메뉴 건너뛰기




Volumn 288, Issue 9, 2013, Pages 6083-6094

HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ASSAY; DOUBLE STRANDED DNA; HUMAN IMMUNODEFICIENCY VIRUS; HYPER MUTATION; MOLECULAR MECHANISM; PROTEASOMAL DEGRADATION; RETROVIRAL RESTRICTION; SINGLE-STRANDED DNA; SLIDING MOVEMENTS; UBIQUITINATION; VIRAL INFECTIVITY FACTORS;

EID: 84874759842     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.421875     Document Type: Article
Times cited : (28)

References (84)
  • 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, A. M., Gaddis, N. C., Choi, J. D., and Malim, M. H. (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
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat, B., Turelli, P., Caron, G., Friedli, M., Perrin, L., and Trono, D. (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, L.5    Trono, D.6
  • 4
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang, H., Yang, B., Pomerantz, R. J., Zhang, C., Arunachalam, S. C., and Gao, L. (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    Gao, L.6
  • 5
    • 48649102498 scopus 로고    scopus 로고
    • APOBEC3G encapsidation into HIV-1 virions: Which RNA is it?
    • Strebel, K., and Khan, M. A. (2008) APOBEC3G encapsidation into HIV-1 virions: which RNA is it? Retrovirology 5, 55
    • (2008) Retrovirology , vol.5 , pp. 55
    • Strebel, K.1    Khan, M.A.2
  • 8
    • 0004131381 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Coffin, J. M., Hughes, S. H., and Varmus, H. E. (1997) Retroviruses, pp. 121-160, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1997) Retroviruses , pp. 121-160
    • Coffin, J.M.1    Hughes, S.H.2    Varmus, H.E.3
  • 9
    • 2942525660 scopus 로고    scopus 로고
    • 'Binding, bending and bonding': Polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus
    • Rausch, J. W., and Le Grice, S. F. (2004) 'Binding, bending and bonding': polypurine tract-primed initiation of plus-strand DNA synthesis in human immunodeficiency virus. Int. J. Biochem. Cell Biol. 36, 1752-1766
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1752-1766
    • Rausch, J.W.1    Le Grice, S.F.2
  • 10
    • 78049501117 scopus 로고    scopus 로고
    • The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F
    • Hu, C., Saenz, D. T., Fadel, H. J., Walker, W., Peretz, M., and Poeschla, E. M. (2010) The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F. J. Virol. 84, 11981-11993
    • (2010) J Virol , vol.84 , pp. 11981-11993
    • Hu, C.1    Saenz, D.T.2    Fadel, H.J.3    Walker, W.4    Peretz, M.5    Poeschla, E.M.6
  • 11
    • 33750210516 scopus 로고    scopus 로고
    • Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication
    • Suspène, R., Rusniok, C., Vartanian, J. P., and Wain-Hobson, S. (2006) Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication. Nucleic Acids Res. 34, 4677-4684
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4677-4684
    • Suspène, R.1    Rusniok, C.2    Vartanian, J.P.3    Wain-Hobson, S.4
  • 12
    • 33745067722 scopus 로고    scopus 로고
    • APOBEC3GDNAdeaminase acts processively 3' → 5' on single-stranded DNA
    • Chelico, L., Pham, P., Calabrese, P., and Goodman, M. F. (2006) APOBEC3GDNAdeaminase acts processively 3' → 5' on single-stranded DNA. Nat. Struct. Mol. Biol. 13, 392-399
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 392-399
    • Chelico, L.1    Pham, P.2    Calabrese, P.3    Goodman, M.F.4
  • 13
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel, P. H., and Berg, O. G. (1989) Facilitated target location in biological systems. J. Biol. Chem. 264, 675-678
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 14
    • 0034387984 scopus 로고    scopus 로고
    • One- and three-dimensional pathways for proteins to reach specific DNA sites
    • Stanford, N. P., Szczelkun, M. D., Marko, J. F., and Halford, S. E. (2000) One- and three-dimensional pathways for proteins to reach specific DNA sites. EMBO J. 19, 6546-6557
    • (2000) EMBO J. , vol.19 , pp. 6546-6557
    • Stanford, N.P.1    Szczelkun, M.D.2    Marko, J.F.3    Halford, S.E.4
  • 15
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford, S. E., and Marko, J. F. (2004) How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 32, 3040-3052
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 16
    • 84860855710 scopus 로고    scopus 로고
    • Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution
    • Senavirathne, G., Jaszczur, M., Auerbach, P. A., Upton, T. G., Chelico, L., Goodman, M. F., and Rueda, D. (2012) Single-stranded DNA scanning and deamination by APOBEC3G cytidine deaminase at single molecule resolution. J. Biol. Chem. 287, 15826-15835
    • (2012) J. Biol. Chem. , vol.287 , pp. 15826-15835
    • Senavirathne, G.1    Jaszczur, M.2    Auerbach, P.A.3    Upton, T.G.4    Chelico, L.5    Goodman, M.F.6    Rueda, D.7
  • 18
    • 60049097628 scopus 로고    scopus 로고
    • Stochastic properties of processive cytidineDNAdeaminases AID and APOBEC3G
    • Chelico, L., Pham, P., and Goodman, M. F. (2009) Stochastic properties of processive cytidineDNAdeaminases AID and APOBEC3G. Philos. Trans. R. Soc. Lond. B Biol. Sci. 364, 583-593
    • (2009) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.364 , pp. 583-593
    • Chelico, L.1    Pham, P.2    Goodman, M.F.3
  • 19
    • 79953214104 scopus 로고    scopus 로고
    • Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain
    • Feng, Y., and Chelico, L. (2011) Intensity of deoxycytidine deamination of HIV-1 proviral DNA by the retroviral restriction factor APOBEC3G is mediated by the noncatalytic domain. J. Biol. Chem. 286, 11415-11426
    • (2011) J. Biol. Chem. , vol.286 , pp. 11415-11426
    • Feng, Y.1    Chelico, L.2
  • 20
    • 15744390742 scopus 로고    scopus 로고
    • The retroviral hypermutation specificity of APOBEC3F andAPOBEC3Gis governed by the C-terminal DNA cytosine deaminase domain
    • Haché, G., Liddament, M. T., and Harris, R. S. (2005) The retroviral hypermutation specificity of APOBEC3F andAPOBEC3Gis governed by the C-terminal DNA cytosine deaminase domain. J. Biol. Chem. 280, 10920-10924
    • (2005) J. Biol. Chem. , vol.280 , pp. 10920-10924
    • Haché, G.1    Liddament, M.T.2    Harris, R.S.3
  • 22
    • 77952399342 scopus 로고    scopus 로고
    • Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G
    • Chelico, L., Prochnow, C., Erie, D. A., Chen, X. S., and Goodman, M. F. (2010) Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G. J. Biol. Chem. 285, 16195-16205
    • (2010) J. Biol. Chem. , vol.285 , pp. 16195-16205
    • Chelico, L.1    Prochnow, C.2    Erie, D.A.3    Chen, X.S.4    Goodman, M.F.5
  • 23
    • 33845972280 scopus 로고    scopus 로고
    • Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits
    • Wedekind, J. E., Gillilan, R., Janda, A., Krucinska, J., Salter, J. D., Bennett, R. P., Raina, J., and Smith, H. C. (2006) Nanostructures of APOBEC3G support a hierarchical assembly model of high molecular mass ribonucleoprotein particles from dimeric subunits. J. Biol. Chem. 281, 38122-38126
    • (2006) J. Biol. Chem. , vol.281 , pp. 38122-38126
    • Wedekind, J.E.1    Gillilan, R.2    Janda, A.3    Krucinska, J.4    Salter, J.D.5    Bennett, R.P.6    Raina, J.7    Smith, H.C.8
  • 24
    • 57749120452 scopus 로고    scopus 로고
    • APOBEC3G subunits self-associate via the C-terminal deaminase domain
    • Bennett, R. P., Salter, J. D., Liu, X., Wedekind, J. E., and Smith, H. C. (2008) APOBEC3G subunits self-associate via the C-terminal deaminase domain. J. Biol. Chem. 283, 33329-33336
    • (2008) J. Biol. Chem. , vol.283 , pp. 33329-33336
    • Bennett, R.P.1    Salter, J.D.2    Liu, X.3    Wedekind, J.E.4    Smith, H.C.5
  • 25
    • 80052200560 scopus 로고    scopus 로고
    • Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes
    • McDougall, W. M., Okany, C., and Smith, H. C. (2011) Deaminase activity on single-stranded DNA (ssDNA) occurs in vitro when APOBEC3G cytidine deaminase forms homotetramers and higher-order complexes. J. Biol. Chem. 286, 30655-30661
    • (2011) J Biol Chem , vol.286 , pp. 30655-30661
    • McDougall, W.M.1    Okany, C.2    Smith, H.C.3
  • 27
    • 70450181508 scopus 로고    scopus 로고
    • Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition
    • Bulliard, Y., Turelli, P., Röhrig, U. F., Zoete, V., Mangeat, B., Michielin, O., and Trono, D. (2009) Functional analysis and structural modeling of human APOBEC3G reveal the role of evolutionarily conserved elements in the inhibition of human immunodeficiency virus type 1 infection and Alu transposition. J. Virol. 83, 12611-12621
    • (2009) J. Virol. , vol.83 , pp. 12611-12621
    • Bulliard, Y.1    Turelli, P.2    Röhrig, U.F.3    Zoete, V.4    Mangeat, B.5    Michielin, O.6    Trono, D.7
  • 28
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, A. M., Gaddis, N. C., and Malim, M. H. (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
  • 29
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., Yu, Y., Liu, B., Luo, K., Kong, W., Mao, P., and Yu, X. F. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-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    Mao, P.6    Yu, X.F.7
  • 30
    • 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., and Greene, W. C. (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
  • 31
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., Rose, K. M., Kozak, S. L., and 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
  • 32
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello, S. G., Harris, R. S., and Neuberger, M. S. (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
  • 34
    • 33646508336 scopus 로고    scopus 로고
    • Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates
    • Zennou, V., and Bieniasz, P. D. (2006) Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates. Virology 349, 31-40
    • (2006) Virology , vol.349 , pp. 31-40
    • Zennou, V.1    Bieniasz, P.D.2
  • 35
    • 84871943090 scopus 로고    scopus 로고
    • APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages
    • Chaipan, C., Smith, J. L., Hu, W. S., and Pathak, V. K. (2013) APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages. J. Virol. 87, 444-453
    • (2013) J. Virol. , vol.87 , pp. 444-453
    • Chaipan, C.1    Smith, J.L.2    Hu, W.S.3    Pathak, V.K.4
  • 36
    • 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., Golem, S., Rose, K. M., Kozak, S. L., and Kabat, D. (2008) Human immunodeficiency virus type 1 Vif functionally interacts with diverse APOBEC3 cytidine deaminases and moves with them between cytoplasmic sites of mRNA metabolism. J. Virol. 82, 987-998
    • (2008) J. Virol. , vol.82 , pp. 987-998
    • Marin, M.1    Golem, S.2    Rose, K.M.3    Kozak, S.L.4    Kabat, D.5
  • 38
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction
    • Zhang, W., Du, J., Evans, S. L., Yu, Y., and Yu, X. F. (2012) T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction. Nature 481, 376-379
    • (2012) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.F.5
  • 39
    • 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., and Gabuzda, D. (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    Gabuzda, D.6
  • 42
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • 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). Proc. Natl. Acad. Sci. U.S.A. 101, 3927-3932
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3927-3932
    • Schröfelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 43
    • 1642367210 scopus 로고    scopus 로고
    • A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor
    • Bogerd, H. P., Doehle, B. P., Wiegand, H. L., and Cullen, B. R. (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
  • 44
    • 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., and 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
  • 45
    • 38949106531 scopus 로고    scopus 로고
    • The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G
    • Miller, J. H., Presnyak, V., and Smith, H. C. (2007) The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G. Retrovirology 4, 81
    • (2007) Retrovirology , vol.4 , pp. 81
    • Miller, J.H.1    Presnyak, V.2    Smith, H.C.3
  • 46
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging ofAPOBEC3G(CEM15), a cellular inhibitor of virus infectivity
    • Kao, S., Khan, M. A., Miyagi, E., Plishka, R., Buckler-White, A., and Strebel, K. (2003) The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging ofAPOBEC3G(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    Strebel, K.6
  • 47
    • 18144374907 scopus 로고    scopus 로고
    • Production of infectious human immunodeficiency virus type 1 does not require depletion ofAPOBEC3Gfrom virus-producing cells
    • Kao, S., Miyagi, E., Khan, M. A., Takeuchi, H., Opi, S., Goila-Gaur, R., and Strebel, K. (2004) Production of infectious human immunodeficiency virus type 1 does not require depletion ofAPOBEC3Gfrom 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    Goila-Gaur, R.6    Strebel, K.7
  • 48
    • 58149517747 scopus 로고    scopus 로고
    • Differential sensitivity of "old" versus "new" APOBEC3G to human immunodeficiency virus type 1 vif
    • Goila-Gaur, R., Khan, M. A., Miyagi, E., and Strebel, K. (2009) Differential sensitivity of "old" versus "new" APOBEC3G to human immunodeficiency virus type 1 vif. J. Virol. 83, 1156-1160
    • (2009) J. Virol. , vol.83 , pp. 1156-1160
    • Goila-Gaur, R.1    Khan, M.A.2    Miyagi, E.3    Strebel, K.4
  • 49
    • 38949152689 scopus 로고    scopus 로고
    • HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexes
    • Goila-Gaur, R., Khan, M. A., Miyagi, E., Kao, S., Opi, S., Takeuchi, H., and Strebel, K. (2008) HIV-1 Vif promotes the formation of high molecular mass APOBEC3G complexes. Virology 372, 136-146
    • (2008) Virology , vol.372 , pp. 136-146
    • Goila-Gaur, R.1    Khan, M.A.2    Miyagi, E.3    Kao, S.4    Opi, S.5    Takeuchi, H.6    Strebel, K.7
  • 50
    • 0029821868 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 Vif particle incorporation
    • Camaur, D., and Trono, D. (1996) Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J. Virol. 70, 6106-6111
    • (1996) J. Virol. , vol.70 , pp. 6106-6111
    • Camaur, D.1    Trono, D.2
  • 51
    • 0037225730 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection
    • Kao, S., Akari, H., Khan, M. A., Dettenhofer, M., Yu, X. F., and Strebel, K. (2003) Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection. J. Virol. 77, 1131-1140
    • (2003) J. Virol. , vol.77 , pp. 1131-1140
    • Kao, S.1    Akari, H.2    Khan, M.A.3    Dettenhofer, M.4    Yu, X.F.5    Strebel, K.6
  • 52
    • 0029961360 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins
    • Fouchier, R. A., Simon, J. H., Jaffe, A. B., and Malim, M. H. (1996) Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins. J. Virol. 70, 8263-8269
    • (1996) J. Virol. , vol.70 , pp. 8263-8269
    • Fouchier, R.A.1    Simon, J.H.2    Jaffe, A.B.3    Malim, M.H.4
  • 53
    • 0029655893 scopus 로고    scopus 로고
    • Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein
    • Karczewski, M. K., and Strebel, K. (1996) Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein. J. Virol. 70, 494-507
    • (1996) J. Virol. , vol.70 , pp. 494-507
    • Karczewski, M.K.1    Strebel, K.2
  • 55
    • 77953769689 scopus 로고    scopus 로고
    • APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis
    • Sadler, H. A., Stenglein, M. D., Harris, R. S., and Mansky, L. M. (2010) APOBEC3G contributes to HIV-1 variation through sublethal mutagenesis. J. Virol. 84, 7396-7404
    • (2010) J Virol , vol.84 , pp. 7396-7404
    • Sadler, H.A.1    Stenglein, M.D.2    Harris, R.S.3    Mansky, L.M.4
  • 56
    • 53549107186 scopus 로고    scopus 로고
    • Hypermutation by intersegmental transfer of APOBEC3G cytidine deaminase
    • Nowarski, R., Britan-Rosich, E., Shiloach, T., and Kotler, M. (2008) Hypermutation by intersegmental transfer of APOBEC3G cytidine deaminase. Nat. Struct. Mol. Biol. 15, 1059-1066
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1059-1066
    • Nowarski, R.1    Britan-Rosich, E.2    Shiloach, T.3    Kotler, M.4
  • 57
    • 33947732622 scopus 로고    scopus 로고
    • Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions
    • Xu, H., Chertova, E., Chen, J., Ott, D. E., Roser, J. D., Hu, W. S., and Pathak, V. K. (2007) Stoichiometry of the antiviral protein APOBEC3G in HIV-1 virions. Virology 360, 247-256
    • (2007) Virology , vol.360 , pp. 247-256
    • Xu, H.1    Chertova, E.2    Chen, J.3    Ott, D.E.4    Roser, J.D.5    Hu, W.S.6    Pathak, V.K.7
  • 58
    • 79960380329 scopus 로고    scopus 로고
    • Multifaceted counter- APOBEC3G mechanisms employed by HIV-1 Vif
    • Britan-Rosich, E., Nowarski, R., and Kotler, M. (2011) Multifaceted counter- APOBEC3G mechanisms employed by HIV-1 Vif. J. Mol. Biol. 410, 1065-1076
    • (2011) J. Mol. Biol. , vol.410 , pp. 1065-1076
    • Britan-Rosich, E.1    Nowarski, R.2    Kotler, M.3
  • 59
    • 15744387175 scopus 로고    scopus 로고
    • HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation
    • Santa-Marta, M., da Silva, F. A., Fonseca, A. M., and Goncalves, J. (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. J. Biol. Chem. 280, 8765-8775
    • (2005) J. Biol. Chem. , vol.280 , pp. 8765-8775
    • Santa-Marta, M.1    Da Silva, F.A.2    Fonseca, A.M.3    Goncalves, J.4
  • 61
    • 84861313225 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC
    • Zuo, T., Liu, D., Lv, W., Wang, X., Wang, J., Lv, M., Huang, W., Wu, J., Zhang, H., Jin, H., Zhang, L., Kong, W., and Yu, X. (2012) Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC. J. Virol. 86, 5497-5507
    • (2012) J. Virol. , vol.86 , pp. 5497-5507
    • Zuo, T.1    Liu, D.2    Lv, W.3    Wang, X.4    Wang, J.5    Lv, M.6    Huang, W.7    Wu, J.8    Zhang, H.9    Jin, H.10    Zhang, L.11    Kong, W.12    Yu, X.13
  • 62
    • 67649888155 scopus 로고    scopus 로고
    • Natural variation in Vif: Differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification
    • Simon, V., Zennou, V., Murray, D., Huang, Y., Ho, D. D., and Bieniasz, P. D. (2005) Natural variation in Vif: differential impact on APOBEC3G/3F and a potential role in HIV-1 diversification. PLoS Pathog. 1, e6
    • (2005) PLoS Pathog. , vol.1
    • Simon, V.1    Zennou, V.2    Murray, D.3    Huang, Y.4    Ho, D.D.5    Bieniasz, P.D.6
  • 63
    • 66349132212 scopus 로고    scopus 로고
    • Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance
    • Jern, P., Russell, R. A., Pathak, V. K., and Coffin, J. M. (2009) Likely role of APOBEC3G-mediated G-to-A mutations in HIV-1 evolution and drug resistance. PLoS Pathog. 5, e1000367
    • (2009) PLoS Pathog. , vol.5
    • Jern, P.1    Russell, R.A.2    Pathak, V.K.3    Coffin, J.M.4
  • 64
    • 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
  • 65
    • 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, K. L., llano, M., Akari, H., Miyagi, E., Poeschla, E. M., Strebel, K., and Bour, S. (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    Llano, M.2    Akari, H.3    Miyagi, E.4    Poeschla, E.M.5    Strebel, K.6    Bour, S.7
  • 66
    • 0025191211 scopus 로고
    • Rapid purification of homodimer and heterodimer HIV-1 reverse transcriptase by metal chelate affinity chromatography
    • Le Grice, S. F., and Grüninger-Leitch, F. (1990) Rapid purification of homodimer and heterodimer HIV-1 reverse transcriptase by metal chelate affinity chromatography. Eur. J. Biochem. 187, 307-314
    • (1990) Eur. J. Biochem. , vol.187 , pp. 307-314
    • Le Grice, S.F.1    Grüninger-Leitch, F.2
  • 67
    • 9544220664 scopus 로고    scopus 로고
    • The heterosexual human immunodeficiency virus type 1 epidemic in Thailand is caused by an intersubtype (A/E) recombinant of African origin
    • Gao, F., Robertson, D. L., Morrison, S. G., Hui, H., Craig, S., Decker, J., Fultz, P. N., Girard, M., Shaw, G. M., Hahn, B. H., and Sharp, P. M. (1996) The heterosexual human immunodeficiency virus type 1 epidemic in Thailand is caused by an intersubtype (A/E) recombinant of African origin. J. Virol. 70, 7013-7029
    • (1996) J. Virol. , vol.70 , pp. 7013-7029
    • Gao, F.1    Robertson, D.L.2    Morrison, S.G.3    Hui, H.4    Craig, S.5    Decker, J.6    Fultz, P.N.7    Girard, M.8    Shaw, G.M.9    Hahn, B.H.10    Sharp, P.M.11
  • 70
    • 0028834955 scopus 로고
    • Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies
    • Creighton, S., Bloom, L. B., and Goodman, M. F. (1995) Gel fidelity assay measuring nucleotide misinsertion, exonucleolytic proofreading, and lesion bypass efficiencies. Methods Enzymol. 262, 232-256
    • (1995) Methods Enzymol. , vol.262 , pp. 232-256
    • Creighton, S.1    Bloom, L.B.2    Goodman, M.F.3
  • 72
    • 46649114007 scopus 로고    scopus 로고
    • A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV
    • Chelico, L., Sacho, E. J., Erie, D. A., and Goodman, M. F. (2008) A model for oligomeric regulation of APOBEC3G cytosine deaminase-dependent restriction of HIV. J. Biol. Chem. 283, 13780-13791
    • (2008) J. Biol. Chem. , vol.283 , pp. 13780-13791
    • Chelico, L.1    Sacho, E.J.2    Erie, D.A.3    Goodman, M.F.4
  • 73
    • 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., 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. J. Virol. 81, 3807-3815
    • (2007) J. Virol. , vol.81 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 75
    • 79957449842 scopus 로고    scopus 로고
    • HIV-1 Vif interaction with APOBEC3 deaminases and its characterization by a new sensitive assay
    • Cadima-Couto, I., Saraiva, N., Santos, A. C., and Goncalves, J. (2011) HIV-1 Vif interaction with APOBEC3 deaminases and its characterization by a new sensitive assay. J. Neuroimmune Pharmacol. 6, 296-307
    • (2011) J. Neuroimmune Pharmacol. , vol.6 , pp. 296-307
    • Cadima-Couto, I.1    Saraiva, N.2    Santos, A.C.3    Goncalves, J.4
  • 76
    • 34548833825 scopus 로고    scopus 로고
    • RNA and DNA binding properties of HIV-1 Vif protein: A fluorescence study
    • Bernacchi, S., Henriet, S., Dumas, P., Paillart, J. C., and Marquet, R. (2007) RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study. J. Biol. Chem. 282, 26361-26368
    • (2007) J. Biol. Chem. , vol.282 , pp. 26361-26368
    • Bernacchi, S.1    Henriet, S.2    Dumas, P.3    Paillart, J.C.4    Marquet, R.5
  • 78
    • 66749141973 scopus 로고    scopus 로고
    • Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors
    • Henriet, S., Mercenne, G., Bernacchi, S., Paillart, J. C., and Marquet, R. (2009) Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors. Microbiol. Mol. Biol. Rev. 73, 211-232
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 211-232
    • Henriet, S.1    Mercenne, G.2    Bernacchi, S.3    Paillart, J.C.4    Marquet, R.5
  • 79
    • 84874768704 scopus 로고    scopus 로고
    • Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G
    • Uyttendaele, I., Lavens, D., Catteeuw, D., Lemmens, I., Bovijn, C., Tavernier, J., and Peelman, F. (2012) Random mutagenesis MAPPIT analysis identifies binding sites for Vif and Gag in both cytidine deaminase domains of Apobec3G. PLoS One 7, e44143
    • (2012) PLoS One , vol.7
    • Uyttendaele, I.1    Lavens, D.2    Catteeuw, D.3    Lemmens, I.4    Bovijn, C.5    Tavernier, J.6    Peelman, F.7
  • 81
    • 78649429705 scopus 로고    scopus 로고
    • Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif
    • Smith, J. L., and Pathak, V. K. (2010) Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif. J. Virol. 84, 12599-12608
    • (2010) J. Virol. , vol.84 , pp. 12599-12608
    • Smith, J.L.1    Pathak, V.K.2
  • 84
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.