메뉴 건너뛰기




Volumn 49, Issue 4, 1996, Pages 621-628

Effects of nucleotide analogues on human immunodeficiency virus type 1 integrase

Author keywords

[No Author keywords available]

Indexed keywords

2',3' DIDEOXY 2' FLUOROADENOSINE; 2',3' DIDEOXY 2' FLUOROADENOSINE TRIPHOSPHATE; 2',3' DIDEOXYNUCLEOSIDE TRIPHOSPHATE; COUMAMYCIN; INTEGRASE; LAMIVUDINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; STAVUDINE; UNCLASSIFIED DRUG; ZIDOVUDINE; ZIDOVUDINE DERIVATIVE;

EID: 0029871472     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (68)

References (41)
  • 2
    • 0028915128 scopus 로고
    • Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication
    • Engelman, A., G. Englund, J. M. Orenstein, M A. Martin, and R Craigie. Multiple effects of mutations in human immunodeficiency virus type 1 integrase on viral replication. J. Virol. 69:2729-2736 (1995).
    • (1995) J. Virol. , vol.69 , pp. 2729-2736
    • Engelman, A.1    Englund, G.2    Orenstein, J.M.3    Martin, M.A.4    Craigie, R.5
  • 3
    • 0028914179 scopus 로고
    • Integration is required for productive infection of monocyte-derived macrophages by human immunodeficiency virus type-1
    • Englund, G., T. S. Theodore, E. O. Freed, A. Engelman, and M. A. Martin. Integration is required for productive infection of monocyte-derived macrophages by human immunodeficiency virus type-1. J. Virol. 69:3216-3219 (1995).
    • (1995) J. Virol. , vol.69 , pp. 3216-3219
    • Englund, G.1    Theodore, T.S.2    Freed, E.O.3    Engelman, A.4    Martin, M.A.5
  • 4
    • 0029062402 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by a hydrophobic cation: The phenanthroline-cuprous complex
    • Mazumder, A., M. Gupta, D. M. Perrin, D. S. Sigman, M. Rabinovitz, and Y. Pommier. Inhibition of human immunodeficiency virus type 1 integrase by a hydrophobic cation: the phenanthroline-cuprous complex. AIDS Res. Hum. Retroviruses 11:115-125 (1995).
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 115-125
    • Mazumder, A.1    Gupta, M.2    Perrin, D.M.3    Sigman, D.S.4    Rabinovitz, M.5    Pommier, Y.6
  • 6
    • 0001587762 scopus 로고
    • Inhibition of the in vitro infectivity and cytopathic effect of human T-lytnphotrophic virus type III/lymphadenopathy-associated virus (HTLV-III/LAV) by 2′,3′-dideoxynucleosides
    • Mitsuya, H., and S. Broder. Inhibition of the in vitro infectivity and cytopathic effect of human T-lytnphotrophic virus type III/lymphadenopathy-associated virus (HTLV-III/LAV) by 2′,3′-dideoxynucleosides. Proc. Natl Acad. Sci. USA 83:1911-1915 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 1911-1915
    • Mitsuya, H.1    Broder, S.2
  • 9
    • 0027981440 scopus 로고
    • Pure nucleoside enantiomers of β-2′,3′-dideoxycytidine analogues are selective inhibitors of hepatitis B virus and human immunodeficiency virus in vitro
    • Schmazi, R. F., G. Gosselin, A. Faraj, B. E. Korba, D. C. Liotta, C. K. Chu, C. Mathe, J.-L. Imbach, and J.-P. Sommadossi. Pure nucleoside enantiomers of β-2′,3′-dideoxycytidine analogues are selective inhibitors of hepatitis B virus and human immunodeficiency virus in vitro. Antimicrob. Agents Chemother. 38:2172-2174 (1994).
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2172-2174
    • Schmazi, R.F.1    Gosselin, G.2    Faraj, A.3    Korba, B.E.4    Liotta, D.C.5    Chu, C.K.6    Mathe, C.7    Imbach, J.-L.8    Sommadossi, J.-P.9
  • 10
    • 0028300765 scopus 로고
    • Divergent antihuman immunodeficiency virus activity and anabolic phosphorylation of 2′:3′-dideoxynucleoside analogs in resting and activated human cells
    • Gao, W.-Y., R. Agbaria, J. S. Driscoll, and H. Mitsuya. Divergent antihuman immunodeficiency virus activity and anabolic phosphorylation of 2′:3′-dideoxynucleoside analogs in resting and activated human cells. J. Biol Chem. 269:12633-12638 (1994).
    • (1994) J. Biol Chem. , vol.269 , pp. 12633-12638
    • Gao, W.-Y.1    Agbaria, R.2    Driscoll, J.S.3    Mitsuya, H.4
  • 12
    • 0027407484 scopus 로고
    • Nucleoside analogs: Similarities and differences
    • Sommadossi, J. P. Nucleoside analogs: similarities and differences. Clin. Infect. Dis. 16:S7-S15 (1993).
    • (1993) Clin. Infect. Dis. , vol.16
    • Sommadossi, J.P.1
  • 13
    • 0029011730 scopus 로고
    • Toward improved anti-HIV chemotherapy: Therapeutic strategies for intervention with HIV infections
    • De Clercq, E. Toward improved anti-HIV chemotherapy: therapeutic strategies for intervention with HIV infections. J. Med. Chem. 38:2491-2517 (1995).
    • (1995) J. Med. Chem. , vol.38 , pp. 2491-2517
    • De Clercq, E.1
  • 14
    • 0029028067 scopus 로고
    • Potential mechanism for sustained antiretroviral efficacy of AZT-3TC combination therapy
    • Larder, B. A., S. D. Kemp, and P. R. Harrigan. Potential mechanism for sustained antiretroviral efficacy of AZT-3TC combination therapy. Science (Washington D. C.) 269:696-699 (1995).
    • (1995) Science (Washington D. C.) , vol.269 , pp. 696-699
    • Larder, B.A.1    Kemp, S.D.2    Harrigan, P.R.3
  • 15
    • 0001369814 scopus 로고
    • Combined chemotherapeutic modalities for viral infections: Rationale and clinical potential
    • (T. C. Chou and D. C. Rideout, eds.). Academic Press, Orlando, FL
    • Schinazi, R. F. Combined chemotherapeutic modalities for viral infections: rationale and clinical potential, in Synergism and Antagonism in Chemotherapy (T. C. Chou and D. C. Rideout, eds.). Academic Press, Orlando, FL, 109-181 (1991).
    • (1991) Synergism and Antagonism in Chemotherapy , pp. 109-181
    • Schinazi, R.F.1
  • 16
    • 0027991415 scopus 로고
    • Combination therapy: More effective control of HIV type 1?
    • Johnson, V. A. Combination therapy: more effective control of HIV type 1? AIDS Res. Hum. Retrouiruses 10:907-912 (1994).
    • (1994) AIDS Res. Hum. Retrouiruses , vol.10 , pp. 907-912
    • Johnson, V.A.1
  • 17
    • 0028242724 scopus 로고
    • Inhibition of human immunodeficiency virus type 1 integrase by 3′-azido-3′-deoxythymidylate
    • Mazumder, A., D. Cooney, R. Agbaria, M. Gupta, and Y. Pommier. Inhibition of human immunodeficiency virus type 1 integrase by 3′-azido-3′-deoxythymidylate. Proc. Natl Acad. Sci. USA 91:5771-5775 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5771-5775
    • Mazumder, A.1    Cooney, D.2    Agbaria, R.3    Gupta, M.4    Pommier, Y.5
  • 19
    • 0024354118 scopus 로고
    • Comparison of the effect of carbovir, AZT, and dideoxynucleoside triphosphates on the activity of HIV reverse transcriptase and selected human polymerases
    • White, E. L., W. B. Parker, L. J. Macy, S. C. Shaddix, G. McCaleb, J. A. Secrist, R. Vince, and W. M. Shannon. Comparison of the effect of carbovir, AZT, and dideoxynucleoside triphosphates on the activity of HIV reverse transcriptase and selected human polymerases. Biochem. Biophys. Res. Commun. 161:393-398 (1989).
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 393-398
    • White, E.L.1    Parker, W.B.2    Macy, L.J.3    Shaddix, S.C.4    McCaleb, G.5    Secrist, J.A.6    Vince, R.7    Shannon, W.M.8
  • 20
    • 0025178618 scopus 로고
    • Inhibition of hepatitis B virus DNA polymerase by 3′-fluorothymidine triphosphate and other modified nucleoside triphosphate analogs
    • Meisel, H., K Reimer, M. von Janta-Lipinski, D. Barwolff, and E. Matthes. Inhibition of hepatitis B virus DNA polymerase by 3′-fluorothymidine triphosphate and other modified nucleoside triphosphate analogs. J. Med. Virol. 30:137-141 (1990).
    • (1990) J. Med. Virol. , vol.30 , pp. 137-141
    • Meisel, H.1    Reimer, K.2    Von Janta-Lipinski, M.3    Barwolff, D.4    Matthes, E.5
  • 21
    • 0026071379 scopus 로고
    • Catabolism of 3′-azido-3′-deoxythymidine in hepatocytes and liver microsomes, with evidence of formation of 3′-amino-3′-deoxythymidine, a highly toxic catabolite for human bone marrow cells
    • Cretton, E. M., M. Y. Xie, R. J. Bevan, N. M. Goudgaon, R. F. Schinazi, and J. P. Sommadossi. Catabolism of 3′-azido-3′-deoxythymidine in hepatocytes and liver microsomes, with evidence of formation of 3′-amino-3′-deoxythymidine, a highly toxic catabolite for human bone marrow cells. Mol. Pharmacol. 39:258-266 (1991)
    • (1991) Mol. Pharmacol. , vol.39 , pp. 258-266
    • Cretton, E.M.1    Xie, M.Y.2    Bevan, R.J.3    Goudgaon, N.M.4    Schinazi, R.F.5    Sommadossi, J.P.6
  • 23
    • 0026703580 scopus 로고
    • Novel nucleoside strategies for anti-HIV and anti-HSV therapy
    • Herdewijn, P. A. M. M. Novel nucleoside strategies for anti-HIV and anti-HSV therapy. Antiviral Res. 19:1-14 (1992)
    • (1992) Antiviral Res. , vol.19 , pp. 1-14
    • Herdewijn, P.A.M.M.1
  • 24
    • 0026697262 scopus 로고
    • Deoxycytidine deaminase-resistant stereoisomer is the active form of (-)-2′,3′-dideoxy-3′-thiacytidine in the inhibition of hepatitis B virus replication
    • Chang, C.-N., S.-L. Doong, J. H. Zhou, J. W. Beach, L. S. Jeong, C. K. Chu, C.-H. Tsai, R. F. Schinazi, D. C. Liotta, and Y.-C. Cheng. Deoxycytidine deaminase-resistant stereoisomer is the active form of (-)-2′,3′-dideoxy-3′-thiacytidine in the inhibition of hepatitis B virus replication. J. Biol. Chem. 267:13938-13942 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13938-13942
    • Chang, C.-N.1    Doong, S.-L.2    Zhou, J.H.3    Beach, J.W.4    Jeong, L.S.5    Chu, C.K.6    Tsai, C.-H.7    Schinazi, R.F.8    Liotta, D.C.9    Cheng, Y.-C.10
  • 27
    • 0027976787 scopus 로고
    • Restriction and enhancement of human immunodeficiency virus type 1 replication by modulation of intracellular deoxynucleoside triphosphate pools
    • Meyerhans, A, J.-P. Vartanian, C. Hultgren, U. Plikat, A. Karlsson, L. Wang, S. Eriksson, and S. Wain-Hobson. Restriction and enhancement of human immunodeficiency virus type 1 replication by modulation of intracellular deoxynucleoside triphosphate pools. J. Virol. 68:535-540 (1994).
    • (1994) J. Virol. , vol.68 , pp. 535-540
    • Meyerhans, A.1    Vartanian, J.-P.2    Hultgren, C.3    Plikat, U.4    Karlsson, A.5    Wang, L.6    Eriksson, S.7    Wain-Hobson, S.8
  • 28
  • 29
    • 0021235437 scopus 로고
    • The purification and characterization of DNA topoisomerases I and II of the yeast Saccharomyces cerevisiae
    • Goto, T., P. Laipis, and J. C. Wang. The purification and characterization of DNA topoisomerases I and II of the yeast Saccharomyces cerevisiae. J. Biol. Chem. 259:10422-10429 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 10422-10429
    • Goto, T.1    Laipis, P.2    Wang, J.C.3
  • 31
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
    • Engelman, A., K. Mizuuchi, and R. Craigie. HIV-1 DNA integration: mechanism of viral DNA cleavage and DNA strand transfer. Cell 67:1211-1221 (1991).
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigie, R.3
  • 32
    • 0026348879 scopus 로고
    • Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein
    • Vink, C., E. Yeheskiely, G. A. van der Marel, J. H. van Boom, and R. H. Plasterk. Site-specific hydrolysis and alcoholysis of human immunodeficiency virus DNA termini mediated by the viral integrase protein. Nucleic Acids Res. 19:6691-6698 (1991).
    • (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
  • 33
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow, S. A., K. A. Vincent, V. Ellison, and P. O. Brown. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science (Washington D. C.) 255:723-726 (1992).
    • (1992) Science (Washington D. C.) , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 34
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman, F. D., A. Engelman, I. Palmer, P. Wingfield, and R. Craigie. Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. Sci. USA 90:3428-3432 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 35
    • 0027173351 scopus 로고
    • Selective action of 4′-azidothymidine triphosphate on reverse transcriptase of human immunodeficiency virus type one and human DNA polymerases alpha and beta
    • Chen, M. S., R. T. Suttman, E. Papp, P. D. Cannon, M. J. McRoberts, C. Bach, W. C. Copeland, and T. S.-F. Wang. Selective action of 4′-azidothymidine triphosphate on reverse transcriptase of human immunodeficiency virus type one and human DNA polymerases alpha and beta. Biochemistry 32:6002-6010 (1993).
    • (1993) Biochemistry , vol.32 , pp. 6002-6010
    • Chen, M.S.1    Suttman, R.T.2    Papp, E.3    Cannon, P.D.4    McRoberts, M.J.5    Bach, C.6    Copeland, W.C.7    Wang, T.S.-F.8
  • 36
    • 0025344520 scopus 로고
    • Cellular pharmacology of 2′:3′-didehydro-2′,3′-dideoxythymidine (D4T) in human peripheral blood mononuclear cells
    • Zhu, Z., H. T. Ho, M. J. Hitchcock, and J. P. Sommadossi. Cellular pharmacology of 2′:3′-didehydro-2′,3′-dideoxythymidine (D4T) in human peripheral blood mononuclear cells. Biochem. Pharmacol. 39:R15-R19 (1990).
    • (1990) Biochem. Pharmacol. , vol.39
    • Zhu, Z.1    Ho, H.T.2    Hitchcock, M.J.3    Sommadossi, J.P.4
  • 37
    • 0025143742 scopus 로고
    • 2′,3′-Dideoxycytidine toxicity in cultured human CEM T lymphoblasts: Effects of combination with 3′-azido-3′-deoxythymidine and thymidine
    • Tornevik, Y., and S. Eriksson. 2′,3′-Dideoxycytidine toxicity in cultured human CEM T lymphoblasts: effects of combination with 3′-azido-3′-deoxythymidine and thymidine. Mol. Pharmacol. 38:237-243 (1990).
    • (1990) Mol. Pharmacol. , vol.38 , pp. 237-243
    • Tornevik, Y.1    Eriksson, S.2
  • 38
    • 0025812772 scopus 로고
    • Inhibition of the RNase H activity of HIV reverse transcriptase by azidothymidylate
    • Tan, C.-K., R. Civil, A. M. Mian, A. G. So, and K. M. Downey. Inhibition of the RNase H activity of HIV reverse transcriptase by azidothymidylate. Biochemistry 30:4831-4835 (1991).
    • (1991) Biochemistry , vol.30 , pp. 4831-4835
    • Tan, C.-K.1    Civil, R.2    Mian, A.M.3    So, A.G.4    Downey, K.M.5
  • 39
    • 0027455742 scopus 로고
    • Effects of 3′-azido-3′-deoxythymidine metabolites on simian virus 40 origin-dependent replication and heteroduplex repair in HeLa cell extracts
    • Bebenek, K., D. C. Thomas, J. D. Roberts, F. Eckstein, and T. A. Kunkel. Effects of 3′-azido-3′-deoxythymidine metabolites on simian virus 40 origin-dependent replication and heteroduplex repair in HeLa cell extracts. Mol. Pharmacol. 43:57-63 (1993).
    • (1993) Mol. Pharmacol. , vol.43 , pp. 57-63
    • Bebenek, K.1    Thomas, D.C.2    Roberts, J.D.3    Eckstein, F.4    Kunkel, T.A.5
  • 40
    • 0027477242 scopus 로고
    • 3′-Azido-3′-deoxythymidine (AZT) monophosphate: An inhibitor of exonudeolytic repair of AZT-terminated DNA
    • Harrington, J. A., J. E. Reardon, and T. Spector. 3′-Azido-3′-deoxythymidine (AZT) monophosphate: an inhibitor of exonudeolytic repair of AZT-terminated DNA. Antimicrob. Agents Chemother. 37:918-920 (1993).
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 918-920
    • Harrington, J.A.1    Reardon, J.E.2    Spector, T.3
  • 41
    • 0027157404 scopus 로고
    • Inhibition of mammalian DNA polymerase-associated 3′ to 5′ exonuclease activity by 5′-monophosphates of 3′-azido-3′-deoxythymidine and 3′-amino-3′-deoxythymidine
    • Bridges, E. G., A. Faraj, and J. P. Sommadossi. Inhibition of mammalian DNA polymerase-associated 3′ to 5′ exonuclease activity by 5′-monophosphates of 3′-azido-3′-deoxythymidine and 3′-amino-3′-deoxythymidine. Biochem. Pharmacol. 45:1571-1576 (1993).
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 1571-1576
    • Bridges, E.G.1    Faraj, A.2    Sommadossi, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.