메뉴 건너뛰기




Volumn 84, Issue 17, 2010, Pages 8561-8570

Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; VIF PROTEIN; APOBEC3F PROTEIN, HUMAN; APOBEC3G PROTEIN, HUMAN; CYTIDINE DEAMINASE; CYTOSINE DEAMINASE; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77956628186     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00960-10     Document Type: Article
Times cited : (33)

References (47)
  • 3
    • 69249215357 scopus 로고    scopus 로고
    • A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G
    • Chen, G., Z. He, T. Wang, R. Xu, and X. F. Yu. 2009. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. J. Virol. 83:8674-8682.
    • (2009) J. Virol. , vol.83 , pp. 8674-8682
    • Chen, G.1    He, Z.2    Wang, T.3    Xu, R.4    Yu, X.F.5
  • 4
    • 77951993429 scopus 로고    scopus 로고
    • Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity
    • Dang, Y., R. W. Davis, I. A. York, and Y. H. Zheng. 2010. Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity. J. Virol. 84:5741-5750.
    • (2010) J. Virol. , vol.84 , pp. 5741-5750
    • Dang, Y.1    Davis, R.W.2    York, I.A.3    Zheng, Y.H.4
  • 5
    • 45549100648 scopus 로고    scopus 로고
    • Human cytidine deaminase APOBEC3H restricts HIV-1 replication
    • Dang, Y., L. M. Siew, X. Wang, Y. Han, R. Lampen, and Y. H. Zheng. 2008. Human cytidine deaminase APOBEC3H restricts HIV-1 replication. J. Biol. Chem. 283:11606-11614.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11606-11614
    • Dang, Y.1    Siew, L.M.2    Wang, X.3    Han, Y.4    Lampen, R.5    Zheng, Y.H.6
  • 6
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang, Y., X. Wang, W. J. Esselman, and Y. H. Zheng. 2006. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 80:10522-10533.
    • (2006) J. Virol. , vol.80 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.H.4
  • 7
    • 69249220263 scopus 로고    scopus 로고
    • Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization
    • Dang, Y., X. Wang, T. Zhou, I. A. York, and Y. H. Zheng. 2009. Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. J. Virol. 83:8544-8552.
    • (2009) J. Virol. , vol.83 , pp. 8544-8552
    • Dang, Y.1    Wang, X.2    Zhou, T.3    York, I.A.4    Zheng, Y.H.5
  • 8
    • 46549089412 scopus 로고    scopus 로고
    • The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
    • Donahue, J. P., M. L. Vetter, N. A. Mukhtar, and R. T. D'Aquila. 2008. The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation. Virology 377:49-53.
    • (2008) Virology , vol.377 , pp. 49-53
    • Donahue, J.P.1    Vetter, M.L.2    Mukhtar, N.A.3    D'Aquila, R.T.4
  • 11
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • He, Z., W. Zhang, G. Chen, R. Xu, and X. F. Yu. 2008. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J. Mol. Biol. 381:1000-1011.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1000-1011
    • He, Z.1    Zhang, W.2    Chen, G.3    Xu, R.4    Yu, X.F.5
  • 12
    • 34247111953 scopus 로고    scopus 로고
    • Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and virion encapsidation
    • Huthoff, H., and M. H. Malim. 2007. Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and virion encapsidation. J. Virol. 81:3807-3815.
    • (2007) J. Virol. , vol.81 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 14
    • 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
  • 15
    • 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
  • 16
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • Luo, K., Z. Xiao, E. Ehrlich, Y. Yu, B. Liu, S. Zheng, and X. F. Yu. 2005. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc. Natl. Acad. Sci. U. S. A. 102:11444-11449.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11444-11449
    • Luo, K.1    Xiao, Z.2    Ehrlich, E.3    Yu, Y.4    Liu, B.5    Zheng, S.6    Yu, X.F.7
  • 17
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • Madani, N., and D. Kabat. 1998. An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. J. Virol. 72:10251-10255.
    • (1998) J. Virol. , vol.72 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 18
    • 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
  • 19
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • Mehle, A., J. Goncalves, M. Santa-Marta, M. McPike, and D. Gabuzda. 2004. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev. 18:2861-2866.
    • (2004) Genes Dev. , vol.18 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 20
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • Mehle, A., E. R. Thomas, K. S. Rajendran, and D. Gabuzda. 2006. A zinc-binding region in Vif binds Cul5 and determines cullin selection. J. Biol. Chem. 281:17259-17265.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 21
    • 77950487440 scopus 로고    scopus 로고
    • Host restriction of HIV-1 by APOBEC3 and viral evasion through Vif
    • Niewiadomska, A. M., and X. F. Yu. 2010. Host restriction of HIV-1 by APOBEC3 and viral evasion through Vif. Curr. Top. Microbiol. Immunol. 339:1-25.
    • (2010) Curr. Top. Microbiol. Immunol. , vol.339 , pp. 1-25
    • Niewiadomska, A.M.1    Yu, X.F.2
  • 22
    • 60049098639 scopus 로고    scopus 로고
    • Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif
    • Pery, E., K. S. Rajendran, A. J. Brazier, and D. Gabuzda. 2009. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J. Virol. 83:2374-2381.
    • (2009) J. Virol. , vol.83 , pp. 2374-2381
    • Pery, E.1    Rajendran, K.S.2    Brazier, A.J.3    Gabuzda, D.4
  • 23
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • Russell, R. A., and V. K. Pathak. 2007. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J. Virol. 81:8201-8210.
    • (2007) J. Virol. , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 24
    • 59649118427 scopus 로고    scopus 로고
    • Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif
    • Russell, R. A., J. Smith, R. Barr, D. Bhattacharyya, and V. K. Pathak. 2009. Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif. J. Virol. 83:1992-2003.
    • (2009) J. Virol. , vol.83 , pp. 1992-2003
    • Russell, R.A.1    Smith, J.2    Barr, R.3    Bhattacharyya, D.4    Pathak, V.K.5
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • Simon, J. H., N. C. Gaddis, R. A. Fouchier, and M. H. Malim. 1998. Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nat. Med. 4:1397-1400.
    • (1998) Nat. Med. , vol.4 , pp. 1397-1400
    • Simon, J.H.1    Gaddis, N.C.2    Fouchier, R.A.3    Malim, M.H.4
  • 28
    • 0033053198 scopus 로고    scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Vif protein
    • Simon, J. H., A. M. Sheehy, E. A. Carpenter, R. A. Fouchier, and M. H. Malim. 1999. Mutational analysis of the human immunodeficiency virus type 1 Vif protein. J. Virol. 73:2675-2681.
    • (1999) J. Virol. , vol.73 , pp. 2675-2681
    • Simon, J.H.1    Sheehy, A.M.2    Carpenter, E.A.3    Fouchier, R.A.4    Malim, M.H.5
  • 29
    • 67649888155 scopus 로고    scopus 로고
    • Natural variation in Vif: Differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
    • Simon, V., V. Zennou, D. Murray, Y. Huang, D. D. Ho, and P. D. Bieniasz. 2005. Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification. PLoS Pathog. 1:e6.
    • (2005) PLoS Pathog. , vol.1
    • Simon, V.1    Zennou, V.2    Murray, D.3    Huang, Y.4    Ho, D.D.5    Bieniasz, P.D.6
  • 30
    • 70449629709 scopus 로고    scopus 로고
    • Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development
    • Smith, J. L., W. Bu, R. C. Burdick, and V. K. Pathak. 2009. Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development. Trends Pharmacol. Sci. 30:638-646.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 638-646
    • Smith, J.L.1    Bu, W.2    Burdick, R.C.3    Pathak, V.K.4
  • 32
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • Stanley, B. J., E. S. Ehrlich, L. Short, Y. Yu, Z. Xiao, X. F. Yu, and Y. Xiong. 2008. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J. Virol. 82:8656-8663.
    • (2008) J. Virol. , vol.82 , pp. 8656-8663
    • Stanley, B.J.1    Ehrlich, E.S.2    Short, L.3    Yu, Y.4    Xiao, Z.5    Yu, X.F.6    Xiong, Y.7
  • 33
    • 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
  • 34
    • 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
  • 35
    • 70350738592 scopus 로고    scopus 로고
    • Human cellular restriction factors that target HIV-1 replication
    • Strebel, K., J. Luban, and K. T. Jeang. 2009. Human cellular restriction factors that target HIV-1 replication. BMC Med. 7:48.
    • (2009) BMC Med. , vol.7 , pp. 48
    • Strebel, K.1    Luban, J.2    Jeang, K.T.3
  • 36
    • 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
  • 37
    • 77951460356 scopus 로고    scopus 로고
    • Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif
    • Walker, R. C., Jr., M. A. Khan, S. Kao, R. Goila-Gaur, E. Miyagi, and K. Strebel. 2010. Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif. J. Virol. 84:5201-5211.
    • (2010) J. Virol. , vol.84 , pp. 5201-5211
    • Walker Jr., R.C.1    Khan, M.A.2    Kao, S.3    Goila-Gaur, R.4    Miyagi, E.5    Strebel, K.6
  • 38
    • 33847261162 scopus 로고    scopus 로고
    • Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle
    • Wang, X., P. T. Dolan, Y. Dang, and Y. H. Zheng. 2007. Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle. J. Biol. Chem. 282:1585-1594.
    • (2007) J. Biol. Chem. , vol.282 , pp. 1585-1594
    • Wang, X.1    Dolan, P.T.2    Dang, Y.3    Zheng, Y.H.4
  • 39
    • 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
  • 40
    • 77953757638 scopus 로고    scopus 로고
    • Dissection of HIV Vif interaction with the human E3 ubiquitin ligase
    • Wolfe, L. S., B. J. Stanley, C. Liu, W. K. Eliason, and Y. Xiong. 2010. Dissection of HIV Vif interaction with the human E3 ubiquitin ligase. J. Virol. 84:7135-7139.
    • (2010) J. Virol. , vol.84 , pp. 7135-7139
    • Wolfe, L.S.1    Stanley, B.J.2    Liu, C.3    Eliason, W.K.4    Xiong, Y.5
  • 41
    • 33646866382 scopus 로고    scopus 로고
    • Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif
    • Xiao, Z., E. Ehrlich, Y. Yu, K. Luo, T. Wang, C. Tian, and X. F. Yu. 2006. Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. Virology 349:290-299.
    • (2006) Virology , vol.349 , pp. 290-299
    • Xiao, Z.1    Ehrlich, E.2    Yu, Y.3    Luo, K.4    Wang, T.5    Tian, C.6    Yu, X.F.7
  • 42
    • 54049112596 scopus 로고    scopus 로고
    • Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F
    • Yamashita, T., K. Kamada, K. Hatcho, A. Adachi, and M. Nomaguchi. 2008. Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F. Microbes Infect. 10:1142-1149.
    • (2008) Microbes Infect. , vol.10 , pp. 1142-1149
    • Yamashita, T.1    Kamada, K.2    Hatcho, K.3    Adachi, A.4    Nomaguchi, M.5
  • 43
    • 0035895896 scopus 로고    scopus 로고
    • The multimerization of human immunodeficiency virus type I Vif protein: A requirement for Vif function in the viral life cycle
    • Yang, S., Y. Sun, and H. Zhang. 2001. The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J. Biol. Chem. 276:4889-4893.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4889-4893
    • Yang, S.1    Sun, Y.2    Zhang, H.3
  • 44
    • 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
  • 45
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • Yu, Y., Z. Xiao, E. S. Ehrlich, X. Yu, and X. F. Yu. 2004. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev. 18:2867-2872.
    • (2004) Genes Dev. , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 46
    • 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
  • 47
    • 65749106717 scopus 로고    scopus 로고
    • A novel HIV-1 restriction factor that is biologically distinct from APOBEC3 cytidine deaminases in a human T cell line CEM.NKR
    • Zhou, T., Y. Han, Y. Dang, X. Wang, and Y. H. Zheng. 2009. A novel HIV-1 restriction factor that is biologically distinct from APOBEC3 cytidine deaminases in a human T cell line CEM.NKR. Retrovirology 6:31.
    • (2009) Retrovirology , vol.6 , pp. 31
    • Zhou, T.1    Han, Y.2    Dang, Y.3    Wang, X.4    Zheng, Y.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.