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Volumn 81, Issue 15, 2007, Pages 8236-8246

Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; PROTEASOME; RIBONUCLEASE; VIF PROTEIN;

EID: 34547130033     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02694-06     Document Type: Article
Times cited : (82)

References (52)
  • 1
    • 4544232464 scopus 로고    scopus 로고
    • APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
    • Alce, T. M., and W. Popik. 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
  • 2
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop, K. N., R. K. Holmes, and M. H. Malim. 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
  • 3
    • 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., B. P. Doehle, H. L. Wiegand, and B. R. Cullen. 2004. A single amino acid difference in the host APOBEC3G protein controls the primate species specificity of HIV type 1 virion infectivity factor. Proc. Natl. Acad. Sci. USA 101:3770-3774.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3770-3774
    • Bogerd, H.P.1    Doehle, B.P.2    Wiegand, H.L.3    Cullen, B.R.4
  • 5
    • 0027174989 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: The cytoplasmic domain of CD4 contributes to Vpu sensitivity
    • Chen, M. Y., F. Maldarelli, M. K. Karczewski, R. L. Willey, and K. Strebel. 1993. Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivity. J. Virol. 67:3877-3884.
    • (1993) J. Virol , vol.67 , pp. 3877-3884
    • Chen, M.Y.1    Maldarelli, F.2    Karczewski, M.K.3    Willey, R.L.4    Strebel, K.5
  • 8
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello, S. G., R. S. Harris, and M. S. Neuberger. 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
  • 11
    • 33847193509 scopus 로고    scopus 로고
    • Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules
    • Gallois-Montbrun, S., B. Kramer, C. M. Swanson, H. Byers, S. Lynham, M. Ward, and M. H. Malim. 2007. Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules. J. Virol. 81:2165-2178.
    • (2007) J. Virol , vol.81 , pp. 2165-2178
    • Gallois-Montbrun, S.1    Kramer, B.2    Swanson, C.M.3    Byers, H.4    Lynham, S.5    Ward, M.6    Malim, M.H.7
  • 12
    • 33751206549 scopus 로고    scopus 로고
    • Lys-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication
    • Lys-primed reverse transcription by human APOBEC3G during human immunodeficiency virus type 1 replication. J. Virol. 80:11710-11722.
    • (2007) J. Virol , vol.80 , pp. 11710-11722
    • Guo, F.1    Cen, S.2    Niu, M.3    Saadatmand, J.4    Kleiman, L.5
  • 15
    • 0037225730 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif is efficiently packaged into virions during productive but not chronic infection
    • Kao, S., H. Akari, M. A. Khan, M. Dettenhofer, X. F. Yu, and K. Strebel. 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
  • 16
    • 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., M. A. Khan, E. Miyagi, R. Plishka, A. Buckler-White, and K. Strebel. 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    Strebel, K.6
  • 17
    • 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., E. Miyagi, M. A. Khan, H. Takeuchi, S. Opi, R. Goila-Gaur, and K. Strebel. 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    Goila-Gaur, R.6    Strebel, K.7
  • 18
    • 0029655893 scopus 로고    scopus 로고
    • Cytoskeleton association and virion incorporation of the human immunodeficiency virus type 1 Vif protein
    • Karczewski, M. K., and K. Strebel. 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
  • 19
    • 0034899286 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA
    • Khan, M. A., C. Aberham, S. Kao, H. Akari, R. Gorelick, S. Bour, and K. Strebel. 2001. Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA. J. Virol. 75:7252-7265.
    • (2001) J. Virol , vol.75 , pp. 7252-7265
    • Khan, M.A.1    Aberham, C.2    Kao, S.3    Akari, H.4    Gorelick, R.5    Bour, S.6    Strebel, K.7
  • 20
    • 20244381403 scopus 로고    scopus 로고
    • Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes
    • Khan, M. A., S. Kao, E. Miyagi, H. Takeuchi, R. Goila-Gaur, S. Opi, C. L. Gipson, T. G. Parslow, H. Ly, and K. Strebel. 2005. Viral RNA is required for the association of APOBEC3G with human immunodeficiency virus type 1 nucleoprotein complexes. J. Virol. 79:5870-5874.
    • (2005) J. Virol , vol.79 , pp. 5870-5874
    • Khan, M.A.1    Kao, S.2    Miyagi, E.3    Takeuchi, H.4    Goila-Gaur, R.5    Opi, S.6    Gipson, C.L.7    Parslow, T.G.8    Ly, H.9    Strebel, K.10
  • 21
    • 33749384520 scopus 로고    scopus 로고
    • The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules
    • Kozak, S. L., M. Marin, K. M. Rose, C. Bystrom, and D. Kabat. 2006. The anti-HIV-1 editing enzyme APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules. J. Biol. Chem. 281:29105-29119.
    • (2006) J. Biol. Chem , vol.281 , pp. 29105-29119
    • Kozak, S.L.1    Marin, M.2    Rose, K.M.3    Bystrom, C.4    Kabat, D.5
  • 22
    • 0028085932 scopus 로고
    • Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene
    • Lau, P. P., H. J. Zhu, A. Baldini, C. Charnsangavej, and L. Chan. 1994. Dimeric structure of a human apolipoprotein B mRNA editing protein and cloning and chromosomal localization of its gene. Proc. Natl. Acad. Sci. USA 91:8522-8526.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8522-8526
    • Lau, P.P.1    Zhu, H.J.2    Baldini, A.3    Charnsangavej, C.4    Chan, L.5
  • 23
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier, D., F. Bouchonnet, F. Clavel, and A. J. Hance. 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
  • 24
    • 7444268898 scopus 로고    scopus 로고
    • Functional domains of APOBEC3G required for antiviral activity
    • Li, J., M. J. Potash, and D. J. Volsky. 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
  • 25
    • 0842347676 scopus 로고    scopus 로고
    • Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G
    • Liu, B., X. Yu, K. Luo, Y. Yu, and X. F. Yu. 2004. Influence of primate lentiviral Vif and proteasome inhibitors on human immunodeficiency virus type 1 virion packaging of APOBEC3G. J. Virol. 78:2072-2081.
    • (2004) J. Virol , vol.78 , pp. 2072-2081
    • Liu, B.1    Yu, X.2    Luo, K.3    Yu, Y.4    Yu, X.F.5
  • 26
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
    • Luo, K., B. Liu, Z. Xiao, Y. Yu, X. Yu, R. Gorelick, and X. F. Yu. 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, X.5    Gorelick, R.6    Yu, X.F.7
  • 27
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • Mangeat, B., P. Turelli, G. Caron, M. Friedli, L. Perrin, and D. Trono. 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
  • 28
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • Mangeat, B., P. Turelli, S. Liao, and D. Trono. 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
    • 0038107587 scopus 로고    scopus 로고
    • Mariani, R., D. Chen, B. Schrofelbauer, F. Navarro, R. Konig, B. Bollman, C. Munk, H. Nymark-McMahon, and N. R. Landau. 2003. Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114:21-31.
    • Mariani, R., D. Chen, B. Schrofelbauer, F. Navarro, R. Konig, B. Bollman, C. Munk, H. Nymark-McMahon, and N. R. Landau. 2003. Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114:21-31.
  • 30
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin, M., K. M. Rose, S. L. Kozak, and D. Kabat. 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
  • 31
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle, A., B. Strack, P. Ancuta, C. Zhang, M. McPike, and D. Gabuzda. 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
  • 34
    • 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., M. Ilano, H. Akari, E. Miyagi, E. M. Poeschla, K. Strebel, and S. Bour. 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    Strebel, K.6    Bour, S.7
  • 36
    • 0034255169 scopus 로고    scopus 로고
    • LuSIV cells: A reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication
    • Roos, J. W., M. F. Maughan, Z. Liao, J. E. Hildreth, and J. E. Clements. 2000. LuSIV cells: a reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication. Virology 273:307-315.
    • (2000) Virology , vol.273 , pp. 307-315
    • Roos, J.W.1    Maughan, M.F.2    Liao, Z.3    Hildreth, J.E.4    Clements, J.E.5
  • 37
    • 33744965939 scopus 로고    scopus 로고
    • Association of RNA helicase A with human immunodeficiency virus type 1 particles
    • Roy, B. B., J. Hu, X. Guo, R. S. Russell, F. Guo, L. Kleiman, and C. Liang. 2006. Association of RNA helicase A with human immunodeficiency virus type 1 particles. J. Biol. Chem. 281:12625-12635.
    • (2006) J. Biol. Chem , vol.281 , pp. 12625-12635
    • Roy, B.B.1    Hu, J.2    Guo, X.3    Russell, R.S.4    Guo, F.5    Kleiman, L.6    Liang, C.7
  • 38
    • 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., H. P. Bogerd, and B. R. Cullen. 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
  • 39
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • Schrofelbauer, B., D. Chen, and N. R. Landau. 2004. A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif). Proc. Natl. Acad. Sci. USA 101:3927-3932.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 40
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy, A. M., N. C. Gaddis, and M. H. Malim. 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
  • 41
    • 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
    • Shindo, K., A. Takaori-Kondo, M. Kobayashi, A. Abudu, K. Fukunaga, and T. Uchiyama. 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. J. Biol. Chem. 278:44412-44416.
    • (2003) J. Biol. Chem , vol.278 , pp. 44412-44416
    • Shindo, K.1    Takaori-Kondo, A.2    Kobayashi, M.3    Abudu, A.4    Fukunaga, K.5    Uchiyama, T.6
  • 42
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • Stopak, K., C. de Noronha, W. Yonemoto, and W. C. Greene. 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
  • 43
    • 0023267788 scopus 로고
    • The HIV 'A' (sor) gene product is essential for virus infectivity
    • Strebel, K., D. Daugherty, K. Clouse, D. Cohen, T. Folks, and M. A. Martin. 1987. The HIV 'A' (sor) gene product is essential for virus infectivity. Nature 328:728-730.
    • (1987) Nature , vol.328 , pp. 728-730
    • Strebel, K.1    Daugherty, D.2    Clouse, K.3    Cohen, D.4    Folks, T.5    Martin, M.A.6
  • 44
    • 4143124683 scopus 로고    scopus 로고
    • Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) is incorporated into HIV-1 virions through interactions with viral and nonviral RNAs
    • Svarovskaia, E. S., H. Xu, J. L. Mbisa, R. Barr, R. J. Gorelick, A. Ono, E. O. Freed, W. S. Hu, and V. K. Pathak. 2004. Human apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G (APOBEC3G) 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    Ono, A.6    Freed, E.O.7    Hu, W.S.8    Pathak, V.K.9
  • 45
    • 12844284575 scopus 로고    scopus 로고
    • Production of infectious SIVagm from human cells requires functional inactivation but not viral exclusion of human APOBEC3G
    • Takeuchi, H., S. Kao, E. Miyagi, M. A. Khan, A. Buckler-White, R. Plishka, and K. Strebel. 2005. Production of infectious SIVagm from human cells requires functional inactivation but not viral exclusion of human APOBEC3G. J. Biol. Chem. 280:375-382.
    • (2005) J. Biol. Chem , vol.280 , pp. 375-382
    • Takeuchi, H.1    Kao, S.2    Miyagi, E.3    Khan, M.A.4    Buckler-White, A.5    Plishka, R.6    Strebel, K.7
  • 46
    • 14844288923 scopus 로고    scopus 로고
    • Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: Correlating function and subcellular localization
    • Wichroski, M. J., K. Ichiyama, and T. M. Rana. 2005. Analysis of HIV-1 viral infectivity factor-mediated proteasome-dependent depletion of APOBEC3G: correlating function and subcellular localization. J. Biol. Chem. 280:8387-8396.
    • (2005) J. Biol. Chem , vol.280 , pp. 8387-8396
    • Wichroski, M.J.1    Ichiyama, K.2    Rana, T.M.3
  • 47
    • 33646924568 scopus 로고    scopus 로고
    • Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies
    • Wichroski, M. J., G. B. Robb, and T. M. Rana. 2006. Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathogens 2:e41.
    • (2006) PLoS Pathogens , vol.2
    • Wichroski, M.J.1    Robb, G.B.2    Rana, T.M.3
  • 48
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand, H. L., B. P. Doehle, H. P. Bogerd, and B. R. Cullen. 2004. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23:2451-2458.
    • (2004) EMBO J , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 49
    • 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., E. S. Svarovskaia, R. Barr, Y. Zhang, M. A. Khan, K. Strebel, and V. K. Pathak. 2004. A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc. Natl. Acad. Sci. USA 101:5652-5657.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5652-5657
    • Xu, H.1    Svarovskaia, E.S.2    Barr, R.3    Zhang, Y.4    Khan, M.A.5    Strebel, K.6    Pathak, V.K.7
  • 51
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X. F. Yu. 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
  • 52
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang, H., B. Yang, R. J. Pomerantz, C. Zhang, S. C. Arunachalam, and L. Gao. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.