메뉴 건너뛰기




Volumn 31, Issue 5, 2010, Pages 383-397

HIV-1 Vif versus the APOBEC3 cytidine deaminases: An intracellular duel between pathogen and host restriction factors

Author keywords

HIV 1

Indexed keywords

ANTIVIRUS AGENT; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CULLIN; CYTIDINE DEAMINASE; IMB 26; IMB 35; PROTEASOME; RN 18; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIF PROTEIN;

EID: 77958486207     PISSN: 00982997     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mam.2010.06.001     Document Type: Review
Times cited : (60)

References (197)
  • 3
    • 42749089384 scopus 로고    scopus 로고
    • APOBEC3G restricts early HIV-1 replication in the cytoplasm of target cells
    • Anderson J.L., Hope T.J. APOBEC3G restricts early HIV-1 replication in the cytoplasm of target cells. Virology 2008, 375:1-12.
    • (2008) Virology , vol.375 , pp. 1-12
    • Anderson, J.L.1    Hope, T.J.2
  • 4
    • 34548713478 scopus 로고    scopus 로고
    • Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity
    • Auclair J.R., Green K.M., Shandilya S., Evans J.E., Somasundaran M., Schiffer C.A. Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity. Proteins 2007, 69:270-284.
    • (2007) Proteins , vol.69 , pp. 270-284
    • Auclair, J.R.1    Green, K.M.2    Shandilya, S.3    Evans, J.E.4    Somasundaran, M.5    Schiffer, C.A.6
  • 5
    • 0034771945 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 Vif with Gag and Gag-Pol precursors: co-encapsidation and interference with viral protease-mediated Gag processing
    • Bardy M., Gay B., Pebernard S., Chazal N., Courcoul M., Vigne R., Decroly E., Boulanger P. Interaction of human immunodeficiency virus type 1 Vif with Gag and Gag-Pol precursors: co-encapsidation and interference with viral protease-mediated Gag processing. J. Gen. Virol. 2001, 82:2719-2733.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2719-2733
    • Bardy, M.1    Gay, B.2    Pebernard, S.3    Chazal, N.4    Courcoul, M.5    Vigne, R.6    Decroly, E.7    Boulanger, P.8
  • 6
    • 4444298202 scopus 로고    scopus 로고
    • APOBEC3G versus reverse transcriptase in the generation of HIV-1 drug-resistance mutations
    • Berkhout B., de Ronde A. APOBEC3G versus reverse transcriptase in the generation of HIV-1 drug-resistance mutations. AIDS 2004, 18:1861-1863.
    • (2004) AIDS , vol.18 , pp. 1861-1863
    • Berkhout, B.1    de Ronde, A.2
  • 7
    • 34548833825 scopus 로고    scopus 로고
    • RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study
    • Bernacchi S., Henriet S., Dumas P., Paillart J.C., Marquet R. RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study. J. Biol. Chem. 2007, 282:26361-26368.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26361-26368
    • Bernacchi, S.1    Henriet, S.2    Dumas, P.3    Paillart, J.C.4    Marquet, R.5
  • 8
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex
    • Betts L., Xiang S., Short S.A., Wolfenden R., Carter C.W. Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex. J. Mol. Biol. 1994, 235:635-656.
    • (1994) J. Mol. Biol. , vol.235 , pp. 635-656
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter, C.W.5
  • 9
    • 33947416193 scopus 로고    scopus 로고
    • Apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G: a possible role in the resistance to HIV of HIV-exposed seronegative individuals
    • Biasin M., Piacentini L., Lo Caputo S., Kanari Y., Magri G., Trabattoni D., Naddeo V., Lopalco L., Clivio A., Cesana E., et al. Apolipoprotein B mRNA-editing enzyme, catalytic polypeptide-like 3G: a possible role in the resistance to HIV of HIV-exposed seronegative individuals. J. Infect. Dis. 2007, 195:960-964.
    • (2007) J. Infect. Dis. , vol.195 , pp. 960-964
    • Biasin, M.1    Piacentini, L.2    Lo Caputo, S.3    Kanari, Y.4    Magri, G.5    Trabattoni, D.6    Naddeo, V.7    Lopalco, L.8    Clivio, A.9    Cesana, E.10
  • 10
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: a front-line defense against viral attack
    • Bieniasz P.D. Intrinsic immunity: a front-line defense against viral attack. Nat. Immunol. 2004, 5:1109-1115.
    • (2004) Nat. Immunol. , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 11
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop K.N., Holmes R.K., Malim M.H. Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J. Virol. 2006, 80:8450-8458.
    • (2006) J. Virol. , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 15
    • 44149089334 scopus 로고    scopus 로고
    • Single-stranded RNA facilitates nucleocapsid: APOBEC3G complex formation
    • Bogerd H.P., Cullen B.R. Single-stranded RNA facilitates nucleocapsid: APOBEC3G complex formation. RNA 2008, 14:1228-1236.
    • (2008) RNA , vol.14 , pp. 1228-1236
    • Bogerd, H.P.1    Cullen, B.R.2
  • 16
    • 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., Doehle B.P., Wiegand H.L., Cullen B.R. 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 2004, 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
  • 17
    • 34249892197 scopus 로고    scopus 로고
    • The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains
    • Bogerd H.P., Wiegand H.L., Doehle B.P., Cullen B.R. The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains. Virology 2007, 364:486-493.
    • (2007) Virology , vol.364 , pp. 486-493
    • Bogerd, H.P.1    Wiegand, H.L.2    Doehle, B.P.3    Cullen, B.R.4
  • 18
    • 36048934237 scopus 로고    scopus 로고
    • Target cell APOBEC3C can induce limited G-to-A mutation in HIV-1
    • Bourara K., Liegler T.J., Grant R.M. Target cell APOBEC3C can induce limited G-to-A mutation in HIV-1. PLoS Pathog. 2007, 3:1477-1485.
    • (2007) PLoS Pathog. , vol.3 , pp. 1477-1485
    • Bourara, K.1    Liegler, T.J.2    Grant, R.M.3
  • 19
    • 34248335849 scopus 로고    scopus 로고
    • APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker
    • Burnett A., Spearman P. APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker. J. Virol. 2007, 81:5000-5013.
    • (2007) J. Virol. , vol.81 , pp. 5000-5013
    • Burnett, A.1    Spearman, P.2
  • 20
    • 0029821868 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 Vif particle incorporation
    • Camaur D., Trono D. Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J. Virol. 1996, 70:6106-6111.
    • (1996) J. Virol. , vol.70 , pp. 6106-6111
    • Camaur, D.1    Trono, D.2
  • 21
    • 24144468961 scopus 로고    scopus 로고
    • High-throughput human immunodeficiency virus type 1 (HIV-1) full replication assay that includes HIV-1 Vif as an antiviral target
    • Cao J., Isaacson J., Patick A.K., Blair W.S. High-throughput human immunodeficiency virus type 1 (HIV-1) full replication assay that includes HIV-1 Vif as an antiviral target. Antimicrob. Agents Chemother. 2005, 49:3833-3841.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3833-3841
    • Cao, J.1    Isaacson, J.2    Patick, A.K.3    Blair, W.S.4
  • 22
    • 77952781524 scopus 로고    scopus 로고
    • Wang Yu-Ping Liu, Fei, Shao, Rong-Guang, Zhao, Li-Xun, Yu, Liyan, Jiang, Jian-Dong, 2010. Small molecular inhibitors for HIV-1 replication through specifically stabilizing APOBEC3G. J. Biol. Chem. April 2.
    • Cen, S., Peng, Z., Li, X., Li, Z., Ma, J., Wang, Y., Bo Fan, X.-F.Y., Wang, Yu-Ping, Liu, Fei, Shao, Rong-Guang, Zhao, Li-Xun, Yu, Liyan, Jiang, Jian-Dong, 2010. Small molecular inhibitors for HIV-1 replication through specifically stabilizing APOBEC3G. J. Biol. Chem. April 2.
    • Cen, S.1    Peng, Z.2    Li, X.3    Li, Z.4    Ma, J.5    Wang, Y.6    Bo Fan, X.-F.Y.7
  • 23
    • 33745067722 scopus 로고    scopus 로고
    • APOBEC3G DNA deaminase acts processively 3′→5′ on single-stranded DNA
    • Chelico L., Pham P., Calabrese P., Goodman M.F. APOBEC3G DNA deaminase acts processively 3′→5′ on single-stranded DNA. Nat. Struct. Mol. Biol. 2006, 13:392-399.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 392-399
    • Chelico, L.1    Pham, P.2    Calabrese, P.3    Goodman, M.F.4
  • 24
    • 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., He Z., Wang T., Xu R., Yu X.F. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. J. Virol. 2009, 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
  • 26
    • 42649120310 scopus 로고    scopus 로고
    • The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements
    • Chiu Y.L., Greene W.C. The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu. Rev. Immunol. 2008, 26:317-353.
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 317-353
    • Chiu, Y.L.1    Greene, W.C.2
  • 28
    • 32444434763 scopus 로고    scopus 로고
    • APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count
    • Cho S.J., Drechsler H., Burke R.C., Arens M.Q., Powderly W., Davidson N.O. APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count. J. Virol. 2006, 80:2069-2072.
    • (2006) J. Virol. , vol.80 , pp. 2069-2072
    • Cho, S.J.1    Drechsler, H.2    Burke, R.C.3    Arens, M.Q.4    Powderly, W.5    Davidson, N.O.6
  • 29
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello S.G., Harris R.S., Neuberger M.S. The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr. Biol. 2003, 13:2009-2013.
    • (2003) Curr. Biol. , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 31
    • 0028926644 scopus 로고
    • Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps
    • Courcoul M., Patience C., Rey F., Blanc D., Harmache A., Sire J., Vigne R., Spire B. Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps. J. Virol. 1995, 69:2068-2074.
    • (1995) J. Virol. , vol.69 , pp. 2068-2074
    • Courcoul, M.1    Patience, C.2    Rey, F.3    Blanc, D.4    Harmache, A.5    Sire, J.6    Vigne, R.7    Spire, B.8
  • 32
    • 77951993429 scopus 로고    scopus 로고
    • Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 virus Vif that regulate APOBEC3G and APOBEC3F neutralizing activity
    • Dang Y., Davis R.W., York I.A., Zheng Y.H. Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 virus Vif that regulate APOBEC3G and APOBEC3F neutralizing activity. J. Virol. 2010, 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
  • 33
    • 45549100648 scopus 로고    scopus 로고
    • Human cytidine deaminase APOBEC3H restricts HIV-1 replication
    • Dang Y., Siew L.M., Wang X., Han Y., Lampen R., Zheng Y.H. Human cytidine deaminase APOBEC3H restricts HIV-1 replication. J. Biol. Chem. 2008, 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
  • 34
    • 45149106103 scopus 로고    scopus 로고
    • APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated
    • Dang Y., Siew L.M., Zheng Y.H. APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated. J. Biol. Chem. 2008, 283:13124-13131.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13124-13131
    • Dang, Y.1    Siew, L.M.2    Zheng, Y.H.3
  • 35
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang Y., Wang X., Esselman W.J., Zheng Y.H. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 2006, 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
  • 36
    • 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., Wang X., Zhou T., York I.A., Zheng Y.H. 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. 2009, 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
  • 37
    • 50949102976 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif induces cell cycle delay via recruitment of the same E3 ubiquitin ligase complex that targets APOBEC3 proteins for degradation
    • DeHart J.L., Bosque A., Harris R.S., Planelles V. Human immunodeficiency virus type 1 Vif induces cell cycle delay via recruitment of the same E3 ubiquitin ligase complex that targets APOBEC3 proteins for degradation. J. Virol. 2008, 82:9265-9272.
    • (2008) J. Virol. , vol.82 , pp. 9265-9272
    • DeHart, J.L.1    Bosque, A.2    Harris, R.S.3    Planelles, V.4
  • 38
    • 0032935035 scopus 로고    scopus 로고
    • Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions
    • Dettenhofer M., Yu X.F. Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions. J. Virol. 1999, 73:1460-1467.
    • (1999) J. Virol. , vol.73 , pp. 1460-1467
    • Dettenhofer, M.1    Yu, X.F.2
  • 40
    • 23844483541 scopus 로고    scopus 로고
    • Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif
    • Doehle B.P., Schafer A., Cullen B.R. Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif. Virology 2005, 339:281-288.
    • (2005) Virology , vol.339 , pp. 281-288
    • Doehle, B.P.1    Schafer, A.2    Cullen, B.R.3
  • 41
    • 46549089412 scopus 로고    scopus 로고
    • The HIV-1 motif is necessary for human APOBEC3G binding and degradation
    • Donahue J.P., Vetter M.L., Mukhtar N.A., D'Aquila R.T. The HIV-1 motif is necessary for human APOBEC3G binding and degradation. Virology 2008, 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
  • 42
    • 0026786712 scopus 로고
    • Cell-free transmission of Vif mutants of HIV-1
    • Fan L., Peden K. Cell-free transmission of Vif mutants of HIV-1. Virology 1992, 190:19-29.
    • (1992) Virology , vol.190 , pp. 19-29
    • Fan, L.1    Peden, K.2
  • 44
    • 0029961360 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins
    • Fouchier R.A., Simon J.H., Jaffe A.B., Malim M.H. Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins. J. Virol. 1996, 70:8263-8269.
    • (1996) J. Virol. , vol.70 , pp. 8263-8269
    • Fouchier, R.A.1    Simon, J.H.2    Jaffe, A.B.3    Malim, M.H.4
  • 45
    • 67649669726 scopus 로고    scopus 로고
    • Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA
    • Friew Y.N., Boyko V., Hu W.S., Pathak V.K. Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA. Retrovirology 2009, 6:56.
    • (2009) Retrovirology , vol.6 , pp. 56
    • Friew, Y.N.1    Boyko, V.2    Hu, W.S.3    Pathak, V.K.4
  • 46
    • 3242702452 scopus 로고    scopus 로고
    • Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation
    • Fujita M., Akari H., Sakurai A., Yoshida A., Chiba T., Tanaka K., Strebel K., Adachi A. Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation. Microbes Infect. 2004, 6:791-798.
    • (2004) Microbes Infect. , vol.6 , pp. 791-798
    • Fujita, M.1    Akari, H.2    Sakurai, A.3    Yoshida, A.4    Chiba, T.5    Tanaka, K.6    Strebel, K.7    Adachi, A.8
  • 47
    • 0037225677 scopus 로고    scopus 로고
    • Amino acid residues 88 and 89 in the central hydrophilic region of human immunodeficiency virus type 1 Vif are critical for viral infectivity by enhancing the steady-state expression of Vif
    • Fujita M., Sakurai A., Yoshida A., Miyaura M., Koyama A.H., Sakai K., Adachi A. Amino acid residues 88 and 89 in the central hydrophilic region of human immunodeficiency virus type 1 Vif are critical for viral infectivity by enhancing the steady-state expression of Vif. J. Virol. 2003, 77:1626-1632.
    • (2003) J. Virol. , vol.77 , pp. 1626-1632
    • Fujita, M.1    Sakurai, A.2    Yoshida, A.3    Miyaura, M.4    Koyama, A.H.5    Sakai, K.6    Adachi, A.7
  • 50
    • 0037630009 scopus 로고    scopus 로고
    • Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions
    • Gaddis N.C., Chertova E., Sheehy A.M., Henderson L.E., Malim M.H. Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. J. Virol. 2003, 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
  • 52
    • 40149092360 scopus 로고    scopus 로고
    • Role of APOBEC3G/F-mediated hypermutation in the control of human immunodeficiency virus type 1 in elite suppressors
    • Gandhi S.K., Siliciano J.D., Bailey J.R., Siliciano R.F., Blankson J.N. Role of APOBEC3G/F-mediated hypermutation in the control of human immunodeficiency virus type 1 in elite suppressors. J. Virol. 2008, 82:3125-3130.
    • (2008) J. Virol. , vol.82 , pp. 3125-3130
    • Gandhi, S.K.1    Siliciano, J.D.2    Bailey, J.R.3    Siliciano, R.F.4    Blankson, J.N.5
  • 53
    • 77958040891 scopus 로고    scopus 로고
    • Conformational analysis of a peptide approximating the HCCH motif in HIV-1 Vif
    • Giri K., Maynard E.L. Conformational analysis of a peptide approximating the HCCH motif in HIV-1 Vif. Biopolymers 2009, 92:417-425.
    • (2009) Biopolymers , vol.92 , pp. 417-425
    • Giri, K.1    Maynard, E.L.2
  • 54
    • 58149517747 scopus 로고    scopus 로고
    • Differential sensitivity of " old" versus " new" APOBEC3G to human immunodeficiency virus type 1 vif
    • Goila-Gaur R., Khan M.A., Miyagi E., Strebel K. Differential sensitivity of " old" versus " new" APOBEC3G to human immunodeficiency virus type 1 vif. J. Virol. 2009, 83:1156-1160.
    • (2009) J. Virol. , vol.83 , pp. 1156-1160
    • Goila-Gaur, R.1    Khan, M.A.2    Miyagi, E.3    Strebel, K.4
  • 55
    • 0029861076 scopus 로고    scopus 로고
    • Role of Vif in human immunodeficiency virus type 1 reverse transcription
    • Goncalves J., Korin Y., Zack J., Gabuzda D. Role of Vif in human immunodeficiency virus type 1 reverse transcription. J. Virol. 1996, 70:8701-8709.
    • (1996) J. Virol. , vol.70 , pp. 8701-8709
    • Goncalves, J.1    Korin, Y.2    Zack, J.3    Gabuzda, D.4
  • 56
    • 48949084728 scopus 로고    scopus 로고
    • Functional domain organization of human APOBEC3G
    • Gooch B.D., Cullen B.R. Functional domain organization of human APOBEC3G. Virology 2008, 379:118-124.
    • (2008) Virology , vol.379 , pp. 118-124
    • Gooch, B.D.1    Cullen, B.R.2
  • 57
    • 33751206549 scopus 로고    scopus 로고
    • Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • Guo F., Cen S., Niu M., Saadatmand J., Kleiman L. Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. J. Virol. 2006, 80:11710-11722.
    • (2006) J. Virol. , vol.80 , pp. 11710-11722
    • Guo, F.1    Cen, S.2    Niu, M.3    Saadatmand, J.4    Kleiman, L.5
  • 58
    • 35148824006 scopus 로고    scopus 로고
    • The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA
    • Guo F., Cen S., Niu M., Yang Y., Gorelick R.J., Kleiman L. The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA. J. Virol. 2007, 81:11322-11331.
    • (2007) J. Virol. , vol.81 , pp. 11322-11331
    • Guo, F.1    Cen, S.2    Niu, M.3    Yang, Y.4    Gorelick, R.J.5    Kleiman, L.6
  • 59
    • 67749147464 scopus 로고    scopus 로고
    • Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) annealing to viral RNA in human immunodeficiency virus type 1
    • Guo F., Saadatmand J., Niu M., Kleiman L. Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) annealing to viral RNA in human immunodeficiency virus type 1. J. Virol. 2009, 83:8099-8107.
    • (2009) J. Virol. , vol.83 , pp. 8099-8107
    • Guo, F.1    Saadatmand, J.2    Niu, M.3    Kleiman, L.4
  • 60
    • 15744390742 scopus 로고    scopus 로고
    • The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain
    • Hache G., Liddament M.T., Harris R.S. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J. Biol. Chem. 2005, 280:10920-10924.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10920-10924
    • Hache, G.1    Liddament, M.T.2    Harris, R.S.3
  • 61
    • 58149374613 scopus 로고    scopus 로고
    • Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H
    • Harari A., Ooms M., Mulder L.C., Simon V. Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H. J. Virol. 2009, 83:295-303.
    • (2009) J. Virol. , vol.83 , pp. 295-303
    • Harari, A.1    Ooms, M.2    Mulder, L.C.3    Simon, V.4
  • 64
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • He Z., Zhang W., Chen G., Xu R., Yu X.F. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J. Mol. Biol. 2008, 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
  • 65
    • 66749141973 scopus 로고    scopus 로고
    • Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors
    • Henriet S., Mercenne G., Bernacchi S., Paillart J.C., Marquet R. Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors. Microbiol. Mol. Biol. Rev. 2009, 73:211-232.
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 211-232
    • Henriet, S.1    Mercenne, G.2    Bernacchi, S.3    Paillart, J.C.4    Marquet, R.5
  • 67
    • 0028200823 scopus 로고
    • Role of vif during packing of the core of HIV-1
    • Hoglund S., Ohagen A., Lawrence K., Gabuzda D. Role of vif during packing of the core of HIV-1. Virology 1994, 201:349-355.
    • (1994) Virology , vol.201 , pp. 349-355
    • Hoglund, S.1    Ohagen, A.2    Lawrence, K.3    Gabuzda, D.4
  • 69
    • 33847625391 scopus 로고    scopus 로고
    • APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G
    • Holmes R.K., Koning F.A., Bishop K.N., Malim M.H. APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J. Biol. Chem. 2007, 282:2587-2595.
    • (2007) J. Biol. Chem. , vol.282 , pp. 2587-2595
    • Holmes, R.K.1    Koning, F.A.2    Bishop, K.N.3    Malim, M.H.4
  • 71
    • 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., Malim M.H. Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation. J. Virol. 2007, 81:3807-3815.
    • (2007) J. Virol. , vol.81 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 74
    • 33744929618 scopus 로고    scopus 로고
    • Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect
    • Iwatani Y., Takeuchi H., Strebel K., Levin J.G. Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect. J. Virol. 2006, 80:5992-6002.
    • (2006) J. Virol. , vol.80 , pp. 5992-6002
    • Iwatani, Y.1    Takeuchi, H.2    Strebel, K.3    Levin, J.G.4
  • 76
    • 23844483865 scopus 로고    scopus 로고
    • APOBEC3G/CEM15 (hA3G) mRNA levels associate inversely with human immunodeficiency virus viremia
    • Jin X., Brooks A., Chen H., Bennett R., Reichman R., Smith H. APOBEC3G/CEM15 (hA3G) mRNA levels associate inversely with human immunodeficiency virus viremia. J. Virol. 2005, 79:11513-11516.
    • (2005) J. Virol. , vol.79 , pp. 11513-11516
    • Jin, X.1    Brooks, A.2    Chen, H.3    Bennett, R.4    Reichman, R.5    Smith, H.6
  • 77
    • 30344440118 scopus 로고    scopus 로고
    • Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G
    • Kaiser S.M., Emerman M. Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G. J. Virol. 2006, 80:875-882.
    • (2006) J. Virol. , vol.80 , pp. 875-882
    • Kaiser, S.M.1    Emerman, M.2
  • 78
    • 63449095109 scopus 로고    scopus 로고
    • Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells
    • Kamata M., Nagaoka Y., Chen I.S. Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells. PLoS Pathog. 2009, 5:e1000342.
    • (2009) PLoS Pathog. , vol.5
    • Kamata, M.1    Nagaoka, Y.2    Chen, I.S.3
  • 79
    • 36048964842 scopus 로고    scopus 로고
    • Production of infectious virus and degradation of APOBEC3G are separable functional properties of human immunodeficiency virus type 1 Vif
    • Kao S., Goila-Gaur R., Miyagi E., Khan M.A., Opi S., Takeuchi H., Strebel K. Production of infectious virus and degradation of APOBEC3G are separable functional properties of human immunodeficiency virus type 1 Vif. Virology 2007, 369:329-339.
    • (2007) Virology , vol.369 , pp. 329-339
    • Kao, S.1    Goila-Gaur, R.2    Miyagi, E.3    Khan, M.A.4    Opi, S.5    Takeuchi, H.6    Strebel, K.7
  • 80
    • 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., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K. 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. 2003, 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
  • 81
    • 18144374907 scopus 로고    scopus 로고
    • Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells
    • Kao S., Miyagi E., Khan M.A., Takeuchi H., Opi S., Goila-Gaur R., Strebel K. Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells. Retrovirology 2004, 1:27.
    • (2004) Retrovirology , vol.1 , pp. 27
    • Kao, S.1    Miyagi, E.2    Khan, M.A.3    Takeuchi, H.4    Opi, S.5    Goila-Gaur, R.6    Strebel, K.7
  • 82
    • 67649888378 scopus 로고    scopus 로고
    • Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase
    • Kataropoulou A., Bovolenta C., Belfiore A., Trabatti S., Garbelli A., Porcellini S., Lupo R., Maga G. Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase. Nucleic Acids Res. 2009, 37:3660-3669.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3660-3669
    • Kataropoulou, A.1    Bovolenta, C.2    Belfiore, A.3    Trabatti, S.4    Garbelli, A.5    Porcellini, S.6    Lupo, R.7    Maga, G.8
  • 84
    • 0034899286 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA
    • Khan M.A., Aberham C., Kao S., Akari H., Gorelick R., Bour S., Strebel K. Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA. J. Virol. 2001, 75:7252-7265.
    • (2001) J. Virol. , vol.75 , pp. 7252-7265
    • Khan, M.A.1    Aberham, C.2    Kao, S.3    Akari, H.4    Gorelick, R.5    Bour, S.6    Strebel, K.7
  • 85
    • 70749116130 scopus 로고    scopus 로고
    • Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization
    • Khan M.A., Goila-Gaur R., Kao S., Miyagi E., Walker R.C., Strebel K. Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization. Retrovirology 2009, 6:99.
    • (2009) Retrovirology , vol.6 , pp. 99
    • Khan, M.A.1    Goila-Gaur, R.2    Kao, S.3    Miyagi, E.4    Walker, R.C.5    Strebel, K.6
  • 86
    • 34548040898 scopus 로고    scopus 로고
    • Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions
    • Khan M.A., Goila-Gaur R., Opi S., Miyagi E., Takeuchi H., Kao S., Strebel K. Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions. Retrovirology 2007, 4:48.
    • (2007) Retrovirology , vol.4 , pp. 48
    • Khan, M.A.1    Goila-Gaur, R.2    Opi, S.3    Miyagi, E.4    Takeuchi, H.5    Kao, S.6    Strebel, K.7
  • 88
    • 13744255000 scopus 로고    scopus 로고
    • G→A hypermutation in protease and reverse transcriptase regions of human immunodeficiency virus type 1 residing in resting CD4+ T cells in vivo
    • Kieffer T.L., Kwon P., Nettles R.E., Han Y., Ray S.C., Siliciano R.F. G→A hypermutation in protease and reverse transcriptase regions of human immunodeficiency virus type 1 residing in resting CD4+ T cells in vivo. J. Virol. 2005, 79:1975-1980.
    • (2005) J. Virol. , vol.79 , pp. 1975-1980
    • Kieffer, T.L.1    Kwon, P.2    Nettles, R.E.3    Han, Y.4    Ray, S.C.5    Siliciano, R.F.6
  • 90
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-ElonginB-ElonginC complex is essential for Vif function
    • Kobayashi M., Takaori-Kondo A., Miyauchi Y., Iwai K., Uchiyama T. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-ElonginB-ElonginC complex is essential for Vif function. J. Biol. Chem. 2005, 280:18573-18578.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18573-18578
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3    Iwai, K.4    Uchiyama, T.5
  • 91
    • 69449103867 scopus 로고    scopus 로고
    • Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets
    • Koning F.A., Newman E.N., Kim E.Y., Kunstman K.J., Wolinsky S.M., Malim M.H. Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets. J. Virol. 2009, 83:9474-9485.
    • (2009) J. Virol. , vol.83 , pp. 9474-9485
    • Koning, F.A.1    Newman, E.N.2    Kim, E.Y.3    Kunstman, K.J.4    Wolinsky, S.M.5    Malim, M.H.6
  • 93
    • 33645862586 scopus 로고    scopus 로고
    • Endogenous factors enhance HIV infection of tissue naive CD4 T cells by stimulating high molecular mass APOBEC3G complex formation
    • Kreisberg J.F., Yonemoto W., Greene W.C. Endogenous factors enhance HIV infection of tissue naive CD4 T cells by stimulating high molecular mass APOBEC3G complex formation. J. Exp. Med. 2006, 203:865-870.
    • (2006) J. Exp. Med. , vol.203 , pp. 865-870
    • Kreisberg, J.F.1    Yonemoto, W.2    Greene, W.C.3
  • 95
    • 49149090397 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya
    • Land A.M., Ball T.B., Luo M., Pilon R., Sandstrom P., Embree J.E., Wachihi C., Kimani J., Plummer F.A. Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya. J. Virol. 2008, 82:8172-8182.
    • (2008) J. Virol. , vol.82 , pp. 8172-8182
    • Land, A.M.1    Ball, T.B.2    Luo, M.3    Pilon, R.4    Sandstrom, P.5    Embree, J.E.6    Wachihi, C.7    Kimani, J.8    Plummer, F.A.9
  • 96
    • 42449109442 scopus 로고    scopus 로고
    • Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1
    • Langlois M.A., Neuberger M.S. Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1. J. Virol. 2008, 82:4660-4664.
    • (2008) J. Virol. , vol.82 , pp. 4660-4664
    • Langlois, M.A.1    Neuberger, M.S.2
  • 97
    • 7444268898 scopus 로고    scopus 로고
    • Functional domains of APOBEC3G required for antiviral activity
    • Li J., Potash M.J., Volsky D.J. Functional domains of APOBEC3G required for antiviral activity. J. Cell Biochem. 2004, 92:560-572.
    • (2004) J. Cell Biochem. , vol.92 , pp. 560-572
    • Li, J.1    Potash, M.J.2    Volsky, D.J.3
  • 98
    • 72849138650 scopus 로고    scopus 로고
    • The range of human APOBEC3H sensitivity to lentiviral Vif proteins
    • Li M.M., Wu L.I., Emerman M. The range of human APOBEC3H sensitivity to lentiviral Vif proteins. J. Virol. 2009, 84:88-95.
    • (2009) J. Virol. , vol.84 , pp. 88-95
    • Li, M.M.1    Wu, L.I.2    Emerman, M.3
  • 99
    • 36148995875 scopus 로고    scopus 로고
    • APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
    • Li X.Y., Guo F., Zhang L., Kleiman L., Cen S. APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription. J. Biol. Chem. 2007, 282:32065-32074.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32065-32074
    • Li, X.Y.1    Guo, F.2    Zhang, L.3    Kleiman, L.4    Cen, S.5
  • 100
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament M.T., Brown W.L., Schumacher A.J., Harris R.S. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr. Biol. 2004, 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
  • 101
    • 0028805216 scopus 로고
    • The Vif protein of human and simian immunodeficiency viruses is packaged into virions and associates with viral core structures
    • Liu H., Wu X., Newman M., Shaw G.M., Hahn B.H., Kappes J.C. The Vif protein of human and simian immunodeficiency viruses is packaged into virions and associates with viral core structures. J. Virol. 1995, 69:7630-7638.
    • (1995) J. Virol. , vol.69 , pp. 7630-7638
    • Liu, H.1    Wu, X.2    Newman, M.3    Shaw, G.M.4    Hahn, B.H.5    Kappes, J.C.6
  • 102
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
    • Luo K., Liu B., Xiao Z., Yu Y., Yu X., Gorelick R., Yu X.F. Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging. J. Virol. 2004, 78:11841-11852.
    • (2004) J. Virol. , vol.78 , pp. 11841-11852
    • Luo, K.1    Liu, B.2    Xiao, Z.3    Yu, Y.4    Yu, X.5    Gorelick, R.6    Yu, X.F.7
  • 103
    • 34250857925 scopus 로고    scopus 로고
    • Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
    • Luo K., Wang T., Liu B., Tian C., Xiao Z., Kappes J., Yu X.F. Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J. Virol. 2007, 81:7238-7248.
    • (2007) J. Virol. , vol.81 , pp. 7238-7248
    • Luo, K.1    Wang, T.2    Liu, B.3    Tian, C.4    Xiao, Z.5    Kappes, J.6    Yu, X.F.7
  • 104
    • 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., Xiao Z., Ehrlich E., Yu Y., Liu B., Zheng S., Yu X.F. 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. USA 2005, 102:11444-11449.
    • (2005) Proc. Natl. Acad. Sci. USA , 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
  • 105
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • Madani N., Kabat D. An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. J. Virol. 1998, 72:10251-10255.
    • (1998) J. Virol. , vol.72 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 106
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins - ensuring viral survival in a hostile environment
    • Malim M.H., Emerman M. HIV-1 accessory proteins - ensuring viral survival in a hostile environment. Cell Host Microbe 2008, 3:388-398.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 107
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., Trono D. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 2003, 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
  • 108
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat B., Turelli P., Liao S., Trono D. A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J. Biol. Chem. 2004, 279:14481-14483.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 110
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M., Rose K.M., Kozak S.L., Kabat D. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 2003, 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
  • 112
    • 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., Goncalves J., Santa-Marta M., McPike M., Gabuzda D. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev. 2004, 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
  • 113
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A., Strack B., Ancuta P., Zhang C., McPike M., Gabuzda D. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 2004, 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
  • 114
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • Mehle A., Thomas E.R., Rajendran K.S., Gabuzda D. A zinc-binding region in Vif binds Cul5 and determines cullin selection. J. Biol. Chem. 2006, 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
  • 116
    • 38949106531 scopus 로고    scopus 로고
    • The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G
    • Miller J.H., Presnyak V., Smith H.C. The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G. Retrovirology 2007, 4:81.
    • (2007) Retrovirology , vol.4 , pp. 81
    • Miller, J.H.1    Presnyak, V.2    Smith, H.C.3
  • 117
    • 37049032574 scopus 로고    scopus 로고
    • Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1
    • Miyagi E., Opi S., Takeuchi H., Khan M., Goila-Gaur R., Kao S., Strebel K. Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1. J. Virol. 2007, 81:13346-13353.
    • (2007) J. Virol. , vol.81 , pp. 13346-13353
    • Miyagi, E.1    Opi, S.2    Takeuchi, H.3    Khan, M.4    Goila-Gaur, R.5    Kao, S.6    Strebel, K.7
  • 118
    • 44449093971 scopus 로고    scopus 로고
    • Cytidine deamination induced HIV-1 drug resistance
    • Mulder L.C., Harari A., Simon V. Cytidine deamination induced HIV-1 drug resistance. Proc. Natl. Acad. Sci. USA 2008, 105:5501-5506.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5501-5506
    • Mulder, L.C.1    Harari, A.2    Simon, V.3
  • 124
    • 0026544438 scopus 로고
    • Conservation of amino-acid sequence motifs in lentivirus Vif proteins
    • Oberste M.S., Gonda M.A. Conservation of amino-acid sequence motifs in lentivirus Vif proteins. Virus Genes 1992, 6:95-102.
    • (1992) Virus Genes , vol.6 , pp. 95-102
    • Oberste, M.S.1    Gonda, M.A.2
  • 125
    • 50849100134 scopus 로고    scopus 로고
    • Antiretroelement activity of APOBEC3H was lost twice in recent human evolution
    • OhAinle M., Kerns J.A., Li M.M., Malik H.S., Emerman M. Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host Microbe 2008, 4:249-259.
    • (2008) Cell Host Microbe , vol.4 , pp. 249-259
    • OhAinle, M.1    Kerns, J.A.2    Li, M.M.3    Malik, H.S.4    Emerman, M.5
  • 126
    • 33645760962 scopus 로고    scopus 로고
    • Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H
    • OhAinle M., Kerns J.A., Malik H.S., Emerman M. Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J. Virol. 2006, 80:3853-3862.
    • (2006) J. Virol. , vol.80 , pp. 3853-3862
    • OhAinle, M.1    Kerns, J.A.2    Malik, H.S.3    Emerman, M.4
  • 127
    • 34547130033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant
    • Opi S., Kao S., Goila-Gaur R., Khan M.A., Miyagi E., Takeuchi H., Strebel K. Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant. J. Virol. 2007, 81:8236-8246.
    • (2007) J. Virol. , vol.81 , pp. 8236-8246
    • Opi, S.1    Kao, S.2    Goila-Gaur, R.3    Khan, M.A.4    Miyagi, E.5    Takeuchi, H.6    Strebel, K.7
  • 128
    • 33748511879 scopus 로고    scopus 로고
    • Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation
    • Pace C., Keller J., Nolan D., James I., Gaudieri S., Moore C., Mallal S. Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation. J. Virol. 2006, 80:9259-9269.
    • (2006) J. Virol. , vol.80 , pp. 9259-9269
    • Pace, C.1    Keller, J.2    Nolan, D.3    James, I.4    Gaudieri, S.5    Moore, C.6    Mallal, S.7
  • 129
    • 33845505955 scopus 로고    scopus 로고
    • Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions
    • Paul I., Cui J., Maynard E.L. Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions. Proc. Natl. Acad. Sci. USA 2006, 103:18475-18480.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18475-18480
    • Paul, I.1    Cui, J.2    Maynard, E.L.3
  • 131
    • 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., Rajendran K.S., Brazier A.J., Gabuzda D. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J. Virol. 2009, 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
  • 132
    • 67749116433 scopus 로고    scopus 로고
    • Analysis of the percentage of human immunodeficiency virus type 1 sequences that are hypermutated and markers of disease progression in a longitudinal cohort, including one individual with a partially defective Vif
    • Piantadosi A., Humes D., Chohan B., McClelland R.S., Overbaugh J. Analysis of the percentage of human immunodeficiency virus type 1 sequences that are hypermutated and markers of disease progression in a longitudinal cohort, including one individual with a partially defective Vif. J. Virol. 2009, 83:7805-7814.
    • (2009) J. Virol. , vol.83 , pp. 7805-7814
    • Piantadosi, A.1    Humes, D.2    Chohan, B.3    McClelland, R.S.4    Overbaugh, J.5
  • 134
    • 33846555779 scopus 로고    scopus 로고
    • The APOBEC-2 crystal structure and functional implications for the deaminase AID
    • Prochnow C., Bransteitter R., Klein M.G., Goodman M.F., Chen X.S. The APOBEC-2 crystal structure and functional implications for the deaminase AID. Nature 2007, 445:447-451.
    • (2007) Nature , vol.445 , pp. 447-451
    • Prochnow, C.1    Bransteitter, R.2    Klein, M.G.3    Goodman, M.F.4    Chen, X.S.5
  • 135
    • 74249120676 scopus 로고    scopus 로고
    • Werner, Lise, Mlisana, Koleka, Abdool, Karim, Salim, S., Ndung'u, Thumbi, the CAPRISA Acute Infection Study Team, 2010. APOBEC3G expression is dysregulated in primary HIV-1 infection and polymorphic variants influence CD4+ T-cell counts and plasma viral load. AIDS 24
    • Reddy, K.W., Cheryl, A., Werner, Lise, Mlisana, Koleka, Abdool, Karim, Salim, S., Ndung'u, Thumbi, the CAPRISA Acute Infection Study Team, 2010. APOBEC3G expression is dysregulated in primary HIV-1 infection and polymorphic variants influence CD4+ T-cell counts and plasma viral load. AIDS 24, 195-204.
    • Reddy, K.W.1    Cheryl, A.2
  • 137
    • 63049108063 scopus 로고    scopus 로고
    • APOBEC3G induces a hypermutation gradient: purifying selection at multiple steps during HIV-1 replication results in levels of G-to-A mutations that are high in DNA, intermediate in cellular viral RNA, and low in virion RNA
    • Russell R.A., Moore M.D., Hu W.S., Pathak V.K. APOBEC3G induces a hypermutation gradient: purifying selection at multiple steps during HIV-1 replication results in levels of G-to-A mutations that are high in DNA, intermediate in cellular viral RNA, and low in virion RNA. Retrovirology 2009, 6:16.
    • (2009) Retrovirology , vol.6 , pp. 16
    • Russell, R.A.1    Moore, M.D.2    Hu, W.S.3    Pathak, V.K.4
  • 138
    • 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., Pathak V.K. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J. Virol. 2007, 81:8201-8210.
    • (2007) J. Virol. , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 139
    • 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., Smith J., Barr R., Bhattacharyya D., Pathak V.K. Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif. J. Virol. 2009, 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
  • 140
    • 33644764832 scopus 로고    scopus 로고
    • The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest
    • Sakai K., Dimas J., Lenardo M.J. The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest. Proc. Natl. Acad. Sci. USA 2006, 103:3369-3374.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3369-3374
    • Sakai, K.1    Dimas, J.2    Lenardo, M.J.3
  • 141
    • 15744387175 scopus 로고    scopus 로고
    • HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation
    • Santa-Marta M., da Silva F.A., Fonseca A.M., Goncalves J. HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation. J. Biol. Chem. 2005, 280:8765-8775.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8765-8775
    • Santa-Marta, M.1    da Silva, F.A.2    Fonseca, A.M.3    Goncalves, J.4
  • 142
    • 68749115269 scopus 로고    scopus 로고
    • APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection
    • Santoni de Sio F.R., Trono D. APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection. PLoS One 2009, 4:e6571.
    • (2009) PLoS One , vol.4
    • Santoni de Sio, F.R.1    Trono, D.2
  • 143
    • 19344362934 scopus 로고    scopus 로고
    • Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
    • Sawyer S.L., Emerman M., Malik H.S. Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G. PLoS Biol. 2004, 2:E275.
    • (2004) PLoS Biol. , vol.2
    • Sawyer, S.L.1    Emerman, M.2    Malik, H.S.3
  • 144
    • 5344222683 scopus 로고    scopus 로고
    • Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor
    • Schafer A., Bogerd H.P., Cullen B.R. Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor. Virology 2004, 328:163-168.
    • (2004) Virology , vol.328 , pp. 163-168
    • Schafer, A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 145
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • Schrofelbauer B., Chen D., Landau N.R. A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc. Natl. Acad. Sci. USA 2004, 101:3927-3932.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 146
    • 33744939997 scopus 로고    scopus 로고
    • Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G
    • Schrofelbauer B., Senger T., Manning G., Landau N.R. Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G. J. Virol. 2006, 80:5984-5991.
    • (2006) J. Virol. , vol.80 , pp. 5984-5991
    • Schrofelbauer, B.1    Senger, T.2    Manning, G.3    Landau, N.R.4
  • 147
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
    • Schrofelbauer B., Yu Q., Zeitlin S.G., Landau N.R. Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J. Virol. 2005, 79:10978-10987.
    • (2005) J. Virol. , vol.79 , pp. 10978-10987
    • Schrofelbauer, B.1    Yu, Q.2    Zeitlin, S.G.3    Landau, N.R.4
  • 148
    • 40149102165 scopus 로고    scopus 로고
    • The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction
    • Schumacher A.J., Hache G., Macduff D.A., Brown W.L., Harris R.S. The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction. J. Virol. 2008, 82:2652-2660.
    • (2008) J. Virol. , vol.82 , pp. 2652-2660
    • Schumacher, A.J.1    Hache, G.2    Macduff, D.A.3    Brown, W.L.4    Harris, R.S.5
  • 149
    • 77950845533 scopus 로고    scopus 로고
    • Polyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif
    • Shao Q., Wang Yudi, Hildreth James E.K., Liu Bindong Polyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif. J. Virol. 2010, 84:4840-4844.
    • (2010) J. Virol. , vol.84 , pp. 4840-4844
    • Shao, Q.1    Wang, Y.2    Hildreth, J.E.K.3    Liu, B.4
  • 150
    • 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., Gaddis N.C., Choi J.D., Malim M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002, 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
  • 151
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy A.M., Gaddis N.C., Malim M.H. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 2003, 9:1404-1407.
    • (2003) Nat. Med. , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 152
    • 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., Takaori-Kondo A., Kobayashi M., Abudu A., Fukunaga K., Uchiyama T. 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. 2003, 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
  • 153
    • 0029056704 scopus 로고
    • Aberrant Gag protein composition of a human immunodeficiency virus type 1 vif mutant produced in primary lymphocytes
    • Simm M., Shahabuddin M., Chao W., Allan J.S., Volsky D.J. Aberrant Gag protein composition of a human immunodeficiency virus type 1 vif mutant produced in primary lymphocytes. J. Virol. 1995, 69:4582-4586.
    • (1995) J. Virol. , vol.69 , pp. 4582-4586
    • Simm, M.1    Shahabuddin, M.2    Chao, W.3    Allan, J.S.4    Volsky, D.J.5
  • 154
    • 0033052695 scopus 로고    scopus 로고
    • Vif and the p55(Gag) polyprotein of human immunodeficiency virus type 1 are present in colocalizing membrane-free cytoplasmic complexes
    • Simon J.H., Carpenter E.A., Fouchier R.A., Malim M.H. Vif and the p55(Gag) polyprotein of human immunodeficiency virus type 1 are present in colocalizing membrane-free cytoplasmic complexes. J. Virol. 1999, 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
  • 155
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • Simon J.H., Gaddis N.C., Fouchier R.A., Malim M.H. Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nat. Med. 1998, 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
  • 156
    • 0029956256 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
    • Simon J.H., Malim M.H. The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. J. Virol. 1996, 70:5297-5305.
    • (1996) J. Virol. , vol.70 , pp. 5297-5305
    • Simon, J.H.1    Malim, M.H.2
  • 157
    • 0032169163 scopus 로고    scopus 로고
    • Virion incorporation of human immunodeficiency virus type-1 Vif is determined by intracellular expression level and may not be necessary for function
    • Simon J.H., Miller D.L., Fouchier R.A., Malim M.H. Virion incorporation of human immunodeficiency virus type-1 Vif is determined by intracellular expression level and may not be necessary for function. Virology 1998, 248:182-187.
    • (1998) Virology , vol.248 , pp. 182-187
    • Simon, J.H.1    Miller, D.L.2    Fouchier, R.A.3    Malim, M.H.4
  • 158
    • 67649888155 scopus 로고    scopus 로고
    • Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
    • Simon V., Zennou V., Murray D., Huang Y., Ho D.D., Bieniasz P.D. Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification. PLoS Pathog. 2005, 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
  • 160
    • 33847246310 scopus 로고    scopus 로고
    • Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H
    • Soros V.B., Yonemoto W., Greene W.C. Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H. PLoS Pathog. 2007, 3:e15.
    • (2007) PLoS Pathog. , vol.3
    • Soros, V.B.1    Yonemoto, W.2    Greene, W.C.3
  • 161
    • 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., Volsky D.J. Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1. J. Virol. 1993, 67:6322-6326.
    • (1993) J. Virol. , vol.67 , pp. 6322-6326
    • Sova, P.1    Volsky, D.J.2
  • 162
    • 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., Ehrlich E.S., Short L., Yu Y., Xiao Z., Yu X.F., Xiong Y. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J. Virol. 2008, 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
  • 163
    • 0025238945 scopus 로고
    • HIV-1 replication is controlled at the level of T cell activation and proviral integration
    • Stevenson M., Stanwick T.L., Dempsey M.P., Lamonica C.A. HIV-1 replication is controlled at the level of T cell activation and proviral integration. EMBO J. 1990, 9:1551-1560.
    • (1990) EMBO J. , vol.9 , pp. 1551-1560
    • Stevenson, M.1    Stanwick, T.L.2    Dempsey, M.P.3    Lamonica, C.A.4
  • 164
    • 33947518167 scopus 로고    scopus 로고
    • Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells
    • Stopak K.S., Chiu Y.L., Kropp J., Grant R.M., Greene W.C. Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells. J. Biol. Chem. 2007, 282:3539-3546.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3539-3546
    • Stopak, K.S.1    Chiu, Y.L.2    Kropp, J.3    Grant, R.M.4    Greene, W.C.5
  • 165
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak K., de Noronha C., Yonemoto W., Greene W.C. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 2003, 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
  • 167
    • 33750210516 scopus 로고    scopus 로고
    • Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication
    • Suspene R., Rusniok C., Vartanian J.P., Wain-Hobson S. Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication. Nucleic Acids Res. 2006, 34:4677-4684.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4677-4684
    • Suspene, R.1    Rusniok, C.2    Vartanian, J.P.3    Wain-Hobson, S.4
  • 169
    • 4143124683 scopus 로고    scopus 로고
    • Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs
    • Svarovskaia E.S., Xu H., Mbisa J.L., Barr R., Gorelick R.J., Ono A., Freed E.O., Hu W.S., Pathak V.K. Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. J. Biol. Chem. 2004, 279:35822-35828.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35822-35828
    • Svarovskaia, E.S.1    Xu, H.2    Mbisa, J.L.3    Barr, R.4    Gorelick, R.J.5    Ono, A.6    Freed, E.O.7    Hu, W.S.8    Pathak, V.K.9
  • 170
    • 33644752777 scopus 로고    scopus 로고
    • Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F
    • Tian C., Yu X., Zhang W., Wang T., Xu R., Yu X.F. Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J. Virol. 2006, 80:3112-3115.
    • (2006) J. Virol. , vol.80 , pp. 3112-3115
    • Tian, C.1    Yu, X.2    Zhang, W.3    Wang, T.4    Xu, R.5    Yu, X.F.6
  • 171
    • 0025977774 scopus 로고
    • Selection, recombination, and G-A hypermutation of human immunodeficiency virus type 1 genomes
    • Vartanian J.P., Meyerhans A., Asjo B., Wain-Hobson S. Selection, recombination, and G-A hypermutation of human immunodeficiency virus type 1 genomes. J. Virol. 1991, 65:1779-1788.
    • (1991) J. Virol. , vol.65 , pp. 1779-1788
    • Vartanian, J.P.1    Meyerhans, A.2    Asjo, B.3    Wain-Hobson, S.4
  • 172
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
    • von Schwedler U., Song J., Aiken C., Trono D. Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells. J. Virol. 1993, 67:4945-4955.
    • (1993) J. Virol. , vol.67 , pp. 4945-4955
    • von Schwedler, U.1    Song, J.2    Aiken, C.3    Trono, D.4
  • 173
    • 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., Khan M.A., Kao S., Goila-Gaur R., Miyagi E., Strebel K. 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. 2010, 84:5201-5211.
    • (2010) J. Virol. , vol.84 , pp. 5201-5211
    • Walker, R.C.1    Khan, M.A.2    Kao, S.3    Goila-Gaur, R.4    Miyagi, E.5    Strebel, K.6
  • 175
    • 36348962513 scopus 로고    scopus 로고
    • 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G
    • Wang T., Tian C., Zhang W., Luo K., Sarkis P.T., Yu L., Liu B., Yu Y., Yu X.F. 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G. J. Virol. 2007, 81:13112-13124.
    • (2007) J. Virol. , vol.81 , pp. 13112-13124
    • Wang, T.1    Tian, C.2    Zhang, W.3    Luo, K.4    Sarkis, P.T.5    Yu, L.6    Liu, B.7    Yu, Y.8    Yu, X.F.9
  • 176
    • 14844288923 scopus 로고    scopus 로고
    • Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: correlating function and subcellular localization
    • Wichroski M.J., Ichiyama K., Rana T.M. Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: correlating function and subcellular localization. J. Biol. Chem. 2005, 280:8387-8396.
    • (2005) J. Biol. Chem. , vol.280 , pp. 8387-8396
    • Wichroski, M.J.1    Ichiyama, K.2    Rana, T.M.3
  • 177
    • 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., Doehle B.P., Bogerd H.P., Cullen B.R. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 2004, 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
  • 178
    • 33845996549 scopus 로고    scopus 로고
    • Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
    • Xiao Z., Ehrlich E., Luo K., Xiong Y., Yu X.F. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J. 2007, 21:217-222.
    • (2007) FASEB J. , vol.21 , pp. 217-222
    • Xiao, Z.1    Ehrlich, E.2    Luo, K.3    Xiong, Y.4    Yu, X.F.5
  • 179
    • 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., Ehrlich E., Yu Y., Luo K., Wang T., Tian C., Yu X.F. Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. Virology 2006, 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
  • 181
    • 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., Svarovskaia E.S., Barr R., Zhang Y., Khan M.A., Strebel K., Pathak V.K. 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 2004, 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
  • 182
    • 54049112596 scopus 로고    scopus 로고
    • Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F
    • Yamashita T., Kamada K., Hatcho K., Adachi A., Nomaguchi M. Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F. Microbes Infect. 2008, 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
  • 183
    • 75149172243 scopus 로고    scopus 로고
    • Status of APOBEC3G/F in cells and progeny virions modulated by Vif determines HIV-1 infectivity
    • Yamashita T., Nomaguchi M., Miyake A., Uchiyama T., Adachi A. Status of APOBEC3G/F in cells and progeny virions modulated by Vif determines HIV-1 infectivity. Microbes Infect. 2010, 12:166-171.
    • (2010) Microbes Infect. , vol.12 , pp. 166-171
    • Yamashita, T.1    Nomaguchi, M.2    Miyake, A.3    Uchiyama, T.4    Adachi, A.5
  • 184
    • 34249671724 scopus 로고    scopus 로고
    • Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA
    • Yang B., Chen K., Zhang C., Huang S., Zhang H. Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA. J. Biol. Chem. 2007, 282:11667-11675.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11667-11675
    • Yang, B.1    Chen, K.2    Zhang, C.3    Huang, S.4    Zhang, H.5
  • 185
    • 0037458718 scopus 로고    scopus 로고
    • Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins
    • Yang B., Gao L., Li L., Lu Z., Fan X., Patel C.A., Pomerantz R.J., DuBois G.C., Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. J. Biol. Chem. 2003, 278:6596-6602.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6596-6602
    • Yang, B.1    Gao, L.2    Li, L.3    Lu, Z.4    Fan, X.5    Patel, C.A.6    Pomerantz, R.J.7    DuBois, G.C.8    Zhang, H.9
  • 186
    • 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., Sun Y., Zhang H. The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J. Biol. Chem. 2001, 276:4889-4893.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4889-4893
    • Yang, S.1    Sun, Y.2    Zhang, H.3
  • 188
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X., Yu Y., Liu B., Luo K., Kong W., Mao P., Yu X.F. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003, 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
  • 189
    • 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., Xiao Z., Ehrlich E.S., Yu X., Yu X.F. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev. 2004, 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
  • 190
    • 0025342694 scopus 로고
    • HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure
    • Zack J.A., Arrigo S.J., Weitsman S.R., Go A.S., Haislip A., Chen I.S. HIV-1 entry into quiescent primary lymphocytes: molecular analysis reveals a labile, latent viral structure. Cell 1990, 61:213-222.
    • (1990) Cell , vol.61 , pp. 213-222
    • Zack, J.A.1    Arrigo, S.J.2    Weitsman, S.R.3    Go, A.S.4    Haislip, A.5    Chen, I.S.6
  • 191
    • 33646508336 scopus 로고    scopus 로고
    • Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates
    • Zennou V., Bieniasz P.D. Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates. Virology 2006, 349:31-40.
    • (2006) Virology , vol.349 , pp. 31-40
    • Zennou, V.1    Bieniasz, P.D.2
  • 192
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou V., Perez-Caballero D., Gottlinger H., Bieniasz P.D. APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J. Virol. 2004, 78:12058-12061.
    • (2004) J. Virol. , vol.78 , pp. 12058-12061
    • Zennou, V.1    Perez-Caballero, D.2    Gottlinger, H.3    Bieniasz, P.D.4
  • 193
    • 0033863969 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process
    • Zhang H., Pomerantz R.J., Dornadula G., Sun Y. Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process. J. Virol. 2000, 74:8252-8261.
    • (2000) J. Virol. , vol.74 , pp. 8252-8261
    • Zhang, H.1    Pomerantz, R.J.2    Dornadula, G.3    Sun, Y.4
  • 194
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., Gao L. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 2003, 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
  • 196
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng Y.H., Irwin D., Kurosu T., Tokunaga K., Sata T., Peterlin B.M. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J. Virol. 2004, 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.