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Volumn 93, Issue 3, 2012, Pages 565-576

The innate antiviral factor APOBEC3G targets replication of measles, mumps and respiratory syncytial viruses

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ADENOSINE DEAMINASE ACTING ON THE RNA; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CYTIDINE; GUANINE; UNCLASSIFIED DRUG; URIDINE; VIRUS ENZYME; VIRUS RNA;

EID: 84857082722     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.038919-0     Document Type: Article
Times cited : (49)

References (64)
  • 1
    • 43049113468 scopus 로고    scopus 로고
    • APOBEC3 proteins and reverse transcription
    • Aguiar, R. S. & Peterlin, B. M. (2008). APOBEC3 proteins and reverse transcription. Virus Res 134, 74-85.
    • (2008) Virus Res , vol.134 , pp. 74-85
    • Aguiar, R.S.1    Peterlin, B.M.2
  • 3
    • 18044389684 scopus 로고    scopus 로고
    • Identification of naturally occurring amino acid variations that affect the ability of the measles virus C protein to regulate genome replication and transcription
    • Bankamp, B., Wilson, J., Bellini, W. J. & Rota, P. A. (2005). Identification of naturally occurring amino acid variations that affect the ability of the measles virus C protein to regulate genome replication and transcription. Virology 336, 120-129.
    • (2005) Virology , vol.336 , pp. 120-129
    • Bankamp, B.1    Wilson, J.2    Bellini, W.J.3    Rota, P.A.4
  • 4
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • Bass, B. L. (2002). RNA editing by adenosine deaminases that act on RNA. Annu Rev Biochem 71, 817-846.
    • (2002) Annu Rev Biochem , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 6
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • Bishop, K. N., Holmes, R. K. & Malim, M. H. (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
  • 8
    • 33745541663 scopus 로고    scopus 로고
    • Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication
    • Bonvin, M., Achermann, F., Greeve, I., Stroka, D., Keogh, A., Inderbitzin, D., Candinas, D., Sommer, P., Wain-Hobson, S.(2006). Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication. Hepatology 43, 1364-1374.
    • (2006) Hepatology , vol.43 , pp. 1364-1374
    • Bonvin, M.1    Achermann, F.2    Greeve, I.3    Stroka, D.4    Keogh, A.5    Inderbitzin, D.6    Candinas, D.7    Sommer, P.8    Wain-Hobson, S.9
  • 9
    • 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. & 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
  • 10
    • 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
  • 11
    • 0023763122 scopus 로고
    • Biased hypermutation and other genetic changes in defective measles viruses in human brain infections
    • Cattaneo, R., Schmid, A., Eschle, D., Baczko, K., Ter-Meulen, V. & Billeter, M. A. (1988). Biased hypermutation and other genetic changes in defective measles viruses in human brain infections. Cell 55, 255-265.
    • (1988) Cell , vol.55 , pp. 255-265
    • Cattaneo, R.1    Schmid, A.2    Eschle, D.3    Baczko, K.4    Ter-Meulen, V.5    Billeter, M.A.6
  • 12
    • 70849135482 scopus 로고    scopus 로고
    • Molecular differences between two Jeryl Lynn mumps virus vaccine component strains, JL5 and JL2
    • Chambers, P., Rima, B. K. & Duprex, W. P. (2009). Molecular differences between two Jeryl Lynn mumps virus vaccine component strains, JL5 and JL2. J Gen Virol 90, 2973-2981.
    • (2009) J Gen Virol , vol.90 , pp. 2973-2981
    • Chambers, P.1    Rima, B.K.2    Duprex, W.P.3
  • 13
    • 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. & 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
  • 15
    • 77958460177 scopus 로고    scopus 로고
    • Interferon-alpha induces high expression of APOBEC3G and STAT-1 in vitro and in vivo
    • Chen, H., Wang, L. W., Huang, Y. Q. & Gong, Z. J. (2010). Interferon-alpha induces high expression of APOBEC3G and STAT-1 in vitro and in vivo. Int J Mol Sci 11, 3501-3512.
    • (2010) Int J Mol Sci , vol.11 , pp. 3501-3512
    • Chen, H.1    Wang, L.W.2    Huang, Y.Q.3    Gong, Z.J.4
  • 18
    • 50349093233 scopus 로고    scopus 로고
    • The AID/APOBEC family of nucleic acid mutators
    • Conticello, S. G. (2008). The AID/APOBEC family of nucleic acid mutators. Genome Biol 9, 229.
    • (2008) Genome Biol , vol.9 , pp. 229
    • Conticello, S.G.1
  • 20
    • 33847193509 scopus 로고    scopus 로고
    • Antiviral protein APOBEC3G localizes to ribonucleoprotein complexes found in P bodies and stress granules
    • Gallois-Montbrun, S., Kramer, B., Swanson, C. M., Byers, H., Lynham, S., Ward, M. & Malim, M. H. (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
  • 21
    • 43949090162 scopus 로고    scopus 로고
    • Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins
    • Gallois-Montbrun, S., Holmes, R. K., Swanson, C. M., Fernández-Ocaña, M., Byers, H. L., Ward, M. A. & Malim, M. H. (2008). Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins. J Virol 82, 5636-5642.
    • (2008) J Virol , vol.82 , pp. 5636-5642
    • Gallois-Montbrun, S.1    Holmes, R.K.2    Swanson, C.M.3    Fernández-Ocaña, M.4    Byers, H.L.5    Ward, M.A.6    Malim, M.H.7
  • 22
    • 0033766989 scopus 로고    scopus 로고
    • Glycosaminoglycan sulfation requirements for respiratory syncytial virus infection
    • Hallak, L. K., Spillmann, D., Collins, P. L. & Peeples, M. E. (2000). Glycosaminoglycan sulfation requirements for respiratory syncytial virus infection. J Virol 74, 10508-10513.
    • (2000) J Virol , vol.74 , pp. 10508-10513
    • Hallak, L.K.1    Spillmann, D.2    Collins, P.L.3    Peeples, M.E.4
  • 23
    • 48249102331 scopus 로고    scopus 로고
    • APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication
    • Han, Y., Wang, X., Dang, Y. & Zheng, Y. H. (2008). APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication. PLoS Pathog 4, e1000095.
    • (2008) PLoS Pathog , vol.4
    • Han, Y.1    Wang, X.2    Dang, Y.3    Zheng, Y.H.4
  • 25
    • 0036284385 scopus 로고    scopus 로고
    • SLAM (CD150)-independent measles virus entry as revealed by recombinant virus expressing green fluorescent protein
    • Hashimoto, K., Ono, N., Tatsuo, H., Minagawa, H., Takeda, M., Takeuchi, K. & Yanagi, Y. (2002). SLAM (CD150)-independent measles virus entry as revealed by recombinant virus expressing green fluorescent protein. J Virol 76, 6743-6749.
    • (2002) J Virol , vol.76 , pp. 6743-6749
    • Hashimoto, K.1    Ono, N.2    Tatsuo, H.3    Minagawa, H.4    Takeda, M.5    Takeuchi, K.6    Yanagi, Y.7
  • 26
    • 33847636341 scopus 로고    scopus 로고
    • APOBEC-mediated viral restriction: Not simply editing?
    • Holmes, R. K., Malim, M. H. & Bishop, K. N. (2007). APOBEC-mediated viral restriction: not simply editing? Trends Biochem Sci 32, 118-128.
    • (2007) Trends Biochem Sci , vol.32 , pp. 118-128
    • Holmes, R.K.1    Malim, M.H.2    Bishop, K.N.3
  • 27
    • 33746342112 scopus 로고    scopus 로고
    • Full-length sequence analysis of subacute sclerosing panencephalitis (SSPE) virus, a mutant of measles virus, isolated from brain tissues of a patient shortly after onset of SSPE
    • Hotta, H., Nihei, K., Abe, Y., Kato, S., Jiang, D. P., Nagano-Fujii, M. & Sada, K. (2006). Full-length sequence analysis of subacute sclerosing panencephalitis (SSPE) virus, a mutant of measles virus, isolated from brain tissues of a patient shortly after onset of SSPE. Microbiol Immunol 50, 525-534.
    • (2006) Microbiol Immunol , vol.50 , pp. 525-534
    • Hotta, H.1    Nihei, K.2    Abe, Y.3    Kato, S.4    Jiang, D.P.5    Nagano-Fujii, M.6    Sada, K.7
  • 28
    • 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, 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
  • 32
    • 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., Kao, S., Miyagi, E., Takeuchi, H., Goila-Gaur, R., Opi, S., Gipson, C. L., Parslow, T. G., Ly, H. & Strebel, K. (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
  • 33
    • 34548040898 scopus 로고    scopus 로고
    • Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions
    • Khan, M. A., Goila-Gaur, R., Opi, S., Miyagi, E., Takeuchi, H., Kao, S. & Strebel, K. (2007). Analysis of the contribution of cellular and viral RNA to the packaging of APOBEC3G into HIV-1 virions. Retrovirology 4, 48.
    • (2007) Retrovirology , vol.4 , pp. 48
    • Khan, M.A.1    Goila-Gaur, R.2    Opi, S.3    Miyagi, E.4    Takeuchi, H.5    Kao, S.6    Strebel, K.7
  • 34
    • 69449103867 scopus 로고    scopus 로고
    • Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets
    • Koning, F. A., Newman, E. N., Kim, E. Y., Kunstman, K. J., Wolinsky, S. M. & Malim, M. H. (2009). Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets. J Virol 83, 9474-9485.
    • (2009) J Virol , vol.83 , pp. 9474-9485
    • Koning, F.A.1    Newman, E.N.2    Kim, E.Y.3    Kunstman, K.J.4    Wolinsky, S.M.5    Malim, M.H.6
  • 35
    • 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., Marin, M., Rose, K. M., Bystrom, C. & Kabat, D. (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
  • 36
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • Lecossier, D., Bouchonnet, F., Clavel, F. & Hance, A. J. (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
  • 38
    • 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. & 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
  • 39
    • 0029056474 scopus 로고
    • Evolutionary origins of apoB mRNA editing: Catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site
    • Navaratnam, N., Bhattacharya, S., Fujino, T., Patel, D., Jarmuz, A. L. & Scott, J. (1995). Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site. Cell 81, 187-195.
    • (1995) Cell , vol.81 , pp. 187-195
    • Navaratnam, N.1    Bhattacharya, S.2    Fujino, T.3    Patel, D.4    Jarmuz, A.L.5    Scott, J.6
  • 41
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • 04
    • Parker, R. & Sheth, U. (2007). P bodies and the control of mRNA translation and degradation. Mol Cell 25, 635-646.04
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 42
    • 65449185824 scopus 로고    scopus 로고
    • High level expression of the anti-retroviral protein APOBEC3G is induced by influenza A virus but does not confer antiviral activity
    • Pauli, E. K., Schmolke, M., Hofmann, H., Ehrhardt, C., Flory, E., Münk, C. & Ludwig, S. (2009). High level expression of the anti-retroviral protein APOBEC3G is induced by influenza A virus but does not confer antiviral activity. Retrovirology 6, 38.
    • (2009) Retrovirology , vol.6 , pp. 38
    • Pauli, E.K.1    Schmolke, M.2    Hofmann, H.3    Ehrhardt, C.4    Flory, E.5    Münk, C.6    Ludwig, S.7
  • 43
    • 31944438580 scopus 로고    scopus 로고
    • Induction of APOBEC3 family proteins, a defensive maneuver underlying interferon-induced anti-HIV-1 activity
    • Peng, G., Lei, K. J., Jin, W., Greenwell-Wild, T. & Wahl, S. M. (2006). Induction of APOBEC3 family proteins, a defensive maneuver underlying interferon-induced anti-HIV-1 activity. J Exp Med 203, 41-46.
    • (2006) J Exp Med , vol.203 , pp. 41-46
    • Peng, G.1    Lei, K.J.2    Jin, W.3    Greenwell-Wild, T.4    Wahl, S.M.5
  • 45
    • 22144465783 scopus 로고    scopus 로고
    • Optimized SYBR green real-time PCR assay to quantify the absolute copy number of measles virus RNAs using gene specific primers
    • Plumet, S. & Gerlier, D. (2005). Optimized SYBR green real-time PCR assay to quantify the absolute copy number of measles virus RNAs using gene specific primers. J Virol Methods 128, 79-87.
    • (2005) J Virol Methods , vol.128 , pp. 79-87
    • Plumet, S.1    Gerlier, D.2
  • 47
    • 35048818442 scopus 로고    scopus 로고
    • Measles virus minigenomes encoding two autofluorescent proteins reveal cell to cell variation in reporter expression dependent on viral sequences between the transcription units
    • Rennick, L. J., Duprex, W. P. & Rima, B. K. (2007). Measles virus minigenomes encoding two autofluorescent proteins reveal cell to cell variation in reporter expression dependent on viral sequences between the transcription units. J Gen Virol 88, 2710-2718.
    • (2007) J Gen Virol , vol.88 , pp. 2710-2718
    • Rennick, L.J.1    Duprex, W.P.2    Rima, B.K.3
  • 48
    • 33744929857 scopus 로고    scopus 로고
    • RNA interference with measles virus N, P, and L mRNAs efficiently prevents and with matrix protein mRNA enhances viral transcription
    • Reuter, T., Weissbrich, B., Schneider-Schaulies, S. & Schneider-Schaulies, J. (2006). RNA interference with measles virus N, P, and L mRNAs efficiently prevents and with matrix protein mRNA enhances viral transcription. J Virol 80, 5951-5957.
    • (2006) J Virol , vol.80 , pp. 5951-5957
    • Reuter, T.1    Weissbrich, B.2    Schneider-Schaulies, S.3    Schneider-Schaulies, J.4
  • 49
    • 33749122058 scopus 로고    scopus 로고
    • STAT1-independent cell type-specific regulation of antiviral APOBEC3G by IFN-a
    • Sarkis, P. T., Ying, S., Xu, R. & Yu, X. F. (2006). STAT1-independent cell type-specific regulation of antiviral APOBEC3G by IFN-a. J Immunol 177, 4530-4540.
    • (2006) J Immunol , vol.177 , pp. 4530-4540
    • Sarkis, P.T.1    Ying, S.2    Xu, R.3    Yu, X.F.4
  • 50
    • 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. & 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
  • 51
    • 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. & 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
  • 52
    • 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, 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
  • 53
    • 33947518167 scopus 로고    scopus 로고
    • Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells
    • Stopak, K. S., Chiu, Y. L., Kropp, J., Grant, R. M. & Greene, W. C. (2007). Distinct patterns of cytokine regulation of APOBEC3G expression and activity in primary lymphocytes, macrophages, and dendritic cells. J Biol Chem 282, 3539-3546.
    • (2007) J Biol Chem , vol.282 , pp. 3539-3546
    • Stopak, K.S.1    Chiu, Y.L.2    Kropp, J.3    Grant, R.M.4    Greene, W.C.5
  • 54
    • 79551705342 scopus 로고    scopus 로고
    • Double-stranded RNA adenosine deaminase ADAR-1-induced hypermutated genomes among inactivated seasonal influenza and live attenuated measles virus vaccines
    • Suspé ne, R., Petit, V., Puyraimond-Zemmour, D., Aynaud, M. M., Henry, M., Guétard, D., Rusniok, C., Wain-Hobson, S. & Vartanian, J. P. (2011). Double-stranded RNA adenosine deaminase ADAR-1-induced hypermutated genomes among inactivated seasonal influenza and live attenuated measles virus vaccines. J Virol 85, 2458-2462.
    • (2011) J Virol , vol.85 , pp. 2458-2462
    • Suspéne, R.1    Petit, V.2    Puyraimond-Zemmour, D.3    Aynaud, M.M.4    Henry, M.5    Guétard, D.6    Rusniok, C.7    Wain-Hobson, S.8    Vartanian, J.P.9
  • 55
    • 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., Xu, H., Mbisa, J. L., Barr, R., Gorelick, R. J., Ono, A., Freed, E. O., Hu, W. S. & Pathak, V. K. (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
  • 57
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by APOBEC3G
    • Turelli, P., Mangeat, B., Jost, S., Vianin, S. & Trono, D. (2004). Inhibition of hepatitis B virus replication by APOBEC3G. Science 303, 1829.
    • (2004) Science , vol.303 , pp. 1829
    • Turelli, P.1    Mangeat, B.2    Jost, S.3    Vianin, S.4    Trono, D.5
  • 58
    • 54249129048 scopus 로고    scopus 로고
    • APOBEC3F and APOBEC3G have no inhibition and hypermu-tation effect on the human influenza A virus
    • Wang, G. F., Lin, S. Y., Zhang, H., Gao, Y. L., Li, W. Z., Xin, G. & Li, K. S. (2008). APOBEC3F and APOBEC3G have no inhibition and hypermu-tation effect on the human influenza A virus. Acta Virol 52, 193-194.
    • (2008) Acta Virol , vol.52 , pp. 193-194
    • Wang, G.F.1    Lin, S.Y.2    Zhang, H.3    Gao, Y.L.4    Li, W.Z.5    Xin, G.6    Li, K.S.7
  • 59
    • 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. & 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
  • 60
    • 33646924568 scopus 로고    scopus 로고
    • Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies
    • Wichroski, M. J., Robb, G. B. & Rana, T. M. (2006). Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathog 2, e41.
    • (2006) PLoS Pathog , vol.e41 , pp. 2
    • Wichroski, M.J.1    Robb, G.B.2    Rana, T.M.3
  • 61
    • 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. & 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
  • 62
    • 6344294871 scopus 로고    scopus 로고
    • APOBEC3G incorporation into human immunodeficiency virus type 1 particles
    • Zennou, V., Perez-Caballero, D., Göttlinger, H. & Bieniasz, P. D. (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    Göttlinger, H.3    Bieniasz, P.D.4
  • 63
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermu-tation in newly synthesized HIV-1 DNA
    • Zhang, H., Yang, B., Pomerantz, R. J., Zhang, C., Arunachalam, S. C. & Gao, L. (2003). The cytidine deaminase CEM15 induces hypermu-tation 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


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