메뉴 건너뛰기




Volumn 79, Issue 17, 2005, Pages 10978-10987

Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG Uracil-DNA glycosylases

Author keywords

[No Author keywords available]

Indexed keywords

CYTIDINE DEAMINASE; CYTOSINE DERIVATIVE; PROTEASOME; PROTEIN APOBEC3; PROTEIN CUL1; PROTEIN CUL4; PROTEIN SMUG; PROTEIN UNG; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; URACIL DERIVATIVE; URACIL DNA GLYCOSYLTRANSFERASE; VPR PROTEIN;

EID: 23844471513     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.17.10978-10987.2005     Document Type: Article
Times cited : (197)

References (56)
  • 1
    • 0028297360 scopus 로고
    • Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: Mutational analysis of a primary HIV-1 isolate
    • Balliet, J. W., D. L. Kolson, G. Eiger, F. M. Kim, K. A. McGann, A. Srinivasan, and R. Collman. 1994. Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: mutational analysis of a primary HIV-1 isolate. Virology 200:623-631.
    • (1994) Virology , vol.200 , pp. 623-631
    • Balliet, J.W.1    Kolson, D.L.2    Eiger, G.3    Kim, F.M.4    McGann, K.A.5    Srinivasan, A.6    Collman, R.7
  • 4
    • 0032478787 scopus 로고    scopus 로고
    • Diversity of HIV-1 Vpr interactions involves usage of the WXXF motif of host cell proteins
    • BouHamdan, M., Y. Xue, Y. Baudat, B. Hu, J. Sire, R. J. Pomerantz, and L. X. Duan. 1998. Diversity of HIV-1 Vpr interactions involves usage of the WXXF motif of host cell proteins. J. Biol. Chem. 273:8009-8016.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8009-8016
    • Bouhamdan, M.1    Xue, Y.2    Baudat, Y.3    Hu, B.4    Sire, J.5    Pomerantz, R.J.6    Duan, L.X.7
  • 5
    • 0035025888 scopus 로고    scopus 로고
    • A quantitative assay for HIV DNA integration in vivo
    • Butler, S. L., M. S. Hansen, and F. D. Bushman. 2001. A quantitative assay for HIV DNA integration in vivo. Nat. Med. 7:631-634.
    • (2001) Nat. Med. , vol.7 , pp. 631-634
    • Butler, S.L.1    Hansen, M.S.2    Bushman, F.D.3
  • 6
    • 3142651460 scopus 로고    scopus 로고
    • Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages
    • Chen, R., E. Le Rouzic, J. A. Kearney, L. M. Mansky, and S. Benichou. 2004. Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages. J. Biol. Chem. 279:28419-28425.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28419-28425
    • Chen, R.1    Le Rouzic, E.2    Kearney, J.A.3    Mansky, L.M.4    Benichou, S.5
  • 7
    • 0036788148 scopus 로고    scopus 로고
    • Roles of uracil-DNA glycosylase and dUTPase in virus replication
    • Chen, R., H. Wang, and L. M. Mansky. 2002. Roles of uracil-DNA glycosylase and dUTPase in virus replication. J. Gen. Virol. 83:2339-2345.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2339-2345
    • Chen, R.1    Wang, H.2    Mansky, L.M.3
  • 8
    • 0025295307 scopus 로고
    • Human immunodeficiency virus vpr product is a virion-associated regulatory protein
    • Cohen, E. A., G. Dehni, J. G. Sodroski, and W. A. Haseltine. 1990. Human immunodeficiency virus vpr product is a virion-associated regulatory protein. J. Virol. 64:3097-3099.
    • (1990) J. Virol. , vol.64 , pp. 3097-3099
    • Cohen, E.A.1    Dehni, G.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 9
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor, R. I., B. K. Chen, S. Choe, and N. R. Landau. 1995. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206:936-944.
    • (1995) Virology , vol.206 , pp. 936-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 11
    • 17144384021 scopus 로고    scopus 로고
    • Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases
    • Dutko, J. A., A. Schafer, A. E. Kenny, B. R. Cullen, and M. J. Curcio. 2005. Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases. Curr. Biol. 15:661-666.
    • (2005) Curr. Biol. , vol.15 , pp. 661-666
    • Dutko, J.A.1    Schafer, A.2    Kenny, A.E.3    Cullen, B.R.4    Curcio, M.J.5
  • 13
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., S. Sadis, B. P. Monia, P. Boucher, D. J. Ecker, S. T. Crooke, and V. Chau. 1994. Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol. 14:5501-5509.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 14
    • 0037630009 scopus 로고    scopus 로고
    • Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions
    • Gaddis, N. C., E. Chertova, A. M. Sheehy, L. E. Henderson, and M. H. Malim. 2003. Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. J. Virol. 77:5810-5820.
    • (2003) J. Virol. , vol.77 , pp. 5810-5820
    • Gaddis, N.C.1    Chertova, E.2    Sheehy, A.M.3    Henderson, L.E.4    Malim, M.H.5
  • 15
    • 0003124066 scopus 로고    scopus 로고
    • HIV-1 Vpr increases viral expression by manipulation of the cell cycle: A mechanism for selection of Vpr in vivo
    • Goh, W. C., M. E. Rogel, C. M. Kinsey, S. F. Michael, P. N. Fultz, M. A. Nowak, B. H. Hahn, and M. Emerman. 1998. HIV-1 Vpr increases viral expression by manipulation of the cell cycle: a mechanism for selection of Vpr in vivo. Nat. Med. 4:65-71.
    • (1998) Nat. Med. , vol.4 , pp. 65-71
    • Goh, W.C.1    Rogel, M.E.2    Kinsey, C.M.3    Michael, S.F.4    Fultz, P.N.5    Nowak, M.A.6    Hahn, B.H.7    Emerman, M.8
  • 18
    • 0034785763 scopus 로고    scopus 로고
    • Biochemical analyses of the interactions between human immunodeficiency virus type 1 Vpr and p6(Gag)
    • Jenkins, Y., O. Pornillos, R. L. Rich, D. G. Myszka, W. I. Sundquist, and M. H. Malim. 2001. Biochemical analyses of the interactions between human immunodeficiency virus type 1 Vpr and p6(Gag). J. Virol. 75:10537-10542.
    • (2001) J. Virol. , vol.75 , pp. 10537-10542
    • Jenkins, Y.1    Pornillos, O.2    Rich, R.L.3    Myszka, D.G.4    Sundquist, W.I.5    Malim, M.H.6
  • 19
    • 2342650905 scopus 로고    scopus 로고
    • Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1
    • Kino, T., and G. N. Pavlakis. 2004. Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. DNA Cell Biol. 23:193-205.
    • (2004) DNA Cell Biol. , vol.23 , pp. 193-205
    • Kino, T.1    Pavlakis, G.N.2
  • 20
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA - Occurrence, consequences and repair
    • Krokan, H. E., F. Drablos, and G. Slupphaug. 2002. Uracil in DNA-occurrence, consequences and repair. Oncogene 21:8935-8948.
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 22
    • 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
  • 23
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament, M. T., W. L. Brown, A. J. Schumacher, and R. S. Harris. 2004. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr. Biol. 14:1385-1391.
    • (2004) Curr. Biol. , vol.14 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 24
    • 0027376064 scopus 로고
    • Human immunodeficiency virus type 1 viral protein R localization in infected cells and virions
    • Lu, Y. L., P. Spearman, and L. Ratner. 1993. Human immunodeficiency virus type 1 viral protein R localization in infected cells and virions. J. Virol. 67:6542-6550.
    • (1993) J. Virol. , vol.67 , pp. 6542-6550
    • Lu, Y.L.1    Spearman, P.2    Ratner, L.3
  • 25
    • 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
  • 26
    • 0033925801 scopus 로고    scopus 로고
    • The interaction of Vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 in vivo mutation rate
    • Mansky, L. M., S. Preveral, L. Selig, R. Benarous, and S. Benichou. 2000. The interaction of Vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 in vivo mutation rate. J. Virol. 74:7039-7047.
    • (2000) J. Virol. , vol.74 , pp. 7039-7047
    • Mansky, L.M.1    Preveral, S.2    Selig, L.3    Benarous, R.4    Benichou, S.5
  • 28
    • 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. Rabat. 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    Rabat, D.4
  • 29
    • 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. 2004. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279:7792-7798.
    • (2004) 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
  • 31
  • 32
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNO gene
    • Nilsen, H., M. Otterlei, T. Haug, K. Solum, T. A. Nagelhus, F. Skorpen, and H. E. Krokan. 1997. Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNO gene. Nucleic Acids Res. 25:750-755.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.A.5    Skorpen, F.6    Krokan, H.E.7
  • 33
    • 0027429412 scopus 로고
    • Incorporation of Vpr into human immunodeficiency virus type-1 virions: Requirement for the p6 region of gag and mutational analysis
    • Paxton, W., R. I. Connor, and N. R. Landau. 1993. Incorporation of Vpr into human immunodeficiency virus type-1 virions: requirement for the p6 region of gag and mutational analysis. J. Virol. 67:7229-7237.
    • (1993) J. Virol. , vol.67 , pp. 7229-7237
    • Paxton, W.1    Connor, R.I.2    Landau, N.R.3
  • 34
    • 0032504065 scopus 로고    scopus 로고
    • Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents
    • Poon, B., K. Grovit-Ferbas, S. A. Stewart, and I. S. Chen. 1998. Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents. Science 281:266-269.
    • (1998) Science , vol.281 , pp. 266-269
    • Poon, B.1    Grovit-Ferbas, K.2    Stewart, S.A.3    Chen, I.S.4
  • 35
    • 13944277344 scopus 로고    scopus 로고
    • HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle
    • Priet, S., N. Gros, J. M. Navarro, J. Boretto, B. Canard, G. Querat, and J. Sire. 2005. HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle. Mol. Cell 17:479-490.
    • (2005) Mol. Cell , vol.17 , pp. 479-490
    • Priet, S.1    Gros, N.2    Navarro, J.M.3    Boretto, J.4    Canard, B.5    Querat, G.6    Sire, J.7
  • 36
    • 0037444303 scopus 로고    scopus 로고
    • Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles
    • Priet, S., J. M. Navarro, N. Gros, G. Querat, and J. Sire. 2003. Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles. Virology 307:283-289.
    • (2003) Virology , vol.307 , pp. 283-289
    • Priet, S.1    Navarro, J.M.2    Gros, N.3    Querat, G.4    Sire, J.5
  • 37
    • 0037687289 scopus 로고    scopus 로고
    • Functional role of HIV-1 virion-associated uracil DNA glycosylase 2 in the correction of G:U mispairs to G:C pairs
    • Priet, S., J. M. Navarro, N. Gros, G. Querat, and J. Sire. 2003. Functional role of HIV-1 virion-associated uracil DNA glycosylase 2 in the correction of G:U mispairs to G:C pairs. J. Biol. Chem. 278:4566-4571.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4566-4571
    • Priet, S.1    Navarro, J.M.2    Gros, N.3    Querat, G.4    Sire, J.5
  • 38
    • 2642511413 scopus 로고    scopus 로고
    • The viral infectivity factor (Vif) of HIV-1 unveiled
    • Rose, K. M., M. Marin, S. L. Kozak, and D. Kabat. 2004. The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol. Med. 10:291-297.
    • (2004) Trends Mol. Med. , vol.10 , pp. 291-297
    • Rose, K.M.1    Marin, M.2    Kozak, S.L.3    Kabat, D.4
  • 40
    • 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
  • 41
    • 2342666701 scopus 로고    scopus 로고
    • New insights into the role of Vif in HIV-1 replication
    • Schrofelbauer, B., Q. Yu, and N. R. Landau. 2004. New insights into the role of Vif in HIV-1 replication. AIDS Rev. 6:34-39.
    • (2004) AIDS Rev. , vol.6 , pp. 34-39
    • Schrofelbauer, B.1    Yu, Q.2    Landau, N.R.3
  • 42
    • 0030958826 scopus 로고    scopus 로고
    • Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest
    • Selig, L., S. Benichou, M. E. Rogel, L. I. Wu, M. A. Vodicka, J. Sire, R. Benarous, and M. Emerman. 1997. Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest. J. Virol. 71:4842-4846.
    • (1997) J. Virol. , vol.71 , pp. 4842-4846
    • Selig, L.1    Benichou, S.2    Rogel, M.E.3    Wu, L.I.4    Vodicka, M.A.5    Sire, J.6    Benarous, R.7    Emerman, M.8
  • 44
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy, 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
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 45
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, 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
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 47
    • 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
  • 48
    • 0035824651 scopus 로고    scopus 로고
    • Sensitivity of mammalian cells expressing mutant ubiquitin to protein-damaging agents
    • Tsirigotis, M., M. Zhang, R. K. Chiu, B. G. Wouters, and D. A. Gray. 2001. Sensitivity of mammalian cells expressing mutant ubiquitin to protein-damaging agents. J. Biol. Chem. 276:46073-46078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46073-46078
    • Tsirigotis, M.1    Zhang, M.2    Chiu, R.K.3    Wouters, B.G.4    Gray, D.A.5
  • 49
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., S. Omura, and R. R. Kopito. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 50
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand, H. L., B. P. Doehle, H. P. Bogerd, and B. R. Cullen. 2004. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23:2451-2458.
    • (2004) EMBO J. , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 51
    • 0032902885 scopus 로고    scopus 로고
    • DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism
    • Willetts, K. E., F. Rey, I. Agostini, J. M. Navarro, Y. Baudat, R. Vigne, and J. Sire. 1999. DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism. J. Virol. 73:1682-1688.
    • (1999) J. Virol. , vol.73 , pp. 1682-1688
    • Willetts, K.E.1    Rey, F.2    Agostini, I.3    Navarro, J.M.4    Baudat, Y.5    Vigne, R.6    Sire, J.7
  • 53
    • 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
  • 55
    • 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
  • 56
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng, Y. H., D. Irwin, T. Kurosu, K. Tokunaga, T. Sata, and B. M. Peterlin. 2004. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J. Virol. 78:6073-6076.
    • (2004) J. Virol. , vol.78 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.