메뉴 건너뛰기




Volumn 22, Issue 5, 2014, Pages 668-684

Structure-guided analysis of the human APOBEC3-HIV restrictome

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3; CYTOSINE DEAMINASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; URACIL; VIF PROTEIN; VIRUS PROTEIN; APOBEC3 PROTEIN, HUMAN; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84899956157     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.02.011     Document Type: Review
Times cited : (57)

References (168)
  • 1
    • 84878155868 scopus 로고    scopus 로고
    • Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase
    • M.B. Adolph, J. Webb, and L. Chelico Retroviral restriction factor APOBEC3G delays the initiation of DNA synthesis by HIV-1 reverse transcriptase PLoS ONE 8 2013 e64196
    • (2013) PLoS ONE , vol.8 , pp. 64196
    • Adolph, M.B.1    Webb, J.2    Chelico, L.3
  • 4
    • 0027723189 scopus 로고
    • Apolipoprotein B mRNA editing in vitro is a zinc-dependent process
    • C. Barnes, and H.C. Smith Apolipoprotein B mRNA editing in vitro is a zinc-dependent process Biochem. Biophys. Res. Commun. 197 1993 1410 1414
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1410-1414
    • Barnes, C.1    Smith, H.C.2
  • 6
    • 57749120452 scopus 로고    scopus 로고
    • APOBEC3G subunits self-associate via the C-terminal deaminase domain
    • R.P. Bennett, J.D. Salter, X. Liu, J.E. Wedekind, and H.C. Smith APOBEC3G subunits self-associate via the C-terminal deaminase domain J. Biol. Chem. 283 2008 33329 33336
    • (2008) J. Biol. Chem. , vol.283 , pp. 33329-33336
    • Bennett, R.P.1    Salter, J.D.2    Liu, X.3    Wedekind, J.E.4    Smith, H.C.5
  • 7
    • 0029763293 scopus 로고    scopus 로고
    • Positional cloning of the mouse retrovirus restriction gene Fv1
    • S. Best, P. Le Tissier, G. Towers, and J.P. Stoye Positional cloning of the mouse retrovirus restriction gene Fv1 Nature 382 1996 826 829
    • (1996) Nature , vol.382 , pp. 826-829
    • Best, S.1    Le Tissier, P.2    Towers, G.3    Stoye, J.P.4
  • 8
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2.3 A crystal structure of an enzyme: Transition-state analog complex
    • L. Betts, S. Xiang, S.A. Short, R. Wolfenden, and C.W. Carter Jr. Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex J. Mol. Biol. 235 1994 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, Jr.C.W.5
  • 9
    • 84855982190 scopus 로고    scopus 로고
    • The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H
    • M. Binka, M. Ooms, M. Steward, and V. Simon The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H J. Virol. 86 2012 49 59
    • (2012) J. Virol. , vol.86 , pp. 49-59
    • Binka, M.1    Ooms, M.2    Steward, M.3    Simon, V.4
  • 10
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • K.N. Bishop, R.K. Holmes, and M.H. Malim Antiviral potency of APOBEC proteins does not correlate with cytidine deamination J. Virol. 80 2006 8450 8458
    • (2006) J. Virol. , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 12
    • 34249892197 scopus 로고    scopus 로고
    • The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains
    • H.P. Bogerd, H.L. Wiegand, B.P. Doehle, and B.R. Cullen The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains Virology 364 2007 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
  • 14
    • 70349335267 scopus 로고    scopus 로고
    • The current structural and functional understanding of APOBEC deaminases
    • R. Bransteitter, C. Prochnow, and X.S. Chen The current structural and functional understanding of APOBEC deaminases Cell. Mol. Life Sci. 66 2009 3137 3147
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3137-3147
    • Bransteitter, R.1    Prochnow, C.2    Chen, X.S.3
  • 15
    • 70450181508 scopus 로고    scopus 로고
    • Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition
    • Y. Bulliard, P. Turelli, U.F. Röhrig, V. Zoete, B. Mangeat, O. Michielin, and D. Trono Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition J. Virol. 83 2009 12611 12621
    • (2009) J. Virol. , vol.83 , pp. 12611-12621
    • Bulliard, Y.1    Turelli, P.2    Röhrig, U.F.3    Zoete, V.4    Mangeat, B.5    Michielin, O.6    Trono, D.7
  • 16
    • 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
    • A. Burnett, and P. Spearman 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. 81 2007 5000 5013
    • (2007) J. Virol. , vol.81 , pp. 5000-5013
    • Burnett, A.1    Spearman, P.2
  • 18
    • 84883356320 scopus 로고    scopus 로고
    • Evidence for APOBEC3B mutagenesis in multiple human cancers
    • M.B. Burns, N.A. Temiz, and R.S. Harris Evidence for APOBEC3B mutagenesis in multiple human cancers Nat. Genet. 45 2013 977 983
    • (2013) Nat. Genet. , vol.45 , pp. 977-983
    • Burns, M.B.1    Temiz, N.A.2    Harris, R.S.3
  • 21
    • 0034699898 scopus 로고    scopus 로고
    • Adverse effects of antiretroviral therapy
    • A. Carr, and D.A. Cooper Adverse effects of antiretroviral therapy Lancet 356 2000 1423 1430
    • (2000) Lancet , vol.356 , pp. 1423-1430
    • Carr, A.1    Cooper, D.A.2
  • 24
    • 84871943090 scopus 로고    scopus 로고
    • APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages
    • C. Chaipan, J.L. Smith, W.-S. Hu, and V.K. Pathak APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages J. Virol. 87 2013 444 453
    • (2013) J. Virol. , vol.87 , pp. 444-453
    • Chaipan, C.1    Smith, J.L.2    Hu, W.-S.3    Pathak, V.K.4
  • 26
    • 33745067722 scopus 로고    scopus 로고
    • APOBEC3G DNA deaminase acts processively 3′ - > 5′ on single-stranded DNA
    • L. Chelico, P. Pham, P. Calabrese, and M.F. Goodman APOBEC3G DNA deaminase acts processively 3′ - > 5′ on single-stranded DNA Nat. Struct. Mol. Biol. 13 2006 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
  • 27
    • 46649114007 scopus 로고    scopus 로고
    • A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV
    • L. Chelico, E.J. Sacho, D.A. Erie, and M.F. Goodman A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV J. Biol. Chem. 283 2008 13780 13791
    • (2008) J. Biol. Chem. , vol.283 , pp. 13780-13791
    • Chelico, L.1    Sacho, E.J.2    Erie, D.A.3    Goodman, M.F.4
  • 28
    • 77952399342 scopus 로고    scopus 로고
    • Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G
    • L. Chelico, C. Prochnow, D.A. Erie, X.S. Chen, and M.F. Goodman Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G J. Biol. Chem. 285 2010 16195 16205
    • (2010) J. Biol. Chem. , vol.285 , pp. 16195-16205
    • Chelico, L.1    Prochnow, C.2    Erie, D.A.3    Chen, X.S.4    Goodman, M.F.5
  • 30
    • 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
    • G. Chen, Z. He, T. Wang, R. Xu, and X.-F. Yu 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 2009 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
  • 31
    • 13444265938 scopus 로고    scopus 로고
    • Structure of human cytidine deaminase bound to a potent inhibitor
    • S.J. Chung, J.C. Fromme, and G.L. Verdine Structure of human cytidine deaminase bound to a potent inhibitor J. Med. Chem. 48 2005 658 660
    • (2005) J. Med. Chem. , vol.48 , pp. 658-660
    • Chung, S.J.1    Fromme, J.C.2    Verdine, G.L.3
  • 32
    • 0004131381 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • J.M. Coffin, S.H. Hughes, and H.E. Varmus Retroviruses 1997 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • (1997) Retroviruses
    • Coffin, J.M.1    Hughes, S.H.2    Varmus, H.E.3
  • 34
    • 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
    • Y. Dang, X. Wang, T. Zhou, I.A. York, and Y.-H. Zheng 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 2009 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
  • 35
    • 77956628186 scopus 로고    scopus 로고
    • Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity
    • Y. Dang, X. Wang, I.A. York, and Y.-H. Zheng Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity J. Virol. 84 2010 8561 8570
    • (2010) J. Virol. , vol.84 , pp. 8561-8570
    • Dang, Y.1    Wang, X.2    York, I.A.3    Zheng, Y.-H.4
  • 36
    • 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
    • Y. Dang, R.W. Davis, I.A. York, and Y.-H. Zheng Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity J. Virol. 84 2010 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
  • 37
    • 46549089412 scopus 로고    scopus 로고
    • The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
    • J.P. Donahue, M.L. Vetter, N.A. Mukhtar, and R.T. D'Aquila The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation Virology 377 2008 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
  • 38
    • 33645529880 scopus 로고    scopus 로고
    • Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses
    • C. Esnault, J. Millet, O. Schwartz, and T. Heidmann Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses Nucleic Acids Res. 34 2006 1522 1531
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1522-1531
    • Esnault, C.1    Millet, J.2    Schwartz, O.3    Heidmann, T.4
  • 39
    • 79953214104 scopus 로고    scopus 로고
    • Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain
    • Y. Feng, and L. Chelico Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain J. Biol. Chem. 286 2011 11415 11426
    • (2011) J. Biol. Chem. , vol.286 , pp. 11415-11426
    • Feng, Y.1    Chelico, L.2
  • 40
    • 84874759842 scopus 로고    scopus 로고
    • HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G
    • Y. Feng, R.P. Love, and L. Chelico HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G J. Biol. Chem. 288 2013 6083 6094
    • (2013) J. Biol. Chem. , vol.288 , pp. 6083-6094
    • Feng, Y.1    Love, R.P.2    Chelico, L.3
  • 42
    • 67649669726 scopus 로고    scopus 로고
    • Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA
    • Y.N. Friew, V. Boyko, W.-S. Hu, and V.K. Pathak Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA Retrovirology 6 2009 56
    • (2009) Retrovirology , vol.6 , pp. 56
    • Friew, Y.N.1    Boyko, V.2    Hu, W.-S.3    Pathak, V.K.4
  • 45
    • 0024429254 scopus 로고
    • Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells
    • D. Gheysen, E. Jacobs, F. de Foresta, C. Thiriart, M. Francotte, D. Thines, and M. De Wilde Assembly and release of HIV-1 precursor Pr55gag virus-like particles from recombinant baculovirus-infected insect cells Cell 59 1989 103 112
    • (1989) Cell , vol.59 , pp. 103-112
    • Gheysen, D.1    Jacobs, E.2    De Foresta, F.3    Thiriart, C.4    Francotte, M.5    Thines, D.6    De Wilde, M.7
  • 46
    • 84873028668 scopus 로고    scopus 로고
    • Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination
    • K. Gillick, D. Pollpeter, P. Phalora, E.-Y. Kim, S.M. Wolinsky, and M.H. Malim Suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4(+) T cells is associated with inhibition of processive reverse transcription as well as excessive cytidine deamination J. Virol. 87 2013 1508 1517
    • (2013) J. Virol. , vol.87 , pp. 1508-1517
    • Gillick, K.1    Pollpeter, D.2    Phalora, P.3    Kim, E.-Y.4    Wolinsky, S.M.5    Malim, M.H.6
  • 47
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Métoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 49
    • 33751206549 scopus 로고    scopus 로고
    • Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • F. Guo, S. Cen, M. Niu, J. Saadatmand, and L. Kleiman Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication J. Virol. 80 2006 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
  • 50
    • 35148824006 scopus 로고    scopus 로고
    • The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA
    • F. Guo, S. Cen, M. Niu, Y. Yang, R.J. Gorelick, and L. Kleiman The interaction of APOBEC3G with human immunodeficiency virus type 1 nucleocapsid inhibits tRNA3Lys annealing to viral RNA J. Virol. 81 2007 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
  • 51
    • 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
    • F. Guo, J. Saadatmand, M. Niu, and L. Kleiman Roles of Gag and NCp7 in facilitating tRNA(Lys)(3) Annealing to viral RNA in human immunodeficiency virus type 1 J. Virol. 83 2009 8099 8107
    • (2009) J. Virol. , vol.83 , pp. 8099-8107
    • Guo, F.1    Saadatmand, J.2    Niu, M.3    Kleiman, L.4
  • 53
    • 15744390742 scopus 로고    scopus 로고
    • The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain
    • G. Haché, M.T. Liddament, and R.S. Harris The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain J. Biol. Chem. 280 2005 10920 10924
    • (2005) J. Biol. Chem. , vol.280 , pp. 10920-10924
    • Haché, G.1    Liddament, M.T.2    Harris, R.S.3
  • 55
    • 0036863733 scopus 로고    scopus 로고
    • RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators
    • R.S. Harris, S.K. Petersen-Mahrt, and M.S. Neuberger RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators Mol. Cell 10 2002 1247 1253
    • (2002) Mol. Cell , vol.10 , pp. 1247-1253
    • Harris, R.S.1    Petersen-Mahrt, S.K.2    Neuberger, M.S.3
  • 58
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • Z. He, W. Zhang, G. Chen, R. Xu, and X.-F. Yu Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction J. Mol. Biol. 381 2008 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
  • 60
    • 33847625391 scopus 로고    scopus 로고
    • APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G
    • R.K. Holmes, F.A. Koning, K.N. Bishop, and M.H. Malim APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G J. Biol. Chem. 282 2007 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
  • 61
    • 0025635705 scopus 로고
    • Retroviral recombination and reverse transcription
    • W.S. Hu, and H.M. Temin Retroviral recombination and reverse transcription Science 250 1990 1227 1233
    • (1990) Science , vol.250 , pp. 1227-1233
    • Hu, W.S.1    Temin, H.M.2
  • 62
    • 80055105950 scopus 로고    scopus 로고
    • Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1
    • J.F. Hultquist, J.A. Lengyel, E.W. Refsland, R.S. LaRue, L. Lackey, W.L. Brown, and R.S. Harris Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1 J. Virol. 85 2011 11220 11234
    • (2011) J. Virol. , vol.85 , pp. 11220-11234
    • Hultquist, J.F.1    Lengyel, J.A.2    Refsland, E.W.3    Larue, R.S.4    Lackey, L.5    Brown, W.L.6    Harris, R.S.7
  • 63
    • 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
    • H. Huthoff, and M.H. Malim Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation J. Virol. 81 2007 3807 3815
    • (2007) J. Virol. , vol.81 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 69
    • 66349132212 scopus 로고    scopus 로고
    • Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance
    • P. Jern, R.A. Russell, V.K. Pathak, and J.M. Coffin Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance PLoS Pathog. 5 2009 e1000367
    • (2009) PLoS Pathog. , vol.5 , pp. 1000367
    • Jern, P.1    Russell, R.A.2    Pathak, V.K.3    Coffin, J.M.4
  • 70
    • 0037176913 scopus 로고    scopus 로고
    • Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution
    • E. Johansson, N. Mejlhede, J. Neuhard, and S. Larsen Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution Biochemistry 41 2002 2563 2570
    • (2002) Biochemistry , vol.41 , pp. 2563-2570
    • Johansson, E.1    Mejlhede, N.2    Neuhard, J.3    Larsen, S.4
  • 71
    • 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
    • S.M. Kaiser, and M. Emerman 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. 80 2006 875 882
    • (2006) J. Virol. , vol.80 , pp. 875-882
    • Kaiser, S.M.1    Emerman, M.2
  • 74
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • L.A. Kelley, and M.J.E. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 75
    • 84895549977 scopus 로고    scopus 로고
    • Viral tropism and antiretroviral drug resistance in HIV-1 subtype C-infected patients failing highly active antiretroviral therapy in Johannesburg, South Africa
    • I. Ketseoglou, A. Lukhwareni, K. Steegen, S. Carmona, W.S. Stevens, and M.A. Papathanasopoulos Viral tropism and antiretroviral drug resistance in HIV-1 subtype C-infected patients failing highly active antiretroviral therapy in Johannesburg, South Africa AIDS Res. Hum. Retroviruses 30 2013 289 293
    • (2013) AIDS Res. Hum. Retroviruses , vol.30 , pp. 289-293
    • Ketseoglou, I.1    Lukhwareni, A.2    Steegen, K.3    Carmona, S.4    Stevens, W.S.5    Papathanasopoulos, M.A.6
  • 77
    • 34548040898 scopus 로고    scopus 로고
    • Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions
    • M.A. Khan, R. Goila-Gaur, S. Opi, E. Miyagi, H. Takeuchi, S. Kao, and K. Strebel Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions Retrovirology 4 2007 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
  • 78
    • 70749116130 scopus 로고    scopus 로고
    • Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization
    • M.A. Khan, R. Goila-Gaur, S. Kao, E. Miyagi, R.C. Walker Jr., and K. Strebel Encapsidation of APOBEC3G into HIV-1 virions involves lipid raft association and does not correlate with APOBEC3G oligomerization Retrovirology 6 2009 99
    • (2009) Retrovirology , vol.6 , pp. 99
    • Khan, M.A.1    Goila-Gaur, R.2    Kao, S.3    Miyagi, E.4    Walker, Jr.R.C.5    Strebel, K.6
  • 80
    • 69249137076 scopus 로고    scopus 로고
    • A portable hot spot recognition loop transfers sequence preferences from APOBEC family members to activation-induced cytidine deaminase
    • R.M. Kohli, S.R. Abrams, K.S. Gajula, R.W. Maul, P.J. Gearhart, and J.T. Stivers A portable hot spot recognition loop transfers sequence preferences from APOBEC family members to activation-induced cytidine deaminase J. Biol. Chem. 284 2009 22898 22904
    • (2009) J. Biol. Chem. , vol.284 , pp. 22898-22904
    • Kohli, R.M.1    Abrams, S.R.2    Gajula, K.S.3    Maul, R.W.4    Gearhart, P.J.5    Stivers, J.T.6
  • 82
    • 84895509400 scopus 로고    scopus 로고
    • Prevalence of drug resistance in human immunodeficiency virus type 1 infected, treatment naïve children in Pune, India
    • M. Kumar, S. Sen, R.K. Gupta, D.N. Chaturbhuj, S.P. Tripathy, and R.S. Paranjape Prevalence of drug resistance in human immunodeficiency virus type 1 infected, treatment naïve children in Pune, India AIDS Res. Hum. Retroviruses 30 2014 294 298
    • (2014) AIDS Res. Hum. Retroviruses , vol.30 , pp. 294-298
    • Kumar, M.1    Sen, S.2    Gupta, R.K.3    Chaturbhuj, D.N.4    Tripathy, S.P.5    Paranjape, R.S.6
  • 84
    • 17144432313 scopus 로고    scopus 로고
    • Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities
    • M.-A. Langlois, R.C.L. Beale, S.G. Conticello, and M.S. Neuberger Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into their DNA target site specificities Nucleic Acids Res. 33 2005 1913 1923
    • (2005) Nucleic Acids Res. , vol.33 , pp. 1913-1923
    • Langlois, M.-A.1    Beale, R.C.L.2    Conticello, S.G.3    Neuberger, M.S.4
  • 88
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • D. Lecossier, F. Bouchonnet, F. Clavel, and A.J. Hance Hypermutation of HIV-1 DNA in the absence of the Vif protein Science 300 2003 1112
    • (2003) Science , vol.300 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 89
    • 84886890355 scopus 로고    scopus 로고
    • Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3G
    • M. Letko, G. Silvestri, B.H. Hahn, F. Bibollet-Ruche, O. Gokcumen, V. Simon, and M. Ooms Vif proteins from diverse primate lentiviral lineages use the same binding site in APOBEC3G J. Virol. 87 2013 11861 11871
    • (2013) J. Virol. , vol.87 , pp. 11861-11871
    • Letko, M.1    Silvestri, G.2    Hahn, B.H.3    Bibollet-Ruche, F.4    Gokcumen, O.5    Simon, V.6    Ooms, M.7
  • 90
    • 36148995875 scopus 로고    scopus 로고
    • APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
    • X.-Y. Li, F. Guo, L. Zhang, L. Kleiman, and S. Cen APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription J. Biol. Chem. 282 2007 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
  • 91
    • 84868035487 scopus 로고    scopus 로고
    • Prevalence and significance of HIV-1 drug resistance mutations among patients on antiretroviral therapy with detectable low-level viremia
    • J.Z. Li, S. Gallien, T.D. Do, J.N. Martin, S. Deeks, D.R. Kuritzkes, and H. Hatano Prevalence and significance of HIV-1 drug resistance mutations among patients on antiretroviral therapy with detectable low-level viremia Antimicrob. Agents Chemother. 56 2012 5998 6000
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 5998-6000
    • Li, J.Z.1    Gallien, S.2    Do, T.D.3    Martin, J.N.4    Deeks, S.5    Kuritzkes, D.R.6    Hatano, H.7
  • 93
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • M.T. Liddament, W.L. Brown, A.J. Schumacher, and R.S. Harris APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo Curr. Biol. 14 2004 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
  • 94
    • 84865791616 scopus 로고    scopus 로고
    • Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A
    • R.P. Love, H. Xu, and L. Chelico Biochemical analysis of hypermutation by the deoxycytidine deaminase APOBEC3A J. Biol. Chem. 287 2012 30812 30822
    • (2012) J. Biol. Chem. , vol.287 , pp. 30812-30822
    • Love, R.P.1    Xu, H.2    Chelico, L.3
  • 95
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
    • K. Luo, B. Liu, Z. Xiao, Y. Yu, X. Yu, R. Gorelick, and X.-F. Yu Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging J. Virol. 78 2004 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
  • 96
    • 34250857925 scopus 로고    scopus 로고
    • Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
    • K. Luo, T. Wang, B. Liu, C. Tian, Z. Xiao, J. Kappes, and X.-F. Yu Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation J. Virol. 81 2007 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
  • 97
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • N. Madani, and D. Kabat An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein J. Virol. 72 1998 10251 10255
    • (1998) J. Virol. , vol.72 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 98
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • B. Mangeat, P. Turelli, G. Caron, M. Friedli, L. Perrin, and D. Trono Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts Nature 424 2003 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
  • 99
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • B. Mangeat, P. Turelli, S. Liao, and D. Trono A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action J. Biol. Chem. 279 2004 14481 14483
    • (2004) J. Biol. Chem. , vol.279 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 101
    • 0034456735 scopus 로고    scopus 로고
    • Management of the adverse effects of antiretroviral therapy and medication adherence
    • B. Max, and R. Sherer Management of the adverse effects of antiretroviral therapy and medication adherence Clin. Infect. Dis. 30 Suppl 2 2000 S96 S116
    • (2000) Clin. Infect. Dis. , vol.30 , Issue.SUPPL. 2
    • Max, B.1    Sherer, R.2
  • 103
    • 77951441141 scopus 로고    scopus 로고
    • APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms
    • J.L. Mbisa, W. Bu, and V.K. Pathak APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms J. Virol. 84 2010 5250 5259
    • (2010) J. Virol. , vol.84 , pp. 5250-5259
    • Mbisa, J.L.1    Bu, W.2    Pathak, V.K.3
  • 104
    • 80052614833 scopus 로고    scopus 로고
    • Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity
    • W.M. McDougall, and H.C. Smith Direct evidence that RNA inhibits APOBEC3G ssDNA cytidine deaminase activity Biochem. Biophys. Res. Commun. 412 2011 612 617
    • (2011) Biochem. Biophys. Res. Commun. , vol.412 , pp. 612-617
    • McDougall, W.M.1    Smith, H.C.2
  • 105
    • 80052200560 scopus 로고    scopus 로고
    • Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes
    • W.M. McDougall, C. Okany, and H.C. Smith Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes J. Biol. Chem. 286 2011 30655 30661
    • (2011) J. Biol. Chem. , vol.286 , pp. 30655-30661
    • McDougall, W.M.1    Okany, C.2    Smith, H.C.3
  • 106
    • 36348946397 scopus 로고    scopus 로고
    • Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding
    • A. Mehle, H. Wilson, C. Zhang, A.J. Brazier, M. McPike, E. Pery, and D. Gabuzda Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding J. Virol. 81 2007 13235 13241
    • (2007) J. Virol. , vol.81 , pp. 13235-13241
    • Mehle, A.1    Wilson, H.2    Zhang, C.3    Brazier, A.J.4    McPike, M.5    Pery, E.6    Gabuzda, D.7
  • 108
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • K. Miyauchi, Y. Kim, O. Latinovic, V. Morozov, and G.B. Melikyan HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes Cell 137 2009 433 444
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 110
    • 84870608030 scopus 로고    scopus 로고
    • Running loose or getting lost: How HIV-1 counters and capitalizes on APOBEC3-induced mutagenesis through its Vif protein
    • C. Münk, B.-E.O. Jensen, J. Zielonka, D. Häussinger, and C. Kamp Running loose or getting lost: how HIV-1 counters and capitalizes on APOBEC3-induced mutagenesis through its Vif protein Viruses 4 2012 3132 3161
    • (2012) Viruses , vol.4 , pp. 3132-3161
    • Münk, C.1    Jensen, B.-E.O.2    Zielonka, J.3    Häussinger, D.4    Kamp, C.5
  • 113
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • S.J.D. Neil, T. Zang, and P.D. Bieniasz Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu Nature 451 2008 425 430
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.D.1    Zang, T.2    Bieniasz, P.D.3
  • 116
    • 84874574872 scopus 로고    scopus 로고
    • The resistance of human APOBEC3H to HIV-1 NL4-3 molecular clone is determined by a single amino acid in Vif
    • M. Ooms, M. Letko, M. Binka, and V. Simon The resistance of human APOBEC3H to HIV-1 NL4-3 molecular clone is determined by a single amino acid in Vif PLoS ONE 8 2013 e57744
    • (2013) PLoS ONE , vol.8 , pp. 57744
    • Ooms, M.1    Letko, M.2    Binka, M.3    Simon, V.4
  • 118
    • 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
    • E. Pery, K.S. Rajendran, A.J. Brazier, and D. Gabuzda 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 2009 2374 2381
    • (2009) J. Virol. , vol.83 , pp. 2374-2381
    • Pery, E.1    Rajendran, K.S.2    Brazier, A.J.3    Gabuzda, D.4
  • 119
    • 33846555779 scopus 로고    scopus 로고
    • The APOBEC-2 crystal structure and functional implications for the deaminase AID
    • C. Prochnow, R. Bransteitter, M.G. Klein, M.F. Goodman, and X.S. Chen The APOBEC-2 crystal structure and functional implications for the deaminase AID Nature 445 2007 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
  • 121
    • 65449141378 scopus 로고    scopus 로고
    • Dissecting APOBEC3G substrate specificity by nucleoside analog interference
    • J.W. Rausch, L. Chelico, M.F. Goodman, and S.F. Le Grice Dissecting APOBEC3G substrate specificity by nucleoside analog interference J. Biol. Chem. 284 2009 7047 7058
    • (2009) J. Biol. Chem. , vol.284 , pp. 7047-7058
    • Rausch, J.W.1    Chelico, L.2    Goodman, M.F.3    Le Grice, S.F.4
  • 122
    • 84864576348 scopus 로고    scopus 로고
    • Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n
    • E.W. Refsland, J.F. Hultquist, and R.S. Harris Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n PLoS Pathog. 8 2012 e1002800
    • (2012) PLoS Pathog. , vol.8 , pp. 1002800
    • Refsland, E.W.1    Hultquist, J.F.2    Harris, R.S.3
  • 125
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • R.A. Russell, and V.K. Pathak Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F J. Virol. 81 2007 8201 8210
    • (2007) J. Virol. , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 126
    • 68549099517 scopus 로고    scopus 로고
    • The contribution of the primer activation signal to differences between Gag- and NCp7-facilitated tRNA(Lys3) annealing in HIV-1
    • J. Saadatmand, M. Niu, L. Kleiman, and F. Guo The contribution of the primer activation signal to differences between Gag- and NCp7-facilitated tRNA(Lys3) annealing in HIV-1 Virology 391 2009 334 341
    • (2009) Virology , vol.391 , pp. 334-341
    • Saadatmand, J.1    Niu, M.2    Kleiman, L.3    Guo, F.4
  • 127
    • 77953769689 scopus 로고    scopus 로고
    • APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis
    • H.A. Sadler, M.D. Stenglein, R.S. Harris, and L.M. Mansky APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis J. Virol. 84 2010 7396 7404
    • (2010) J. Virol. , vol.84 , pp. 7396-7404
    • Sadler, H.A.1    Stenglein, M.D.2    Harris, R.S.3    Mansky, L.M.4
  • 128
    • 70449560591 scopus 로고    scopus 로고
    • A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function
    • J.D. Salter, J. Krucinska, J. Raina, H.C. Smith, and J.E. Wedekind A hydrodynamic analysis of APOBEC3G reveals a monomer-dimer-tetramer self-association that has implications for anti-HIV function Biochemistry 48 2009 10685 10687
    • (2009) Biochemistry , vol.48 , pp. 10685-10687
    • Salter, J.D.1    Krucinska, J.2    Raina, J.3    Smith, H.C.4    Wedekind, J.E.5
  • 129
    • 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
    • M. Santa-Marta, F.A. da Silva, A.M. Fonseca, and J. Goncalves 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. 280 2005 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
  • 131
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • B. Schröfelbauer, D. Chen, and N.R. Landau A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif) Proc. Natl. Acad. Sci. USA 101 2004 3927 3932
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3927-3932
    • Schröfelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 132
    • 40149102165 scopus 로고    scopus 로고
    • The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction
    • A.J. Schumacher, G. Haché, D.A. Macduff, W.L. Brown, and R.S. Harris The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction J. Virol. 82 2008 2652 2660
    • (2008) J. Virol. , vol.82 , pp. 2652-2660
    • Schumacher, A.J.1    Haché, G.2    Macduff, D.A.3    Brown, W.L.4    Harris, R.S.5
  • 133
  • 135
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • A.M. Sheehy, N.C. Gaddis, J.D. Choi, and M.H. Malim Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein Nature 418 2002 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
  • 136
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • A.M. Sheehy, N.C. Gaddis, and M.H. Malim The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif Nat. Med. 9 2003 1404 1407
    • (2003) Nat. Med. , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 137
    • 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
    • K. Shindo, A. Takaori-Kondo, M. Kobayashi, A. Abudu, K. Fukunaga, and T. Uchiyama The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity J. Biol. Chem. 278 2003 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
  • 138
    • 79952801601 scopus 로고    scopus 로고
    • Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G
    • L.S. Shlyakhtenko, A.Y. Lushnikov, M. Li, L. Lackey, R.S. Harris, and Y.L. Lyubchenko Atomic force microscopy studies provide direct evidence for dimerization of the HIV restriction factor APOBEC3G J. Biol. Chem. 286 2011 3387 3395
    • (2011) J. Biol. Chem. , vol.286 , pp. 3387-3395
    • Shlyakhtenko, L.S.1    Lushnikov, A.Y.2    Li, M.3    Lackey, L.4    Harris, R.S.5    Lyubchenko, Y.L.6
  • 141
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • J.H.M. Simon, N.C. Gaddis, R.A.M. Fouchier, and M.H. Malim Evidence for a newly discovered cellular anti-HIV-1 phenotype Nat. Med. 4 1998 1397 1400
    • (1998) Nat. Med. , vol.4 , pp. 1397-1400
    • Simon, J.H.M.1    Gaddis, N.C.2    Fouchier, R.A.M.3    Malim, M.H.4
  • 142
    • 84887276822 scopus 로고    scopus 로고
    • Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F
    • K.K. Siu, A. Sultana, F.C. Azimi, and J.E. Lee Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F Nat. Commun. 4 2013 2593
    • (2013) Nat. Commun. , vol.4 , pp. 2593
    • Siu, K.K.1    Sultana, A.2    Azimi, F.C.3    Lee, J.E.4
  • 143
    • 78649429705 scopus 로고    scopus 로고
    • Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif
    • J.L. Smith, and V.K. Pathak Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif J. Virol. 84 2010 12599 12608
    • (2010) J. Virol. , vol.84 , pp. 12599-12608
    • Smith, J.L.1    Pathak, V.K.2
  • 144
    • 0024652299 scopus 로고
    • Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase
    • B.-H. Song, and J. Neuhard Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase Mol. Gen. Genet. 216 1989 462 468
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 462-468
    • Song, B.-H.1    Neuhard, J.2
  • 145
    • 33847246310 scopus 로고    scopus 로고
    • Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H
    • V.B. Soros, W. Yonemoto, and W.C. Greene Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H PLoS Pathog. 3 2007 e15
    • (2007) PLoS Pathog. , vol.3 , pp. 15
    • Soros, V.B.1    Yonemoto, W.2    Greene, W.C.3
  • 147
    • 0023644926 scopus 로고
    • PH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane
    • B.S. Stein, S.D. Gowda, J.D. Lifson, R.C. Penhallow, K.G. Bensch, and E.G. Engleman pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane Cell 49 1987 659 668
    • (1987) Cell , vol.49 , pp. 659-668
    • Stein, B.S.1    Gowda, S.D.2    Lifson, J.D.3    Penhallow, R.C.4    Bensch, K.G.5    Engleman, E.G.6
  • 148
    • 33947518167 scopus 로고    scopus 로고
    • Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells
    • K.S. Stopak, Y.-L. Chiu, J. Kropp, R.M. Grant, and W.C. Greene Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells J. Biol. Chem. 282 2007 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
  • 149
    • 0029124391 scopus 로고
    • Genetic map of the region surrounding the retrovirus restriction locus, Fv1, on mouse chromosome 4
    • J.P. Stoye, N. Kaushik, S. Jeremiah, and S. Best Genetic map of the region surrounding the retrovirus restriction locus, Fv1, on mouse chromosome 4 Mamm. Genome 6 1995 31 36
    • (1995) Mamm. Genome , vol.6 , pp. 31-36
    • Stoye, J.P.1    Kaushik, N.2    Jeremiah, S.3    Best, S.4
  • 150
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys
    • M. Stremlau, C.M. Owens, M.J. Perron, M. Kiessling, P. Autissier, and J. Sodroski The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys Nature 427 2004 848 853
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5    Sodroski, J.6
  • 151
    • 33746917191 scopus 로고    scopus 로고
    • The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse
    • A.-H. Teh, M. Kimura, M. Yamamoto, N. Tanaka, I. Yamaguchi, and T. Kumasaka The 1.48 A resolution crystal structure of the homotetrameric cytidine deaminase from mouse Biochemistry 45 2006 7825 7833
    • (2006) Biochemistry , vol.45 , pp. 7825-7833
    • Teh, A.-H.1    Kimura, M.2    Yamamoto, M.3    Tanaka, N.4    Yamaguchi, I.5    Kumasaka, T.6
  • 153
    • 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
    • C. Tian, X. Yu, W. Zhang, T. Wang, R. Xu, and X.-F. Yu Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F J. Virol. 80 2006 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
  • 155
    • 37449021340 scopus 로고    scopus 로고
    • Interaction with 7SL RNA but not with HIV-1 genomic RNA or P bodies is required for APOBEC3F virion packaging
    • T. Wang, C. Tian, W. Zhang, P.T.N. Sarkis, and X.-F. Yu Interaction with 7SL RNA but not with HIV-1 genomic RNA or P bodies is required for APOBEC3F virion packaging J. Mol. Biol. 375 2008 1098 1112
    • (2008) J. Mol. Biol. , vol.375 , pp. 1098-1112
    • Wang, T.1    Tian, C.2    Zhang, W.3    Sarkis, P.T.N.4    Yu, X.-F.5
  • 157
    • 84861313985 scopus 로고    scopus 로고
    • The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication
    • X. Wang, Z. Ao, L. Chen, G. Kobinger, J. Peng, and X. Yao The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication J. Virol. 86 2012 3777 3786
    • (2012) J. Virol. , vol.86 , pp. 3777-3786
    • Wang, X.1    Ao, Z.2    Chen, L.3    Kobinger, G.4    Peng, J.5    Yao, X.6
  • 158
    • 33845972280 scopus 로고    scopus 로고
    • Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits
    • J.E. Wedekind, R. Gillilan, A. Janda, J. Krucinska, J.D. Salter, R.P. Bennett, J. Raina, and H.C. Smith Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits J. Biol. Chem. 281 2006 38122 38126
    • (2006) J. Biol. Chem. , vol.281 , pp. 38122-38126
    • Wedekind, J.E.1    Gillilan, R.2    Janda, A.3    Krucinska, J.4    Salter, J.D.5    Bennett, R.P.6    Raina, J.7    Smith, H.C.8
  • 159
    • 14844288923 scopus 로고    scopus 로고
    • Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: Correlating function and subcellular localization
    • M.J. Wichroski, K. Ichiyama, and T.M. Rana Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: correlating function and subcellular localization J. Biol. Chem. 280 2005 8387 8396
    • (2005) J. Biol. Chem. , vol.280 , pp. 8387-8396
    • Wichroski, M.J.1    Ichiyama, K.2    Rana, T.M.3
  • 160
    • 33845996549 scopus 로고    scopus 로고
    • Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
    • Z. Xiao, E. Ehrlich, K. Luo, Y. Xiong, and X.-F. Yu Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G FASEB J. 21 2007 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
  • 162
    • 54049112596 scopus 로고    scopus 로고
    • Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F
    • T. Yamashita, K. Kamada, K. Hatcho, A. Adachi, and M. Nomaguchi Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F Microbes Infect. 10 2008 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
  • 163
    • 34250186071 scopus 로고    scopus 로고
    • Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F
    • Y. Yang, F. Guo, S. Cen, and L. Kleiman Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F Virology 365 2007 92 100
    • (2007) Virology , vol.365 , pp. 92-100
    • Yang, Y.1    Guo, F.2    Cen, S.3    Kleiman, L.4
  • 165
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • H. Zhang, B. Yang, R.J. Pomerantz, C. Zhang, S.C. Arunachalam, and L. Gao The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA Nature 424 2003 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
  • 166
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction
    • W. Zhang, J. Du, S.L. Evans, Y. Yu, and X.-F. Yu T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction Nature 481 2012 376 379
    • (2012) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.-F.5
  • 167
    • 75449093805 scopus 로고    scopus 로고
    • A single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivity
    • A. Zhen, T. Wang, K. Zhao, Y. Xiong, and X.-F. Yu A single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivity J. Virol. 84 2010 1902 1911
    • (2010) J. Virol. , vol.84 , pp. 1902-1911
    • Zhen, A.1    Wang, T.2    Zhao, K.3    Xiong, Y.4    Yu, X.-F.5
  • 168
    • 84861313225 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC
    • T. Zuo, D. Liu, W. Lv, X. Wang, J. Wang, M. Lv, W. Huang, J. Wu, H. Zhang, and H. Jin et al. Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC J. Virol. 86 2012 5497 5507
    • (2012) J. Virol. , vol.86 , pp. 5497-5507
    • Zuo, T.1    Liu, D.2    Lv, W.3    Wang, X.4    Wang, J.5    Lv, M.6    Huang, W.7    Wu, J.8    Zhang, H.9    Jin, H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.