메뉴 건너뛰기




Volumn 3, Issue 4, 2008, Pages

Vpr14-88-Apobec3G fusion protein is efficiently incorporated into vif-positive HIV-1 particles and inhibits viral infection

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CHEMOKINE RECEPTOR CCR5; COMPLEMENTARY DNA; HYBRID PROTEIN; LENTIVIRUS VECTOR; VIF PROTEIN; VIRUS DNA; VPR PROTEIN; VPR14 88 APOBEC3G FUSION PROTEIN; APOBEC3G PROTEIN, HUMAN; CYTIDINE DEAMINASE; VPR PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 44849100325     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001995     Document Type: Article
Times cited : (32)

References (71)
  • 1
    • 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, Gaddis NC, Choi JD, Malim MH (2002) Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418: 646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 2
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, et al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424: 94-98.
    • (2003) Nature , vol.424 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5
  • 4
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier D, Bouchonnet F, Clavel F, Hance AJ (2003) Hypermutation of HIV-1 DNA in the absence of the Vif protein. Science 300: 1112.
    • (2003) Science , vol.300 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 5
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat B, Turelli P, Caron G, Friedli M, Perrin I, et al. (2003) Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 424: 99-103.
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, I.5
  • 6
    • 0038107587 scopus 로고    scopus 로고
    • Mariani R, Chen D, Schrofelbauer B, Navarro F, Konig R, et al. (2003) Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114: 21-31.
    • Mariani R, Chen D, Schrofelbauer B, Navarro F, Konig R, et al. (2003) Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114: 21-31.
  • 7
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells
    • Chiu YL, Soros VB, Kreisberg JF, Stopak K, Yonemoto W, 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    Soros, V.B.2    Kreisberg, J.F.3    Stopak, K.4    Yonemoto, W.5
  • 8
    • 12544256041 scopus 로고    scopus 로고
    • Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity
    • Newman EN, Holmes RK, Craig HM, Klein KC, Lingappa JR, et al. (2005) Antiviral function of APOBEC3G can be dissociated from cytidine deaminase activity. Curr Biol 15: 166-170.
    • (2005) Curr Biol , vol.15 , pp. 166-170
    • Newman, E.N.1    Holmes, R.K.2    Craig, H.M.3    Klein, K.C.4    Lingappa, J.R.5
  • 10
    • 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: 34083-34086.
    • (2004) J Biol Chem , vol.279 , pp. 34083-34086
    • Alce, T.M.1    Popik, W.2
  • 11
    • 20744439203 scopus 로고    scopus 로고
    • Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion
    • Doehle BP, Schafer A, Wiegand HL, Bogerd HP, Cullen BR (2005) Differential sensitivity of murine leukemia virus to APOBEC3-mediated inhibition is governed by virion exclusion. J Virol 79: 8201-8207.
    • (2005) J Virol , vol.79 , pp. 8201-8207
    • Doehle, B.P.1    Schafer, A.2    Wiegand, H.L.3    Bogerd, H.P.4    Cullen, B.R.5
  • 12
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
    • Luo K, Liu B, Xiao Z, Yu Y, Yu Y, et al. (2004) Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging. J Virol 78: 11841-11852.
    • (2004) J Virol , vol.78 , pp. 11841-11852
    • Luo, K.1    Liu, B.2    Xiao, Z.3    Yu, Y.4    Yu, Y.5
  • 13
    • 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: 163-168.
    • (2004) Virology , vol.328 , pp. 163-168
    • Schafer, A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 14
    • 4143124683 scopus 로고    scopus 로고
    • Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APO-BEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs
    • Svarovskaia ES, Xu H, Mbisa JL, Barr R, Gorelick RJ, et al. (2004) Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APO-BEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs. J Biol Chem 279: 35822-35828.
    • (2004) J Biol Chem , vol.279 , pp. 35822-35828
    • Svarovskaia, E.S.1    Xu, H.2    Mbisa, J.L.3    Barr, R.4    Gorelick, R.J.5
  • 15
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou V, Perez-Caballero D, Gottlinger H, Bieniasz PD (2004) APOBEC3G incorporation into human immunodeficiency virus type 1 particles. J Virol 78: 12058-12061.
    • (2004) J Virol , vol.78 , pp. 12058-12061
    • Zennou, V.1    Perez-Caballero, D.2    Gottlinger, H.3    Bieniasz, P.D.4
  • 16
    • 34248335849 scopus 로고    scopus 로고
    • APOBEC3G multimers are recruited to the plasma membrane for packaging into human immunodeficiency virus type 1 virus-like particles in an RNA-dependent process requiring the NC basic linker
    • 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-dependent process requiring the NC basic linker. J Virol 81: 5000-5013.
    • (2007) J Virol , vol.81 , pp. 5000-5013
    • Burnett, A.1    Spearman, P.2
  • 17
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak K, de Noronha C, Yonemoto W, Greene WC (2003) HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell 12: 591-601.
    • (2003) Mol Cell , vol.12 , pp. 591-601
    • Stopak, K.1    de Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 18
    • 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: 1404-1407.
    • (2003) Nat Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 19
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M, Rose KM, Kozak SL, Kabat D (2003) HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 9: 1398-1403.
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 20
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cu15-SCF complex
    • Yu X, Yu Y, Liu B, Luo K, Kong W, et al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cu15-SCF complex. Science 302: 1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5
  • 21
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cu15-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • Yu Y, Xiao Z, Ehrlich ES, Yu X, Yu XF (2004) Selective assembly of HIV-1 Vif-Cu15-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev 18: 2867-2872.
    • (2004) Genes Dev , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 22
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity
    • Kao S, Khan MA, Miyagi E, Plishka R, Buckler-White A, 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. J Virol 77: 11398-11407.
    • (2003) J Virol , vol.77 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5
  • 23
    • 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: 2009-2013.
    • (2003) Curr Biol , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 24
    • 18144374907 scopus 로고    scopus 로고
    • Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells
    • Kao S, Miyagi E, Khan MA, Takeuchi H, Opi S, et al. (2004) Production of infectious human immunodeficiency virus type 1 does not require depletion of APOBEC3G from virus-producing cells. Retrovirology 1: 27.
    • (2004) Retrovirology , vol.1 , pp. 27
    • Kao, S.1    Miyagi, E.2    Khan, M.A.3    Takeuchi, H.4    Opi, S.5
  • 25
    • 36048964842 scopus 로고    scopus 로고
    • Kan S, Goila-Gaur R, Miyagi E, Khan MA, Opi 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: 329-339.
    • Kan S, Goila-Gaur R, Miyagi E, Khan MA, Opi 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: 329-339.
  • 26
    • 34547130033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant
    • Opi S, Kao S, Goila-Gaur R, Khan MA, Miyagi E, et al. (2007) Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant. J Virol 81: 8236-8246.
    • (2007) J Virol , vol.81 , pp. 8236-8246
    • Opi, S.1    Kao, S.2    Goila-Gaur, R.3    Khan, M.A.4    Miyagi, E.5
  • 27
    • 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, Doehle BP, Wiegand HL, Cullen BR (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 U S A 101: 3770-3774.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3770-3774
    • Bogerd, H.P.1    Doehle, B.P.2    Wiegand, H.L.3    Cullen, B.R.4
  • 28
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat B, Turelli P, Liao S, Trono D (2004) A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action. J Biol Chem 279: 14481-14483.
    • (2004) J Biol Chem , vol.279 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 29
    • 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 U S A 101: 3927-3932.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 30
    • 1842732157 scopus 로고    scopus 로고
    • A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion
    • Xu H, Svarovskaia ES, Barr R, Zhang Y, Khan MA, 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 U S A 101: 5652-5657.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5652-5657
    • Xu, H.1    Svarovskaia, E.S.2    Barr, R.3    Zhang, Y.4    Khan, M.A.5
  • 31
    • 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: 3807-3815.
    • (2007) J Virol , vol.81 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 32
    • 0028840657 scopus 로고
    • Mutagenic analysis of human immunodeficiency virus type 1 Vpr: Role of a predicted N-terminal alpha-helical structure in Vpr nuclear localizatton and virion incorporation
    • Yao XJ, Subbramanian RA, Rougeau N, Boisvert F, Bergeron D, et al. (1995) Mutagenic analysis of human immunodeficiency virus type 1 Vpr: role of a predicted N-terminal alpha-helical structure in Vpr nuclear localizatton and virion incorporation. J Virol 69: 7032-7044.
    • (1995) J Virol , vol.69 , pp. 7032-7044
    • Yao, X.J.1    Subbramanian, R.A.2    Rougeau, N.3    Boisvert, F.4    Bergeron, D.5
  • 33
    • 0027429412 scopus 로고
    • Incorporation of Vpr into human immunodeficiency virus type 1 virions: Requirement for the p6 region of Gag and mutational analysis
    • Paxton W, Connor RI, Landau NR (1993) Incorporation of Vpr into human immunodeficiency virus type 1 virions: requirement for the p6 region of Gag and mutational analysis. J. Virol. 67: 7229-7237.
    • (1993) J. Virol , vol.67 , pp. 7229-7237
    • Paxton, W.1    Connor, R.I.2    Landau, N.R.3
  • 34
    • 0027376064 scopus 로고
    • Human immunodeficiency vim type 1 viral protein R localization in infected cells and virions
    • Lu YL, Spearman P, Ratner L (1993) Human immunodeficiency vim type 1 viral protein R localization in infected cells and virions. J Virol 67: 6542-6550.
    • (1993) J Virol , vol.67 , pp. 6542-6550
    • Lu, Y.L.1    Spearman, P.2    Ratner, L.3
  • 35
    • 0028987472 scopus 로고
    • The p6gag domain of human immunodeficiency virus type 1 is sufficient for the incorporation of Vpr into heterologous viral particles
    • Kondo E, Mammano F, Cohen EA, Gottlinger HG (1995) The p6gag domain of human immunodeficiency virus type 1 is sufficient for the incorporation of Vpr into heterologous viral particles. J Virol 69: 2759-2764.
    • (1995) J Virol , vol.69 , pp. 2759-2764
    • Kondo, E.1    Mammano, F.2    Cohen, E.A.3    Gottlinger, H.G.4
  • 36
    • 0028388662 scopus 로고
    • Requirement of the Pr55gag precursor for incorporation of the Vpr product into human immunodeficiency virus type 1 viral particles
    • Lavallee C, Yao XJ, Ladha A, Gottlinger H, Haseltine WA, et al. (1994) Requirement of the Pr55gag precursor for incorporation of the Vpr product into human immunodeficiency virus type 1 viral particles. J Virol 68: 1926-1934.
    • (1994) J Virol , vol.68 , pp. 1926-1934
    • Lavallee, C.1    Yao, X.J.2    Ladha, A.3    Gottlinger, H.4    Haseltine, W.A.5
  • 37
    • 0029039296 scopus 로고
    • Targeting foreign proteins to human immunodeficiency virus particles via fusion with Vpr and Vpx
    • Wu X, Liu H, Xiao H, Kim J, Seshaiah P, et al. (1995) Targeting foreign proteins to human immunodeficiency virus particles via fusion with Vpr and Vpx. J Virol 69: 3389-3398.
    • (1995) J Virol , vol.69 , pp. 3389-3398
    • Wu, X.1    Liu, H.2    Xiao, H.3    Kim, J.4    Seshaiah, P.5
  • 38
    • 0029895892 scopus 로고    scopus 로고
    • Proteolytic activity of human immunodeficiency virus Vpr- and Vpx-protease fusion proteins
    • Wu X, Liu H, Xiao H, Kappes JC (1996) Proteolytic activity of human immunodeficiency virus Vpr- and Vpx-protease fusion proteins. Virology 219: 307-313.
    • (1996) Virology , vol.219 , pp. 307-313
    • Wu, X.1    Liu, H.2    Xiao, H.3    Kappes, J.C.4
  • 39
    • 0030851908 scopus 로고    scopus 로고
    • Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein
    • Wu X, Liu H, Xiao H, Conway JA, Hunter E, et al. (1997) Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein. Embo J 16: 5113-5122.
    • (1997) Embo J , vol.16 , pp. 5113-5122
    • Wu, X.1    Liu, H.2    Xiao, H.3    Conway, J.A.4    Hunter, E.5
  • 40
    • 0031799928 scopus 로고    scopus 로고
    • Virion-targeted viral inactivation of human immunodeficiency virus type 1 by using Vpr fusion proteins
    • Kobinger GP, Borsetti A, Nie Z, Mercier J, Daniel N, et al. (1998) Virion-targeted viral inactivation of human immunodeficiency virus type 1 by using Vpr fusion proteins. J Virol 72: 5441-5448.
    • (1998) J Virol , vol.72 , pp. 5441-5448
    • Kobinger, G.P.1    Borsetti, A.2    Nie, Z.3    Mercier, J.4    Daniel, N.5
  • 41
    • 0032863222 scopus 로고    scopus 로고
    • HIV-1 Vpr-chloramphenicol acetyltransferase fusion proteins: Sequence requirement for virion incorporation and analysis of antiviral effect
    • Yao XJ, Kobinger G, Dandache S, Rougeau N, Cohen E (1999) HIV-1 Vpr-chloramphenicol acetyltransferase fusion proteins: sequence requirement for virion incorporation and analysis of antiviral effect. Gene Ther 6: 1590-1599.
    • (1999) Gene Ther , vol.6 , pp. 1590-1599
    • Yao, X.J.1    Kobinger, G.2    Dandache, S.3    Rougeau, N.4    Cohen, E.5
  • 43
    • 0029994625 scopus 로고    scopus 로고
    • Targeting a foreign protein into virion particles by fusion with the Vpx protein of simian immunodeficiency virus
    • Park IW, Sodroski J (1996) Targeting a foreign protein into virion particles by fusion with the Vpx protein of simian immunodeficiency virus. J Acquir Immune Defic Syndr Hum Retrovirol 11: 341-350.
    • (1996) J Acquir Immune Defic Syndr Hum Retrovirol , vol.11 , pp. 341-350
    • Park, I.W.1    Sodroski, J.2
  • 44
    • 1542317624 scopus 로고    scopus 로고
    • Assessment of the role of the central DNA flap in human immunodeficiency virus type 1 replication by using a single-cycle replication system
    • Ao Z, Yao X, Cohen EA (2004) Assessment of the role of the central DNA flap in human immunodeficiency virus type 1 replication by using a single-cycle replication system. J Virol 78: 3170-3177.
    • (2004) J Virol , vol.78 , pp. 3170-3177
    • Ao, Z.1    Yao, X.2    Cohen, E.A.3
  • 45
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated b-galactosidase gene
    • Kimpton J, Emerman M (1992) Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated b-galactosidase gene. J Virol 66: 2232-2239.
    • (1992) J Virol , vol.66 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 46
    • 1342343136 scopus 로고    scopus 로고
    • Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression
    • Nguyen KL, Ilano M, Akari H, Miyagi E, Poeschla EM, et al. (2004) Codon optimization of the HIV-1 vpu and vif genes stabilizes their mRNA and allows for highly efficient Rev-independent expression. Virology 319: 163-175.
    • (2004) Virology , vol.319 , pp. 163-175
    • Nguyen, K.L.1    Ilano, M.2    Akari, H.3    Miyagi, E.4    Poeschla, E.M.5
  • 47
    • 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: 8450-8458.
    • (2006) J Virol , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 48
    • 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, Koning FA, Bishop KN, Malim MH (2007) APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J Biol Chem 282: 2587-2595.
    • (2007) J Biol Chem , vol.282 , pp. 2587-2595
    • Holmes, R.K.1    Koning, F.A.2    Bishop, K.N.3    Malim, M.H.4
  • 50
    • 27744456221 scopus 로고    scopus 로고
    • Contribution of the C-terminal trilysine regions of human immunodeficiency virus type 1 integrase for efficient reverse transcription and viral DNA nuclear import
    • Ao Z, Fowke KR, Cohen EA, Yao X (2005) Contribution of the C-terminal trilysine regions of human immunodeficiency virus type 1 integrase for efficient reverse transcription and viral DNA nuclear import. Retrovirology 2: 62.
    • (2005) Retrovirology , vol.2 , pp. 62
    • Ao, Z.1    Fowke, K.R.2    Cohen, E.A.3    Yao, X.4
  • 51
    • 0035105820 scopus 로고    scopus 로고
    • Filovirus-pseudotyped lentiviral vector can efficiently and stably transduce airway epithelia in vivo
    • Kobinger GP, Weiner DJ, Yu QC, Wilson JM (2001) Filovirus-pseudotyped lentiviral vector can efficiently and stably transduce airway epithelia in vivo. Nat Biotechnol 19: 225-230.
    • (2001) Nat Biotechnol , vol.19 , pp. 225-230
    • Kobinger, G.P.1    Weiner, D.J.2    Yu, Q.C.3    Wilson, J.M.4
  • 52
    • 0027410459 scopus 로고
    • Induction of cell differentiation by human immunodeficiency virus 1 vpr
    • Levy DN, Fernandes LS, Williams WV, Weiner DB (1993) Induction of cell differentiation by human immunodeficiency virus 1 vpr. Cell 72: 541-550.
    • (1993) Cell , vol.72 , pp. 541-550
    • Levy, D.N.1    Fernandes, L.S.2    Williams, W.V.3    Weiner, D.B.4
  • 53
    • 0028813107 scopus 로고
    • The human immunodeficiency virus type 1 Vpr gene prevents cell proliferation during chronic infection
    • Rogel ME, Wu LI, Emerman M (1995) The human immunodeficiency virus type 1 Vpr gene prevents cell proliferation during chronic infection. J. Virol. 69: 882-888.
    • (1995) J. Virol , vol.69 , pp. 882-888
    • Rogel, M.E.1    Wu, L.I.2    Emerman, M.3
  • 54
    • 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, Choe S, Walker R, Di Marzio P, Morgan DO, 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: 6705-6711.
    • (1995) J Virol , vol.69 , pp. 6705-6711
    • He, J.1    Choe, S.2    Walker, R.3    Di Marzio, P.4    Morgan, D.O.5
  • 55
    • 0028801303 scopus 로고
    • Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2 by inhibiting the activation of p34cdc2-cyclin B
    • Re F, Braaten D, Franke EK, Luban J (1995) Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2 by inhibiting the activation of p34cdc2-cyclin B. J. Virol. 69: 6859-6864.
    • (1995) J. Virol , vol.69 , pp. 6859-6864
    • Re, F.1    Braaten, D.2    Franke, E.K.3    Luban, J.4
  • 56
    • 0031950195 scopus 로고    scopus 로고
    • Vpr stimulates viral expression and induces cell killing in human immunodeficiency virus type 1-infected dividing Jurkat T cells
    • Yao XJ, Mouland AJ, Subbramanian RA, Forget J, Rougeau N, et al. (1998) Vpr stimulates viral expression and induces cell killing in human immunodeficiency virus type 1-infected dividing Jurkat T cells. J Virol 72: 4686-4693.
    • (1998) J Virol , vol.72 , pp. 4686-4693
    • Yao, X.J.1    Mouland, A.J.2    Subbramanian, R.A.3    Forget, J.4    Rougeau, N.5
  • 57
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P, Zhang C, McPike M, et al. (2004) Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem 279: 7792-7798.
    • (2004) J Biol Chem , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5
  • 58
    • 48949116664 scopus 로고    scopus 로고
    • Aguiar RS, Lovsin N, Tanuri A, Peterlin BM (2007) VPR.A3A chimera inhibits HIV replication. J Biol Chem.
    • Aguiar RS, Lovsin N, Tanuri A, Peterlin BM (2007) VPR.A3A chimera inhibits HIV replication. J Biol Chem.
  • 59
    • 0029861076 scopus 로고    scopus 로고
    • Role of Vif in human immunodeficiency virus type 1 reverse transcription
    • Goncalves J, Korin Y, Zack J, Gabuzda D (1996) Role of Vif in human immunodeficiency virus type 1 reverse transcription. J Virol 70: 8701-8709.
    • (1996) J Virol , vol.70 , pp. 8701-8709
    • Goncalves, J.1    Korin, Y.2    Zack, J.3    Gabuzda, D.4
  • 60
    • 7444268898 scopus 로고    scopus 로고
    • Functional domains of APOBEC3G required for antiviral activity
    • Li J, Potash MJ, Volsky DJ (2004) Functional domains of APOBEC3G required for antiviral activity. J Cell Biochem 92: 560-572.
    • (2004) J Cell Biochem , vol.92 , pp. 560-572
    • Li, J.1    Potash, M.J.2    Volsky, D.J.3
  • 62
    • 33751206549 scopus 로고    scopus 로고
    • Inhibition of formula-primed reverse transcription by human APOBEC3G during human immuno-deficiency virus type 1 replication
    • Guo F, Cen S, Niu M, Saadatmand J, Kleiman L (2006) Inhibition of formula-primed reverse transcription by human APOBEC3G during human immuno-deficiency virus type 1 replication. J Virol 80: 11710-11722.
    • (2006) J Virol , vol.80 , pp. 11710-11722
    • Guo, F.1    Cen, S.2    Niu, M.3    Saadatmand, J.4    Kleiman, L.5
  • 63
    • 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: 865-870.
    • (2006) J Exp Med , vol.203 , pp. 865-870
    • Kreisberg, J.F.1    Yonemoto, W.2    Greene, W.C.3
  • 65
    • 33846066628 scopus 로고    scopus 로고
    • The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action
    • Coker HA, Petersen-Mahrt SK (2007) The nuclear DNA deaminase AID functions distributively whereas cytoplasmic APOBEC3G has a processive mode of action. DNA Repair (Amst) 6: 235-243.
    • (2007) DNA Repair (Amst) , vol.6 , pp. 235-243
    • Coker, H.A.1    Petersen-Mahrt, S.K.2
  • 66
    • 13144254209 scopus 로고    scopus 로고
    • DNA deamination in immunity
    • Petersen-Mahrt S (2005) DNA deamination in immunity. Immunol Rev 203: 80-97.
    • (2005) Immunol Rev , vol.203 , pp. 80-97
    • Petersen-Mahrt, S.1
  • 67
    • 34250369626 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 integrase with cellular nuclear import receptor importin 7 and its impact on viral replication
    • Ao Z, Huang G, Yao H, Xu Z, Labine M, et al. (2007) Interaction of human immunodeficiency virus type 1 integrase with cellular nuclear import receptor importin 7 and its impact on viral replication. J Biol Chem 282: 13456-13467.
    • (2007) J Biol Chem , vol.282 , pp. 13456-13467
    • Ao, Z.1    Huang, G.2    Yao, H.3    Xu, Z.4    Labine, M.5
  • 68
    • 0033151621 scopus 로고    scopus 로고
    • The selective downregulation of class I major histocompatibility complex proteins by HIV-1 protects HIV-infected cells from NK cells
    • Cohen GB, Gandhi RT, Davis DM, Mandelboim O, Chen BK, et al. (1999) The selective downregulation of class I major histocompatibility complex proteins by HIV-1 protects HIV-infected cells from NK cells. Immunity 10: 661-671.
    • (1999) Immunity , vol.10 , pp. 661-671
    • Cohen, G.B.1    Gandhi, R.T.2    Davis, D.M.3    Mandelboim, O.4    Chen, B.K.5
  • 69
    • 0029044110 scopus 로고
    • Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: A predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity
    • Yao XJ, Friborg J, Checroune F, Gratton S, Boisvert F, et al. (1995) Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: a predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity. Virology 209: 615-623.
    • (1995) Virology , vol.209 , pp. 615-623
    • Yao, X.J.1    Friborg, J.2    Checroune, F.3    Gratton, S.4    Boisvert, F.5
  • 70
    • 0031950195 scopus 로고    scopus 로고
    • Vpr stimulates viral expression and induces cell killing in human immunodeficiency virus type 1-infected dividing Jurkat T cells
    • Yao XJ, Mouland AJ, Subbramanian RA, Forget J, Rougreau N, et al. (1998) Vpr stimulates viral expression and induces cell killing in human immunodeficiency virus type 1-infected dividing Jurkat T cells. J Virol 72: 4686-4693.
    • (1998) J Virol , vol.72 , pp. 4686-4693
    • Yao, X.J.1    Mouland, A.J.2    Subbramanian, R.A.3    Forget, J.4    Rougreau, N.5
  • 71
    • 0029956256 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes
    • Simon JHM, Malim MH (1996) The human immunodeficiency virus type 1 Vif protein modulates the postpenetration stability of viral nucleoprotein complexes. J. Virol. 70: 5297-5305.
    • (1996) J. Virol , vol.70 , pp. 5297-5305
    • Simon, J.H.M.1    Malim, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.