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Volumn 78, Issue 21, 2004, Pages 11841-11852

Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; GAG PROTEIN; GENOMIC RNA; VIRUS PROTEIN; VIRUS RNA;

EID: 6344294123     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.21.11841-11852.2004     Document Type: Article
Times cited : (180)

References (96)
  • 1
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • Accola, M. A., B. Strack, and H. G. Gottlinger. 2000. Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J. Virol. 74:5395-5402.
    • (2000) J. Virol. , vol.74 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 2
    • 0028057881 scopus 로고
    • Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome
    • Allain, B., M. Lapadat-Tapolsky, C. Berlioz, and J. L. Darlix. 1994. Transactivation of the minus-strand DNA transfer by nucleocapsid protein during reverse transcription of the retroviral genome. EMBO J. 13:973-981.
    • (1994) EMBO J. , vol.13 , pp. 973-981
    • Allain, B.1    Lapadat-Tapolsky, M.2    Berlioz, C.3    Darlix, J.L.4
  • 3
    • 0029004350 scopus 로고
    • apobec-1, the catalytic subunit of the mammalian apolipoprotein B mRNA editing enzyme, is a novel RNA-binding protein
    • Anant, S., A. J. MacGinnitie, and N. O. Davidson. 1995. apobec-1, the catalytic subunit of the mammalian apolipoprotein B mRNA editing enzyme, is a novel RNA-binding protein. J. Biol. Chem. 270:14762-14767.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14762-14767
    • Anant, S.1    MacGinnitie, A.J.2    Davidson, N.O.3
  • 4
    • 1642367210 scopus 로고    scopus 로고
    • A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor
    • Bogerd, H. P., B. P. Doehle, H. L. Wiegand, and B. R. Cullen. 2004. A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor. Proc. Natl. Acad. Sci. USA 101:3770-3774.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3770-3774
    • Bogerd, H.P.1    Doehle, B.P.2    Wiegand, H.L.3    Cullen, B.R.4
  • 5
    • 0036202384 scopus 로고    scopus 로고
    • Structural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: Comparison with the heat-annealed complex
    • Brule, F., R. Marquet, L. Rong, M. A. Wainberg, B. P. Roques, S. F. Le Grice, B. Ehresmann, and C. Ehresmann. 2002. Structural and functional properties of the HIV-1 RNA-tRNA(Lys)3 primer complex annealed by the nucleocapsid protein: comparison with the heat-annealed complex. RNA 8: 8-15.
    • (2002) RNA , vol.8 , pp. 8-15
    • Brule, F.1    Marquet, R.2    Rong, L.3    Wainberg, M.A.4    Roques, B.P.5    Le Grice, S.F.6    Ehresmann, B.7    Ehresmann, C.8
  • 6
    • 0030899871 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 coreceptors participate in postentry stages in the virus replication cycle and function in simian immunodeficiency virus infection
    • Chackerian, B., E. M. Long, P. A. Luciw, and J. Overbaugh. 1997. Human immunodeficiency virus type 1 coreceptors participate in postentry stages in the virus replication cycle and function in simian immunodeficiency virus infection. J. Virol. 71:3932-3939.
    • (1997) J. Virol. , vol.71 , pp. 3932-3939
    • Chackerian, B.1    Long, E.M.2    Luciw, P.A.3    Overbaugh, J.4
  • 7
    • 0026672676 scopus 로고
    • Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: Definition of critical amino acids involved in cell tropism
    • Chesebro, B., K. Wehrly, J. Nishio, and S. Perryman. 1992. Macrophage-tropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 8
    • 0034011267 scopus 로고    scopus 로고
    • Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA
    • Cimarelli, A., S. Sandin, S. Hoglund, and J. Luban. 2000. Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA. J. Virol. 74:3046-3057.
    • (2000) J. Virol. , vol.74 , pp. 3046-3057
    • Cimarelli, A.1    Sandin, S.2    Hoglund, S.3    Luban, J.4
  • 9
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello, S. G., R. S. Harris, and M. S. Neuberger. 2003. The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr. Biol. 13:2009-2013.
    • (2003) Curr. Biol. , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 10
    • 0037066788 scopus 로고    scopus 로고
    • Two proteins essential for apolipoprotein B mRNA editing are expressed from a single gene through alternative splicing
    • Dance, G. S., M. P. Sowden, L. Cartegni, E. Cooper, A. R. Krainer, and H. C. Smith. 2002. Two proteins essential for apolipoprotein B mRNA editing are expressed from a single gene through alternative splicing. J. Biol. Chem. 277: 12703-12709.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12703-12709
    • Dance, G.S.1    Sowden, M.P.2    Cartegni, L.3    Cooper, E.4    Krainer, A.R.5    Smith, H.C.6
  • 11
    • 0346373724 scopus 로고    scopus 로고
    • A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions
    • Derdowski, A., L. Ding, and P. Spearman. 2004. A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions. J. Virol. 78:1230-1242.
    • (2004) J. Virol. , vol.78 , pp. 1230-1242
    • Derdowski, A.1    Ding, L.2    Spearman, P.3
  • 12
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies, R. J. 1999. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev Biol. 15:435-467.
    • (1999) Annu. Rev. Cell Dev Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 14
    • 0028836727 scopus 로고
    • Hum. immunodeficiency virus nucleocapsid protein stimulates strand transfer from internal regions of heteropolymeric RNA templates
    • DeStefano, J. J. 1995. Hum. immunodeficiency virus nucleocapsid protein stimulates strand transfer from internal regions of heteropolymeric RNA templates. Arch Virol. 140:1775-1789.
    • (1995) Arch Virol. , vol.140 , pp. 1775-1789
    • Destefano, J.J.1
  • 15
    • 0033798414 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription
    • Dettenhofer, M., S. Cen, B. A. Carlson, L. Kleiman, and X. F. Yu. 2000. Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription. J. Virol. 74:8938-8945.
    • (2000) J. Virol. , vol.74 , pp. 8938-8945
    • Dettenhofer, M.1    Cen, S.2    Carlson, B.A.3    Kleiman, L.4    Yu, X.F.5
  • 16
    • 0032935035 scopus 로고    scopus 로고
    • Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions
    • Dettenhofer, M., and X. F. Yu. 1999. Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions. J. Virol. 73: 1460-1467.
    • (1999) J. Virol. , vol.73 , pp. 1460-1467
    • Dettenhofer, M.1    Yu, X.F.2
  • 17
    • 0027411503 scopus 로고
    • Retroviral nucleocapsid proteins possess potent nucleic acid strand renaturation activity
    • Dib-Hajj, F., R. Khan, and D. P. Giedroc. 1993. Retroviral nucleocapsid proteins possess potent nucleic acid strand renaturation activity. Protein Sci. 2:231-243.
    • (1993) Protein Sci. , vol.2 , pp. 231-243
    • Dib-Hajj, F.1    Khan, R.2    Giedroc, D.P.3
  • 18
    • 0034089206 scopus 로고    scopus 로고
    • Partial rescue of the Vif-negative phenotype of mutant human immunodeficiency virus type 1 strains from nonpermissive cells by intravirion reverse transcription
    • Dornadula, G., S. Yang, R. J. Pomerantz, and H. Zhang. 2000. Partial rescue of the Vif-negative phenotype of mutant human immunodeficiency virus type 1 strains from nonpermissive cells by intravirion reverse transcription. J. Virol. 74:2594-2602.
    • (2000) J. Virol. , vol.74 , pp. 2594-2602
    • Dornadula, G.1    Yang, S.2    Pomerantz, R.J.3    Zhang, H.4
  • 20
    • 0032928073 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Gag polyprotein has nucleic acid chaperone activity: Possible role in dimerization of genomic RNA and placement of tRNA on the primer binding site
    • Feng, Y. X., S. Campbell, D. Harvin, B. Ehresmann, C. Ehresmann, and A. Rein. 1999. The human immunodeficiency virus type 1 Gag polyprotein has nucleic acid chaperone activity: possible role in dimerization of genomic RNA and placement of tRNA on the primer binding site. J. Virol. 73: 4251-4256.
    • (1999) J. Virol. , vol.73 , pp. 4251-4256
    • Feng, Y.X.1    Campbell, S.2    Harvin, D.3    Ehresmann, B.4    Ehresmann, C.5    Rein, A.6
  • 23
    • 0028293115 scopus 로고
    • Construction and in vitro properties of SIVmac mutants with deletions in "nonessential" genes
    • Gibbs, J. S., D. A. Regier, and R. C. Desrosiers. 1994. Construction and in vitro properties of SIVmac mutants with deletions in "nonessential" genes. AIDS Res. Hum. Retroviruses 10:607-616.
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 607-616
    • Gibbs, J.S.1    Regier, D.A.2    Desrosiers, R.C.3
  • 24
    • 0029861076 scopus 로고    scopus 로고
    • Role of Vif in human immunodeficiency virus type 1 reverse transcription
    • Goncalves, J., Y. Korin, J. Zack, and D. Gabuzda. 1996. Role of Vif in human immunodeficiency virus type 1 reverse transcription. J. Virol. 70: 8701-8709.
    • (1996) J. Virol. , vol.70 , pp. 8701-8709
    • Goncalves, J.1    Korin, Y.2    Zack, J.3    Gabuzda, D.4
  • 25
    • 0027197020 scopus 로고
    • The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent
    • Gorelick, R. J., D. J. Chabot, A. Rein, L. E. Henderson, and L. O. Arthur. 1993. The two zinc fingers in the human immunodeficiency virus type 1 nucleocapsid protein are not functionally equivalent. J. Virol. 67:4027-4036.
    • (1993) J. Virol. , vol.67 , pp. 4027-4036
    • Gorelick, R.J.1    Chabot, D.J.2    Rein, A.3    Henderson, L.E.4    Arthur, L.O.5
  • 26
    • 0031007620 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA
    • Guo, J., L. E. Henderson, J. Bess, B. Kane, and J. G. Levin. 1997. Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA. J. Virol. 71:5178-5188.
    • (1997) J. Virol. , vol.71 , pp. 5178-5188
    • Guo, J.1    Henderson, L.E.2    Bess, J.3    Kane, B.4    Levin, J.G.5
  • 27
    • 0036227658 scopus 로고    scopus 로고
    • Specific incorporation of heat shock protein 70 family members into primate lentiviral virions
    • Gurer, C., A. Cimarelli, and J. Luban. 2002. Specific incorporation of heat shock protein 70 family members into primate lentiviral virions. J. Virol. 76: 4666-4670.
    • (2002) J. Virol. , vol.76 , pp. 4666-4670
    • Gurer, C.1    Cimarelli, A.2    Luban, J.3
  • 29
    • 0029940950 scopus 로고    scopus 로고
    • Replication in goats in vivo of caprine arthritis-encephalitis virus deleted in vif or tat genes: Possible use of these deletion mutants as live vaccines
    • Harmache, A., P. Russo, C. Vitu, F. Guiguen, J. F. Mornex, M. Pepin, R. Vigne, and M. Suzan. 1996. Replication in goats in vivo of caprine arthritis-encephalitis virus deleted in vif or tat genes: possible use of these deletion mutants as live vaccines. AIDS Res. Hum. Retroviruses 12:409-411.
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , pp. 409-411
    • Harmache, A.1    Russo, P.2    Vitu, C.3    Guiguen, F.4    Mornex, J.F.5    Pepin, M.6    Vigne, R.7    Suzan, M.8
  • 31
    • 0035846449 scopus 로고    scopus 로고
    • Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene
    • Henderson, J. O., V. Blanc, and N. O. Davidson. 2001. Isolation, characterization and developmental regulation of the human apobec-1 complementation factor (ACF) gene. Biochim. Biophys. Acta 1522:22-30.
    • (2001) Biochim. Biophys. Acta , vol.1522 , pp. 22-30
    • Henderson, J.O.1    Blanc, V.2    Davidson, N.O.3
  • 33
    • 10344262588 scopus 로고    scopus 로고
    • Roles of the auxiliary genes and AP-1 binding site in the long terminal repeat of feline immunodeficiency virus in the early stage of infection in cats
    • Inoshima, Y., M. Kohmoto, Y. Ikeda, H. Yamada, Y. Kawaguchi, K. Tomonaga, T. Miyazawa, C. Kai, T. Umemura, and T. Mikami. 1996. Roles of the auxiliary genes and AP-1 binding site in the long terminal repeat of feline immunodeficiency virus in the early stage of infection in cats. J. Virol. 70: 8518-8526.
    • (1996) J. Virol. , vol.70 , pp. 8518-8526
    • Inoshima, Y.1    Kohmoto, M.2    Ikeda, Y.3    Yamada, H.4    Kawaguchi, Y.5    Tomonaga, K.6    Miyazawa, T.7    Kai, C.8    Umemura, T.9    Mikami, T.10
  • 34
    • 0031971737 scopus 로고    scopus 로고
    • The roles of vif and ORF-A genes and AP-1 binding site in in vivo replication of feline immunodeficiency virus
    • Inoshima, Y., T. Miyazawa, and T. Mikami. 1998. The roles of vif and ORF-A genes and AP-1 binding site in in vivo replication of feline immunodeficiency virus. Arch. Virol. 143:789-795.
    • (1998) Arch. Virol. , vol.143 , pp. 789-795
    • Inoshima, Y.1    Miyazawa, T.2    Mikami, T.3
  • 36
    • 0030067973 scopus 로고    scopus 로고
    • Effect of human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro
    • Ji, X., G. J. Klarmann, and B. D. Preston. 1996. Effect of human immunodeficiency virus type 1 (HIV-1) nucleocapsid protein on HIV-1 reverse transcriptase activity in vitro. Biochemistry 35:132-143.
    • (1996) Biochemistry , vol.35 , pp. 132-143
    • Ji, X.1    Klarmann, G.J.2    Preston, B.D.3
  • 37
    • 0036827828 scopus 로고    scopus 로고
    • Nucleic acid-independent retrovirus assembly can be driven by dimerization
    • Johnson, M. C., H. M. Scobie, Y. M. Ma, and V. M. Vogt. 2002. Nucleic acid-independent retrovirus assembly can be driven by dimerization. J. Virol. 76:11177-11185.
    • (2002) J. Virol. , vol.76 , pp. 11177-11185
    • Johnson, M.C.1    Scobie, H.M.2    Ma, Y.M.3    Vogt, V.M.4
  • 39
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity
    • Kao, S., M. A. Khan, E. Miyagi, R. Plishka, A. Buckler-White, and K. Strebel. 2003. The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity. J. Virol. 77:11398-11407.
    • (2003) J. Virol. , vol.77 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5    Strebel, K.6
  • 40
    • 0026730765 scopus 로고
    • Recombinant human immunodeficiency virus type 1 nucleocapsid (NCp7) protein unwinds tRNA
    • Khan, R., and D. P. Giedroc. 1992. Recombinant human immunodeficiency virus type 1 nucleocapsid (NCp7) protein unwinds tRNA. J. Biol. Chem. 267: 6689-6695.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6689-6695
    • Khan, R.1    Giedroc, D.P.2
  • 41
    • 0000333554 scopus 로고    scopus 로고
    • Evidence for a unique mechanism of strand transfer from the transactivation response region of HIV-1
    • Kim, J. K., C. Palaniappan, W. Wu, P. J. Fay, and R. A. Bambara. 1997. Evidence for a unique mechanism of strand transfer from the transactivation response region of HIV-1. J. Biol. Chem. 272:16769-16777.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16769-16777
    • Kim, J.K.1    Palaniappan, C.2    Wu, W.3    Fay, P.J.4    Bambara, R.A.5
  • 42
    • 0027258736 scopus 로고
    • Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle
    • Lapadat-Tapolsky, M., H. De Rocquigny, D. Van Gent, B. Roques, R. Plasterk, and J. L. Darlix. 1993. Interactions between HIV-1 nucleocapsid protein and viral DNA may have important functions in the viral life cycle. Nucleic Acids Res. 21:831-839.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 831-839
    • Lapadat-Tapolsky, M.1    De Rocquigny, H.2    Van Gent, D.3    Roques, B.4    Plasterk, R.5    Darlix, J.L.6
  • 43
    • 0029044016 scopus 로고
    • Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1
    • Lapadat-Tapolsky, M., C. Pernelle, C. Borie, and J. L. Darlix. 1995. Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1. Nucleic Acids Res. 23:2434-2441.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2434-2441
    • Lapadat-Tapolsky, M.1    Pernelle, C.2    Borie, C.3    Darlix, J.L.4
  • 44
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier, D., F. Bouchonnet, F. Clavel, and A. J. Hance. 2003. Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300:1112.
    • (2003) Science , vol.300 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 45
    • 0022680624 scopus 로고
    • A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses
    • Lee, T. H., J. E. Coligan, J. S. Allan, M. F. McLane, J. E. Groopman, and M. Essex. 1986. A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses. Science 231:1546-1549.
    • (1986) Science , vol.231 , pp. 1546-1549
    • Lee, T.H.1    Coligan, J.E.2    Allan, J.S.3    McLane, M.F.4    Groopman, J.E.5    Essex, M.6
  • 46
    • 0032990415 scopus 로고    scopus 로고
    • Formation of virus assembly intermediate complexes in the cytoplasm by wild-type and assembly-defective mutant human immunodeficiency virus type 1 and their association with membranes
    • Lee, Y. M., B. Liu, and X. F. Yu. 1999. Formation of virus assembly intermediate complexes in the cytoplasm by wild-type and assembly-defective mutant human immunodeficiency virus type 1 and their association with membranes. J. Virol. 73:5654-5662.
    • (1999) J. Virol. , vol.73 , pp. 5654-5662
    • Lee, Y.M.1    Liu, B.2    Yu, X.F.3
  • 48
    • 0034733528 scopus 로고    scopus 로고
    • Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex
    • Lellek, H., R. Kirsten, I. Diehl, F. Apostel, F. Buck, and J. Greeve. 2000. Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex. J. Biol. Chem. 275:19848-19856.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19848-19856
    • Lellek, H.1    Kirsten, R.2    Diehl, I.3    Apostel, F.4    Buck, F.5    Greeve, J.6
  • 49
    • 0032509267 scopus 로고    scopus 로고
    • Involvement of HIV-I nucleocapsid protein in the recruitment of reverse transcriptase into nucleoprotein complexes formed in vitro
    • Lener, D., V. Tanchou, B. P. Roques, S. F. Le Grice, and J. L. Darlix. 1998. Involvement of HIV-I 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.4    Darlix, J.L.5
  • 50
    • 0031044374 scopus 로고    scopus 로고
    • A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system
    • Lingappa, J. R., R. L. Hill, M. L. Wong, and R. S. Hegde. 1997. A multistep, ATP-dependent pathway for assembly of human immunodeficiency virus capsids in a cell-free system. J. Cell Biol. 136:567-581.
    • (1997) J. Cell Biol. , vol.136 , pp. 567-581
    • Lingappa, J.R.1    Hill, R.L.2    Wong, M.L.3    Hegde, R.S.4
  • 51
    • 0842347676 scopus 로고    scopus 로고
    • Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G
    • Liu, B., X. Yu, K. Luo, Y. Yu, and X. F. Yu. 2004. Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G. J. Virol. 78:2072-2081.
    • (2004) J. Virol. , vol.78 , pp. 2072-2081
    • Liu, B.1    Yu, X.2    Luo, K.3    Yu, Y.4    Yu, X.F.5
  • 52
    • 0034691524 scopus 로고    scopus 로고
    • Protective immunity against feline immunodeficiency virus induced by inoculation with vif-deleted proviral DNA
    • Lockridge, K. M., M. Chien, G. A. Dean, K. S. Cole, R. C. Montelaro, P. A. Luciw, and E. E. Sparger. 2000. Protective immunity against feline immunodeficiency virus induced by inoculation with vif-deleted proviral DNA. Virology 273:67-79.
    • (2000) Virology , vol.273 , pp. 67-79
    • Lockridge, K.M.1    Chien, M.2    Dean, G.A.3    Cole, K.S.4    Montelaro, R.C.5    Luciw, P.A.6    Sparger, E.E.7
  • 53
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat, B., P. Turelli, G. Caron, M. Friedli, L. Perrin, and D. Trono. 2003. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424:99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 54
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat, B., P. Turelli, S. Liao, and D. Trono. 2004. A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J. Biol. Chem. 279:14481-14483.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 56
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., K. M. Rose, S. L. Kozak, and D. Kabat. 2003. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9:1398-1403.
    • (2003) Nat. Med. , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 57
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle, A., B. Strack, P. Ancuta, C. Zhang, M. McPike, and D. Gabuzda. 2003. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279: 7792-7798.
    • (2003) J. Biol. Chem. , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 58
    • 0033970066 scopus 로고    scopus 로고
    • Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA
    • Mehta, A., M. T. Kinter, N. E. Sherman, and D. M. Driscoll. 2000. Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA. Mol. Cell. Biol. 20: 1846-1854.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1846-1854
    • Mehta, A.1    Kinter, M.T.2    Sherman, N.E.3    Driscoll, D.M.4
  • 59
    • 0027451949 scopus 로고
    • The human immunodeficiency virus type 1 (HIV-1) vif protein is located in the cytoplasm of infected cells and its effect on viral replication is equivalent in HIV-2
    • Michaels, F. H., N. Hattori, R. C. Gallo, and G. Franchini. 1993. The human immunodeficiency virus type 1 (HIV-1) vif protein is located in the cytoplasm of infected cells and its effect on viral replication is equivalent in HIV-2. AIDS Res. Hum. Retroviruses 9:1025-1030.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1025-1030
    • Michaels, F.H.1    Hattori, N.2    Gallo, R.C.3    Franchini, G.4
  • 60
    • 0029056474 scopus 로고
    • Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
    • Navaratnam, N., S. Bhattacharya, T. Fujino, D. Patel, A. L. Jarmuz, and J. Scott. 1995. Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site. Cell 81:187-195.
    • (1995) Cell , vol.81 , pp. 187-195
    • Navaratnam, N.1    Bhattacharya, S.2    Fujino, T.3    Patel, D.4    Jarmuz, A.L.5    Scott, J.6
  • 61
    • 0034467080 scopus 로고    scopus 로고
    • Role of Vif in stability of the human immunodeficiency virus type 1 core
    • Ohagen, A., and D. Gabuzda. 2000. Role of Vif in stability of the human immunodeficiency virus type 1 core. J. Virol. 74:11055-11066.
    • (2000) J. Virol. , vol.74 , pp. 11055-11066
    • Ohagen, A.1    Gabuzda, D.2
  • 62
    • 0028171533 scopus 로고
    • Effects of vif mutations on cell-free infectivity and replication of simian immunodeficiency virus
    • Park, I. W., K. Myrick, and J. Sodroski. 1994. Effects of vif mutations on cell-free infectivity and replication of simian immunodeficiency virus. J. Acquir. Immune Defic. Syndr. 7:1228-1236.
    • (1994) J. Acquir. Immune Defic. Syndr. , vol.7 , pp. 1228-1236
    • Park, I.W.1    Myrick, K.2    Sodroski, J.3
  • 63
    • 84937346333 scopus 로고
    • Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity
    • Peliska, J. A., S. Balasubramanian, D. P. Giedroc, and S. J. Benkovic. 1994. Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activity. Biochemistry 33:13817-13823.
    • (1994) Biochemistry , vol.33 , pp. 13817-13823
    • Peliska, J.A.1    Balasubramanian, S.2    Giedroc, D.P.3    Benkovic, S.J.4
  • 64
    • 0034468391 scopus 로고    scopus 로고
    • A recent outbreak of human immunodeficiency virus type 1 infection in southern China was initiated by two highly homogeneous, geographically separated strains, circulating recombinant form AE and a novel BC recombinant
    • Piyasirisilp, S., F. E. McCutchan, J. K. Carr, E. Sanders-Buell, W. Liu, J. Chen, R. Wagner, H. Wolf, Y. Shao, S. Lai, C. Beyrer, and X. F. Yu. 2000. A recent outbreak of human immunodeficiency virus type 1 infection in southern China was initiated by two highly homogeneous, geographically separated strains, circulating recombinant form AE and a novel BC recombinant. J. Virol. 74:11286-11295.
    • (2000) J. Virol. , vol.74 , pp. 11286-11295
    • Piyasirisilp, S.1    McCutchan, F.E.2    Carr, J.K.3    Sanders-Buell, E.4    Liu, W.5    Chen, J.6    Wagner, R.7    Wolf, H.8    Shao, Y.9    Lai, S.10    Beyrer, C.11    Yu, X.F.12
  • 65
    • 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., 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.1    Wu, J.2    Aldovini, A.3
  • 66
    • 0032826098 scopus 로고    scopus 로고
    • Evaluation of novel human immunodeficiency virus type 1 Gag DNA vaccines for protein expression in mammalian cells and induction of immune responses
    • Qiu, J. T., R. Song, M. Dettenhofer, C. Tian, T. August, B. K. Felber, G. N. Pavlakis, and X. F. Yu. 1999. Evaluation of novel human immunodeficiency virus type 1 Gag DNA vaccines for protein expression in mammalian cells and induction of immune responses. J. Virol. 73:9145-9152.
    • (1999) J. Virol. , vol.73 , pp. 9145-9152
    • Qiu, J.T.1    Song, R.2    Dettenhofer, M.3    Tian, C.4    August, T.5    Felber, B.K.6    Pavlakis, G.N.7    Yu, X.F.8
  • 67
    • 0033586736 scopus 로고    scopus 로고
    • Kinetic analysis of the effect of HIV nucleocapsid protein (NCp) on internal strand transfer reactions
    • Raja, A., and J. J. DeStefano. 1999. Kinetic analysis of the effect of HIV nucleocapsid protein (NCp) on internal strand transfer reactions. Biochemistry 38:5178-5184.
    • (1999) Biochemistry , vol.38 , pp. 5178-5184
    • Raja, A.1    Destefano, J.J.2
  • 68
    • 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
  • 69
    • 0029009007 scopus 로고
    • Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro
    • Rodriguez-Rodriguez, L., Z. Tsuchihashi, G. M. Fuentes, R. A. Bambara, and P. J. Fay. 1995. Influence of human immunodeficiency virus nucleocapsid protein on synthesis and strand transfer by the reverse transcriptase in vitro. J. Biol. Chem. 270:15005-15011.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15005-15011
    • Rodriguez-Rodriguez, L.1    Tsuchihashi, Z.2    Fuentes, G.M.3    Bambara, R.A.4    Fay, P.J.5
  • 70
    • 0031686764 scopus 로고    scopus 로고
    • Roles of the human immunodeficiency virus type 1 nucleocapsid protein in annealing and initiation versus elongation in reverse transcription of viral negative-strand strong-stop DNA
    • Rong, L., C. Liang, M. Hsu, L. Kleiman, P. Petitjean, H. de Rocquigny, B. P. Roques, and M. A. Wainberg. 1998. Roles of the human immunodeficiency virus type 1 nucleocapsid protein in annealing and initiation versus elongation in reverse transcription of viral negative-strand strong-stop DNA. J. Virol. 72:9353-9358.
    • (1998) J. Virol. , vol.72 , pp. 9353-9358
    • Rong, L.1    Liang, C.2    Hsu, M.3    Kleiman, L.4    Petitjean, P.5    De Rocquigny, H.6    Roques, B.P.7    Wainberg, M.A.8
  • 71
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • Schrofelbauer, B., D. Chen, and N. R. Landau. 2004. A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc. Natl. Acad. Sci. USA 101:3927-3932.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 73
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheeny, A. M., N. C. Gaddis, J. D. Choi, and M. H. Malim. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheeny, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 74
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheeny, A. M., N. C. Gaddis, and M. H. Malim. 2003. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9:1404-1407.
    • (2003) Nat. Med. , vol.9 , pp. 1404-1407
    • Sheeny, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 75
    • 0242497878 scopus 로고    scopus 로고
    • The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity
    • Shindo, K., A. Takaori-Kondo, M. Kobayashi, A. Abudu, K. Fukunaga, and T. Uchiyama. 2003. The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity. J. Biol. Chem. 278:44412-44416.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44412-44416
    • Shindo, K.1    Takaori-Kondo, A.2    Kobayashi, M.3    Abudu, A.4    Fukunaga, K.5    Uchiyama, T.6
  • 76
    • 0033052695 scopus 로고    scopus 로고
    • Gag polyprotein of human immunodeficiency virus type 1 are present in colocalizing membrane-free cytoplasmic complexes
    • Gag polyprotein of human immunodeficiency virus type 1 are present in colocalizing membrane-free cytoplasmic complexes. J. Virol. 73: 2667-2674.
    • (1999) J. Virol. , vol.73 , pp. 2667-2674
    • Simon, J.H.1    Carpenter, E.A.2    Fouchier, R.A.3    Malim, M.H.4
  • 77
    • 0030985926 scopus 로고    scopus 로고
    • The Vif and Gag proteins of human immunodeficiency virus type 1 colocalize in infected human T cells
    • Simon, J. H., R. A. Fouchier, T. E. Southerling, C. B. Guerra, C. K. Grant, and M. H. Malim. 1997. The Vif and Gag proteins of human immunodeficiency virus type 1 colocalize in infected human T cells. J. Virol. 71:5259-5267.
    • (1997) J. Virol. , vol.71 , pp. 5259-5267
    • Simon, J.H.1    Fouchier, R.A.2    Southerling, T.E.3    Guerra, C.B.4    Grant, C.K.5    Malim, M.H.6
  • 78
    • 0029956256 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
    • Simon, J. H., and M. H. Malim. 1996. The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. J. Virol. 70:5297-5305.
    • (1996) J. Virol. , vol.70 , pp. 5297-5305
    • Simon, J.H.1    Malim, M.H.2
  • 80
    • 0027183349 scopus 로고
    • Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1
    • Sova, P., and D. J. Volsky. 1993. Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1. J. Virol. 67:6322-6326.
    • (1993) J. Virol. , vol.67 , pp. 6322-6326
    • Sova, P.1    Volsky, D.J.2
  • 81
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak, K., C. de Noronha, W. Yonemoto, and W. C. Greene. 2003. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12:591-601.
    • (2003) Mol. Cell , vol.12 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 82
    • 0023267788 scopus 로고
    • The HIV 'A' (sor) gene product is essential for virus infectivity
    • Strebel, K., D. Daugherty, K. Clouse, D. Cohen, T. Folks, and M. A. Martin. 1987. The HIV 'A' (sor) gene product is essential for virus infectivity. Nature 328:728-730.
    • (1987) Nature , vol.328 , pp. 728-730
    • Strebel, K.1    Daugherty, D.2    Clouse, K.3    Cohen, D.4    Folks, T.5    Martin, M.A.6
  • 83
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • Swanstrom, R. A., and J. W. Wills. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.A.1    Wills, J.W.2
  • 85
    • 0028129970 scopus 로고
    • DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein
    • Tsuchihashi, Z., and P. O. Brown. 1994. DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol. 68:5863-5870.
    • (1994) J. Virol. , vol.68 , pp. 5863-5870
    • Tsuchihashi, Z.1    Brown, P.O.2
  • 86
    • 0033583086 scopus 로고    scopus 로고
    • Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: Elucidation of the structural determinants for function
    • Urbaneja, M. A., B. P. Kane, D. G. Johnson, R. J. Gorelick, L. E. Henderson, and J. R. Casas-Finet. 1999. Binding properties of the human immunodeficiency virus type 1 nucleocapsid protein p7 to a model RNA: elucidation of the structural determinants for function. J. Mol. Biol. 287:59-75.
    • (1999) J. Mol. Biol. , vol.287 , pp. 59-75
    • Urbaneja, M.A.1    Kane, B.P.2    Johnson, D.G.3    Gorelick, R.J.4    Henderson, L.E.5    Casas-Finet, J.R.6
  • 87
    • 0036307597 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein as a nucleic acid chaperone: Spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity
    • Urbaneja, M. A., M. Wu, J. R. Casas-Finet, and R. L. Karpel. 2002. HIV-1 nucleocapsid protein as a nucleic acid chaperone: spectroscopic study of its helix-destabilizing properties, structural binding specificity, and annealing activity. J. Mol. Biol. 318:749-764.
    • (2002) J. Mol. Biol. , vol.318 , pp. 749-764
    • Urbaneja, M.A.1    Wu, M.2    Casas-Finet, J.R.3    Karpel, R.L.4
  • 88
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
    • von Schwedler, U., J. Song, C. Aiken, and D. Trono. 1993. Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells. J. Virol. 67:4945-4955.
    • (1993) J. Virol. , vol.67 , pp. 4945-4955
    • Von Schwedler, U.1    Song, J.2    Aiken, C.3    Trono, D.4
  • 89
    • 0345270035 scopus 로고    scopus 로고
    • Messenger RNA editing in mammals: New members of the APOBEC family seeking roles in the family business
    • Wedekind, J. E., G. S. Dance, M. P. Sowden, and H. C. Smith. 2003. Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business. Trends Genet. 19:207-216.
    • (2003) Trends Genet. , vol.19 , pp. 207-216
    • Wedekind, J.E.1    Dance, G.S.2    Sowden, M.P.3    Smith, H.C.4
  • 91
    • 1842732157 scopus 로고    scopus 로고
    • A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion
    • Xu, H., E. S. Svarovskaia, R. Barr, Y. Zhang, M. A. Khan, K. Strebel, and V. K. Pathak. 2004. A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc. Natl. Acad. Sci. USA 101:5652-5657.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5652-5657
    • Xu, H.1    Svarovskaia, E.S.2    Barr, R.3    Zhang, Y.4    Khan, M.A.5    Strebel, K.6    Pathak, V.K.7
  • 92
    • 0028113905 scopus 로고
    • Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription
    • You, J. C., and C. S. McHenry. 1994. Human immunodeficiency virus nucleocapsid protein accelerates strand transfer of the terminally redundant sequences involved in reverse transcription. J. Biol. Chem. 269: 31491-31495.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31491-31495
    • You, J.C.1    McHenry, C.S.2
  • 93
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X. F. Yu. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 94
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang, H., B. Yang, R. J. Pomerantz, C. Zhang, S. C. Arunachalam, and L. Gao. 2003. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94-98.
    • (2003) Nature , vol.424 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 95
    • 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
  • 96
    • 0031910808 scopus 로고    scopus 로고
    • Analysis of the assembly function of the human immunodeficiency virus type 1 Gag protein nucleocapsid domain
    • Zhang, Y., H. Qian, Z. Love, and E. Barklis. 1998. Analysis of the assembly function of the human immunodeficiency virus type 1 Gag protein nucleocapsid domain. J. Virol. 72:1782-1789.
    • (1998) J. Virol. , vol.72 , pp. 1782-1789
    • Zhang, Y.1    Qian, H.2    Love, Z.3    Barklis, E.4


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