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Volumn 88, Issue 7, 2014, Pages 3850-3860

Biochemical and biological studies of mouse APOBEC3

Author keywords

[No Author keywords available]

Indexed keywords

CYTIDINE DEAMINASE; DEAMINASE; GLUTATHIONE TRANSFERASE MA3 FUSION PROTEIN; HYBRID PROTEIN; NUCLEIC ACID; PROTEIN APOBEC3; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 84895434941     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03456-13     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0036200070 scopus 로고    scopus 로고
    • An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22
    • Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, Navaratnam N. 2002. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79:285-296. http: //dx.doi.org/10.1006/geno.2002.6718.
    • (2002) Genomics , vol.79 , pp. 285-296
    • Jarmuz, A.1    Chester, A.2    Bayliss, J.3    Gisbourne, J.4    Dunham, I.5    Scott, J.6    Navaratnam, N.7
  • 2
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris RS, Liddament MT. 2004. Retroviral restriction by APOBEC proteins. Nat. Rev. Immunol. 4:868-877. http://dx.doi.org/10.1038/nri1489.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 3
    • 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. http://dx.doi.org/10.1038/nature00939.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 4
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity ofAPOBEC3Gby promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabuzda D. 2004. Vif overcomes the innate antiviral activity ofAPOBEC3Gby promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279: 7792-7798. http://dx.doi.org/10.1074/jbc.M313093200.
    • (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
  • 5
    • 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 XF. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060. http://dx.doi.org/10.1126/science.1089591.
    • (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
  • 7
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by humanAPOBEC3Gthrough lethal editing of nascent reverse transcripts
    • Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D. 2003. Broad antiretroviral defence by humanAPOBEC3Gthrough lethal editing of nascent reverse transcripts. Nature 424:99-103. http://dx.doi.org/10 .1038/nature01709.
    • (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
  • 8
    • 38349096771 scopus 로고    scopus 로고
    • Species-specific restriction of apobec3-mediated hypermutation
    • Browne EP, Littman DR. 2008. Species-specific restriction of apobec3-mediated hypermutation. J. Virol. 82:1305-1313. http://dx.doi.org/10 .1128/JVI.01371-07.
    • (2008) J. Virol. , vol.82 , pp. 1305-1313
    • Browne, E.P.1    Littman, D.R.2
  • 12
    • 0034887093 scopus 로고    scopus 로고
    • Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors
    • Derse D, Hill SA, Lloyd PA, Chung H, Morse BA. 2001. Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors. J. Virol. 75:8461-8468. http: //dx.doi.org/10.1128/JVI.75.18.8461-8468.2001.
    • (2001) J. Virol. , vol.75 , pp. 8461-8468
    • Derse, D.1    Hill, S.A.2    Lloyd, P.A.3    Chung, H.4    Morse, B.A.5
  • 13
    • 33744929618 scopus 로고    scopus 로고
    • Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect
    • Iwatani Y, Takeuchi H, Strebel K, Levin JG. 2006. Biochemical activities of highly purified, catalytically active human APOBEC3G: correlation with antiviral effect. J. Virol. 80:5992-6002. http://dx.doi.org/10.1128/JVI .02680-05.
    • (2006) J. Virol. , vol.80 , pp. 5992-6002
    • Iwatani, Y.1    Takeuchi, H.2    Strebel, K.3    Levin, J.G.4
  • 14
    • 13844270834 scopus 로고    scopus 로고
    • Complementary function of the two catalytic domains of APOBEC3G
    • Navarro F, Bollman B, Chen H, Konig R, Yu Q, Chiles K, Landau NR. 2005. Complementary function of the two catalytic domains of APOBEC3G. Virology 333:374-386. http://dx.doi.org/10.1016/j.virol .2005.01.011.
    • (2005) Virology , vol.333 , pp. 374-386
    • Navarro, F.1    Bollman, B.2    Chen, H.3    Konig, R.4    Yu, Q.5    Chiles, K.6    Landau, N.R.7
  • 15
    • 60049091300 scopus 로고    scopus 로고
    • Assembly properties of human immunodeficiency virus type 1 Gag-leucine zipper chimeras: implications for retrovirus assembly
    • Crist RM, Datta SA, Stephen AG, Soheilian F, Mirro J, Fisher RJ, Nagashima K, Rein A. 2009. Assembly properties of human immunodeficiency virus type 1 Gag-leucine zipper chimeras: implications for retrovirus assembly. J. Virol. 83:2216-2225. http://dx.doi.org/10.1128/JVI .02031-08.
    • (2009) J. Virol. , vol.83 , pp. 2216-2225
    • Crist, R.M.1    Datta, S.A.2    Stephen, A.G.3    Soheilian, F.4    Mirro, J.5    Fisher, R.J.6    Nagashima, K.7    Rein, A.8
  • 16
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371. http://dx.doi .org/10.1038/nprot.2009.2.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 19
    • 77957656529 scopus 로고    scopus 로고
    • Adaptive evolution of Mus Apobec3 includes retroviral insertion and positive selection at two clusters of residues flanking the substrate groove
    • Sanville B, Dolan MA, Wollenberg K, Yan Y, Martin C, Yeung ML, Strebel K, Buckler-White A, Kozak CA. 2010. Adaptive evolution of Mus Apobec3 includes retroviral insertion and positive selection at two clusters of residues flanking the substrate groove. PLoS Pathog. 6:e1000974. http: //dx.doi.org/10.1371/journal.ppat.1000974.
    • (2010) PLoS Pathog. , vol.6
    • Sanville, B.1    Dolan, M.A.2    Wollenberg, K.3    Yan, Y.4    Martin, C.5    Yeung, M.L.6    Strebel, K.7    Buckler-White, A.8    Kozak, C.A.9
  • 20
    • 33846031136 scopus 로고    scopus 로고
    • Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains
    • Hakata Y, Landau NR. 2006. Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. J. Biol. Chem. 281: 36624-36631. http://dx.doi.org/10.1074/jbc.M604980200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36624-36631
    • Hakata, Y.1    Landau, N.R.2
  • 21
    • 63449090379 scopus 로고    scopus 로고
    • RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1
    • Huthoff H, Autore F, Gallois-Montbrun S, Fraternali F, Malim MH. 2009. RNA-dependent oligomerization of APOBEC3G is required for restriction of HIV-1. PLoS Pathog. 5:e1000330. http://dx.doi.org/10.1371 /journal.ppat.1000330.
    • (2009) PLoS Pathog. , vol.5
    • Huthoff, H.1    Autore, F.2    Gallois-Montbrun, S.3    Fraternali, F.4    Malim, M.H.5
  • 22
    • 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. http://dx.doi .org/10.1128/JVI.02795-06.
    • (2007) J. Virol. , vol.81 , pp. 3807-3815
    • Huthoff, H.1    Malim, M.H.2
  • 23
    • 36348962513 scopus 로고    scopus 로고
    • 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G
    • Wang T, Tian C, Zhang W, Luo K, Sarkis PT, Yu L, Liu B, Yu Y, Yu XF.2007. 7SL RNA mediates virion packaging of the antiviral cytidine deaminase APOBEC3G. J. Virol. 81:13112-13124. http://dx.doi.org/10.1128 /JVI.00892-07.
    • (2007) J. Virol. , vol.81 , pp. 13112-13124
    • Wang, T.1    Tian, C.2    Zhang, W.3    Luo, K.4    Sarkis, P.T.5    Yu, L.6    Liu, B.7    Yu, Y.8    Yu, X.F.9
  • 24
    • 37449021340 scopus 로고    scopus 로고
    • Interaction with 7SL RNA but not with HIV-1 genomic RNA or P bodies is required for APOBEC3F virion packaging
    • Wang T, Tian C, Zhang W, Sarkis PT, Yu XF. 2008. Interaction with 7SL RNA but not with HIV-1 genomic RNA or P bodies is required for APOBEC3F virion packaging. J. Mol. Biol. 375:1098-1112. http://dx.doi .org/10.1016/j.jmb.2007.11.017.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1098-1112
    • Wang, T.1    Tian, C.2    Zhang, W.3    Sarkis, P.T.4    Yu, X.F.5
  • 25
    • 84864456753 scopus 로고    scopus 로고
    • Reduced APOBEC3H variant anti-viral activities are associated with altered RNA binding activities
    • Zhen A, Du J, Zhou X, Xiong Y, Yu XF. 2012. Reduced APOBEC3H variant anti-viral activities are associated with altered RNA binding activities. PLoS One 7:e38771. http://dx.doi.org/10.1371/journal.pone.0038771.
    • (2012) PLoS One , vol.7
    • Zhen, A.1    Du, J.2    Zhou, X.3    Xiong, Y.4    Yu, X.F.5
  • 26
    • 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 ES, Xu H, Mbisa JL, Barr R, Gorelick RJ, Ono A, Freed EO, Hu WS, Pathak VK. 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. http://dx.doi.org/10.1074/jbc.M405761200.
    • (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
  • 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, Rohrig UF, 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. http://dx.doi.org/10.1128/JVI .01491-09.
    • (2009) J. Virol. , vol.83 , pp. 12611-12621
    • Bulliard, Y.1    Turelli, P.2    Rohrig, U.F.3    Zoete, V.4    Mangeat, B.5    Michielin, O.6    Trono, D.7
  • 28
    • 67649669726 scopus 로고    scopus 로고
    • Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA
    • Friew YN, Boyko V, Hu WS, Pathak VK. 2009. Intracellular interactions between APOBEC3G, RNA, and HIV-1 Gag: APOBEC3G multimerization is dependent on its association with RNA. Retrovirology 6:56. http: //dx.doi.org/10.1186/1742-4690-6-56.
    • (2009) Retrovirology , vol.6 , pp. 56
    • Friew, Y.N.1    Boyko, V.2    Hu, W.S.3    Pathak, V.K.4
  • 29
    • 79960691652 scopus 로고    scopus 로고
    • Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein
    • Demorest ZL, Li M, Harris RS. 2011. Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein. J. Biol. Chem. 286:26568-26575. http://dx.doi.org/10.1074/jbc.M111.235721.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26568-26575
    • Demorest, Z.L.1    Li, M.2    Harris, R.S.3
  • 30
    • 84867517494 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 Vif with APOBEC3G is not dependent on serine/threonine phosphorylation status
    • Kopietz F, Jaguva Vasudevan AA, Kramer M, Muckenfuss H, Sanzenbacher R, Cichutek K, Flory E, Munk C. 2012. Interaction of human immunodeficiency virus type 1 Vif with APOBEC3G is not dependent on serine/threonine phosphorylation status. J. Gen. Virol. 93:2425-2430. http://dx.doi.org/10.1099/vir.0.043273-0.
    • (2012) J. Gen. Virol. , vol.93 , pp. 2425-2430
    • Kopietz, F.1    Jaguva Vasudevan, A.A.2    Kramer, M.3    Muckenfuss, H.4    Sanzenbacher, R.5    Cichutek, K.6    Flory, E.7    Munk, C.8
  • 32
    • 33745067722 scopus 로고    scopus 로고
    • APOBEC3G DNA deaminase acts processively 3'→5' on single-stranded DNA
    • Chelico L, Pham P, Calabrese P, Goodman MF. 2006. APOBEC3G DNA deaminase acts processively 3'→5' on single-stranded DNA. Nat. Struct. Mol. Biol. 13:392-399. http://dx.doi.org/10.1038/nsmb1086.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 392-399
    • Chelico, L.1    Pham, P.2    Calabrese, P.3    Goodman, M.F.4
  • 34
    • 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, Wain-Hobson S. 2006. Twin gradients in APOBEC3 edited HIV-1 DNA reflect the dynamics of lentiviral replication. Nucleic Acids Res. 34:4677-4684. http://dx.doi.org/10 .1093/nar/gkl555.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4677-4684
    • Suspène, R.1    Rusniok, C.2    Vartanian, J.-P.3    Wain-Hobson, S.4
  • 35
    • 78049501117 scopus 로고    scopus 로고
    • The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F
    • Hu C, Saenz DT, Fadel HJ, Walker W, Peretz M, Poeschla EM. 2010. The HIV-1 central polypurine tract functions as a second line of defense against APOBEC3G/F. J. Virol. 84:11981-11993. http://dx.doi.org/10 .1128/JVI.00723-10.
    • (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
  • 36
    • 77952399342 scopus 로고    scopus 로고
    • Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G
    • Chelico L, Prochnow C, Erie DA, Chen XS, Goodman MF. 2010. Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G. J. Biol. Chem. 285:16195-16205. http://dx.doi.org/10.1074/jbc.M110.107987.
    • (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
  • 37
    • 0026506252 scopus 로고
    • A second origin of DNA plusstrand synthesis is required for optimal human immunodeficiency virus replication
    • Charneau P, Alizon M, Clavel F. 1992. A second origin of DNA plusstrand synthesis is required for optimal human immunodeficiency virus replication. J. Virol. 66:2814-2820.
    • (1992) J. Virol. , vol.66 , pp. 2814-2820
    • Charneau, P.1    Alizon, M.2    Clavel, F.3
  • 38
    • 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. http://dx.doi.org/10.1128/JVI.00839-06.
    • (2006) J. Virol. , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 39
    • 33847636341 scopus 로고    scopus 로고
    • APOBEC-mediated viral restriction: not simply editing? Trends Biochem
    • Holmes RK, Malim MH, Bishop KN. 2007. APOBEC-mediated viral restriction: not simply editing? Trends Biochem. Sci. 32:118-128. http: //dx.doi.org/10.1016/j.tibs.2007.01.004.
    • (2007) Sci. , vol.32 , pp. 118-128
    • Holmes, R.K.1    Malim, M.H.2    Bishop, K.N.3
  • 44
    • 84878429046 scopus 로고    scopus 로고
    • Murine leukemia virus glycosylated Gag blocks apolipoprotein B editing complex 3 and cytosolic sensor access to the reverse transcription complex
    • U. S. A.
    • Stavrou S, Nitta T, Kotla S, Ha D, Nagashima K, Rein AR, Fan H, Ross SR. 2013. Murine leukemia virus glycosylated Gag blocks apolipoprotein B editing complex 3 and cytosolic sensor access to the reverse transcription complex. Proc. Natl. Acad. Sci. U. S. A. 110:9078-9083. http://dx.doi.org /10.1073/pnas.1217399110.
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , pp. 9078-9083
    • Stavrou, S.1    Nitta, T.2    Kotla, S.3    Ha, D.4    Nagashima, K.5    Rein, A.R.6    Fan, H.7    Ross, S.R.8
  • 45
    • 35948967657 scopus 로고    scopus 로고
    • Role of APOBEC3 in genetic diversity among endogenous murine leukemia viruses
    • Jern P, Stoye JP, Coffin JM. 2007. Role of APOBEC3 in genetic diversity among endogenous murine leukemia viruses. PLoS Genet. 3:2014-2022. http://dx.doi.org/10.1371/journal.pgen.0030183.
    • (2007) PLoS Genet. , vol.3 , pp. 2014-2022
    • Jern, P.1    Stoye, J.P.2    Coffin, J.M.3
  • 46
    • 84865319212 scopus 로고    scopus 로고
    • Moloney murine leukemia virus glyco-gag facilitates xenotropic murine leukemia virusrelated virus replication through human APOBEC3-independent mechanisms
    • Nitta T, Lee S, Ha D, Arias M, Kozak CA, Fan H. 2012. Moloney murine leukemia virus glyco-gag facilitates xenotropic murine leukemia virusrelated virus replication through human APOBEC3-independent mechanisms. Retrovirology 9:58. http://dx.doi.org/10.1186/1742-4690-9-58.
    • (2012) Retrovirology , vol.9 , pp. 58
    • Nitta, T.1    Lee, S.2    Ha, D.3    Arias, M.4    Kozak, C.A.5    Fan, H.6
  • 47
    • 60749085330 scopus 로고    scopus 로고
    • Enhanced replication and pathogenesis of Moloney murine leukemia virus in mice defective in the murine APOBEC3 gene
    • Low A, Okeoma CM, Lovsin N, de las Heras M, Taylor TH, Peterlin BM, Ross SR, Fan H. 2009. Enhanced replication and pathogenesis of Moloney murine leukemia virus in mice defective in the murine APOBEC3 gene. Virology 385:455-463. http://dx.doi.org/10.1016/j.virol.2008 .11.051.
    • (2009) Virology , vol.385 , pp. 455-463
    • Low, A.1    Okeoma, C.M.2    Lovsin, N.3    De Las Heras, M.4    Taylor, T.H.5    Peterlin, B.M.6    Ross, S.R.7    Fan, H.8
  • 50
    • 70350312835 scopus 로고    scopus 로고
    • The Akv murine leukemia virus is restricted and hypermutated by mouse Apobec3
    • Langlois MA, Kemmerich K, Rada C, Neuberger MS. 2009. The Akv murine leukemia virus is restricted and hypermutated by mouse Apobec3. J. Virol. 83:11550-11559. http://dx.doi.org/10.1128/JVI.01430-09.
    • (2009) J. Virol. , vol.83 , pp. 11550-11559
    • Langlois, M.A.1    Kemmerich, K.2    Rada, C.3    Neuberger, M.S.4
  • 51
    • 84876329767 scopus 로고    scopus 로고
    • APOBEC3 inhibition of mouse mammary tumor virus infection: the role of cytidine deamination versus inhibition of reverse transcription
    • MacMillan AL, Kohli RM, Ross SR. 2013. APOBEC3 inhibition of mouse mammary tumor virus infection: the role of cytidine deamination versus inhibition of reverse transcription. J. Virol. 87:4808-4817. http://dx.doi .org/10.1128/JVI.00112-13.
    • (2013) J. Virol. , vol.87 , pp. 4808-4817
    • MacMillan, A.L.1    Kohli, R.M.2    Ross, S.R.3
  • 52
    • 78650181511 scopus 로고    scopus 로고
    • APOBEC3 proteins expressed in mammary epithelial cells are packaged into retroviruses and can restrict transmission of milk-borne virions
    • Okeoma CM, Huegel AL, Lingappa J, Feldman MD, Ross SR. 2010. APOBEC3 proteins expressed in mammary epithelial cells are packaged into retroviruses and can restrict transmission of milk-borne virions. Cell Host Microbe 8:534-543. http://dx.doi.org/10.1016/j.chom.2010.11.003.
    • (2010) Cell Host Microbe , vol.8 , pp. 534-543
    • Okeoma, C.M.1    Huegel, A.L.2    Lingappa, J.3    Feldman, M.D.4    Ross, S.R.5
  • 53
    • 33847200788 scopus 로고    scopus 로고
    • APOBEC3 inhibits mouse mammary tumour virus replication in vivo
    • Okeoma CM, Lovsin N, Peterlin BM, Ross SR. 2007. APOBEC3 inhibits mouse mammary tumour virus replication in vivo. Nature 445:927-930. http://dx.doi.org/10.1038/nature05540.
    • (2007) Nature , vol.445 , pp. 927-930
    • Okeoma, C.M.1    Lovsin, N.2    Peterlin, B.M.3    Ross, S.R.4
  • 54
    • 63149110871 scopus 로고    scopus 로고
    • Expression of murine APOBEC3 alleles in different mouse strains and their effect on mouse mammary tumor virus infection
    • Okeoma CM, Petersen J, Ross SR. 2009. Expression of murine APOBEC3 alleles in different mouse strains and their effect on mouse mammary tumor virus infection. J. Virol. 83:3029-3038. http://dx.doi.org/10.1128 /JVI.02536-08.
    • (2009) J. Virol. , vol.83 , pp. 3029-3038
    • Okeoma, C.M.1    Petersen, J.2    Ross, S.R.3


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