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Volumn 73, Issue 12, 1999, Pages 10000-10009

Multiple effects of an anti-human immunodeficiency virus nucleocapsid inhibitor on virus morphology and replication

Author keywords

[No Author keywords available]

Indexed keywords

BENZAMIDE DERIVATIVE; NUCLEOCAPSID PROTEIN; VIRUS DNA; ZINC FINGER PROTEIN;

EID: 0344671562     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.12.10000-10009.1999     Document Type: Article
Times cited : (38)

References (51)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi, A., H. E. Gendelman, S. Koenig, T. Folks, R. Willey, A. Rabson, and M. A. Martin. 1986. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 59:284-291.
    • (1986) J. Virol. , vol.59 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 2
    • 0025266663 scopus 로고
    • Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus
    • Aldovini, A., and R. A. Young. 1990. Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus. J. Virol. 64:1920-1926.
    • (1990) J. Virol. , vol.64 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 3
    • 0033548084 scopus 로고    scopus 로고
    • Role of post-transcriptional modifications of primer tRNALys.3 in the fidelity and efficacy of plus strand DNA transfer during HIV-1 reverse transcription
    • Auxilien, S., G. Keith, S. F. J. Le Grice, and J.-L. Darlix. 1999. Role of post-transcriptional modifications of primer tRNALys.3 in the fidelity and efficacy of plus strand DNA transfer during HIV-1 reverse transcription. J. Biol. Chem. 274:4412-4420.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4412-4420
    • Auxilien, S.1    Keith, G.2    Le Grice, S.F.J.3    Darlix, J.-L.4
  • 4
    • 1842300493 scopus 로고    scopus 로고
    • Mutations in the N-terminal domain of human immunodeficiency virus type 1 nucleocapsid protein affect virion core structure and proviral DNA synthesis
    • Berthoux, L., C. Péchoux, M. Ottmann, G. Morel, and J. L. Darlix. 1997. Mutations in the N-terminal domain of human immunodeficiency virus type 1 nucleocapsid protein affect virion core structure and proviral DNA synthesis. J. Virol. 71:6973-6981.
    • (1997) J. Virol. , vol.71 , pp. 6973-6981
    • Berthoux, L.1    Péchoux, C.2    Ottmann, M.3    Morel, G.4    Darlix, J.L.5
  • 5
    • 0023392945 scopus 로고
    • High efficiency transformation of mammalian cells by plasmid DNA
    • Chen, C., and H. Okayama. 1987. High efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7:2745-2752.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 6
    • 0028012053 scopus 로고
    • Fusion from without directed by human immunodeficiency virus particles
    • Clavel, F., and P. Charneau. 1994. Fusion from without directed by human immunodeficiency virus particles. J. Virol. 68:1179-1185.
    • (1994) J. Virol. , vol.68 , pp. 1179-1185
    • Clavel, F.1    Charneau, P.2
  • 7
    • 0028301896 scopus 로고
    • The kinetics of human immunodeficiency virus reverse transcription are slower in primary human macrophages than in lymphoid cell line
    • Collin, M., and S. Gordon. 1994. The kinetics of human immunodeficiency virus reverse transcription are slower in primary human macrophages than in lymphoid cell line. Virology 200:114-120.
    • (1994) Virology , vol.200 , pp. 114-120
    • Collin, M.1    Gordon, S.2
  • 8
    • 0345684821 scopus 로고    scopus 로고
    • Unpublished results
    • Darlix, J.-L. Unpublished results.
    • Darlix, J.-L.1
  • 9
    • 0025598002 scopus 로고
    • Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1
    • Darlix, J.-L., C. Gabus, M. T. Nugeyre, F. Clavel, and F. Barré-Sinoussi. 1990. Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1. J. Mol. Biol. 216:689-699.
    • (1990) J. Mol. Biol. , vol.216 , pp. 689-699
    • Darlix, J.-L.1    Gabus, C.2    Nugeyre, M.T.3    Clavel, F.4    Barré-Sinoussi, F.5
  • 10
    • 0029585377 scopus 로고
    • First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses
    • Darlix, J.-L., M. Lapadat-Tapolsky, H. de Rocquigny, and B. P. Roques. 1995. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses. J. Mol. Biol. 254:523-537.
    • (1995) J. Mol. Biol. , vol.254 , pp. 523-537
    • Darlix, J.-L.1    Lapadat-Tapolsky, M.2    De Rocquigny, H.3    Roques, B.P.4
  • 11
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 PSI-RNA recognition element
    • de Guzman, R., Z. Rong Wu, C. C. Stalling, L. Pappalardo, P. N. Borer, and M. F. Summers. 1998. Structure of the HIV-1 nucleocapsid protein bound to the SL3 PSI-RNA recognition element. Science 279:384-388.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.1    Rong Wu, Z.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 12
    • 0027220120 scopus 로고
    • Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type-1 nucleocapsid protein
    • Dorfman, T., J. Luban, S. P. Goff, W. A. Haseltine, and H. G. Göttlinger. 1993. Mapping of functionally important residues of a cysteine-histidine box in the human immunodeficiency virus type-1 nucleocapsid protein. J. Virol. 67:6159-6169.
    • (1993) J. Virol. , vol.67 , pp. 6159-6169
    • Dorfman, T.1    Luban, J.2    Goff, S.P.3    Haseltine, W.A.4    Göttlinger, H.G.5
  • 13
    • 0032577449 scopus 로고    scopus 로고
    • Viral dynamics in HIV-1 infection
    • Finzi, D., and R. F. Siliciano. 1998. Viral dynamics in HIV-1 infection. Cell 93:665-671.
    • (1998) Cell , vol.93 , pp. 665-671
    • Finzi, D.1    Siliciano, R.F.2
  • 14
    • 0032506207 scopus 로고    scopus 로고
    • HIV-1 Gag proteins: Diverse functions in the virus life cycle
    • Freed, E. O. 1998. HIV-1 Gag proteins: diverse functions in the virus life cycle. Virology 251:1-15.
    • (1998) Virology , vol.251 , pp. 1-15
    • Freed, E.O.1
  • 15
    • 0028338652 scopus 로고
    • Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions
    • Fu, W., R. J. Gorelick, and A. Rein. 1994. Characterization of human immunodeficiency virus type 1 dimeric RNA from wild-type and protease-defective virions. J. Virol. 68:5013-5018.
    • (1994) J. Virol. , vol.68 , pp. 5013-5018
    • Fu, W.1    Gorelick, R.J.2    Rein, A.3
  • 16
    • 0030987672 scopus 로고    scopus 로고
    • HIV-1 infection of non-dividing cells through the recognition of integrase by the importin/karyopherin pathway
    • Gallay, P., T. Hope, T. Chin, and D. Trono. 1997. HIV-1 infection of non-dividing cells through the recognition of integrase by the importin/karyopherin pathway. Proc. Natl. Acad. Sci. USA 94:9825-9830.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9825-9830
    • Gallay, P.1    Hope, T.2    Chin, T.3    Trono, D.4
  • 17
    • 0028839344 scopus 로고
    • HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase
    • Gallay, P., S. Swingler, J. Song, F. Bushman, and D. Trono. 1995. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase. Cell 83:569-576.
    • (1995) Cell , vol.83 , pp. 569-576
    • Gallay, P.1    Swingler, S.2    Song, J.3    Bushman, F.4    Trono, D.5
  • 19
    • 0019507492 scopus 로고
    • Isolation and properties of Moloney murine leukemia virus mutants: Use of rapid assay for release of virion reverse transcriptase
    • Goff, S., P. Traktman, and D. Baltimore. 1981. Isolation and properties of Moloney murine leukemia virus mutants: use of rapid assay for release of virion reverse transcriptase. J. Virol. 38:239-248.
    • (1981) J. Virol. , vol.38 , pp. 239-248
    • Goff, S.1    Traktman, P.2    Baltimore, D.3
  • 20
    • 2642704250 scopus 로고    scopus 로고
    • Human immunodeficiency virus replication and genotypic resistance in blood and lymph nodes after a year of potent antiretroviral therapy
    • Günthard, H. F., J. K. Wong, C. C. Ignacio, J. C. Guatelli, N. L. Riggs, D. V. Havlir, and D. D. Richman. 1998. Human immunodeficiency virus replication and genotypic resistance in blood and lymph nodes after a year of potent antiretroviral therapy. J. Virol. 72:2422-2428.
    • (1998) J. Virol. , vol.72 , pp. 2422-2428
    • Günthard, H.F.1    Wong, J.K.2    Ignacio, C.C.3    Guatelli, J.C.4    Riggs, N.L.5    Havlir, D.V.6    Richman, D.D.7
  • 21
    • 0032560189 scopus 로고
    • Anti-HIV agents that selectively target retroviral nucleocapsid protein zinc fingers without affecting cellular zinc finger proteins
    • Huang, M., A. Maynard, J. A. Turpin, L. Graham, G. M. Janini, D. G. Covell, and W. G. Rice. 1988. Anti-HIV agents that selectively target retroviral nucleocapsid protein zinc fingers without affecting cellular zinc finger proteins. J. Med. Chem. 41:1371-1381.
    • (1988) J. Med. Chem. , vol.41 , pp. 1371-1381
    • Huang, M.1    Maynard, A.2    Turpin, J.A.3    Graham, L.4    Janini, G.M.5    Covell, D.G.6    Rice, W.G.7
  • 22
    • 0028046638 scopus 로고
    • Genetic differences between blood- and brain-derived viral sequences from human immunodeficiency virus type 1-infected patients: Evidence of conserved elements in the V3 region of the envelope protein of brain-derived sequences
    • Korber, B. T., K. J. Kunstman, B. K. Patterson, M. Furtado, M. M. McEvilly, R. Levy, and S. M. Wolinsky. 1994. Genetic differences between blood- and brain-derived viral sequences from human immunodeficiency virus type 1-infected patients: evidence of conserved elements in the V3 region of the envelope protein of brain-derived sequences. J. Virol. 68:7467-7481.
    • (1994) J. Virol. , vol.68 , pp. 7467-7481
    • Korber, B.T.1    Kunstman, K.J.2    Patterson, B.K.3    Furtado, M.4    McEvilly, M.M.5    Levy, R.6    Wolinsky, S.M.7
  • 24
    • 0029559244 scopus 로고
    • Viral resistance and the selection of antiretroviral recombination
    • Larder, B. A. 1995. Viral resistance and the selection of antiretroviral recombination. J. AIDS Hum. Retroviruses 10:S28-S33.
    • (1995) J. AIDS Hum. Retroviruses , vol.10
    • Larder, B.A.1
  • 25
    • 0032509267 scopus 로고    scopus 로고
    • Involvement of HIV-1 nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro
    • Lener, D., V. Tanchou, B. P. Roques, S. F. J. Le Grice, and J.-L. Darlix. 1998. Involvement of HIV-1 nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro. J. Biol. Chem. 273:33781-33786.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33781-33786
    • Lener, D.1    Tanchou, V.2    Roques, B.P.3    Le Grice, S.F.J.4    Darlix, J.-L.5
  • 27
    • 0024507854 scopus 로고
    • Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein
    • Meric, C., and S. P. Goff. 1989. Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein. J. Virol. 63:1558-1568.
    • (1989) J. Virol. , vol.63 , pp. 1558-1568
    • Meric, C.1    Goff, S.P.2
  • 30
    • 0028858759 scopus 로고
    • The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivity
    • Ottmann, M., C. Gabus, and J. L. Darlix. 1995. The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivity. J. Virol. 69:1778-84.
    • (1995) J. Virol. , vol.69 , pp. 1778-1784
    • Ottmann, M.1    Gabus, C.2    Darlix, J.L.3
  • 31
    • 0025005828 scopus 로고
    • Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity
    • Page, K. A., N. R. Landau, and D. R. Littman. 1990. Construction and use of a human immunodeficiency virus vector for analysis of virus infectivity. J. Virol. 64:5270-5276.
    • (1990) J. Virol. , vol.64 , pp. 5270-5276
    • Page, K.A.1    Landau, N.R.2    Littman, D.R.3
  • 33
    • 8044226891 scopus 로고
    • In situ hybridization in semithin sections
    • G. Morel (ed.). CRC Press, Inc., Boca Raton, Fla.
    • Péchoux, C., and G. Morel. 1993. In situ hybridization in semithin sections, p. 101-138. In G. Morel (ed.), Hybridization techniques for electron microscopy. CRC Press, Inc., Boca Raton, Fla.
    • (1993) Hybridization Techniques for Electron Microscopy , pp. 101-138
    • Péchoux, C.1    Morel, G.2
  • 34
    • 0027971621 scopus 로고
    • The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions
    • Pettit, S. C., M. D. Moody, R. S. Wehbie, A. H. Kaplan, P. V. Nantermet, C. A. Klein, and R. Swanstrom. 1994. The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions. J. Virol. 68:8017-8027.
    • (1994) J. Virol. , vol.68 , pp. 8017-8027
    • Pettit, S.C.1    Moody, M.D.2    Wehbie, R.S.3    Kaplan, A.H.4    Nantermet, P.V.5    Klein, C.A.6    Swanstrom, R.7
  • 35
    • 0029817879 scopus 로고    scopus 로고
    • Charged amino acid residues of human immunodeficiency virus type 1 nucleocapsid p7 protein involved in RNA packaging and infectivity
    • Poon, D. T. K., J. Wu, and A. Aldovini. 1996. Charged amino acid residues of human immunodeficiency virus type 1 nucleocapsid p7 protein involved in RNA packaging and infectivity. J. Virol. 70:6607-6616.
    • (1996) J. Virol. , vol.70 , pp. 6607-6616
    • Poon, D.T.K.1    Wu, J.2    Aldovini, A.3
  • 36
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: Significance for viral replication
    • Rein, A., L. E. Henderson, and J. G. Levin. 1998. Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem. Sci. 23:297-301.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 42
    • 0021719086 scopus 로고
    • Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines
    • Smith, S. D., M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader. 1984. Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines. Cancer Res. 44:5657-5660.
    • (1984) Cancer Res. , vol.44 , pp. 5657-5660
    • Smith, S.D.1    Shatsky, M.2    Cohen, P.S.3    Warnke, R.4    Link, M.P.5    Glader, B.E.6
  • 43
    • 0025917010 scopus 로고
    • C-terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain
    • South, T. L., P. R. Blake, D. R. Hare, and M. F. Summers. 1991. C-terminal retroviral-type zinc finger domain from the HIV-1 nucleocapsid protein is structurally similar to the N-terminal zinc finger domain. Biochemistry 30: 6342-6349.
    • (1991) Biochemistry , vol.30 , pp. 6342-6349
    • South, T.L.1    Blake, P.R.2    Hare, D.R.3    Summers, M.F.4
  • 44
    • 0031956156 scopus 로고    scopus 로고
    • Role of the N-terminal zinc finger of human immunodeficiency virus type 1 nucleocapsid protein in virus structure and replication
    • Tanchou, V., D. Décimo, C. Péchoux, D. Lener, V. Rogemond, L. Berthoux, M. Ottmann, and J.-L. Darlix. 1998. Role of the N-terminal zinc finger of human immunodeficiency virus type 1 nucleocapsid protein in virus structure and replication. J. Virol. 72:4442-4447.
    • (1998) J. Virol. , vol.72 , pp. 4442-4447
    • Tanchou, V.1    Décimo, D.2    Péchoux, C.3    Lener, D.4    Rogemond, V.5    Berthoux, L.6    Ottmann, M.7    Darlix, J.-L.8
  • 45
    • 0030019808 scopus 로고    scopus 로고
    • The in vitro ejection of zinc from human immunodeficiency virus type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity
    • Tummino, P. J., J. D. Scholten, P. J. Harvey, T. P. Holler, L. Maloney, R. Gogliotti, J. Domagala, and D. Hupe. 1996. The in vitro ejection of zinc from human immunodeficiency virus type 1 nucleocapsid protein by disulfide benzamides with cellular anti-HIV activity. Proc. Natl. Acad. Sci. USA 93: 969-973.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 969-973
    • Tummino, P.J.1    Scholten, J.D.2    Harvey, P.J.3    Holler, T.P.4    Maloney, L.5    Gogliotti, R.6    Domagala, J.7    Hupe, D.8
  • 46
    • 0033552881 scopus 로고    scopus 로고
    • Synthesis and biological properties of novel pyridinioalkanoyl thiolesters (PATE) as anti-HIV-1 agents that target the viral nucleocapsid protein zinc fingers
    • Turpin, J. A., Y. Song, J. K. Inman, M. Huang, A. Wallqvist, A. Maynard, D. G. Covell, W. G. Rice, and E. Appella. 1999. Synthesis and biological properties of novel pyridinioalkanoyl thiolesters (PATE) as anti-HIV-1 agents that target the viral nucleocapsid protein zinc fingers. J. Med. Chem. 42:67-86.
    • (1999) J. Med. Chem. , vol.42 , pp. 67-86
    • Turpin, J.A.1    Song, Y.2    Inman, J.K.3    Huang, M.4    Wallqvist, A.5    Maynard, A.6    Covell, D.G.7    Rice, W.G.8    Appella, E.9
  • 47
    • 0029791790 scopus 로고    scopus 로고
    • Inhibitors of human immunodeficiency virus type 1 zinc fingers prevent normal processing of Gag precursors and result in the release of noninfectious viral particles
    • Turpin, J. A., S. J. Terpening, C. A. Schaeffer, G. Yu, C. J. Glover, R. L. Felsted, E. A. Sausville, and W. G. Rice. 1996. Inhibitors of human immunodeficiency virus type 1 zinc fingers prevent normal processing of Gag precursors and result in the release of noninfectious viral particles. J. Virol. 70:6180-6189.
    • (1996) J. Virol. , vol.70 , pp. 6180-6189
    • Turpin, J.A.1    Terpening, S.J.2    Schaeffer, C.A.3    Yu, G.4    Glover, C.J.5    Felsted, R.L.6    Sausville, E.A.7    Rice, W.G.8
  • 49
    • 0024578841 scopus 로고
    • New soluble-formazan assay for HIV-1 cytopathic effects: Application to high-flux screening of synthetic and natural products for AIDS-antiviral activity
    • Weislow, O. S., R. Kiser, D. L. Fine, J. Bader, R. H. Shoemaker, and M. R. Boyd. 1989. New soluble-formazan assay for HIV-1 cytopathic effects: application to high-flux screening of synthetic and natural products for AIDS-antiviral activity. J. Natl. Cancer Inst. 81:577-586.
    • (1989) J. Natl. Cancer Inst. , vol.81 , pp. 577-586
    • Weislow, O.S.1    Kiser, R.2    Fine, D.L.3    Bader, J.4    Shoemaker, R.H.5    Boyd, M.R.6
  • 50
    • 0030795040 scopus 로고    scopus 로고
    • Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation
    • Zhang, Y., and E. Barklis. 1997. Effects of nucleocapsid mutations on human immunodeficiency virus assembly and RNA encapsidation. J. Virol. 71:6765-6776.
    • (1997) J. Virol. , vol.71 , pp. 6765-6776
    • Zhang, Y.1    Barklis, E.2
  • 51
    • 0030769354 scopus 로고    scopus 로고
    • Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites
    • Zhang, Y.-M., H. Imamichi, T. Imamichi, H. Clifford Lane, J. Falloon, M. B. Vasudevachari, and N. P. Salzman. 1997. Drug resistance during indinavir therapy is caused by mutations in the protease gene and in its Gag substrate cleavage sites. J. Virol. 71:6662-6670.
    • (1997) J. Virol. , vol.71 , pp. 6662-6670
    • Zhang, Y.-M.1    Imamichi, H.2    Imamichi, T.3    Lane, H.C.4    Falloon, J.5    Vasudevachari, M.B.6    Salzman, N.P.7


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