메뉴 건너뛰기




Volumn 12, Issue , 2010, Pages

Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: Implications for therapeutics

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 1; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3F; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; COMPLEMENTARY DNA; CYTIDINE; UNCLASSIFIED DRUG; VIRION INFECTIVITY FACTOR; VIRUS DNA; VIRUS PROTEIN; VIRUS RNA; APOBEC3 PROTEIN, HUMAN; CYTOSINE DEAMINASE; VIF PROTEIN;

EID: 77953035055     PISSN: 14623994     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1462399409001343     Document Type: Review
Times cited : (161)

References (168)
  • 1
    • 42649120310 scopus 로고    scopus 로고
    • The APOBEC3 cytidine deaminases: An innate defensive network opposing exogenous retroviruses and endogenous retroelements
    • Chiu, Y.L. and Greene, W.C. (2008) The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annual Review of Immunology 26, 317-353
    • (2008) Annual Review of Immunology , vol.26 , pp. 317-353
    • Chiu, Y.L.1    Greene, W.C.2
  • 2
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • DOI 10.1038/nri1489
    • Harris, R.S. and Liddament, M.T. (2004) Retroviral restriction by APOBEC proteins. Nature Reviews Immunology 4, 868-877 (Pubitemid 39490762)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.11 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 3
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 Accessory Proteins-Ensuring Viral Survival in a Hostile Environment
    • DOI 10.1016/j.chom.2008.04.008, PII S1931312808001261
    • Malim, M.H. and Emerman, M. (2008) HIV-1 accessory proteins-ensuring viral survival in a hostile environment. Cell Host and Microbe 3, 388-398 (Pubitemid 351784365)
    • (2008) Cell Host and Microbe , vol.3 , Issue.6 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 4
    • 61449214207 scopus 로고    scopus 로고
    • Accessories to the crime: Recent advances in HIVaccessory protein biology
    • Gramberg, T., Sunseri, N. and Landau, N.R. (2009) Accessories to the crime: recent advances in HIVaccessory protein biology. Current HIV/AIDS Reports 6, 36-42
    • (2009) Current HIV/AIDS Reports , vol.6 , pp. 36-42
    • Gramberg, T.1    Sunseri, N.2    Landau, N.R.3
  • 5
    • 0026084954 scopus 로고
    • Rev activates expression of the human immunodeficiency virus type 1 vif and vpr gene products
    • Garrett, E.D., Tiley, L.S. and Cullen, B.R. (1991) Rev activates expression of the human immunodeficiency virus type 1 vif and vpr gene products. Journal of Virology 65, 1653-1657
    • (1991) Journal of Virology , vol.65 , pp. 1653-1657
    • Garrett, E.D.1    Tiley, L.S.2    Cullen, B.R.3
  • 6
    • 0025766073 scopus 로고
    • Expression of human immunodeficiency virus type 1 vif and vpr mRNAs is Rev-dependent and regulated by splicing
    • Schwartz, S., Felber, B.K. and Pavlakis, G.N. (1991) Expression of human immunodeficiency virus type 1 vif and vpr mRNAs is Rev-dependent and regulated by splicing. Virology 183, 677-686
    • (1991) Virology , vol.183 , pp. 677-686
    • Schwartz, S.1    Felber, B.K.2    Pavlakis, G.N.3
  • 7
    • 0022678249 scopus 로고
    • Identification of HTLV-III/LAV sor gene product and detection of antibodies in human sera
    • Kan, N.C. et al. (1986) Identification of HTLV-III/ LAV sor gene product and detection of antibodies in human sera. Science 231, 1553-1555 (Pubitemid 16050723)
    • (1986) Science , vol.231 , Issue.4745 , pp. 1553-1555
    • Kan, N.C.1    Franchini, G.2    Wong-Staal, F.3
  • 8
    • 0022680624 scopus 로고
    • A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses
    • Lee, T.H. et al. (1986)A new HTLV-III/LAV protein encoded by a gene found in cytopathic retroviruses. Science 231, 1546-1549
    • (1986) Science , vol.231 , pp. 1546-1549
    • Lee, T.H.1
  • 9
    • 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, 1549-1553 (Pubitemid 16050722)
    • (1986) Science , vol.231 , Issue.4745 , pp. 1549-1553
    • Sodroski, J.1    Goh, W.C.2    Rosen, C.3
  • 11
    • 0023267788 scopus 로고
    • The HIV 'A' (sor) gene product is essential for virus infectivity
    • DOI 10.1038/328728a0
    • Strebel, K. et al. (1987) The HIV 'A' (sor) gene product is essential for virus infectivity. Nature 328, 728-730 (Pubitemid 17125778)
    • (1987) Nature , vol.328 , Issue.6132 , pp. 728-730
    • Strebel, K.1    Daugherty, D.2    Clouse, K.3
  • 12
    • 0026649561 scopus 로고
    • Role of Vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes
    • Gabuzda, D.H. et al. (1992) Role of Vif in replication of human immunodeficiency virus type 1 in CD4+ T lymphocytes. Journal of Virology 66, 6489-6495
    • (1992) Journal of Virology , vol.66 , pp. 6489-6495
    • Gabuzda, D.H.1
  • 13
    • 0028170078 scopus 로고
    • Essential role of vif in establishing productive HIV-1 infection in peripheral blood T lymphocytes and monocyte/ macrophages
    • Gabuzda, D.H. et al. (1994) Essential role of vif in establishing productive HIV-1 infection in peripheral blood T lymphocytes and monocyte/ macrophages. Journal of Acquired Immune Deficiency Syndromes 7, 908-915
    • (1994) Journal of Acquired Immune Deficiency Syndromes , vol.7 , pp. 908-915
    • Gabuzda, D.H.1
  • 14
    • 0023191658 scopus 로고
    • The sor gene of HIV-1 is required for efficient virus transmission in vitro
    • Fisher, A.G. et al. (1987) The sor gene of HIV-1 is required for efficient virus transmission in vitro. Science 237, 888-893 (Pubitemid 17128277)
    • (1987) Science , vol.237 , Issue.4817 , pp. 888-893
    • Fisher, A.G.1    Ensoli, B.2    Ivanoff, L.3
  • 15
    • 0029956256 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 vif protein modulates the postpenetration stability of viral nucleoprotein complexes
    • Simon, J.H. and Malim, M.H. (1996) The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. Journal of Virology 70, 5297-5305 (Pubitemid 26240703)
    • (1996) Journal of Virology , vol.70 , Issue.8 , pp. 5297-5305
    • Simon, J.H.M.1    Malim, M.H.2
  • 16
    • 0028926644 scopus 로고
    • Peripheral blood mononuclear cells produce normal amounts of defective Vif- Human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps
    • Courcoul, M. et al. (1995) Peripheral blood mononuclear cells produce normal amounts of defective Vif- human immunodeficiency virus type 1 particles which are restricted for the preretrotranscription steps. Journal of Virology 69, 2068-2074
    • (1995) Journal of Virology , vol.69 , pp. 2068-2074
    • Courcoul, M.1
  • 17
    • 0029861076 scopus 로고    scopus 로고
    • Role of Vif in human immunodeficiency virus type 1 reverse transcription
    • Goncalves, J. et al. (1996) Role of Vif in human immunodeficiency virus type 1 reverse transcription. Journal of Virology 70, 8701-8709 (Pubitemid 26378452)
    • (1996) Journal of Virology , vol.70 , Issue.12 , pp. 8701-8709
    • Goncalves, J.1    Korin, Y.2    Zack, J.3    Gabuzda, D.4
  • 18
    • 0027183349 scopus 로고
    • Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1
    • Sova, P. and Volsky, D.J. (1993) Efficiency of viral DNA synthesis during infection of permissive and nonpermissive cells with vif-negative human immunodeficiency virus type 1. Journal of Virology 67, 6322-6326 (Pubitemid 23277551)
    • (1993) Journal of Virology , vol.67 , Issue.10 , pp. 6322-6326
    • Sova, P.1    Volsky, D.J.2
  • 19
    • 0031797865 scopus 로고    scopus 로고
    • An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein
    • Madani, N. and Kabat, D. (1998) An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. Journal of Virology 72, 10251-10255 (Pubitemid 28520900)
    • (1998) Journal of Virology , vol.72 , Issue.12 , pp. 10251-10255
    • Madani, N.1    Kabat, D.2
  • 20
    • 0031788565 scopus 로고    scopus 로고
    • Evidence for a newly discovered cellular anti-HIV-1 phenotype
    • DOI 10.1038/3987
    • Simon, J.H. et al. (1998) Evidence for a newly discovered cellular anti-HIV-1 phenotype. Nature Medicine 4, 1397-1400 (Pubitemid 28553462)
    • (1998) Nature Medicine , vol.4 , Issue.12 , pp. 1397-1400
    • Simon, J.H.M.1    Gaddis, N.C.2    Fouchier, R.A.M.3    Malim, M.H.4
  • 21
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy, A.M. et al. (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418, 646-650
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1
  • 22
    • 44349179677 scopus 로고    scopus 로고
    • Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G
    • Haché, G. et al. (2008) Evolution of HIV-1 isolates that use a novel Vif-independent mechanism to resist restriction by human APOBEC3G. Current Biology 18, 819-824
    • (2008) Current Biology , vol.18 , pp. 819-824
    • Haché, G.1
  • 24
    • 0037019315 scopus 로고    scopus 로고
    • AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification
    • DOI 10.1038/nature00862
    • Petersen-Mahrt, S.K., Harris, R.S. and Neuberger, M.S. (2002) AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature 418, 99-103 (Pubitemid 34742579)
    • (2002) Nature , vol.418 , Issue.6893 , pp. 99-103
    • Petersen-Mahrt, S.K.1    Harris, R.S.2    Neuberger, M.S.3
  • 25
    • 0036863733 scopus 로고    scopus 로고
    • RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators
    • DOI 10.1016/S1097-2765(02)00742-6
    • Harris, R.S., Petersen-Mahrt, S.K. and Neuberger, M.S. (2002) RNA editing enzyme APOBEC1 and some of its homologs can act as DNA mutators. Molecular Cell 10, 1247-1253 (Pubitemid 35453840)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 1247-1253
    • Harris, R.S.1    Petersen-Mahrt, S.K.2    Neuberger, M.S.3
  • 27
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • DOI 10.1038/nature01709
    • Mangeat, B. et al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424, 99-103 (Pubitemid 36834849)
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 28
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • DOI 10.1038/nature01707
    • Zhang, H. et al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424, 94-98 (Pubitemid 36834848)
    • (2003) Nature , vol.424 , Issue.6944 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 29
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • DOI 10.1126/science.1083338
    • Lecossier, D. et al. (2003) Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300, 1112 (Pubitemid 36583087)
    • (2003) Science , vol.300 , Issue.5622 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 30
    • 64849104502 scopus 로고    scopus 로고
    • Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent
    • Browne, E.P., Allers, C. and Landau, N.R. (2009) Restriction of HIV-1 by APOBEC3G is cytidine deaminase-dependent. Virology 387, 313-321
    • (2009) Virology , vol.387 , pp. 313-321
    • Browne, E.P.1    Allers, C.2    Landau, N.R.3
  • 31
    • 33847625391 scopus 로고    scopus 로고
    • APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation: Comparisons with APOBEC3G
    • DOI 10.1074/jbc.M607298200
    • Holmes, R.K. et al. (2007) APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. Journal of Biological Chemistry 282, 2587-2595 (Pubitemid 47076764)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.4 , pp. 2587-2595
    • Holmes, R.K.1    Koning, F.A.2    Bishop, K.N.3    Malim, M.H.4
  • 32
    • 37049032574 scopus 로고    scopus 로고
    • Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1
    • DOI 10.1128/JVI.01361-07
    • Miyagi, E. et al. (2007) Enzymatically active APOBEC3G is required for efficient inhibition of human immunodeficiency virus type 1. Journal of Virology 81, 13346-13353 (Pubitemid 350247831)
    • (2007) Journal of Virology , vol.81 , Issue.24 , pp. 13346-13353
    • Miyagi, E.1    Opi, S.2    Takeuchi, H.3    Khan, M.4    Goila-Gaur, R.5    Kao, S.6    Strebel, H.7
  • 33
    • 40149102165 scopus 로고    scopus 로고
    • The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction
    • DOI 10.1128/JVI.02391-07
    • Schumacher, A.J. et al. (2008) The DNA deaminase activity of human APOBEC3G is required for Ty1, MusD, and human immunodeficiency virus type 1 restriction. Journal of Virology 82, 2652-2660 (Pubitemid 351329156)
    • (2008) Journal of Virology , vol.82 , Issue.6 , pp. 2652-2660
    • Schumacher, A.J.1    Hache, G.2    MacDuff, D.A.3    Brown, W.L.4    Harris, R.S.5
  • 34
    • 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
    • DOI 10.1074/jbc.C300376200
    • Shindo, K. et al. (2003) 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. Journal of Biological Chemistry 278, 44412-44416 (Pubitemid 37377191)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44412-44416
    • Shindo, K.1    Takaori-Kondo, A.2    Kobayashi, M.3    Abudu, A.4    Fukunaga, K.5    Uchiyama, T.6
  • 35
    • 12544256041 scopus 로고    scopus 로고
    • Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
    • Newman, E.N. et al. (2005) Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Current Biology 15, 166-170
    • (2005) Current Biology , vol.15 , pp. 166-170
    • Newman, E.N.1
  • 36
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • DOI 10.1128/JVI.00839-06
    • Bishop, K.N., Holmes, R.K. and Malim, M.H. (2006) Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. Journal of Virology 80, 8450-8458 (Pubitemid 44384857)
    • (2006) Journal of Virology , vol.80 , Issue.17 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 37
    • 58149237802 scopus 로고    scopus 로고
    • APOBEC3G inhibits elongation of HIV-1 reverse transcripts
    • Bishop, K.N. et al. (2008) APOBEC3G inhibits elongation of HIV-1 reverse transcripts. PLoS Pathogens 4, e1000231
    • (2008) PLoS Pathogens , vol.4
    • Bishop, K.N.1
  • 38
    • 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 Research 35, 7096-7108
    • (2007) Nucleic Acids Research , vol.35 , pp. 7096-7108
    • Iwatani, Y.1
  • 39
    • 33751206549 scopus 로고    scopus 로고
    • Lys-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • DOI 10.1128/JVI.01038-06
    • Guo, F. et al. (2006) Inhibition of formula-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. Journal of Virology 80, 11710-11722 (Pubitemid 44788884)
    • (2006) Journal of Virology , vol.80 , Issue.23 , pp. 11710-11722
    • Guo, F.1    Cen, S.2    Niu, M.3    Saadatmand, J.4    Kleiman, L.5
  • 40
    • 34250186071 scopus 로고    scopus 로고
    • Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F
    • DOI 10.1016/j.virol.2007.03.022, PII S0042682207001821
    • Yang, Y. et al. (2007) Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F. Virology 365, 92-100 (Pubitemid 46907232)
    • (2007) Virology , vol.365 , Issue.1 , pp. 92-100
    • Yang, Y.1    Guo, F.2    Cen, S.3    Kleiman, L.4
  • 41
    • 36148995875 scopus 로고    scopus 로고
    • APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription
    • Li, X.Y. et al. (2007) APOBEC3G inhibits DNA strand transfer during HIV-1 reverse transcription. Journal of Biological Chemistry 282, 32065-32074
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 32065-32074
    • Li, X.Y.1
  • 42
    • 34250857925 scopus 로고    scopus 로고
    • Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation
    • DOI 10.1128/JVI.02584-06
    • Luo, K. et al. (2007) Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. Journal of Virology 81, 7238-7248 (Pubitemid 46986660)
    • (2007) Journal of Virology , vol.81 , Issue.13 , 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
  • 45
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of Hepatitis B Virus Replication by APOBEC3G
    • DOI 10.1126/science.1092066
    • Turelli, P. et al. (2004) Inhibition of hepatitis B virus replication by APOBEC3G. Science 303, 1829 (Pubitemid 38374868)
    • (2004) Science , vol.303 , Issue.5665 , pp. 1829
    • Turelli, P.1    Mangeat, B.2    Jost, S.3    Vianin, S.4    Trono, D.5
  • 48
    • 33745184896 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism
    • Stenglein, M.D. and Harris, R.S. (2006) APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. Journal of Biological Chemistry 281, 16837-16841
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 16837-16841
    • Stenglein, M.D.1    Harris, R.S.2
  • 49
    • 33847636341 scopus 로고    scopus 로고
    • APOBEC-mediated viral restriction: not simply editing?
    • DOI 10.1016/j.tibs.2007.01.004, PII S0968000407000308
    • Holmes, R.K., Malim, M.H. and Bishop, K.N. (2007) APOBEC-mediated viral restriction: not simply editing? Trends in Biochemical Sciences 32, 118-128 (Pubitemid 46367691)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.3 , pp. 118-128
    • Holmes, R.K.1    Malim, M.H.2    Bishop, K.N.3
  • 50
    • 42949138262 scopus 로고    scopus 로고
    • Hepatitis B: Modern concepts in pathogenesis - APOBEC3 cytidine deaminases as effectors in innate immunity against the hepatitis B virus
    • DOI 10.1097/QCO.0b013e3282fe1bb2, PII 0000143220080600000014
    • Bonvin, M. and Greeve, J. (2008) Hepatitis B: modern concepts in pathogenesis - APOBEC3 cytidine deaminases as effectors in innate immunity against the hepatitis B virus. Current Opinion in Infectious Diseases 21, 298-303 (Pubitemid 351620385)
    • (2008) Current Opinion in Infectious Diseases , vol.21 , Issue.3 , pp. 298-303
    • Bonvin, M.1    Greeve, J.2
  • 51
    • 0038825009 scopus 로고    scopus 로고
    • DNA deamination: Not just a trigger for antibody diversification but also a mechanism for defense against retroviruses
    • DOI 10.1038/ni0703-641
    • Harris, R.S. et al. (2003)DNAdeamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses. Nature Immunology 4, 641-643 (Pubitemid 36874436)
    • (2003) Nature Immunology , vol.4 , Issue.7 , pp. 641-643
    • Harris, R.S.1    Sheehy, A.M.2    Craig, H.M.3    Malim, M.H.4    Neuberger, M.S.5
  • 52
    • 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
    • DOI 10.1074/jbc.M606864200
    • Yang, B. et al. (2007) Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA. Journal of Biological Chemistry 282, 11667-11675 (Pubitemid 47100658)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 11667-11675
    • Yang, B.1    Chen, K.2    Zhang, C.3    Huang, S.4    Zhang, H.5
  • 53
    • 3142651460 scopus 로고    scopus 로고
    • Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages
    • DOI 10.1074/jbc.M403875200
    • Chen, R. et al. (2004) Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages. Journal of Biological Chemistry 279, 28419-28425 (Pubitemid 38900122)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28419-28425
    • Chen, R.1    Le, R.E.2    Kearney, J.A.3    Mansky, L.M.4    Benichou, S.5
  • 54
    • 0033925801 scopus 로고    scopus 로고
    • The interaction of Vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 in vivo mutation rate
    • DOI 10.1128/JVI.74.15.7039-7047.2000
    • Mansky, L.M. et al. (2000) The interaction of vpr with uracil DNA glycosylase modulates the human immunodeficiency virus type 1 In vivo mutation rate. Journal of Virology 74, 7039-7047 (Pubitemid 30470687)
    • (2000) Journal of Virology , vol.74 , Issue.15 , pp. 7039-7047
    • Mansky, L.M.1    Preveral, S.2    Selig, L.3    Benarous, R.4    Benichou, S.5
  • 55
    • 13944277344 scopus 로고    scopus 로고
    • HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle
    • DOI 10.1016/j.molcel.2005.01.016
    • Priet, S. et al. (2005) HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle. Molecular Cell 17, 479-490 (Pubitemid 40269113)
    • (2005) Molecular Cell , vol.17 , Issue.4 , pp. 479-490
    • Priet, S.1    Gros, N.2    Navarro, J.-M.3    Boretto, J.4    Canard, B.5    Querat, G.6    Sire, J.7
  • 56
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG Uracil-DNA glycosylases
    • DOI 10.1128/JVI.79.17.10978-10987.2005
    • Schröfelbauer, B. et al. (2005) Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. Journal of Virology 79, 10978-10987 (Pubitemid 41170639)
    • (2005) Journal of Virology , vol.79 , Issue.17 , pp. 10978-10987
    • Schrofelbauer, B.1    Yu, Q.2    Zeitlin, S.G.3    Landau, N.R.4
  • 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
    • DOI 10.1128/JVI.80.2.875-882.2006
    • Kaiser, S.M. and 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. Journal of Virology 80, 875-882 (Pubitemid 43062899)
    • (2006) Journal of Virology , vol.80 , Issue.2 , pp. 875-882
    • Kaiser, S.M.1    Emerman, M.2
  • 58
    • 0242709301 scopus 로고    scopus 로고
    • The Vif Protein of HIV Triggers Degradation of the Human Antiretroviral DNA Deaminase APOBEC3G
    • DOI 10.1016/j.cub.2003.10.034
    • Conticello, S.G., Harris, R.S. and Neuberger, M.S. (2003) The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Current Biology 13, 2009-2013 (Pubitemid 37425213)
    • (2003) Current Biology , vol.13 , Issue.22 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 59
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • DOI 10.1038/nm946
    • Marin, M. et al. (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nature Medicine 9, 1398-1403 (Pubitemid 37466189)
    • (2003) Nature Medicine , vol.9 , Issue.11 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 60
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • DOI 10.1038/nm945
    • Sheehy, A.M., Gaddis, N.C. and Malim, M.H. (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nature Medicine 9, 1404-1407 (Pubitemid 37466190)
    • (2003) Nature Medicine , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 61
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • DOI 10.1016/S1097-2765(03)00353-8
    • Stopak, K. et al. (2003)HIV-1Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Molecular Cell 12, 591-601 (Pubitemid 37222482)
    • (2003) Molecular Cell , vol.12 , Issue.3 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 62
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex
    • DOI 10.1126/science.1089591
    • Yu, X. et al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif- Cul5-SCF complex. Science 302, 1056-1060 (Pubitemid 37386201)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.-F.7
  • 63
    • 1542379821 scopus 로고    scopus 로고
    • Vif Overcomes the Innate Antiviral Activity of APOBEC3G by Promoting Its Degradation in the Ubiquitin-Proteasome Pathway
    • DOI 10.1074/jbc.M313093200
    • Mehle, A. et al. (2004) Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. Journal of Biological Chemistry 279, 7792-7798 (Pubitemid 38294663)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 64
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • DOI 10.1101/gad.1249904
    • 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 and Development 18, 2861-2866 (Pubitemid 39602304)
    • (2004) Genes and Development , vol.18 , Issue.23 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 65
    • 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
    • DOI 10.1101/gad.1250204
    • Yu, Y. et al. (2004) Selective assembly of HIV-1 Vif- Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes and Development 18, 2867-2872 (Pubitemid 39602305)
    • (2004) Genes and Development , vol.18 , Issue.23 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.-F.5
  • 66
    • 0142092452 scopus 로고    scopus 로고
    • The Human Immunodeficiency Virus Type 1 Vif Protein Reduces Intracellular Expression and Inhibits Packaging of APOBEC3G (CEM15), a Cellular Inhibitor of Virus Infectivity
    • DOI 10.1128/JVI.77.21.11398-11407.2003
    • Kao, S. et al. (2003) The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity. Journal of Virology 77, 11398-11407 (Pubitemid 37271638)
    • (2003) Journal of Virology , vol.77 , Issue.21 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5    Strebel, K.6
  • 68
    • 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
    • DOI 10.1074/jbc.M409309200
    • Santa-Marta, M. et al. (2005) 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. Journal of Biological Chemistry 280, 8765-8775 (Pubitemid 40409564)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 8765-8775
    • Santa-Marta, M.1    Da, S.F.A.2    Fonseca, A.M.3    Goncalves, J.4
  • 70
    • 0345270035 scopus 로고    scopus 로고
    • Messenger RNA editing in mammals: New members of the APOBEC family seeking roles in the family business
    • DOI 10.1016/S0168-9525(03)00054-4
    • Wedekind, J.E. et al. (2003) Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business. Trends in Genetics 19, 207-216 (Pubitemid 36398423)
    • (2003) Trends in Genetics , vol.19 , Issue.4 , pp. 207-216
    • Wedekind, J.E.1    Dance, G.S.C.2    Sowden, M.P.3    Smith, H.C.4
  • 72
    • 68149168652 scopus 로고    scopus 로고
    • Microarray analysis of lymphatic tissue reveals stage-specific, gene expression signatures in HIV-1 infection
    • Li, Q. et al. (2009) Microarray analysis of lymphatic tissue reveals stage-specific, gene expression signatures in HIV-1 infection. Journal of Immunology 183, 1975-1982
    • (2009) Journal of Immunology , vol.183 , pp. 1975-1982
    • Li, Q.1
  • 73
    • 50849100134 scopus 로고    scopus 로고
    • Antiretroelement activity of APOBEC3H was lost twice in recent human evolution
    • Oh Ainle, M. et al. (2008) Antiretroelement activity of APOBEC3H was lost twice in recent human evolution. Cell Host and Microbe 4, 249-259
    • (2008) Cell Host and Microbe , vol.4 , pp. 249-259
    • Oh Ainle, M.1
  • 74
    • 58149374613 scopus 로고    scopus 로고
    • Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H
    • Harari, A. et al. (2009) Polymorphisms and splice variants influence the antiretroviral activity of human APOBEC3H. Journal of Virology 83, 295-303
    • (2009) Journal of Virology , vol.83 , pp. 295-303
    • Harari, A.1
  • 75
    • 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. (2009) Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory activity against retrotransposons and HIV-1. FASEB Journal 23, 279-287
    • (2009) FASEB Journal , vol.23 , pp. 279-287
    • Tan, L.1
  • 76
    • 11144244647 scopus 로고    scopus 로고
    • APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication
    • DOI 10.1074/jbc.M408802200
    • Yu, Q. et al. (2004) APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. Journal of Biological Chemistry 279, 53379-53386 (Pubitemid 40051843)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53379-53386
    • Yu, Q.1    Chen, D.2    Konig, R.3    Mariani, R.4    Unutmaz, D.5    Landau, N.R.6
  • 79
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • DOI 10.1016/j.cub.2004.06.050, PII S096098220400466X
    • Liddament, M.T. et al. (2004) APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Current Biology 14, 1385-1391 (Pubitemid 39081642)
    • (2004) Current Biology , vol.14 , Issue.15 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 80
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • DOI 10.1038/sj.emboj.7600246
    • Wiegand, H.L. et al. (2004) A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO Journal 23, 2451-2458 (Pubitemid 38954852)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 81
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng, Y.H. et al. (2004) Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. Journal of Virology 78, 6073-6076
    • (2004) Journal of Virology , vol.78 , pp. 6073-6076
    • Zheng, Y.H.1
  • 82
    • 68449092202 scopus 로고    scopus 로고
    • Architecture and secondary structure of an entire HIV-1 RNA genome
    • Watts, J.M. et al. (2009) Architecture and secondary structure of an entire HIV-1 RNA genome. Nature 460, 711-716
    • (2009) Nature , vol.460 , pp. 711-716
    • Watts, J.M.1
  • 83
    • 0034878971 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 DNA sequences genetically damaged by hypermutation are often abundant in patient peripheral blood mononuclear cells and may be generated during near-simultaneous infection and activation of CD4(+) Tcells
    • Janini, M. et al. (2001) Human immunodeficiency virus type 1 DNA sequences genetically damaged by hypermutation are often abundant in patient peripheral blood mononuclear cells and may be generated during near-simultaneous infection and activation of CD4(+) Tcells. Journal of Virology 75, 7973-7986
    • (2001) Journal of Virology , vol.75 , pp. 7973-7986
    • Janini, M.1
  • 84
    • 0025977774 scopus 로고
    • Selection, recombination, and G - A hypermutation of human immunodeficiency virus type 1 genomes
    • Vartanian, J.P. et al. (1991) Selection, recombination, and G - A hypermutation of human immunodeficiency virus type 1 genomes. Journal of Virology 65, 1779-1788
    • (1991) Journal of Virology , vol.65 , pp. 1779-1788
    • Vartanian, J.P.1
  • 86
    • 0025030676 scopus 로고
    • Broad spectrum of in vivo forward mutations, hypermutations, and mutational hotspots in a retroviral shuttle vector after a single replication cycle: Substitutions, frameshifts, and hypermutations
    • Pathak, V.K. and Temin, H.M. (1990) Broad spectrum of in vivo forward mutations, hypermutations, and mutational hotspots in a retroviral shuttle vector after a single replication cycle: substitutions, frameshifts, and hypermutations. Proceedings of the National Academy of Sciences of the United States of America 87, 6019-6023
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , pp. 6019-6023
    • Pathak, V.K.1    Temin, H.M.2
  • 87
    • 13744255000 scopus 로고    scopus 로고
    • + T cells in vivo
    • DOI 10.1128/JVI.79.3.1975-1980.2005
    • Kieffer, T.L. et al. (2005) G - >. A hypermutation in protease and reverse transcriptase regions of human immunodeficiency virus type 1 residing in resting CD4+ Tcells in vivo. Journal of Virology 79, 1975-1980 (Pubitemid 40459148)
    • (2005) Journal of Virology , vol.79 , Issue.3 , pp. 1975-1980
    • Kieffer, T.L.1    Kwon, P.2    Nettles, R.E.3    Han, Y.4    Ray, S.C.5    Siliciano, R.F.6
  • 88
    • 33748511879 scopus 로고    scopus 로고
    • Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation
    • DOI 10.1128/JVI.00888-06
    • Pace, C. et al. (2006) Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation. Journal of Virology 80, 9259-9269 (Pubitemid 44359998)
    • (2006) Journal of Virology , vol.80 , Issue.18 , pp. 9259-9269
    • Pace, C.1    Keller, J.2    Nolan, D.3    James, I.4    Gaudieri, S.5    Moore, C.6    Mallal, S.7
  • 89
    • 67749116433 scopus 로고    scopus 로고
    • Analysis of the percentage of human immunodeficiency virus type 1 sequences that are hypermutated and markers of disease progression in a longitudinal cohort, including one individual with a partially defective Vif
    • Piantadosi, A. et al. (2009) Analysis of the percentage of human immunodeficiency virus type 1 sequences that are hypermutated and markers of disease progression in a longitudinal cohort, including one individual with a partially defective Vif. Journal of Virology 83, 7805-7814
    • (2009) Journal of Virology , vol.83 , pp. 7805-7814
    • Piantadosi, A.1
  • 90
    • 49149090397 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya
    • Land, A.M. et al. (2008)Human immunodeficiency virus (HIV) type 1 proviral hypermutation correlates with CD4 count in HIV-infected women from Kenya. Journal of Virology 82, 8172-8182
    • (2008) Journal of Virology , vol.82 , pp. 8172-8182
    • Land, A.M.1
  • 91
    • 40149092360 scopus 로고    scopus 로고
    • Role of APOBEC3G/F-mediated hypermutation in the control of human immunodeficiency virus type 1 in elite suppressors
    • DOI 10.1128/JVI.01533-07
    • Gandhi, S.K. et al. (2008) Role of APOBEC3G/F-mediated hypermutation in the control of human immunodeficiency virus type 1 in elite suppressors. Journal of Virology 82, 3125-3130 (Pubitemid 351329200)
    • (2008) Journal of Virology , vol.82 , Issue.6 , pp. 3125-3130
    • Gandhi, S.K.1    Siliciano, J.D.2    Bailey, J.R.3    Siliciano, R.F.4    Blankson, J.N.5
  • 92
    • 53849138762 scopus 로고    scopus 로고
    • The level of APOBEC3G (hA3G)-related G-to-A mutations does not correlate with viral load in HIV type 1-infected individuals
    • Ulenga, N.K. et al. (2008) The level of APOBEC3G (hA3G)-related G-to-A mutations does not correlate with viral load in HIV type 1-infected individuals. AIDS Research and Human Retroviruses 24, 1285-1290
    • (2008) AIDS Research and Human Retroviruses , vol.24 , pp. 1285-1290
    • Ulenga, N.K.1
  • 93
    • 34247623286 scopus 로고    scopus 로고
    • Population stratification of a common APOBEC gene deletion polymorphism
    • Kidd, J.M. et al. (2007) Population stratification of a common APOBEC gene deletion polymorphism. PLoS Genetics 3, e63
    • (2007) PLoS Genetics , vol.3
    • Kidd, J.M.1
  • 95
    • 4444298202 scopus 로고    scopus 로고
    • APOBEC3G versus reverse transcriptase in the generation of HIV-1 drug-resistance mutations [4]
    • DOI 10.1097/00002030-200409030-00022
    • Berkhout, B. and de Ronde, A. (2004) APOBEC3G versus reverse transcriptase in the generation of HIV-1 drug-resistance mutations. AIDS 18, 1861-1863 (Pubitemid 39179645)
    • (2004) AIDS , vol.18 , Issue.13 , pp. 1861-1863
    • Berkhout, B.1    De Ronde, A.2
  • 96
    • 33750288097 scopus 로고    scopus 로고
    • Human APOBEC3 proteins, retrovirus restriction and HIV drug resistance
    • Haché, G., Mansky, L.M. and Harris, R.S. (2006) Human APOBEC3 proteins, retrovirus restriction, and HIV drug resistance. AIDS Reviews 8, 148-157 (Pubitemid 44614032)
    • (2006) AIDS Reviews , vol.8 , Issue.3 , pp. 148-157
    • Hache, G.1    Mansky, L.M.2    Harris, R.S.3
  • 97
    • 42449152863 scopus 로고    scopus 로고
    • Turning up the volume on mutational pressure: Is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3)
    • Pillai, S.K., Wong, J.K. and Barbour, J.D. (2008) Turning up the volume on mutational pressure: is more of a good thing always better? (A case study of HIV-1 Vif and APOBEC3). Retrovirology 5, 26
    • (2008) Retrovirology , vol.5 , pp. 26
    • Pillai, S.K.1    Wong, J.K.2    Barbour, J.D.3
  • 98
    • 66349132212 scopus 로고    scopus 로고
    • Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance
    • Jern, P. et al. (2009) Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance. PLoS Pathogens 5, e1000367
    • (2009) PLoS Pathogens , vol.5
    • Jern, P.1
  • 99
    • 67249140561 scopus 로고    scopus 로고
    • HIV evolution in early infection: Selection pressures, patterns of insertion and deletion, and the impact of APOBEC
    • Wood, N. et al. (2009) HIV evolution in early infection: selection pressures, patterns of insertion and deletion, and the impact of APOBEC. PLoS Pathogens 5, e1000414
    • (2009) PLoS Pathogens , vol.5
    • Wood, N.1
  • 100
    • 63549121125 scopus 로고    scopus 로고
    • APOBEC3G mRNA expression in exposed seronegative and early stage HIV infected individuals decreases with removal of exposure and with disease progression
    • Vázquez-Pérez, J.A. et al. (2009) APOBEC3G mRNA expression in exposed seronegative and early stage HIV infected individuals decreases with removal of exposure and with disease progression. Retrovirology 6, 23
    • (2009) Retrovirology , vol.6 , pp. 23
    • Vázquez-Pérez, J.A.1
  • 101
    • 23844483865 scopus 로고    scopus 로고
    • APOBEC3G/CEM15 (hA3G) mRNA levels associate inversely with human immunodeficiency virus viremia
    • DOI 10.1128/JVI.79.17.11513-11516.2005
    • Jin, X. et al. (2005) APOBEC3G/CEM15 (hA3G) mRNA levels associate inversely with human immunodeficiency virus viremia. Journal of Virology 79, 11513-11516 (Pubitemid 41170693)
    • (2005) Journal of Virology , vol.79 , Issue.17 , pp. 11513-11516
    • Jin, X.1    Brooks, A.2    Chen, H.3    Bennett, R.4    Reichman, R.5    Smith, H.6
  • 102
    • 32444434763 scopus 로고    scopus 로고
    • APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count
    • Cho, S.J. et al. (2006) APOBEC3F and APOBEC3G mRNA levels do not correlate with human immunodeficiency virus type 1 plasma viremia or CD4+ T-cell count. Journal of Virology 80, 2069-2072
    • (2006) Journal of Virology , vol.80 , pp. 2069-2072
    • Cho, S.J.1
  • 103
    • 48749099260 scopus 로고    scopus 로고
    • Relationship between human immunodeficiency type 1 infection and expression of human APOBEC3G and APOBEC3F
    • Ulenga, N.K. et al. (2008) Relationship between human immunodeficiency type 1 infection and expression of human APOBEC3G and APOBEC3F. Journal of Infectious Diseases 198, 486-492
    • (2008) Journal of Infectious Diseases , vol.198 , pp. 486-492
    • Ulenga, N.K.1
  • 107
    • 33748898695 scopus 로고    scopus 로고
    • APOBEC3G genetic variants and their association with risk of HIV infection in highly exposed Caucasians
    • DOI 10.1097/01.aids.0000247124.35129.e1, PII 0000203020061003000015
    • Valcke, H.S. et al. (2006) APOBEC3G genetic variants and their association with risk of HIV infection in highly exposed Caucasians. AIDS 20, 1984-1986 (Pubitemid 44427620)
    • (2006) AIDS , vol.20 , Issue.15 , pp. 1984-1986
    • Valcke, H.S.1    Bernard, N.F.2    Bruneau, J.3    Alary, M.4    Tsoukas, C.M.5    Roger, M.6
  • 108
    • 70349310335 scopus 로고    scopus 로고
    • APOBEC3B deletion and risk of HIV-1 acquisition
    • An, P. et al. (2009) APOBEC3B deletion and risk of HIV-1 acquisition. Journal of Infectious Diseases 200, 1054-1058
    • (2009) Journal of Infectious Diseases , vol.200 , pp. 1054-1058
    • An, P.1
  • 109
    • 33645760962 scopus 로고    scopus 로고
    • Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H
    • OhAinle, M. et al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. Journal of Virology 80, 3853-3862
    • (2006) Journal of Virology , vol.80 , pp. 3853-3862
    • OhAinle, M.1
  • 110
    • 19344362934 scopus 로고    scopus 로고
    • Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G
    • Sawyer, S.L., Emerman, M. and Malik, H.S. (2004) Ancient adaptive evolution of the primate antiviral DNA-editing enzyme APOBEC3G. PLoS Biology 2, E275
    • (2004) PLoS Biology , vol.2
    • Sawyer, S.L.1    Emerman, M.2    Malik, H.S.3
  • 111
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells
    • Chiu, Y.L. et al. (2005)Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature 435, 108-114
    • (2005) Nature , vol.435 , pp. 108-114
    • Chiu, Y.L.1
  • 113
    • 68749115269 scopus 로고    scopus 로고
    • APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection
    • Santoni de Sio, F.R. and Trono, D. (2009) APOBEC3G-depleted resting CD4+ T cells remain refractory to HIV1 infection. PLoS One 4, e6571
    • (2009) PLoS One , vol.4
    • Santoni De Sio, F.R.1    Trono, D.2
  • 114
    • 63449095109 scopus 로고    scopus 로고
    • Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells
    • Kamata, M., Nagaoka, Y. and Chen, I.S. (2009) Reassessing the role of APOBEC3G in human immunodeficiency virus type 1 infection of quiescent CD4+ T-cells. PLoS Pathogens 5, e1000342
    • (2009) PLoS Pathogens , vol.5
    • Kamata, M.1    Nagaoka, Y.2    Chen, I.S.3
  • 115
    • 61449129570 scopus 로고    scopus 로고
    • Differences in APOBEC3G expression in CD4+ T helper lymphocyte subtypes modulate HIV-1 infectivity
    • Vetter, M.L. et al. (2009) Differences in APOBEC3G expression in CD4+ T helper lymphocyte subtypes modulate HIV-1 infectivity. PLoS Pathogens 5, e1000292
    • (2009) PLoS Pathogens , vol.5
    • Vetter, M.L.1
  • 116
    • 69449103867 scopus 로고    scopus 로고
    • Defining APOBEC3 Expression Patterns in Human Tissues and Hematopoietic Cell Subsets
    • Koning, F.A. et al. (2009) Defining APOBEC3 Expression Patterns in Human Tissues and Hematopoietic Cell Subsets. Journal of Virology 83, 9474-9485
    • (2009) Journal of Virology , vol.83 , pp. 9474-9485
    • Koning, F.A.1
  • 119
    • 31944438580 scopus 로고    scopus 로고
    • Induction of APOBEC3 family proteins, a defensive maneuver underlying interferon-induced anti-HIV-1 activity
    • Peng, G. et al. (2006) Induction of APOBEC3 family proteins, a defensive maneuver underlying interferon-induced anti-HIV-1 activity. Journal of Experimental Medicine 203, 41-46
    • (2006) Journal of Experimental Medicine , vol.203 , pp. 41-46
    • Peng, G.1
  • 120
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • DOI 10.1128/JVI.00395-07
    • Russell, R.A. and Pathak, V.K. (2007) Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. Journal of Virology 81, 8201-8210 (Pubitemid 47101506)
    • (2007) Journal of Virology , vol.81 , Issue.15 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 121
    • 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 Pathogens 1, e6
    • (2005) PLoS Pathogens , vol.1
    • Simon, V.1
  • 122
    • 58049217469 scopus 로고    scopus 로고
    • Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host antiviral proteins
    • Zhang, W. et al. (2008) Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host antiviral proteins. PLoS One 3, e3963
    • (2008) PLoS One , vol.3
    • Zhang, W.1
  • 123
    • 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. Journal of Molecular Biology 381, 1000-1011
    • (2008) Journal of Molecular Biology , vol.381 , pp. 1000-1011
    • He, Z.1
  • 124
    • 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
    • DOI 10.1128/JVI.80.6.3112-3115.2006
    • 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. Journal of Virology 80, 3112-3115 (Pubitemid 43346410)
    • (2006) Journal of Virology , vol.80 , Issue.6 , pp. 3112-3115
    • Tian, C.1    Yu, X.2    Zhang, W.3    Wang, T.4    Xu, R.5    Yu, X.-F.6
  • 125
    • 54049112596 scopus 로고    scopus 로고
    • Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F
    • Yamashita, T. et al. (2008) Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F. Microbes and Infection 10, 1142-1149
    • (2008) Microbes and Infection , vol.10 , pp. 1142-1149
    • Yamashita, T.1
  • 126
    • 63449090379 scopus 로고    scopus 로고
    • RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1
    • Huthoff, H. et al. (2009) RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1. PLoS Pathogens 5, e1000330
    • (2009) PLoS Pathogens , vol.5
    • Huthoff, H.1
  • 127
    • 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
    • DOI 10.1128/JVI.02795-06
    • Huthoff, H. and Malim, M.H. (2007) Identification of amino acid residues in APOBEC3G required for regulation by human immunodeficiency virus type 1 Vif and Virion encapsidation. Journal of Virology 81, 3807-3815 (Pubitemid 46586878)
    • (2007) Journal of Virology , vol.81 , Issue.8 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 128
    • 59649118427 scopus 로고    scopus 로고
    • Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif
    • Russell, R.A. et al. (2009) Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif. Journal of Virology 83, 1992-2003
    • (2009) Journal of Virology , vol.83 , pp. 1992-2003
    • Russell, R.A.1
  • 129
    • 36549004535 scopus 로고    scopus 로고
    • Function analysis of sequences in human APOBEC3G involved in Vif-mediated degradation
    • DOI 10.1016/j.virol.2007.08.027, PII S0042682207005612
    • Zhang, L. et al. (2008) Function analysis of sequences in human APOBEC3G involved in Vif-mediated degradation. Virology 370, 113-121 (Pubitemid 350179917)
    • (2008) Virology , vol.370 , Issue.1 , pp. 113-121
    • Zhang, L.1    Saadatmand, J.2    Li, X.3    Guo, F.4    Niu, M.5    Jiang, J.6    Kleiman, L.7    Cen, S.8
  • 130
    • 60049098639 scopus 로고    scopus 로고
    • Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif
    • Pery, E. et al. (2009) Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. Journal of Virology 83, 2374-2381
    • (2009) Journal of Virology , vol.83 , pp. 2374-2381
    • Pery, E.1
  • 131
    • 69249215357 scopus 로고    scopus 로고
    • A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G
    • Chen, G. et al. (2009) A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. Journal of Virology 83, 8674-8682
    • (2009) Journal of Virology , vol.83 , pp. 8674-8682
    • Chen, G.1
  • 132
    • 69249220263 scopus 로고    scopus 로고
    • Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization
    • Dang, Y. et al. (2009) Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. Journal of Virology 83, 8544-8552
    • (2009) Journal of Virology , vol.83 , pp. 8544-8552
    • Dang, Y.1
  • 133
    • 67349258491 scopus 로고    scopus 로고
    • An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model
    • Harjes, E. et al. (2009) An extended structure of the APOBEC3G catalytic domain suggests a unique holoenzyme model. Journal of Molecular Biology 389, 819-832
    • (2009) Journal of Molecular Biology , vol.389 , pp. 819-832
    • Harjes, E.1
  • 134
    • 53649086178 scopus 로고    scopus 로고
    • Small-molecule inhibition of HIV-1 Vif
    • Nathans, R. et al. (2008) Small-molecule inhibition of HIV-1 Vif. Nature Biotechnology 26, 1187-1192
    • (2008) Nature Biotechnology , vol.26 , pp. 1187-1192
    • Nathans, R.1
  • 135
    • 40449114441 scopus 로고    scopus 로고
    • Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G
    • Chen, K.M. et al. (2008) Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Nature 452, 116-119
    • (2008) Nature , vol.452 , pp. 116-119
    • Chen, K.M.1
  • 136
    • 55549098517 scopus 로고    scopus 로고
    • Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications
    • Holden, L.G. et al. (2008) Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature 456, 121-124
    • (2008) Nature , vol.456 , pp. 121-124
    • Holden, L.G.1
  • 137
    • 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 Journal 28, 440-451
    • (2009) EMBO Journal , vol.28 , pp. 440-451
    • Furukawa, A.1
  • 138
    • 33846555779 scopus 로고    scopus 로고
    • The APOBEC-2 crystal structure and functional implications for the deaminase AID
    • DOI 10.1038/nature05492, PII NATURE05492
    • Prochnow, C. et al. (2007) The APOBEC-2 crystal structure and functional implications for the deaminase AID. Nature 445, 447-451 (Pubitemid 46160914)
    • (2007) Nature , vol.445 , Issue.7126 , pp. 447-451
    • Prochnow, C.1    Bransteitter, R.2    Klein, M.G.3    Goodman, M.F.4    Chen, X.S.5
  • 139
  • 140
    • 62049083710 scopus 로고    scopus 로고
    • Phase 2 gene therapy trial of an anti-HIV ribozyme in autologous CD34+ cells
    • Mitsuyasu, R.T. et al. (2009) Phase 2 gene therapy trial of an anti-HIV ribozyme in autologous CD34+ cells. Nature Medicine 15, 285-292
    • (2009) Nature Medicine , vol.15 , pp. 285-292
    • Mitsuyasu, R.T.1
  • 141
    • 60549090253 scopus 로고    scopus 로고
    • Long-term control of HIV by CCR5 Delta32/Delta32 stem-cell transplantation
    • Hutter, G. et al. (2009) Long-term control of HIV by CCR5 Delta32/Delta32 stem-cell transplantation. New England Journal of Medicine 360, 692-698
    • (2009) New England Journal of Medicine , vol.360 , pp. 692-698
    • Hutter, G.1
  • 142
    • 36849028631 scopus 로고    scopus 로고
    • Genetic therapies against HIV
    • DOI 10.1038/nbt1367, PII NBT1367
    • Rossi, J.J., June, C.H. and Kohn, D.B. (2007) Genetic therapies against HIV. Nature Biotechnology 25, 1444-1454 (Pubitemid 350233141)
    • (2007) Nature Biotechnology , vol.25 , Issue.12 , pp. 1444-1454
    • Rossi, J.J.1    June, C.H.2    Kohn, D.B.3
  • 143
  • 144
    • 2442511993 scopus 로고    scopus 로고
    • A Single Amino Acid Determinant Governs the Species-specific Sensitivity of APOBEC3G to Vif Action
    • DOI 10.1074/jbc.C400060200
    • Mangeat, B. et al. (2004) A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. Journal of Biological Chemistry 279, 14481-14483 (Pubitemid 38618833)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 145
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • DOI 10.1073/pnas.0307132101
    • Schröfelbauer, B., Chen, D. and Landau, N.R. (2004) A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proceedings of the National Academy of Sciences of the United States of America 101, 3927-3932 (Pubitemid 38381079)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.11 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 147
    • 52049111036 scopus 로고    scopus 로고
    • APOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replication
    • Li, L. et al. (2008) APOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replication. Retrovirology 5, 72
    • (2008) Retrovirology , vol.5 , pp. 72
    • Li, L.1
  • 148
    • 0029159759 scopus 로고
    • Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals
    • Yamanaka, S. et al. (1995) Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals. Proceedings of the National Academy of Sciences of the United States of America 92, 8483-8487
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , pp. 8483-8487
    • Yamanaka, S.1
  • 149
    • 44849100325 scopus 로고    scopus 로고
    • Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection
    • Ao, Z. et al. (2008) Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection. PLoS One 3, e1995
    • (2008) PLoS One , vol.3
    • Ao, Z.1
  • 150
    • 41449116464 scopus 로고    scopus 로고
    • Vpr.A3A chimera inhibits HIV replication
    • Aguiar, R.S. et al. (2008) Vpr.A3A chimera inhibits HIV replication. Journal of Biological Chemistry 283, 2518-2525
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 2518-2525
    • Aguiar, R.S.1
  • 151
    • 67649410579 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: A non-pathogenic Nef mutant-based anti-HIV strategy
    • Green, L.A., Liu, Y. and He, J.J. (2009) Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: a non-pathogenic Nef mutant-based anti-HIV strategy. Journal of Biological Chemistry 284, 13363-13372
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 13363-13372
    • Green, L.A.1    Liu, Y.2    He, J.J.3
  • 152
    • 35448976039 scopus 로고    scopus 로고
    • Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity
    • Goila-Gaur, R. et al. (2007) Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity. Retrovirology 4, 61
    • (2007) Retrovirology , vol.4 , pp. 61
    • Goila-Gaur, R.1
  • 153
    • 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. Journal of Virology 82, 987-998
    • (2008) Journal of Virology , vol.82 , pp. 987-998
    • Marin, M.1
  • 154
    • 23444450544 scopus 로고    scopus 로고
    • Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G
    • DOI 10.1089/aid.2005.21.611
    • Rose, K.M. et al. (2005) Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G. AIDS Research and Human Retroviruses 21, 611-619 (Pubitemid 41113649)
    • (2005) AIDS Research and Human Retroviruses , vol.21 , Issue.7 , pp. 611-619
    • Rose, K.M.1    Marin, M.2    Kozak, S.L.3    Kabat, D.4
  • 155
    • 56449092831 scopus 로고    scopus 로고
    • Equine infectious anemia virus resists the antiretroviral activity of equine APOBEC3 proteins through a packaging-independent mechanism
    • Bogerd, H.P. et al. (2008) Equine infectious anemia virus resists the antiretroviral activity of equine APOBEC3 proteins through a packaging-independent mechanism. Journal of Virology 82, 11889-11901
    • (2008) Journal of Virology , vol.82 , pp. 11889-11901
    • Bogerd, H.P.1
  • 156
    • 31644442239 scopus 로고    scopus 로고
    • APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells
    • DOI 10.1093/nar/gkj416
    • Bogerd, H.P. et al. (2006) APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells. Nucleic Acids Research 34, 89-95 (Pubitemid 43167918)
    • (2006) Nucleic Acids Research , vol.34 , Issue.1 , pp. 89-95
    • Bogerd, H.P.1    Wiegand, H.L.2    Doehle, B.P.3    Lueders, K.K.4    Cullen, B.R.5
  • 158
    • 48949084728 scopus 로고    scopus 로고
    • Functional domain organization of human APOBEC3G
    • Gooch, B.D. and Cullen, B.R. (2008) Functional domain organization of human APOBEC3G. Virology 379, 118-124
    • (2008) Virology , vol.379 , pp. 118-124
    • Gooch, B.D.1    Cullen, B.R.2
  • 160
    • 34249892197 scopus 로고    scopus 로고
    • The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains
    • DOI 10.1016/j.virol.2007.03.019, PII S0042682207001778
    • Bogerd, H.P. et al. (2007) The intrinsic antiretroviral factor APOBEC3B contains two enzymatically active cytidine deaminase domains. Virology 364, 486-493 (Pubitemid 46873711)
    • (2007) Virology , vol.364 , Issue.2 , pp. 486-493
    • Bogerd, H.P.1    Wiegand, H.L.2    Doehle, B.P.3    Cullen, B.R.4
  • 161
    • 23844483541 scopus 로고    scopus 로고
    • Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif
    • DOI 10.1016/j.virol.2005.06.005, PII S0042682205003338
    • Doehle, B.P., Schafer, A. and Cullen, B.R. (2005) Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif. Virology 339, 281-288 (Pubitemid 41169795)
    • (2005) Virology , vol.339 , Issue.2 , pp. 281-288
    • Doehle, B.P.1    Schafer, A.2    Cullen, B.R.3
  • 162
    • 33846031136 scopus 로고    scopus 로고
    • Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains
    • DOI 10.1074/jbc.M604980200
    • Hakata, Y. and Landau, N.R. (2006) Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. Journal of Biological Chemistry 281, 36624-36631 (Pubitemid 46042129)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.48 , pp. 36624-36631
    • Hakata, Y.1    Landau, N.R.2
  • 163
    • 17144432313 scopus 로고    scopus 로고
    • Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into theirDNAtarget site specificities
    • Langlois, M.A. et al. (2005) Mutational comparison of the single-domained APOBEC3C and double-domained APOBEC3F/G anti-retroviral cytidine deaminases provides insight into theirDNAtarget site specificities. Nucleic Acids Research 33, 1913-1923
    • (2005) Nucleic Acids Research , vol.33 , pp. 1913-1923
    • Langlois, M.A.1
  • 164
    • 45549100648 scopus 로고    scopus 로고
    • Human cytidine deaminase APOBEC3H restricts HIV-1 replication
    • Dang, Y. et al. (2008) Human cytidine deaminase APOBEC3H restricts HIV-1 replication. Journal of Biological Chemistry 283, 11606-11614
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 11606-11614
    • Dang, Y.1
  • 165
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • DOI 10.1128/JVI.01123-06
    • Dang, Y. et al. (2006) Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. Journal of Virology80, 10522-10533 (Pubitemid 44628899)
    • (2006) Journal of Virology , vol.80 , Issue.21 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.-H.4
  • 166
    • 48249102331 scopus 로고    scopus 로고
    • APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication
    • Han, Y. et al. (2008) APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication. PLoS Pathogens 4, e1000095
    • (2008) PLoS Pathogens , vol.4
    • Han, Y.1
  • 167
    • 72849138650 scopus 로고    scopus 로고
    • The range of human APOBEC3H sensitivity to lentiviral Vif proteins
    • Li, M.M., Wu, L.I. and Emerman, M. (2010) The range of human APOBEC3H sensitivity to lentiviral Vif proteins. Journal of Virology 84, 88-95
    • (2010) Journal of Virology , vol.84 , pp. 88-95
    • Li, M.M.1    Wu, L.I.2    Emerman, M.3
  • 168
    • 76349094670 scopus 로고    scopus 로고
    • APOBEC3 proteins mediate the clearance of foreign DNA from human cells
    • Jan 10; Epub ahead of print
    • Stenglein, M.D. et al. (2010) APOBEC3 proteins mediate the clearance of foreign DNA from human cells. Nature Structural & Molecular Biology Jan 10; [Epub ahead of print]
    • (2010) Nature Structural & Molecular Biology
    • Stenglein, M.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.