol.6 , pp. 391-413
    • Zhou, Z.1    Lin, X.2    Madura, J.D.3
  • 33
    • 33746948397 scopus 로고    scopus 로고
    • Structure-activity relationships of [2′,5′-bis-O-(tert-butyldimethylsilyl)-β-D- ribofuranosyl]-3′-spiro-5″-(4″-amino-1″, 2″-oxathiole-2″,2″-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization
    • Sluis-Cremer, N., Hamamouch, N., San Felix, A., Velazquez, S., Balzarini, J., and Camarasa, M. J. (2006) Structure-activity relationships of [2′,5′-bis-O-(tert-butyldimethylsilyl)-β-D- ribofuranosyl]-3′-spiro-5″-(4″-amino-1″, 2″-oxathiole-2″,2″-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization, J. Med. Chem. 49, 4834-4841.
    • (2006) J. Med. Chem , vol.49 , pp. 4834-4841
    • Sluis-Cremer, N.1    Hamamouch, N.2    San Felix, A.3    Velazquez, S.4    Balzarini, J.5    Camarasa, M.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.