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Volumn 339, Issue 1, 2009, Pages 1-25

Host restriction of HIV-1 by APOBEC3 and viral evasion through Vif

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION INDUCED CYTIDINE DEAMINASE; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 1; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 2; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3A; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3B; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3C; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3DE; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3H; CYTIDINE DEAMINASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIF PROTEIN; APOBEC3 PROTEIN, HUMAN; CYTOSINE DEAMINASE; PROTEASOME; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77950487440     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-642-02175-6_1     Document Type: Review
Times cited : (22)

References (177)
  • 1
    • 41449116464 scopus 로고    scopus 로고
    • Vpr.A3A chimera inhibits HIV replication
    • Aguiar RS et al (2008) Vpr.A3A chimera inhibits HIV replication. J Biol Chem 283(5):2518-2525
    • (2008) J Biol Chem , vol.283 , Issue.5 , pp. 2518-2525
    • Aguiar, R.S.1
  • 2
    • 4544232464 scopus 로고    scopus 로고
    • APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
    • Alce TM, Popik W (2004) APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein. J Biol Chem 279(33):34083-34086
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 34083-34086
    • Alce, T.M.1    Popik, W.2
  • 3
    • 42749089384 scopus 로고    scopus 로고
    • APOBEC3G restricts early HIV-1 replication in the cytoplasm of target cells
    • Anderson JL, Hope TJ (2008) APOBEC3G restricts early HIV-1 replication in the cytoplasm of target cells. Virology 375(1):1-12
    • (2008) Virology , vol.375 , Issue.1 , pp. 1-12
    • Anderson, J.L.1    Hope, T.J.2
  • 4
    • 48649083907 scopus 로고    scopus 로고
    • Characterization of APOBEC3G binding to 7SL RNA
    • Bach D et al (2008) Characterization of APOBEC3G binding to 7SL RNA. Retrovirology 5:54
    • (2008) Retrovirology , vol.5 , pp. 54
    • Bach, D.1
  • 5
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogenous DNA base damage in mammalian cells
    • Barnes DE, Lindahl T (2004) Repair and genetic consequences of endogenous DNA base damage in mammalian cells. Annu Rev Genet 38:445-476
    • (2004) Annu Rev Genet , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 6
    • 34548779664 scopus 로고    scopus 로고
    • Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C
    • Baumert TF et al (2007) Hepatitis B virus DNA is subject to extensive editing by the human deaminase APOBEC3C. Hepatology 46(3):683-689
    • (2007) Hepatology , vol.46 , Issue.3 , pp. 683-689
    • Baumert, T.F.1
  • 7
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi R, Pandolfi PP (2007) Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol 8(12):1006-1016
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 8
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: A front-line defense against viral attack
    • Bieniasz PD (2004) Intrinsic immunity: a front-line defense against viral attack. Nat Immunol 5 (11):1109-1115
    • (2004) Nat Immunol , vol.5 , Issue.11 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 9
    • 0028965266 scopus 로고
    • Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporin A analog with activity against human immunodeficiency virus (HIV) type 1: Interference with HIV protein-cyclophilin A interactions
    • Billich A et al (1995) Mode of action of SDZ NIM 811, a nonimmunosuppressive cyclosporin A analog with activity against human immunodeficiency virus (HIV) type 1: interference with HIV protein-cyclophilin A interactions. J Virol 69(4):2451-2461
    • (1995) J Virol , vol.69 , Issue.4 , pp. 2451-2461
    • Billich, A.1
  • 10
    • 4143092717 scopus 로고    scopus 로고
    • Cytidine deamination of retroviral DNA by diverse APOBEC proteins
    • Bishop KN et al (2004) Cytidine deamination of retroviral DNA by diverse APOBEC proteins. Curr Biol 14(15):1392-1396
    • (2004) Curr Biol , vol.14 , Issue.15 , pp. 1392-1396
    • Bishop, K.N.1
  • 11
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop KN, Holmes RK, Malim MH (2006) Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J Virol 80(17):8450-8458
    • (2006) J Virol , vol.80 , Issue.17 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 12
    • 58149237802 scopus 로고    scopus 로고
    • APOBEC3G inhibits elongation of HIV-1 reverse transcripts
    • Bishop KN et al (2008) APOBEC3G inhibits elongation of HIV-1 reverse transcripts. PLoS Pathog 4(12):e1000231
    • (2008) PLoS Pathog , vol.4 , Issue.12
    • Bishop, K.N.1
  • 13
    • 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 HP et al (2004) A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor. Proc Natl Acad Sci USA 101 (11):3770-3774
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.11 , pp. 3770-3774
    • Bogerd, H.P.1
  • 14
    • 33745044396 scopus 로고    scopus 로고
    • Cellular inhibitors of long interspersed element 1 and Alu retrotransposi-tion
    • Bogerd HP et al (2006a) Cellular inhibitors of long interspersed element 1 and Alu retrotransposi-tion. Proc Natl Acad Sci USA 103(23):8780-8785
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.23 , pp. 8780-8785
    • Bogerd, H.P.1
  • 15
    • 31644442239 scopus 로고    scopus 로고
    • APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotran-sposon function in human cells
    • Bogerd HP et al (2006b) APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotran-sposon function in human cells. Nucleic Acids Res 34(1):89-95
    • (2006) Nucleic Acids Res , vol.34 , Issue.1 , pp. 89-95
    • Bogerd, H.P.1
  • 16
    • 33745541663 scopus 로고    scopus 로고
    • Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication
    • Bonvin M et al (2006) Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication. Hepatology 43(6):1364-1374
    • (2006) Hepatology , vol.43 , Issue.6 , pp. 1364-1374
    • Bonvin, M.1
  • 17
    • 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-depen-dent process requiring the NC basic linker
    • Burnett A, Spearman P (2007) APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-depen-dent process requiring the NC basic linker. J Virol 81(10):5000-5013
    • (2007) J Virol , vol.81 , Issue.10 , pp. 5000-5013
    • Burnett, A.1    Spearman, P.2
  • 18
    • 0027518205 scopus 로고
    • Kinetics of deoxyribonucleotide insertion and extension at abasic template lesions in different sequence contexts using HIV-1 reverse transcriptase
    • Cai H et al (1993) Kinetics of deoxyribonucleotide insertion and extension at abasic template lesions in different sequence contexts using HIV-1 reverse transcriptase. J Biol Chem 268 (231):23567-23572
    • (1993) J Biol Chem , vol.268 , Issue.231 , pp. 23567-23572
    • Cai, H.1
  • 19
    • 4043118380 scopus 로고    scopus 로고
    • The interaction between HIV-1 Gag and APOBEC3G
    • Cen S et al (2004) The interaction between HIV-1 Gag and APOBEC3G. J Biol Chem 279 (32):33177-33184
    • (2004) J Biol Chem , vol.279 , Issue.32 , pp. 33177-33184
    • Cen, S.1
  • 20
    • 0034850529 scopus 로고    scopus 로고
    • Hck SH3 domain-dependent abrogation of Nef-induced class 1 MHC down-regulation
    • Chang AH, O'Shaughnessy MV, Jirik FR (2001) Hck SH3 domain-dependent abrogation of Nef-induced class 1 MHC down-regulation. Eur J Immunol 31(8):2382-2387
    • (2001) Eur J Immunol , vol.31 , Issue.8 , pp. 2382-2387
    • Chang, A.H.1    O'Shaughnessy, M.V.2    Jirik, F.R.3
  • 21
    • 33644769083 scopus 로고    scopus 로고
    • APOBEC3A is a potent inhibitor of adeno-associated virus and retrotranspo-sons
    • Chen H et al (2006) APOBEC3A is a potent inhibitor of adeno-associated virus and retrotranspo-sons. Curr Biol 16(5):480-485
    • (2006) Curr Biol , vol.16 , Issue.5 , pp. 480-485
    • Chen, H.1
  • 22
    • 40449114441 scopus 로고    scopus 로고
    • Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
    • Chen KM et al (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452(7183):116-119
    • (2008) Nature , vol.452 , Issue.7183 , pp. 116-119
    • Chen, K.M.1
  • 23
    • 42649120310 scopus 로고    scopus 로고
    • The APOBEC3 cytidine deaminases: An innate defensive network opposing exogenous retroviruses and endogenous retroelements
    • Chiu YL, Greene WC (2008) The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu Rev Immunol 26:317-353
    • (2008) Annu Rev Immunol , vol.26 , pp. 317-353
    • Chiu, Y.L.1    Greene, W.C.2
  • 24
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells
    • Chiu YL et al (2005) Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature 435(7038):108-114
    • (2005) Nature , vol.435 , Issue.7038 , pp. 108-114
    • Chiu, Y.L.1
  • 25
    • 33750379905 scopus 로고    scopus 로고
    • High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition
    • Chiu YL et al (2006) High-molecular-mass APOBEC3G complexes restrict Alu retrotransposition. Proc Natl Acad Sci USA 103(42):15588-15593
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.42 , pp. 15588-15593
    • Chiu, Y.L.1
  • 26
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello SG, Harris RS, Neuberger MS (2003) The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr Biol 13(22):2009-2013
    • (2003) Curr Biol , vol.13 , Issue.22 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 27
    • 11844269804 scopus 로고    scopus 로고
    • Evolution of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases
    • Conticello SG et al (2005) Evolution of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases. Mol Biol Evol 22(2):367-377
    • (2005) Mol Biol Evol , vol.22 , Issue.2 , pp. 367-377
    • Conticello, S.G.1
  • 28
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang Y et al (2006) Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J Virol 80(21):10522-10533
    • (2006) J Virol , vol.80 , Issue.21 , pp. 10522-10533
    • Dang, Y.1
  • 29
    • 34347376505 scopus 로고    scopus 로고
    • HIV-1 Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system
    • Dehart JL et al (2007) HIV-1 Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system. Virol J 4(1):57
    • (2007) Virol J , vol.4 , Issue.1 , pp. 57
    • Dehart, J.L.1
  • 30
    • 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 JL et al (2008) 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 82(18):9265-9272
    • (2008) J Virol , vol.82 , Issue.18 , pp. 9265-9272
    • Dehart, J.L.1
  • 31
    • 33847244948 scopus 로고    scopus 로고
    • Resistance of human T cell leukemia virus type 1 to APOBEC3G restriction is mediated by elements in nucleocapsid
    • Derse D et al (2007) Resistance of human T cell leukemia virus type 1 to APOBEC3G restriction is mediated by elements in nucleocapsid. Proc Natl Acad Sci USA 104(8):2915-2920
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.8 , pp. 2915-2920
    • Derse, D.1
  • 32
    • 4344601964 scopus 로고    scopus 로고
    • HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles
    • Douaisi M et al (2004) HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles. Biochem Biophys Res Commun 321(3):566-573
    • (2004) Biochem Biophys Res Commun , vol.321 , Issue.3 , pp. 566-573
    • Douaisi, M.1
  • 33
    • 17144384021 scopus 로고    scopus 로고
    • Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases
    • Dutko JA et al (2005) Inhibition of a yeast LTR retrotransposon by human APOBEC3 cytidine deaminases. Curr Biol 15(7):661-666
    • (2005) Curr Biol , vol.15 , Issue.7 , pp. 661-666
    • Dutko, J.A.1
  • 34
    • 33645529880 scopus 로고    scopus 로고
    • Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses
    • Esnault C et al (2006) Dual inhibitory effects of APOBEC family proteins on retrotransposition of mammalian endogenous retroviruses. Nucleic Acids Res 34(5):1522-1531
    • (2006) Nucleic Acids Res , vol.34 , Issue.5 , pp. 1522-1531
    • Esnault, C.1
  • 35
    • 60549109045 scopus 로고    scopus 로고
    • Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G
    • Furukawa A et al (2009) Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G. Embo J 28(4):440-451
    • (2009) Embo J , vol.28 , Issue.4 , pp. 440-451
    • Furukawa, A.1
  • 36
    • 0026649561 scopus 로고
    • Role of vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes
    • Gabuzda DH et al (1992) Role of vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes. J Virol 66(11):6489-6495
    • (1992) J Virol , vol.66 , Issue.11 , pp. 6489-6495
    • Gabuzda, D.H.1
  • 37
    • 0041589542 scopus 로고    scopus 로고
    • Death by deamination: A novel host restriction system for HIV-1
    • Goff SP (2003) Death by deamination: a novel host restriction system for HIV-1. Cell 114 (3):281-283
    • (2003) Cell , vol.114 , Issue.3 , pp. 281-283
    • Goff, S.P.1
  • 38
    • 48949118733 scopus 로고    scopus 로고
    • HIV-1 Vif, APOBEC, and intrinsic immunity
    • Goila-Gaur R, Strebel K (2008) HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 5:51
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 39
    • 38949152689 scopus 로고    scopus 로고
    • HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexes
    • Goila-Gaur R et al (2008) HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexes. Virology 372(1):136-146
    • (2008) Virology , vol.372 , Issue.1 , pp. 136-146
    • Goila-Gaur, R.1
  • 40
    • 33751206549 scopus 로고    scopus 로고
    • Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • Guo F et al (2006) Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. J Virol 80(23):11710-11722
    • (2006) J Virol , vol.80 , Issue.23 , pp. 11710-11722
    • Guo, F.1
  • 41
    • 35148824006 scopus 로고    scopus 로고
    • The interaction of APOBEC3G with HIV-1 nucleocapsid inhibits tRNALys3 annealing to viral RNA
    • doi:10.1128/JVI.00162-07
    • Guo F, et al. (2007) The interaction of APOBEC3G with HIV-1 nucleocapsid inhibits tRNALys3 annealing to viral RNA. J Virol doi:10.1128/JVI.00162-07
    • (2007) J Virol
    • Guo, F.1
  • 42
    • 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 MT, Harris RS (2005) The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J Biol Chem 280(12):10920-10924
    • (2005) J Biol Chem , vol.280 , Issue.12 , pp. 10920-10924
    • Hache, G.1    Liddament, M.T.2    Harris, R.S.3
  • 43
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris RS, Liddament MT (2004) Retroviral restriction by APOBEC proteins. Nat Rev Immunol 4 (11):868-877
    • (2004) Nat Rev Immunol , vol.4 , Issue.11 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 44
    • 0036863733 scopus 로고    scopus 로고
    • RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators
    • Harris RS, Petersen-Mahrt SK, Neuberger MS (2002) RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Mol Cell 10(5):1247-1253
    • (2002) Mol Cell , vol.10 , Issue.5 , pp. 1247-1253
    • Harris, R.S.1    Petersen-Mahrt, S.K.2    Neuberger, M.S.3
  • 45
    • 0038681901 scopus 로고    scopus 로고
    • DNA deamination mediates innate immunity to retroviral infection
    • Harris RS et al (2003) DNA deamination mediates innate immunity to retroviral infection. Cell 113(6):803-809
    • (2003) Cell , vol.113 , Issue.6 , pp. 803-809
    • Harris, R.S.1
  • 46
    • 0035907306 scopus 로고    scopus 로고
    • The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein
    • Hassaine G et al (2001) The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein. J Biol Chem 276(20):16885-16893
    • (2001) J Biol Chem , vol.276 , Issue.20 , pp. 16885-16893
    • Hassaine, G.1
  • 47
    • 0028853961 scopus 로고
    • Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity
    • He J et al (1995) Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity. J Virol 69(11):6705-6711
    • (1995) J Virol , vol.69 , Issue.11 , pp. 6705-6711
    • He, J.1
  • 48
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • He Z et al (2008) Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J Mol Biol 381(4):1000-1011
    • (2008) J Mol Biol , vol.381 , Issue.4 , pp. 1000-1011
    • He, Z.1
  • 49
    • 55549098517 scopus 로고    scopus 로고
    • Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
    • Holden LG et al (2008) Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456(7218):121-124
    • (2008) Nature , vol.456 , Issue.7218 , pp. 121-124
    • Holden, L.G.1
  • 50
    • 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 RK et al (2007) APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J Biol Chem 4:2587-2595
    • (2007) J Biol Chem , vol.4 , pp. 2587-2595
    • Holmes, R.K.1
  • 51
    • 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 MH (2007) Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and virion encapsidation. J Virol 81(8):3807-3815
    • (2007) J Virol , vol.81 , Issue.8 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 52
    • 33744929618 scopus 로고    scopus 로고
    • Biochemical activities of highly purified, catalytically active human APOBEC3G: Correlation with antiviral effect
    • Iwatani Y et al (2006) Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect. J Virol 80(12):5992-6002
    • (2006) J Virol , vol.80 , Issue.12 , pp. 5992-6002
    • Iwatani, Y.1
  • 53
    • 37549025779 scopus 로고    scopus 로고
    • Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G
    • Iwatani Y et al (2007) Deaminase-independent inhibition of HIV-1 reverse transcription by APOBEC3G. Nucleic Acids Res 35(21):7096-7108
    • (2007) Nucleic Acids Res , vol.35 , Issue.21 , pp. 7096-7108
    • Iwatani, Y.1
  • 54
    • 0036200070 scopus 로고    scopus 로고
    • An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22
    • Jarmuz A et al (2002) An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79(3):285-296
    • (2002) Genomics , vol.79 , Issue.3 , pp. 285-296
    • Jarmuz, A.1
  • 55
    • 34648834022 scopus 로고    scopus 로고
    • Induction of antiviral cytidine deaminases does not explain the inhibition of hepatitis B virus replication by interferons
    • Jost S et al (2007) Induction of antiviral cytidine deaminases does not explain the inhibition of hepatitis B virus replication by interferons. J Virol 81(19):10588-10596
    • (2007) J Virol , vol.81 , Issue.19 , pp. 10588-10596
    • Jost, S.1
  • 56
    • 0029165291 scopus 로고
    • The human immunodeficiency virus type 1 vpr gene arrests infected T cells in the G2 + M phase of the cell cycle
    • Jowett JB et al (1995) The human immunodeficiency virus type 1 vpr gene arrests infected T cells in the G2 + M phase of the cell cycle. J Virol 69(10):6304-6313
    • (1995) J Virol , vol.69 , Issue.10 , pp. 6304-6313
    • Jowett, J.B.1
  • 57
    • 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 SM, Emerman M (2006) 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(2):875-882
    • (2006) J Virol , vol.80 , Issue.2 , pp. 875-882
    • Kaiser, S.M.1    Emerman, M.2
  • 58
    • 0022678249 scopus 로고
    • Identification of HTLV-III/LAV sor gene product and detection of antibodies in human sera
    • Kan NC et al (1986) Identification of HTLV-III/LAV sor gene product and detection of antibodies in human sera. Science 231(4745):1553-1555
    • (1986) Science , vol.231 , Issue.4745 , pp. 1553-1555
    • Kan, N.C.1
  • 59
    • 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 et al (2007) Production of infectious virus and degradation of APOBEC3G are separable functional properties of human immunodeficiency virus type 1 Vif. Virology 369(2):329-339
    • (2007) Virology , vol.369 , Issue.2 , pp. 329-339
    • Kao, S.1
  • 60
    • 20244381403 scopus 로고    scopus 로고
    • Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes
    • Khan MA et al (2005) Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes. J Virol 79(9):5870-5874
    • (2005) J Virol , vol.79 , Issue.9 , pp. 5870-5874
    • Khan, M.A.1
  • 61
    • 34548040898 scopus 로고    scopus 로고
    • Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions
    • Khan MA et al (2007) Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions. Retrovirology 4:48
    • (2007) Retrovirology , vol.4 , pp. 48
    • Khan, M.A.1
  • 62
    • 0037424364 scopus 로고    scopus 로고
    • Incorporation of uracil into minus strand DNA affects the specificity of plus strand synthesis initiation during lentiviral reverse transcription
    • Klarmann GJ et al (2003) Incorporation of uracil into minus strand DNA affects the specificity of plus strand synthesis initiation during lentiviral reverse transcription. J Biol Chem 278 (10):7902-7909
    • (2003) J Biol Chem , vol.278 , Issue.10 , pp. 7902-7909
    • Klarmann, G.J.1
  • 63
    • 3242732065 scopus 로고    scopus 로고
    • APOBEC3G targets specific virus species
    • Kobayashi M et al (2004) APOBEC3G targets specific virus species. J Virol 78(15):8238-8244
    • (2004) J Virol , vol.78 , Issue.15 , pp. 8238-8244
    • Kobayashi, M.1
  • 64
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function
    • Kobayashi M et al (2005) Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. J Biol Chem 280(19):18573-18578
    • (2005) J Biol Chem , vol.280 , Issue.19 , pp. 18573-18578
    • Kobayashi, M.1
  • 65
    • 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 JF, Yonemoto W, Greene WC (2006) Endogenous factors enhance HIV infection of tissue naive CD4 T cells by stimulating high molecular mass APOBEC3G complex formation. J Exp Med 203(4):865-870
    • (2006) J Exp Med , vol.203 , Issue.4 , pp. 865-870
    • Kreisberg, J.F.1    Yonemoto, W.2    Greene, W.C.3
  • 66
    • 42449109442 scopus 로고    scopus 로고
    • Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1
    • Langlois MA, Neuberger MS (2008) Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1. J Virol 82(9):4660-4664
    • (2008) J Virol , vol.82 , Issue.9 , pp. 4660-4664
    • Langlois, M.A.1    Neuberger, M.S.2
  • 67
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier D et al (2003) Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300(5622):1112
    • (2003) Science , vol.300 , Issue.5622 , pp. 1112
    • Lecossier, D.1
  • 68
    • 33846542981 scopus 로고    scopus 로고
    • Reconstitution of an infectious human endogenous retrovirus
    • Lee YN, Bieniasz PD (2007) Reconstitution of an infectious human endogenous retrovirus. PLoS Pathog 3(1):e10
    • (2007) PLoS Pathog , vol.3 , Issue.1
    • Lee, Y.N.1    Bieniasz, P.D.2
  • 69
    • 0022680624 scopus 로고
    • A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses
    • Lee TH et al (1986) A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses. Science 231(4745):1546-1549
    • (1986) Science , vol.231 , Issue.4745 , pp. 1546-1549
    • Lee, T.H.1
  • 70
    • 0033609149 scopus 로고    scopus 로고
    • Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages
    • Lee B et al (1999) Quantification of CD4, CCR5, and CXCR4 levels on lymphocyte subsets, dendritic cells, and differentially conditioned monocyte-derived macrophages. Proc Natl Acad Sci USA 96(9):5215-5220
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.9 , pp. 5215-5220
    • Lee, B.1
  • 71
    • 50149083663 scopus 로고    scopus 로고
    • Hypermutation of an ancient human retrovirus by APOBEC3G
    • Lee YN, Malim MH, Bieniasz PD (2008) Hypermutation of an ancient human retrovirus by APOBEC3G. J Virol 82(17):8762-8770
    • (2008) J Virol , vol.82 , Issue.17 , pp. 8762-8770
    • Lee, Y.N.1    Malim, M.H.2    Bieniasz, P.D.3
  • 72
    • 0035876374 scopus 로고    scopus 로고
    • Role of the non-homologous DNA end joining pathway in the early steps of retroviral infection
    • Li L et al (2001) Role of the non-homologous DNA end joining pathway in the early steps of retroviral infection. Embo J 20(12):3272-3281
    • (2001) Embo J , vol.20 , Issue.12 , pp. 3272-3281
    • Li, L.1
  • 73
    • 36148995875 scopus 로고    scopus 로고
    • APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
    • Li XY et al (2007) APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription. J Biol Chem 282(44):32065-32074
    • (2007) J Biol Chem , vol.282 , Issue.44 , pp. 32065-32074
    • Li, X.Y.1
  • 74
    • 0033526865 scopus 로고    scopus 로고
    • APOBEC-2, a cardiac-and skeletal muscle-specific member of the cytidine deaminase supergene family
    • Liao W et al (1999) APOBEC-2, a cardiac-and skeletal muscle-specific member of the cytidine deaminase supergene family. Biochem Biophys Res Commun 260(2):398-404
    • (1999) Biochem Biophys Res Commun , vol.260 , Issue.2 , pp. 398-404
    • Liao, W.1
  • 75
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament MT et al (2004) APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr Biol 14(15):1385-1391
    • (2004) Curr Biol , vol.14 , Issue.15 , pp. 1385-1391
    • Liddament, M.T.1
  • 76
    • 0842347676 scopus 로고    scopus 로고
    • Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G
    • Liu B et al (2004) Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G. J Virol 78(4):2072-2081
    • (2004) J Virol , vol.78 , Issue.4 , pp. 2072-2081
    • Liu, B.1
  • 77
    • 22544465590 scopus 로고    scopus 로고
    • Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase
    • Liu B et al (2005) Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol 79(15):9579-9587
    • (2005) J Virol , vol.79 , Issue.15 , pp. 9579-9587
    • Liu, B.1
  • 78
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleo-capsid is required for human APOBEC3G packaging
    • Luo K et al (2004) Amino-terminal region of the human immunodeficiency virus type 1 nucleo-capsid is required for human APOBEC3G packaging. J Virol 78(21):11841-11852
    • (2004) J Virol , vol.78 , Issue.21 , pp. 11841-11852
    • Luo, K.1
  • 79
    • 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 et al (2005) Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci USA 102(32):11444-11449
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.32 , pp. 11444-11449
    • Luo, K.1
  • 80
    • 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 et al (2007) Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J Virol 81 (13):7238-7248
    • (2007) J Virol , vol.81 , Issue.13 , pp. 7238-7248
    • Luo, K.1
  • 81
    • 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 (1998) An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. J Virol 72(12):10251-10255
    • (1998) J Virol , vol.72 , Issue.12 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 82
    • 0036839055 scopus 로고    scopus 로고
    • Implication of the lymphocyte-specific nuclear body protein Sp140 in an innate response to human immunodeficiency virus type 1
    • Madani N et al (2002) Implication of the lymphocyte-specific nuclear body protein Sp140 in an innate response to human immunodeficiency virus type 1. J Virol 76(21):11133-11138
    • (2002) J Virol , vol.76 , Issue.21 , pp. 11133-11138
    • Madani, N.1
  • 83
    • 23844500835 scopus 로고    scopus 로고
    • Extensive editing of a small fraction of human T-cell leukemia virus type 1 genomes by four APOBEC3 cytidine deaminases
    • Mahieux R et al (2005) Extensive editing of a small fraction of human T-cell leukemia virus type 1 genomes by four APOBEC3 cytidine deaminases. J Gen Virol 86(Pt 9):2489-2494
    • (2005) J Gen Virol , vol.86 , Issue.PART 9 , pp. 2489-2494
    • Mahieux, R.1
  • 84
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B et al (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424(6944):99-103
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1
  • 85
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat B et al (2004) A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J Biol Chem 279(15):14481-14483
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14481-14483
    • Mangeat, B.1
  • 86
    • 0033925801 scopus 로고    scopus 로고
    • The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 in vivo mutation rate
    • Mansky LM et al (2000) The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 In vivo mutation rate. J Virol 74(15):7039-7047
    • (2000) J Virol , vol.74 , Issue.15 , pp. 7039-7047
    • Mansky, L.M.1
  • 87
    • 0038107587 scopus 로고    scopus 로고
    • Species-specific exclusion of APOBEC3G from HIV-1 virions by vif
    • Mariani R et al (2003) Species-Specific Exclusion of APOBEC3G from HIV-1 Virions by Vif. Cell 114(1):21-31
    • (2003) Cell , vol.114 , Issue.1 , pp. 21-31
    • Mariani, R.1
  • 88
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M et al (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 9(11):1398-1403
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1398-1403
    • Marin, M.1
  • 89
    • 37849030910 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif functionally interacts with diverse APOBEC3 cytidine deaminases and moves with them between cytoplasmic sites of mRNA metabolism
    • Marin M et al (2008) Human immunodeficiency virus type 1 Vif functionally interacts with diverse APOBEC3 cytidine deaminases and moves with them between cytoplasmic sites of mRNA metabolism. J Virol 82(2):987-998
    • (2008) J Virol , vol.82 , Issue.2 , pp. 987-998
    • Marin, M.1
  • 90
    • 34250880090 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration
    • Mbisa JL et al (2007) Human immunodeficiency virus type 1 cDNAs produced in the presence of APOBEC3G exhibit defects in plus-strand DNA transfer and integration. J Virol 81 (13):7099-7110
    • (2007) J Virol , vol.81 , Issue.13 , pp. 7099-7110
    • Mbisa, J.L.1
  • 91
    • 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 et al (2004) Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev 18(23):2861-2866
    • (2004) Genes Dev , vol.18 , Issue.23 , pp. 2861-2866
    • Mehle, A.1
  • 92
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • Mehle A et al (2006) A zinc-binding region in Vif binds Cul5 and determines cullin selection. J Biol Chem 281(25):17259-17265
    • (2006) J Biol Chem , vol.281 , Issue.25 , pp. 17259-17265
    • Mehle, A.1
  • 93
    • 36348946397 scopus 로고    scopus 로고
    • Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding
    • Mehle A et al (2007) Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding. J Virol 81(23):13235-13241
    • (2007) J Virol , vol.81 , Issue.23 , pp. 13235-13241
    • Mehle, A.1
  • 94
    • 23344440307 scopus 로고    scopus 로고
    • Mice deficient in APOBEC2 and APOBEC3
    • Mikl MC et al (2005) Mice deficient in APOBEC2 and APOBEC3. Mol Cell Biol 25 (16):7270-7277
    • (2005) Mol Cell Biol , vol.25 , Issue.16 , pp. 7270-7277
    • Mikl, M.C.1
  • 95
    • 37049032574 scopus 로고    scopus 로고
    • Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1
    • Miyagi E et al (2007) Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1. J Virol 81(24):13346-13353
    • (2007) J Virol , vol.81 , Issue.24 , pp. 13346-13353
    • Miyagi, E.1
  • 96
    • 33746792780 scopus 로고    scopus 로고
    • APOBEC3 proteins inhibit human LINE-1 retrotransposition
    • Muckenfuss H et al (2006) APOBEC3 proteins inhibit human LINE-1 retrotransposition. J Biol Chem 281(31):22161-22172
    • (2006) J Biol Chem , vol.281 , Issue.31 , pp. 22161-22172
    • Muckenfuss, H.1
  • 97
    • 3042753796 scopus 로고    scopus 로고
    • Recent insights into HIV-1 Vif
    • Navarro F, Landau NR (2004) Recent insights into HIV-1 Vif. Curr Opin Immunol 16(4):477-482
    • (2004) Curr Opin Immunol , vol.16 , Issue.4 , pp. 477-482
    • Navarro, F.1    Landau, N.R.2
  • 98
    • 13844270834 scopus 로고    scopus 로고
    • Complementary function of the two catalytic domains of APOBEC3G
    • Navarro F et al (2005) Complementary function of the two catalytic domains of APOBEC3G. Virology 333(2):374-386
    • (2005) Virology , vol.333 , Issue.2 , pp. 374-386
    • Navarro, F.1
  • 99
    • 12544256041 scopus 로고    scopus 로고
    • Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
    • Newman EN et al (2005) Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Curr Biol 15(2):166-170
    • (2005) Curr Biol , vol.15 , Issue.2 , pp. 166-170
    • Newman, E.N.1
  • 100
    • 34247635482 scopus 로고    scopus 로고
    • Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G
    • Nguyen DH, Gummuluru S, Hu J (2007) Deamination-independent inhibition of hepatitis B virus reverse transcription by APOBEC3G. J Virol 81(9):4465-4472
    • (2007) J Virol , vol.81 , Issue.9 , pp. 4465-4472
    • Nguyen, D.H.1    Gummuluru, S.2    Hu, J.3
  • 101
    • 34548155661 scopus 로고    scopus 로고
    • Differential inhibition of long interspersed element 1 by APO-BEC3 does not correlate with high-molecular-mass-complex formation or P-body association
    • Niewiadomska AM et al (2007) Differential inhibition of long interspersed element 1 by APO-BEC3 does not correlate with high-molecular-mass-complex formation or P-body association. J Virol 81(17):9577-9583
    • (2007) J Virol , vol.81 , Issue.17 , pp. 9577-9583
    • Niewiadomska, A.M.1
  • 102
    • 14244254668 scopus 로고    scopus 로고
    • G to A hypermutation of hepatitis B virus
    • Noguchi C et al (2005) G to A hypermutation of hepatitis B virus. Hepatology 41(3):626-33
    • (2005) Hepatology , vol.41 , Issue.3 , pp. 626-633
    • Noguchi, C.1
  • 103
    • 50849100134 scopus 로고    scopus 로고
    • Antiretroelement activity of APOBEC3H was lost twice in recent human evolution
    • OhAinle M et al (2008) Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host Microbe 4(3):249-259
    • (2008) Cell Host Microbe , vol.4 , Issue.3 , pp. 249-259
    • Ohainle, M.1
  • 104
    • 33845195151 scopus 로고    scopus 로고
    • Human T cell leukemia virus type i is resistant to the antiviral effects of APOBEC3
    • Ohsugi T, Koito A (2007) Human T cell leukemia virus type I is resistant to the antiviral effects of APOBEC3. J Virol Methods 139(1):93-96
    • (2007) J Virol Methods , vol.139 , Issue.1 , pp. 93-96
    • Ohsugi, T.1    Koito, A.2
  • 105
    • 33645473868 scopus 로고    scopus 로고
    • 7SL RNA, but not the 54-kd signal recognition particle protein, is an abundant component of both infectious HIV-1 and minimal viruslike particles
    • Onafuwa-Nuga AA, Telesnitsky A, King SR (2006) 7SL RNA, but not the 54-kd signal recognition particle protein, is an abundant component of both infectious HIV-1 and minimal viruslike particles. Rna 12(4):542-546
    • (2006) Rna , vol.12 , Issue.4 , pp. 542-546
    • Onafuwa-Nuga, A.A.1    Telesnitsky, A.2    King, S.R.3
  • 106
    • 34547130033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant
    • Opi S et al (2007) Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant. J Virol 81(15):8236-8246
    • (2007) J Virol , vol.81 , Issue.15 , pp. 8236-8246
    • Opi, S.1
  • 107
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • Pickart CM (2004) Back to the future with ubiquitin. Cell 116(2):181-190
    • (2004) Cell , vol.116 , Issue.2 , pp. 181-190
    • Pickart, C.M.1
  • 108
    • 0037444303 scopus 로고    scopus 로고
    • Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles
    • Priet S et al (2003) Differential incorporation of uracil DNA glycosylase UNG2 into HIV-1, HIV-2, and SIV(MAC) viral particles. Virology 307(2):283-289
    • (2003) Virology , vol.307 , Issue.2 , pp. 283-289
    • Priet, S.1
  • 109
    • 25444527785 scopus 로고    scopus 로고
    • APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases predicted by computational analysis
    • Rogozin IB et al (2005) APOBEC4, a new member of the AID/APOBEC family of polynucleotide (deoxy) cytidine deaminases predicted by computational analysis. Cell Cycle 4(9):1281-1285
    • (2005) Cell Cycle , vol.4 , Issue.9 , pp. 1281-1285
    • Rogozin, I.B.1
  • 110
    • 4744374755 scopus 로고    scopus 로고
    • Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus
    • Rose KM et al (2004) Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus. J Biol Chem 279(40):41744-41749
    • (2004) J Biol Chem , vol.279 , Issue.40 , pp. 41744-41749
    • Rose, K.M.1
  • 111
    • 23044514707 scopus 로고    scopus 로고
    • APOBEC-mediated interference with hepadnavirus production
    • Rosler C et al (2005) APOBEC-mediated interference with hepadnavirus production. Hepatology 42(2):301-309
    • (2005) Hepatology , vol.42 , Issue.2 , pp. 301-309
    • Rosler, C.1
  • 112
    • 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 RA, Pathak VK (2007) Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J Virol 81 (15):8201-8210
    • (2007) J Virol , vol.81 , Issue.15 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 113
    • 59649118427 scopus 로고    scopus 로고
    • Distinct domains within apobec3g and apobec3f interact with separate regions of hiv-1 Vif
    • Russell RA et al (2008) Distinct domains within apobec3g and apobec3f interact with separate regions of hiv-1 Vif. J Virol 83(4):1992-2003
    • (2008) J Virol , vol.83 , Issue.4 , pp. 1992-2003
    • Russell, R.A.1
  • 114
    • 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 MJ (2006) The Vif and Vpr accessory proteins independently cause HIV-1-induced T cell cytopathicity and cell cycle arrest. Proc Natl Acad Sci USA 103(9):3369-3374
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.9 , pp. 3369-3374
    • Sakai, K.1    Dimas, J.2    Lenardo, M.J.3
  • 115
    • 0028878783 scopus 로고
    • Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4
    • Saksela K, Cheng G, Baltimore D (1995) Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4. Embo J 14(3):484-491
    • (1995) Embo J , vol.14 , Issue.3 , pp. 484-491
    • Saksela, K.1    Cheng, G.2    Baltimore, D.3
  • 116
    • 15744387175 scopus 로고    scopus 로고
    • HIV-1 Vif can directly inhibit APOBEC3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation
    • Santa-Marta M et al (2004) HIV-1 Vif can directly inhibit APOBEC3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation. J Biol Chem 280(10):8765-8775
    • (2004) J Biol Chem , vol.280 , Issue.10 , pp. 8765-8775
    • Santa-Marta, M.1
  • 117
    • 33747840698 scopus 로고    scopus 로고
    • HIV-1 Vif protein blocks the cytidine deaminase activity of B-cell specific AID in E. coli by a similar mechanism of action
    • Santa-Marta M et al (2007) HIV-1 Vif protein blocks the cytidine deaminase activity of B-cell specific AID in E. coli by a similar mechanism of action. Mol Immunol 44(4):583-590
    • (2007) Mol Immunol , vol.44 , Issue.4 , pp. 583-590
    • Santa-Marta, M.1
  • 118
    • 25444447177 scopus 로고    scopus 로고
    • APOBEC3G targets human T-cell leukemia virus type 1
    • Sasada A et al (2005) APOBEC3G targets human T-cell leukemia virus type 1. Retrovirology 2 (1):32
    • (2005) Retrovirology , vol.2 , Issue.1 , pp. 32
    • Sasada, A.1
  • 119
    • 19344362934 scopus 로고    scopus 로고
    • Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
    • Sawyer SL, Emerman M, Malik HS (2004) Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G. PLoS Biol 2(9):E275
    • (2004) PLoS Biol , vol.2 , Issue.9
    • Sawyer, S.L.1    Emerman, M.2    Malik, H.S.3
  • 120
    • 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 HP, Cullen BR (2004) Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor. Virology 328 (2):163-168
    • (2004) Virology , vol.328 , Issue.2 , pp. 163-168
    • Schafer, A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 121
    • 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 NR (2004) A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc Natl Acad Sci USA 101 (11):3927-3932
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.11 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 122
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
    • Schrofelbauer B et al (2005) Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J Virol 79(17):10978-10987
    • (2005) J Virol , vol.79 , Issue.17 , pp. 10978-10987
    • Schrofelbauer, B.1
  • 123
    • 33744939997 scopus 로고    scopus 로고
    • Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G
    • Schrofelbauer B et al (2006) Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G. J Virol 80(12):5984-5991
    • (2006) J Virol , vol.80 , Issue.12 , pp. 5984-5991
    • Schrofelbauer, B.1
  • 124
    • 22244448696 scopus 로고    scopus 로고
    • APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast
    • Schumacher AJ, Nissley DV, Harris RS (2005) APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast. Proc Natl Acad Sci USA 102(28):9854-9859
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.28 , pp. 9854-9859
    • Schumacher, A.J.1    Nissley, D.V.2    Harris, R.S.3
  • 125
    • 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 AJ et al (2008) The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction. J Virol 82(6):2652-2660
    • (2008) J Virol , vol.82 , Issue.6 , pp. 2652-2660
    • Schumacher, A.J.1
  • 126
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy AM et al (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418(6898):646-650
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1
  • 127
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy AM, Gaddis NC, Malim MH (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med 9(11):1404-1407
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 128
    • 55549136017 scopus 로고    scopus 로고
    • Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif
    • Shirakawa K et al (2008) Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif. Nat Struct Mol Biol 15(11):1184-1191
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.11 , pp. 1184-1191
    • Shirakawa, K.1
  • 129
    • 0029956256 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
    • Simon JH, Malim MH (1996) The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. J Virol 70(8):5297-5305
    • (1996) J Virol , vol.70 , Issue.8 , pp. 5297-5305
    • Simon, J.H.1    Malim, M.H.2
  • 130
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • Simon JH et al (1998) Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nat Med 4 (12):1397-1400
    • (1998) Nat Med , vol.4 , Issue.12 , pp. 1397-1400
    • Simon, J.H.1
  • 131
    • 67649888155 scopus 로고    scopus 로고
    • Natural variation in Vif: Differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
    • Simon V et al (2005) Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification. PLoS Pathog 1(1):e6
    • (2005) PLoS Pathog , vol.1 , Issue.1
    • Simon, V.1
  • 132
    • 0022676327 scopus 로고
    • Replicative and cytopathic potential of HTLV-III/LAV with sor gene deletions
    • Sodroski J et al (1986) Replicative and cytopathic potential of HTLV-III/LAV with sor gene deletions. Science 231(4745):1549-1553
    • (1986) Science , vol.231 , Issue.4745 , pp. 1549-1553
    • Sodroski, J.1
  • 133
    • 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 BJ et al (2008) Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J Virol 82(17):8656-8663
    • (2008) J Virol , vol.82 , Issue.17 , pp. 8656-8663
    • Stanley, B.J.1
  • 134
    • 33745184896 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism
    • Stenglein MD, Harris RS (2006) APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. J Biol Chem 281(25):16837-16841
    • (2006) J Biol Chem , vol.281 , Issue.25 , pp. 16837-16841
    • Stenglein, M.D.1    Harris, R.S.2
  • 135
    • 0025238945 scopus 로고
    • HIV-1 replication is controlled at the level of T cell activation and proviral integration
    • Stevenson M et al (1990) HIV-1 replication is controlled at the level of T cell activation and proviral integration. Embo J 9(5):1551-1560
    • (1990) Embo J , vol.9 , Issue.5 , pp. 1551-1560
    • Stevenson, M.1
  • 136
    • 0030920243 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest
    • Stewart SA et al (1997) Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest. J Virol 71(7):5579-5592
    • (1997) J Virol , vol.71 , Issue.7 , pp. 5579-5592
    • Stewart, S.A.1
  • 137
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak K et al (2003) HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell 12(3):591-601
    • (2003) Mol Cell , vol.12 , Issue.3 , pp. 591-601
    • Stopak, K.1
  • 138
    • 33947518167 scopus 로고    scopus 로고
    • Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells
    • Stopak KS et al (2007) Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells. J Biol Chem 282 (6):3539-3546
    • (2007) J Biol Chem , vol.282 , Issue.6 , pp. 3539-3546
    • Stopak, K.S.1
  • 139
    • 0023267788 scopus 로고
    • The HIV 'A' (sor) gene product is essential for virus infectivity
    • Strebel K et al (1987) The HIV 'A' (sor) gene product is essential for virus infectivity. Nature 328 (6132):728-730
    • (1987) Nature , vol.328 , Issue.6132 , pp. 728-730
    • Strebel, K.1
  • 140
    • 2342469410 scopus 로고    scopus 로고
    • APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase
    • Suspene R et al (2004) APOBEC3G is a single-stranded DNA cytidine deaminase and functions independently of HIV reverse transcriptase. Nucleic Acids Res 32(8):2421-2429
    • (2004) Nucleic Acids Res , vol.32 , Issue.8 , pp. 2421-2429
    • Suspene, R.1
  • 141
    • 20444416733 scopus 로고    scopus 로고
    • Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo
    • Suspene R et al (2005) Extensive editing of both hepatitis B virus DNA strands by APOBEC3 cytidine deaminases in vitro and in vivo. Proc Natl Acad Sci USA 102(23):8321-8326
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.23 , pp. 8321-8326
    • Suspene, R.1
  • 142
    • 4143124683 scopus 로고    scopus 로고
    • Human apolipoprotein B mRNA-editing enzyme-catalytic polypep-tide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs
    • Svarovskaia ES et al (2004) Human apolipoprotein B mRNA-editing enzyme-catalytic polypep-tide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. J Biol Chem 279(34):35822-35828
    • (2004) J Biol Chem , vol.279 , Issue.34 , pp. 35822-35828
    • Svarovskaia, E.S.1
  • 143
    • 58249114897 scopus 로고    scopus 로고
    • Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1
    • Tan L et al (2008) Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1. Faseb J 23(1):279-287
    • (2008) Faseb J , vol.23 , Issue.1 , pp. 279-287
    • Tan, L.1
  • 144
    • 31444449299 scopus 로고    scopus 로고
    • Anti-viral protein APOBEC3G is induced by interferon-alpha stimulation in human hepatocytes
    • Tanaka Y et al (2006) Anti-viral protein APOBEC3G is induced by interferon-alpha stimulation in human hepatocytes. Biochem Biophys Res Commun 341(2):314-319
    • (2006) Biochem Biophys Res Commun , vol.341 , Issue.2 , pp. 314-319
    • Tanaka, Y.1
  • 145
    • 0027200620 scopus 로고
    • Molecular cloning of an apolipoprotein B messenger RNA editing protein
    • Teng B, Burant CF, Davidson NO (1993) Molecular cloning of an apolipoprotein B messenger RNA editing protein. Science 260(5115):1816-1819
    • (1993) Science , vol.260 , Issue.5115 , pp. 1816-1819
    • Teng, B.1    Burant, C.F.2    Davidson, N.O.3
  • 146
    • 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 et al (2006) Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J Virol 80(6):3112-3115
    • (2006) J Virol , vol.80 , Issue.6 , pp. 3112-3115
    • Tian, C.1
  • 147
    • 37449029284 scopus 로고    scopus 로고
    • Virion packaging determinants and reverse transcription of SRP RNA in HIV-1 particles
    • Tian C et al (2007) Virion packaging determinants and reverse transcription of SRP RNA in HIV-1 particles. Nucleic Acids Res 35(21):7288-7302
    • (2007) Nucleic Acids Res , vol.35 , Issue.21 , pp. 7288-7302
    • Tian, C.1
  • 148
    • 13844309367 scopus 로고    scopus 로고
    • Editing at the crossroad of innate and adaptive immunity
    • Turelli P, Trono D (2005) Editing at the crossroad of innate and adaptive immunity. Science 307 (5712):1061-1065
    • (2005) Science , vol.307 , Issue.5712 , pp. 1061-1065
    • Turelli, P.1    Trono, D.2
  • 149
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by APOBEC3G
    • Turelli P et al (2004a) Inhibition of hepatitis B virus replication by APOBEC3G. Science 303 (5665):1829
    • (2004) Science , vol.303 , Issue.5665 , pp. 1829
    • Turelli, P.1
  • 150
    • 6344233811 scopus 로고    scopus 로고
    • The innate antiretroviral factor APOBEC3G does not affect human LINE-1 retrotransposition in a cell culture assay
    • Turelli P, Vianin S, Trono D (2004b) The innate antiretroviral factor APOBEC3G does not affect human LINE-1 retrotransposition in a cell culture assay. J Biol Chem 279(42):43371-43373
    • (2004) J Biol Chem , vol.279 , Issue.42 , pp. 43371-43373
    • Turelli, P.1    Vianin, S.2    Trono, D.3
  • 151
    • 42049096136 scopus 로고    scopus 로고
    • Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions
    • Vartanian JP et al (2008) Evidence for editing of human papillomavirus DNA by APOBEC3 in benign and precancerous lesions. Science 320(5873):230-233
    • (2008) Science , vol.320 , Issue.5873 , pp. 230-233
    • Vartanian, J.P.1
  • 152
    • 0027179103 scopus 로고
    • Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells
    • von Schwedler U et al (1993) Vif is crucial for human immunodeficiency virus type 1 proviral DNA synthesis in infected cells. J Virol 67(8):4945-4955
    • (1993) J Virol , vol.67 , Issue.8 , pp. 4945-4955
    • Von Schwedler, U.1
  • 153
    • 36348962513 scopus 로고    scopus 로고
    • 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G
    • Wang T et al (2007a) 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G. J Virol 81(23):13112-13124
    • (2007) J Virol , vol.81 , Issue.23 , pp. 13112-13124
    • Wang, T.1
  • 154
    • 33847076286 scopus 로고    scopus 로고
    • The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells
    • Wang J et al (2007b) The Vif accessory protein alters the cell cycle of human immunodeficiency virus type 1 infected cells. Virology 359(2):243-252
    • (2007) Virology , vol.359 , Issue.2 , pp. 243-252
    • Wang, J.1
  • 155
    • 44949182656 scopus 로고    scopus 로고
    • Distinct viral determinants for the packaging of human cytidine deaminases APOBEC3G and APOBEC3C
    • Wang T et al (2008) Distinct viral determinants for the packaging of human cytidine deaminases APOBEC3G and APOBEC3C. Virology 377(1):71-79
    • (2008) Virology , vol.377 , Issue.1 , pp. 71-79
    • Wang, T.1
  • 156
    • 1542563409 scopus 로고    scopus 로고
    • Initial sequencing and comparative analysis of the mouse genome
    • Waterston RH et al (2002) Initial sequencing and comparative analysis of the mouse genome. Nature 420(6915):520-562
    • (2002) Nature , vol.420 , Issue.6915 , pp. 520-562
    • Waterston, R.H.1
  • 157
    • 0026783587 scopus 로고
    • Inhibition of HIV infection of resting peripheral blood lymphocytes by nucleosides
    • Watson AJ, Wilburn LM (1992) Inhibition of HIV infection of resting peripheral blood lymphocytes by nucleosides. AIDS Res Hum Retroviruses 8(7):1221-1227
    • (1992) AIDS Res Hum Retroviruses , vol.8 , Issue.7 , pp. 1221-1227
    • Watson, A.J.1    Wilburn, L.M.2
  • 158
    • 37049013542 scopus 로고    scopus 로고
    • Inhibition of alpharetrovirus replication by a range of human APOBEC3 proteins
    • Wiegand HL, Cullen BR (2007) Inhibition of alpharetrovirus replication by a range of human APOBEC3 proteins. J Virol 81(24):13694-13699
    • (2007) J Virol , vol.81 , Issue.24 , pp. 13694-13699
    • Wiegand, H.L.1    Cullen, B.R.2
  • 159
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand HL et al (2004) A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. Embo J 23(12):2451-2458
    • (2004) Embo J , vol.23 , Issue.12 , pp. 2451-2458
    • Wiegand, H.L.1
  • 160
    • 0032902885 scopus 로고    scopus 로고
    • DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism
    • Willetts KE et al (1999) DNA repair enzyme uracil DNA glycosylase is specifically incorporated into human immunodeficiency virus type 1 viral particles through a Vpr-independent mechanism. J Virol 73(2):1682-1688
    • (1999) J Virol , vol.73 , Issue.2 , pp. 1682-1688
    • Willetts, K.E.1
  • 161
    • 34748882327 scopus 로고    scopus 로고
    • Characterization of a novel cullin5 binding domain in HIV-1 Vif
    • Xiao Z et al (2007) Characterization of a novel cullin5 binding domain in HIV-1 Vif. J Mol Biol 373(3):541-550
    • (2007) J Mol Biol , vol.373 , Issue.3 , pp. 541-550
    • Xiao, Z.1
  • 162
    • 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 et al (2004) A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc Natl Acad Sci USA 101(15):5652-5657
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.15 , pp. 5652-5657
    • Xu, H.1
  • 163
    • 0032491493 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphorylates and regulates the HIV-1 Vif protein
    • Yang X, Gabuzda D (1998) Mitogen-activated protein kinase phosphorylates and regulates the HIV-1 Vif protein. J Biol Chem 273(45):29879-29887
    • (1998) J Biol Chem , vol.273 , Issue.45 , pp. 29879-29887
    • Yang, X.1    Gabuzda, D.2
  • 164
    • 0029874943 scopus 로고    scopus 로고
    • Phosphorylation of Vif and its role in HIV-1 replication
    • Yang X, Goncalves J, Gabuzda D (1996) Phosphorylation of Vif and its role in HIV-1 replication. J Biol Chem 271(17):10121-10129
    • (1996) J Biol Chem , vol.271 , Issue.17 , pp. 10121-10129
    • Yang, X.1    Goncalves, J.2    Gabuzda, D.3
  • 165
    • 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 et al (2007a) 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 282(16):11667-11675
    • (2007) J Biol Chem , vol.282 , Issue.16 , pp. 11667-11675
    • Yang, B.1
  • 166
    • 34250186071 scopus 로고    scopus 로고
    • Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F
    • Yang Y et al (2007b) Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F. Virology 365(1):92-100
    • (2007) Virology , vol.365 , Issue.1 , pp. 92-100
    • Yang, Y.1
  • 167
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X et al (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302(5647):1056-1060
    • (2003) Science , vol.302 , Issue.5647 , pp. 1056-1060
    • Yu, X.1
  • 168
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • Yu Q et al (2004a) APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J Biol Chem 279(51):53379-53386
    • (2004) J Biol Chem , vol.279 , Issue.51 , pp. 53379-53386
    • Yu, Q.1
  • 169
    • 2342633240 scopus 로고    scopus 로고
    • Single-strand specificity of APOBEC3G accounts for minus-strand deamina-tion of the HIV genome
    • Yu Q et al (2004b) Single-strand specificity of APOBEC3G accounts for minus-strand deamina-tion of the HIV genome. Nat Struct Mol Biol 11(5):435-442
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.5 , pp. 435-442
    • Yu, Q.1
  • 170
    • 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 et al (2004c) Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev 18(23):2867-2872
    • (2004) Genes Dev , vol.18 , Issue.23 , pp. 2867-2872
    • Yu, Y.1
  • 171
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou V et al (2004) APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J Virol 78(21):12058-12061
    • (2004) J Virol , vol.78 , Issue.21 , pp. 12058-12061
    • Zennou, V.1
  • 172
    • 4444290423 scopus 로고    scopus 로고
    • Rapid evolution of primate antiviral enzyme APOBEC3G
    • Zhang J, Webb DM (2004) Rapid evolution of primate antiviral enzyme APOBEC3G. Hum Mol Genet 13(16):1785-1791
    • (2004) Hum Mol Genet , vol.13 , Issue.16 , pp. 1785-1791
    • Zhang, J.1    Webb, D.M.2
  • 173
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H et al (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424(6944):94-98
    • (2003) Nature , vol.424 , Issue.6944 , pp. 94-98
    • Zhang, H.1
  • 174
    • 47549104961 scopus 로고    scopus 로고
    • Conserved and non-conserved features of HIV-1 and SIVagm Vif mediated suppression of APOBEC3 cytidine deaminases
    • Zhang W et al (2008a) Conserved and non-conserved features of HIV-1 and SIVagm Vif mediated suppression of APOBEC3 cytidine deaminases. Cell Microbiol 10(8):1662-1675
    • (2008) Cell Microbiol , vol.10 , Issue.8 , pp. 1662-1675
    • Zhang, W.1
  • 175
    • 58049217469 scopus 로고    scopus 로고
    • Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteins
    • Zhang W et al (2008b) Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteins. PLoS ONE 3(12):e3963
    • (2008) PLoS ONE , vol.3 , Issue.12
    • Zhang, W.1
  • 176
    • 36949041073 scopus 로고    scopus 로고
    • Cytidine deaminase APOBEC3B interacts with heterogeneous nuclear ribonucleoprotein K and suppresses hepatitis B virus expression
    • Zhang W et al (2008c) Cytidine deaminase APOBEC3B interacts with heterogeneous nuclear ribonucleoprotein K and suppresses hepatitis B virus expression. Cell Microbiol 10(1):112-121
    • (2008) Cell Microbiol , vol.10 , Issue.1 , pp. 112-121
    • Zhang, W.1
  • 177
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng YH et al (2004) Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J Virol 78(11):6073-6076
    • (2004) J Virol , vol.78 , Issue.11 , pp. 6073-6076
    • Zheng, Y.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.