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Volumn 43, Issue 27, 2004, Pages 8735-8743

HIV-1 integrase complexes with DNA dissociate in the presence of short oligonucleotides conjugated to acridine

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXATION; DISSOCIATION; DNA; DRUG DOSAGE; ENZYME KINETICS; IMMUNOLOGY; OLIGOMERS;

EID: 3042772950     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049706m     Document Type: Article
Times cited : (28)

References (43)
  • 2
    • 0033984045 scopus 로고    scopus 로고
    • The decay of the latent reservoir of replication-competent HIV-1 is inversely correlated with the extent of residual viral replication during prolonged anti-retroviral therapy
    • Ramratnam, B., Mittler, J. E., Zhang, L., Boden, D., Hurley, A., Fang, F., Macken, C. A., Perelson, A. S., Markowitz, M., and Ho, D. D. (2000) The decay of the latent reservoir of replication-competent HIV-1 is inversely correlated with the extent of residual viral replication during prolonged anti-retroviral therapy, Nat. Med. 6, 82-85.
    • (2000) Nat. Med. , vol.6 , pp. 82-85
    • Ramratnam, B.1    Mittler, J.E.2    Zhang, L.3    Boden, D.4    Hurley, A.5    Fang, F.6    Macken, C.A.7    Perelson, A.S.8    Markowitz, M.9    Ho, D.D.10
  • 5
    • 0035796559 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 integrase: Arrangement of protein domains in active cDNA complexes
    • Gao, K., Butler, S. L., and Bushman, F. (2001) Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes, EMBO J. 20, 3565-3576.
    • (2001) EMBO J. , vol.20 , pp. 3565-3576
    • Gao, K.1    Butler, S.L.2    Bushman, F.3
  • 6
    • 0037137609 scopus 로고    scopus 로고
    • Autodocking dinucleotides to the HIV-1 integrase core domain: Exploring possible binding sites for viral and genomic DNA
    • Perryman, A. L. and McCammon, J. A. (2002) AutoDocking Dinucleotides to the HIV-1 Integrase Core Domain: Exploring Possible Binding Sites for Viral and Genomic DNA, J. Med. Chem. 45, 5624-5627.
    • (2002) J. Med. Chem. , vol.45 , pp. 5624-5627
    • Perryman, A.L.1    McCammon, J.A.2
  • 7
    • 0029864507 scopus 로고    scopus 로고
    • Chemical trapping of ternary complexes of human immunodeficiency virus type 1 integrase, divalent metal, and DNA substrates containing an abasic site. Implications for the role of lysine 136 in DNA binding
    • Mazumder, A., Neamati, N., Pilon, A. A., Sunder, S., and Pommier, Y. (1996) Chemical trapping of ternary complexes of human immunodeficiency virus type 1 integrase, divalent metal, and DNA substrates containing an abasic site. Implications for the role of lysine 136 in DNA binding, J. Biol. Chem. 271, 27330-27338.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27330-27338
    • Mazumder, A.1    Neamati, N.2    Pilon, A.A.3    Sunder, S.4    Pommier, Y.5
  • 9
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photocrosslinking
    • Jenkins, T. M., Esposito, D., Engelman, A., and Craigie, R. (1997) Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photocrosslinking, EMBO J. 16, 6849-6859.
    • (1997) EMBO J. , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 10
    • 0037234457 scopus 로고    scopus 로고
    • Modeling HIV-1 integrase complexes based on their hydrodynamic properties
    • Podtelezhnikov, A. A., Gao, K., Bushman, F. D., and McCammon, J. A. (2003) Modeling HIV-1 integrase complexes based on their hydrodynamic properties, Biopolymers 68, 110-120.
    • (2003) Biopolymers , vol.68 , pp. 110-120
    • Podtelezhnikov, A.A.1    Gao, K.2    Bushman, F.D.3    McCammon, J.A.4
  • 11
    • 0035806221 scopus 로고    scopus 로고
    • Discovery of a nuclease-resistant, nonnatural dinucleotide that inhibits HIV-1 integrase
    • Taktakishvili, M., Neamati, N., Pommier, Y., and Nair, V. (2001) Discovery of a nuclease-resistant, nonnatural dinucleotide that inhibits HIV-1 integrase, Bioorg. Med. Chem. Lett. 11, 1433-1435.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 1433-1435
    • Taktakishvili, M.1    Neamati, N.2    Pommier, Y.3    Nair, V.4
  • 12
    • 0028242724 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by 3′-azido-3′-deoxythymidylate
    • Mazumder, A., Cooney, D., Agbaria, R., Gupta, M., and Pommier, Y. (1994) Inhibition of human immunodeficiency virus type 1 integrase by 3′-azido-3′-deoxythymidylate, Proc. Natl. Acad. Sci. U.S.A. 91, 5771-5775.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5771-5775
    • Mazumder, A.1    Cooney, D.2    Agbaria, R.3    Gupta, M.4    Pommier, Y.5
  • 14
    • 0032546568 scopus 로고    scopus 로고
    • Biochemical characterization of the HIV-1 integrase 3′-processing activity and its inhibition by phosphorothioate oligonucleotides
    • Tramontano, E., Colla, P. L., and Cheng, Y. C. (1998) Biochemical characterization of the HIV-1 integrase 3′-processing activity and its inhibition by phosphorothioate oligonucleotides, Biochemistry 37, 7237-7243.
    • (1998) Biochemistry , vol.37 , pp. 7237-7243
    • Tramontano, E.1    Colla, P.L.2    Cheng, Y.C.3
  • 15
    • 0029964978 scopus 로고    scopus 로고
    • Inhibition of the human immunodeficiency virus type 1 integrase by guanosine quartet structures
    • Mazumder, A., Neamati, N., Ojwang, J. O., Sunder, S., Rando, R. F., and Pommier, Y. (1996) Inhibition of the human immunodeficiency virus type 1 integrase by guanosine quartet structures, Biochemistry 35, 13762-13771.
    • (1996) Biochemistry , vol.35 , pp. 13762-13771
    • Mazumder, A.1    Neamati, N.2    Ojwang, J.O.3    Sunder, S.4    Rando, R.F.5    Pommier, Y.6
  • 16
    • 0032744980 scopus 로고    scopus 로고
    • Branched oligonucleotide-intercalator conjugate forming a parallel stranded structure inhibits HIV-1 integrase
    • Brodin, P., Pinskaya, M., Volkov, E., Romanova, E., Leh, H., Auclair, C., Mouscadet, J. F., and Gottikh, M. (1999) Branched oligonucleotide-intercalator conjugate forming a parallel stranded structure inhibits HIV-1 integrase, FEBS Lett. 460, 270-274.
    • (1999) FEBS Lett. , vol.460 , pp. 270-274
    • Brodin, P.1    Pinskaya, M.2    Volkov, E.3    Romanova, E.4    Leh, H.5    Auclair, C.6    Mouscadet, J.F.7    Gottikh, M.8
  • 18
    • 0028288222 scopus 로고
    • Triple helix formation with short oligonucleotide-intercalator conjugates matching the HIV-1 U3 LTR end sequence
    • Mouscadet, J. F., Ketterle, C., Goulaouic, H., Carteau, S., Subra, F., Le, B. M., and Auclair, C. (1994) Triple helix formation with short oligonucleotide-intercalator conjugates matching the HIV-1 U3 LTR end sequence, Biochemistry 33, 4187-4196.
    • (1994) Biochemistry , vol.33 , pp. 4187-4196
    • Mouscadet, J.F.1    Ketterle, C.2    Goulaouic, H.3    Carteau, S.4    Subra, F.5    Le, B.M.6    Auclair, C.7
  • 20
    • 0029990185 scopus 로고    scopus 로고
    • Alternate strand DNA triple helix-mediated inhibition of HIV-1 U5 long terminal repeat integration in vitro
    • Bouziane, M., Cherny, D. I., Mouscadet, J. F., and Auclair, C. (1996) Alternate strand DNA triple helix-mediated inhibition of HIV-1 U5 long terminal repeat integration in vitro, J. Biol. Chem. 271, 10359-10364.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10359-10364
    • Bouziane, M.1    Cherny, D.I.2    Mouscadet, J.F.3    Auclair, C.4
  • 22
    • 0030026836 scopus 로고    scopus 로고
    • The metal ion-induced cooperative binding of HIV-1 integrase to DNA exhibits a marked preference for Mn(II) rather than Mg(II)
    • Pemberton, I. K., Buckle, M., and Buc, H. (1996) The metal ion-induced cooperative binding of HIV-1 integrase to DNA exhibits a marked preference for Mn(II) rather than Mg(II), J. Biol. Chem. 271, 1498-1506.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1498-1506
    • Pemberton, I.K.1    Buckle, M.2    Buc, H.3
  • 29
    • 0033813928 scopus 로고    scopus 로고
    • Retroviral integrase inhibitors year 2000: Update and perspectives
    • Pommier, Y., Marchand, C., and Neamati, N. (2000) Retroviral integrase inhibitors year 2000: update and perspectives, Antiviral Res. 47, 139-148.
    • (2000) Antiviral Res. , vol.47 , pp. 139-148
    • Pommier, Y.1    Marchand, C.2    Neamati, N.3
  • 30
    • 0037213907 scopus 로고    scopus 로고
    • Disulfide-linked integrase oligomers involving c280 residues are formed in vitro and in vivo but are not essential for human immunodeficiency virus replication
    • Bischerour, J., Leh, H., Deprez, E., Brochon, J. C., and Mouscadet, J. F. (2003) Disulfide-linked integrase oligomers involving c280 residues are formed in vitro and in vivo but are not essential for human immunodeficiency virus replication, J. Virol. 77, 135-141.
    • (2003) J. Virol. , vol.77 , pp. 135-141
    • Bischerour, J.1    Leh, H.2    Deprez, E.3    Brochon, J.C.4    Mouscadet, J.F.5
  • 31
    • 0032811614 scopus 로고    scopus 로고
    • Inhibition of HIV-1 integration by mono- & bifunctionalized triple helix forming oligonucleotides
    • Brodin, P., Gottikh, M., Auclair, C., and Mouscadet, J. F. (1999) Inhibition of HIV-1 integration by mono- & bifunctionalized triple helix forming oligonucleotides, Nucleosides Nucleotides 18, 1717-1718.
    • (1999) Nucleosides Nucleotides , vol.18 , pp. 1717-1718
    • Brodin, P.1    Gottikh, M.2    Auclair, C.3    Mouscadet, J.F.4
  • 32
    • 0032510707 scopus 로고    scopus 로고
    • Photocross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex
    • Heuer, T. S. and Brown, P. O. (1998) Photocross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex, Biochemistry 37, 6667-6678.
    • (1998) Biochemistry , vol.37 , pp. 6667-6678
    • Heuer, T.S.1    Brown, P.O.2
  • 33
    • 0031015166 scopus 로고    scopus 로고
    • Fluorescence spectroscopy as a tool to investigate protein interactions
    • Brown, M. P. and Royer, C. (1997) Fluorescence spectroscopy as a tool to investigate protein interactions, Curr. Opin. Biotechnol. 8, 45-49.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 45-49
    • Brown, M.P.1    Royer, C.2
  • 34
    • 0029764661 scopus 로고    scopus 로고
    • A fluorescence anisotropy study of DNA binding by HPV-11 E2C protein: A hierarchy of E2-binding sites
    • Alexander, K. A. and Phelps, W. C. (1996) A fluorescence anisotropy study of DNA binding by HPV-11 E2C protein: a hierarchy of E2-binding sites, Biochemistry 35, 9864-9872.
    • (1996) Biochemistry , vol.35 , pp. 9864-9872
    • Alexander, K.A.1    Phelps, W.C.2
  • 36
    • 0035964283 scopus 로고    scopus 로고
    • DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    • Deprez, E., Tauc, P., Leh, H., Mouscadet, J. F., Auclair, C., Hawkins, M. E., and Brochon, J. C. (2001) DNA binding induces dissociation of the multimeric form of HIV-1 integrase: a time-resolved fluorescence anisotropy study, Proc. Natl. Acad. Sci. U.S.A. 98, 10090-10095.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10090-10095
    • Deprez, E.1    Tauc, P.2    Leh, H.3    Mouscadet, J.F.4    Auclair, C.5    Hawkins, M.E.6    Brochon, J.C.7
  • 37
    • 0036631776 scopus 로고    scopus 로고
    • Heparin binds to murine leukemia virus and inhibits Env-independent attachment and infection
    • Walker, S. J., Pizzato, M., Takeuchi, Y., and Devereux, S. (2002) Heparin binds to murine leukemia virus and inhibits Env-independent attachment and infection, J. Virol. 76, 6909-6918.
    • (2002) J. Virol. , vol.76 , pp. 6909-6918
    • Walker, S.J.1    Pizzato, M.2    Takeuchi, Y.3    Devereux, S.4
  • 38
    • 0027222149 scopus 로고
    • Inhibitory effect of the polyanionic drug suramin on the in vitro HIV DNA integration reaction
    • Carteau, S., Mouscadet, J. F., Goulaouic, H., Subra, F., and Auclair, C. (1993) Inhibitory effect of the polyanionic drug suramin on the in vitro HIV DNA integration reaction, Arch. Biochem. Biophys. 305, 606-610.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 606-610
    • Carteau, S.1    Mouscadet, J.F.2    Goulaouic, H.3    Subra, F.4    Auclair, C.5
  • 39
    • 0035343895 scopus 로고    scopus 로고
    • Comparative architecture of transposase and integrase complexes
    • Rice, P. A. and Baker, T. A. (2001) Comparative architecture of transposase and integrase complexes, Nat. Struct. Biol. 8, 302-307.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 302-307
    • Rice, P.A.1    Baker, T.A.2
  • 40
    • 0032562165 scopus 로고    scopus 로고
    • Displacement of viral DNA termini from stable HIV-1 integrase nucleoprotein complexes induced by secondary DNA-binding interactions
    • Pemberton, I. K., Buc, H., and Buckle, M. (1998) Displacement of viral DNA termini from stable HIV-1 integrase nucleoprotein complexes induced by secondary DNA-binding interactions, Biochemistry 37, 2682-2690.
    • (1998) Biochemistry , vol.37 , pp. 2682-2690
    • Pemberton, I.K.1    Buc, H.2    Buckle, M.3
  • 41
    • 1342310966 scopus 로고    scopus 로고
    • Antisense targeting protein kinase A type I as a drug for integrated strategies of cancer therapy
    • Tortora, G. and Ciardiello, F. (2003) Antisense Targeting Protein Kinase A Type I as a Drug for Integrated Strategies of Cancer Therapy, Ann. N. Y. Acad. Sci. 1002, 236-243.
    • (2003) Ann. N. Y. Acad. Sci. , vol.1002 , pp. 236-243
    • Tortora, G.1    Ciardiello, F.2
  • 42
    • 0037733977 scopus 로고    scopus 로고
    • Antisense technologies. Improvement through novel chemical modifications
    • Kurreck, J. (2003) Antisense technologies. Improvement through novel chemical modifications, Eur. J. Biochem. 270, 1628-1644.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1628-1644
    • Kurreck, J.1
  • 43
    • 0037107886 scopus 로고    scopus 로고
    • RNAi: Gene-silencing in therapeutic intervention
    • Shuey, D. J., McCallus, D. E., and Giordano, T. (2002) RNAi: gene-silencing in therapeutic intervention, Drug Discov. Today 7, 1040-1046.
    • (2002) Drug Discov. Today , vol.7 , pp. 1040-1046
    • Shuey, D.J.1    McCallus, D.E.2    Giordano, T.3


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