메뉴 건너뛰기




Volumn 85, Issue 23, 2011, Pages 12482-12491

Identification of a Cullin5-Elonginb-Elonginc E3 complex in degradation of feline immunodeficiency virus Vif-mediated feline APOBEC3 proteins

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3; CULLIN; CULLIN 5; ELONGIN B; ELONGIN C; HYDROLASE; PROTEASOME; SUPPRESSOR OF CYTOKINE SIGNALING; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIF PROTEIN; ZINC BINDING PROTEIN;

EID: 81255200313     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05218-11     Document Type: Article
Times cited : (27)

References (63)
  • 1
    • 77954684927 scopus 로고    scopus 로고
    • The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex
    • Bergeron, J. R., et al. 2010. The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex. PLoS Pathog. 6:e1000925.
    • (2010) PLoS Pathog , vol.6
    • Bergeron, J.R.1
  • 2
    • 9244260598 scopus 로고    scopus 로고
    • Intrinsic immunity: a front-line defense against viral attack
    • Bieniasz, P. D. 2004. Intrinsic immunity: a front-line defense against viral attack. Nat. Immunol. 5:1109-1115.
    • (2004) Nat. Immunol. , vol.5 , pp. 1109-1115
    • Bieniasz, P.D.1
  • 3
    • 31644442239 scopus 로고    scopus 로고
    • APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells
    • Bogerd, H. P., H. L. Wiegand, B. P. Doehle, K. K. Lueders, and B. R. Cullen. 2006. APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells. Nucleic Acids Res. 34:89-95.
    • (2006) Nucleic Acids Res , vol.34 , pp. 89-95
    • Bogerd, H.P.1    Wiegand, H.L.2    Doehle, B.P.3    Lueders, K.K.4    Cullen, B.R.5
  • 4
    • 4043118380 scopus 로고    scopus 로고
    • The interaction between HIV-1 Gag and APOBEC3G
    • Cen, S., et al. 2004. The interaction between HIV-1 Gag and APOBEC3G. J. Biol. Chem. 279:33177-33184.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33177-33184
    • Cen, S.1
  • 5
    • 69249215357 scopus 로고    scopus 로고
    • A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G
    • Chen, G., Z. He, T. Wang, R. Xu, and X. F. Yu. 2009. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. J. Virol. 83:8674-8682.
    • (2009) J. Virol. , vol.83 , pp. 8674-8682
    • Chen, G.1    He, Z.2    Wang, T.3    Xu, R.4    Yu, X.F.5
  • 6
    • 77951993429 scopus 로고    scopus 로고
    • Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity
    • Dang, Y., R. W. Davis, I. A. York, and Y. H. Zheng. 2010. Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity. J. Virol. 84:5741-5750.
    • (2010) J. Virol. , vol.84 , pp. 5741-5750
    • Dang, Y.1    Davis, R.W.2    York, I.A.3    Zheng, Y.H.4
  • 7
    • 45549100648 scopus 로고    scopus 로고
    • Human cytidine deaminase APOBEC3H restricts HIV-1 replication
    • Dang, Y., et al. 2008. Human cytidine deaminase APOBEC3H restricts HIV-1 replication. J. Biol. Chem. 283:11606-11614.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11606-11614
    • Dang, Y.1
  • 8
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • Dang, Y., X. Wang, W. J. Esselman, and Y. H. Zheng. 2006. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J. Virol. 80:10522-10533.
    • (2006) J. Virol. , vol.80 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.H.4
  • 9
    • 77956628186 scopus 로고    scopus 로고
    • Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity
    • Dang, Y., X. Wang, I. A. York, and Y. H. Zheng. 2010. Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity. J. Virol. 84:8561-8570.
    • (2010) J. Virol. , vol.84 , pp. 8561-8570
    • Dang, Y.1    Wang, X.2    York, I.A.3    Zheng, Y.H.4
  • 10
    • 69249220263 scopus 로고    scopus 로고
    • Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization
    • Dang, Y., X. Wang, T. Zhou, I. A. York, and Y. H. Zheng. 2009. Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. J. Virol. 83:8544-8552.
    • (2009) J. Virol. , vol.83 , pp. 8544-8552
    • Dang, Y.1    Wang, X.2    Zhou, T.3    York, I.A.4    Zheng, Y.H.5
  • 11
    • 13444282074 scopus 로고    scopus 로고
    • APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses
    • Esnault, C., et al. 2005. APOBEC3G cytidine deaminase inhibits retrotransposition of endogenous retroviruses. Nature 433:430-433.
    • (2005) Nature , vol.433 , pp. 430-433
    • Esnault, C.1
  • 12
    • 0023191658 scopus 로고
    • The sor gene of HIV-1 is required for efficient virus transmission in vitro
    • Fisher, A. G., et al. 1987. The sor gene of HIV-1 is required for efficient virus transmission in vitro. Science 237:888-893.
    • (1987) Science , vol.237 , pp. 888-893
    • Fisher, A.G.1
  • 13
    • 48949118733 scopus 로고    scopus 로고
    • HIV-1 Vif, APOBEC, and intrinsic immunity
    • Goila-Gaur, R., and K. Strebel. 2008. HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 5:51.
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 14
    • 0038681901 scopus 로고    scopus 로고
    • DNA deamination mediates innate immunity to retroviral infection
    • Harris, R. S., et al. 2003. DNA deamination mediates innate immunity to retroviral infection. Cell 113:803-809.
    • (2003) Cell , vol.113 , pp. 803-809
    • Harris, R.S.1
  • 15
    • 8544241736 scopus 로고    scopus 로고
    • Retroviral restriction by APOBEC proteins
    • Harris, R. S., and M. T. Liddament. 2004. Retroviral restriction by APOBEC proteins. Nat. Rev. Immunol. 4:868-877.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 868-877
    • Harris, R.S.1    Liddament, M.T.2
  • 16
    • 19144367904 scopus 로고    scopus 로고
    • An improved plasmid DNA expression vector for direct injection into skeletal muscle
    • Hartikka, J., et al. 1996. An improved plasmid DNA expression vector for direct injection into skeletal muscle. Hum. Gene Ther. 7:1205-1217.
    • (1996) Hum. Gene Ther. , vol.7 , pp. 1205-1217
    • Hartikka, J.1
  • 17
    • 48449104748 scopus 로고    scopus 로고
    • Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction
    • He, Z., W. Zhang, G. Chen, R. Xu, and X. F. Yu. 2008. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J. Mol. Biol. 381:1000-1011.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1000-1011
    • He, Z.1    Zhang, W.2    Chen, G.3    Xu, R.4    Yu, X.F.5
  • 18
    • 0033581899 scopus 로고    scopus 로고
    • Covalent modification of all members of human Cullin family proteins by NEDD8
    • Hori, T., et al. 1999. Covalent modification of all members of human Cullin family proteins by NEDD8. Oncogene 18:6829-6834.
    • (1999) Oncogene , vol.18 , pp. 6829-6834
    • Hori, T.1
  • 19
    • 59049095806 scopus 로고    scopus 로고
    • MDM2 is a novel E3 ligase for HIV-1 Vif
    • Izumi, T., et al. 2009. MDM2 is a novel E3 ligase for HIV-1 Vif. Retrovirology 6:1.
    • (2009) Retrovirology , vol.6 , pp. 1
    • Izumi, T.1
  • 20
    • 41149164155 scopus 로고    scopus 로고
    • The restriction of zoonotic PERV transmission by human APOBEC3G
    • Jonsson, S. R., et al. 2007. The restriction of zoonotic PERV transmission by human APOBEC3G. PLoS One 2:e893.
    • (2007) PLoS One , vol.2
    • Jonsson, S.R.1
  • 21
    • 10644276385 scopus 로고    scopus 로고
    • VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases
    • Kamura, T., et al. 2004. VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases. Genes Dev. 18:3055-3065.
    • (2004) Genes Dev , vol.18 , pp. 3055-3065
    • Kamura, T.1
  • 22
    • 58149517769 scopus 로고    scopus 로고
    • Guidelines for naming nonprimate APOBEC3 genes and proteins
    • LaRue, R. S., et al. 2009. Guidelines for naming nonprimate APOBEC3 genes and proteins. J. Virol. 83:494-497.
    • (2009) J. Virol. , vol.83 , pp. 494-497
    • LaRue, R.S.1
  • 23
    • 77955001423 scopus 로고    scopus 로고
    • Lentiviral Vif degrades the APOBEC3Z3/APOBEC3H protein of its mammalian host and is capable of cross-species activity
    • Larue, R. S., J. Lengyel, S. R. Jonsson, V. Andresdottir, and R. S. Harris. 2010. Lentiviral Vif degrades the APOBEC3Z3/APOBEC3H protein of its mammalian host and is capable of cross-species activity. J. Virol. 84:8193-8201.
    • (2010) J. Virol. , vol.84 , pp. 8193-8201
    • Larue, R.S.1    Lengyel, J.2    Jonsson, S.R.3    Andresdottir, V.4    Harris, R.S.5
  • 24
    • 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
  • 25
    • 79953161456 scopus 로고    scopus 로고
    • Repression of porcine endogenous retrovirus infection by human APOBEC3 proteins
    • Lee, J., et al. 2011. Repression of porcine endogenous retrovirus infection by human APOBEC3 proteins. Biochem. Biophys. Res. Commun. 407:266-270.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 266-270
    • Lee, J.1
  • 26
    • 0022680624 scopus 로고
    • A new HTLV-1II/LAV protein encoded by a gene found in cytopathic retroviruses
    • Lee, T. H., et al. 1986. A new HTLV-1II/LAV protein encoded by a gene found in cytopathic retroviruses. Science 231:1546-1549.
    • (1986) Science , vol.231 , pp. 1546-1549
    • Lee, T.H.1
  • 27
    • 4143071549 scopus 로고    scopus 로고
    • APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo
    • Liddament, M. T., W. L. Brown, A. J. Schumacher, and R. S. Harris. 2004. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr. Biol. 14:1385-1391.
    • (2004) Curr. Biol. , vol.14 , pp. 1385-1391
    • Liddament, M.T.1    Brown, W.L.2    Schumacher, A.J.3    Harris, R.S.4
  • 28
    • 20344379929 scopus 로고    scopus 로고
    • The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein
    • Lochelt, M., et al. 2005. The antiretroviral activity of APOBEC3 is inhibited by the foamy virus accessory Bet protein. Proc. Natl. Acad. Sci. U. S. A. 102:7982-7987.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 7982-7987
    • Lochelt, M.1
  • 29
    • 34249784818 scopus 로고    scopus 로고
    • Adenovirus E4orf6 assembles with Cullin5-ElonginBElonginC E3 ubiquitin ligase through an HIV/SIV Vif-like BC-box to regulate p53
    • Luo, K., et al. 2007. Adenovirus E4orf6 assembles with Cullin5-ElonginBElonginC E3 ubiquitin ligase through an HIV/SIV Vif-like BC-box to regulate p53. FASEB J. 21:1742-1750.
    • (2007) FASEB J , vol.21 , pp. 1742-1750
    • Luo, K.1
  • 30
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors are substrate receptors that assemble with Cullin5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • Luo, K., et al. 2005. Primate lentiviral virion infectivity factors are substrate receptors that assemble with Cullin5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc. Natl. Acad. Sci. U. S. A. 102:11444-11449.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11444-11449
    • Luo, K.1
  • 31
    • 79957966644 scopus 로고    scopus 로고
    • Polarity changes in the transmembrane domain core of HIV-1 Vpu inhibits its anti-tetherin activity
    • Lv, M., et al. 2011. Polarity changes in the transmembrane domain core of HIV-1 Vpu inhibits its anti-tetherin activity. PLoS One 6:e20890.
    • (2011) PLoS One , vol.6
    • Lv, M.1
  • 32
    • 43149097171 scopus 로고    scopus 로고
    • Characterization of Cullin-box sequences that direct recruitment of Cul2-Rbx1 and Cul5-Rbx2 modules to Elongin BCbased ubiquitin ligases
    • Mahrour, N., et al. 2008. Characterization of Cullin-box sequences that direct recruitment of Cul2-Rbx1 and Cul5-Rbx2 modules to Elongin BCbased ubiquitin ligases. J. Biol. Chem. 283:8005-8013.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8005-8013
    • Mahrour, N.1
  • 33
    • 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
  • 34
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • Mehle, A., J. Goncalves, M. Santa-Marta, M. McPike, and D. Gabuzda. 2004. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev. 18: 2861-2866.
    • (2004) Genes Dev , vol.18 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 35
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle, A., et al. 2004. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279:7792-7798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7792-7798
    • Mehle, A.1
  • 36
    • 33745225450 scopus 로고    scopus 로고
    • A zincbinding region in Vif binds Cul5 and determines cullin selection
    • Mehle, A., E. R. Thomas, K. S. Rajendran, and D. Gabuzda. 2006. A zincbinding region in Vif binds Cul5 and determines cullin selection. J. Biol. Chem. 281:17259-17265.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 37
    • 45549105119 scopus 로고    scopus 로고
    • Functions, structure, and read-through alternative splicing of feline APOBEC3 genes
    • Munk, C., et al. 2008. Functions, structure, and read-through alternative splicing of feline APOBEC3 genes. Genome Biol. 9:R48.
    • (2008) Genome Biol , vol.9
    • Munk, C.1
  • 38
    • 75749102530 scopus 로고    scopus 로고
    • Restriction of feline retroviruses: lessons from cat APOBEC3 cytidine deaminases and TRIM5α proteins
    • Munk, C., T. Hechler, S. Chareza, and M. Lochelt. 2010. Restriction of feline retroviruses: lessons from cat APOBEC3 cytidine deaminases and TRIM5α proteins. Vet. Immunol. Immunopathol. 134:14-24.
    • (2010) Vet. Immunol. Immunopathol. , vol.134 , pp. 14-24
    • Munk, C.1    Hechler, T.2    Chareza, S.3    Lochelt, M.4
  • 39
    • 1842591241 scopus 로고    scopus 로고
    • Nedd8 on cullin: building an expressway to protein destruction
    • Pan, Z. Q., A. Kentsis, D. C. Dias, K. Yamoah, and K. Wu. 2004. Nedd8 on cullin: building an expressway to protein destruction. Oncogene 23:1985-1997.
    • (2004) Oncogene , vol.23 , pp. 1985-1997
    • Pan, Z.Q.1    Kentsis, A.2    Dias, D.C.3    Yamoah, K.4    Wu, K.5
  • 40
    • 60049098639 scopus 로고    scopus 로고
    • Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif
    • Pery, E., K. S. Rajendran, A. J. Brazier, and D. Gabuzda. 2009. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J. Virol. 83:2374-2381.
    • (2009) J. Virol. , vol.83 , pp. 2374-2381
    • Pery, E.1    Rajendran, K.S.2    Brazier, A.J.3    Gabuzda, D.4
  • 41
    • 0034117282 scopus 로고    scopus 로고
    • Nedd8 modification of cul-1 activates SCF(β(TrCP))-dependent ubiquitination of I Bα
    • Read, M. A., et al. 2000. Nedd8 modification of cul-1 activates SCF(β(TrCP))-dependent ubiquitination of I Bα. Mol. Cell. Biol. 20:2326-2333.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2326-2333
    • Read, M.A.1
  • 42
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • Russell, R. A., and V. K. Pathak. 2007. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J. Virol. 81:8201-8210.
    • (2007) J. Virol. , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 43
    • 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., N. C. Gaddis, J. D. Choi, and M. H. Malim. 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
  • 44
    • 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
  • 45
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • Stanley, B. J., et al. 2008. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J. Virol. 82:8656-8663.
    • (2008) J. Virol. , vol.82 , pp. 8656-8663
    • Stanley, B.J.1
  • 46
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function
    • Stebbins, C. E., W. G. Kaelin, Jr., and N. P. Pavletich. 1999. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 284:455-461.
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 47
    • 77953776953 scopus 로고    scopus 로고
    • Productive replication of Vif-chimeric HIV-1 in feline cells
    • Stern, M. A., et al. 2010. Productive replication of Vif-chimeric HIV-1 in feline cells. J. Virol. 84:7378-7395.
    • (2010) J. Virol. , vol.84 , pp. 7378-7395
    • Stern, M.A.1
  • 48
    • 0023267788 scopus 로고
    • The HIV "A" (sor) gene product is essential for virus infectivity
    • Strebel, K., et al. 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
  • 49
    • 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., et al. 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
  • 50
    • 1642308939 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by APOBEC3G
    • Turelli, P., B. Mangeat, S. Jost, S. Vianin, and D. Trono. 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
  • 51
    • 77951460356 scopus 로고    scopus 로고
    • Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif
    • Walker, R. C., Jr., et al. 2010. Identification of dominant negative human immunodeficiency virus type 1 Vif mutants that interfere with the functional inactivation of APOBEC3G by virus-encoded Vif. J. Virol. 84:5201-5211.
    • (2010) J. Virol. , vol.84 , pp. 5201-5211
    • Walker Jr., R.C.1
  • 52
    • 77953757638 scopus 로고    scopus 로고
    • Dissection of the HIV Vif interaction with human E3 ubiquitin ligase
    • Wolfe, L. S., B. J. Stanley, C. Liu, W. K. Eliason, and Y. Xiong. 2010. Dissection of the HIV Vif interaction with human E3 ubiquitin ligase. J. Virol. 84:7135-7139.
    • (2010) J. Virol. , vol.84 , pp. 7135-7139
    • Wolfe, L.S.1    Stanley, B.J.2    Liu, C.3    Eliason, W.K.4    Xiong, Y.5
  • 53
    • 33845996549 scopus 로고    scopus 로고
    • Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
    • Xiao, Z., E. Ehrlich, K. Luo, Y. Xiong, and X. F. Yu. 2007. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J. 21:217-222.
    • (2007) FASEB J , vol.21 , pp. 217-222
    • Xiao, Z.1    Ehrlich, E.2    Luo, K.3    Xiong, Y.4    Yu, X.F.5
  • 54
    • 33646866382 scopus 로고    scopus 로고
    • Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif
    • Xiao, Z., et al. 2006. Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. Virology 349:290-299.
    • (2006) Virology , vol.349 , pp. 290-299
    • Xiao, Z.1
  • 55
    • 37449003586 scopus 로고    scopus 로고
    • Association of human APOBEC3 cytidine deaminases with the generation of hepatitis virus B x antigen mutants and hepatocellular carcinoma
    • Xu, R., et al. 2007. Association of human APOBEC3 cytidine deaminases with the generation of hepatitis virus B x antigen mutants and hepatocellular carcinoma. Hepatology 46:1810-1820.
    • (2007) Hepatology , vol.46 , pp. 1810-1820
    • Xu, R.1
  • 56
    • 0035895896 scopus 로고    scopus 로고
    • The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle
    • Yang, S., Y. Sun, and H. Zhang. 2001. The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J. Biol. Chem. 276:4889-4893.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4889-4893
    • Yang, S.1    Sun, Y.2    Zhang, H.3
  • 57
    • 2342633240 scopus 로고    scopus 로고
    • Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome
    • Yu, Q., et al. 2004. Single-strand specificity of APOBEC3G accounts for minus-strand deamination of the HIV genome. Nat. Struct. Mol. Biol. 11: 435-442.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 435-442
    • Yu, Q.1
  • 58
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., et al. 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
  • 59
    • 33750096153 scopus 로고    scopus 로고
    • Innate cellular defenses of APOBEC3 cytidine deaminases and viral counter-defenses
    • Yu, X. F. 2006. Innate cellular defenses of APOBEC3 cytidine deaminases and viral counter-defenses. Curr. Opin. HIV AIDS 1:187-193.
    • (2006) Curr. Opin. HIV AIDS , vol.1 , pp. 187-193
    • Yu, X.F.1
  • 60
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • Yu, Y., Z. Xiao, E. S. Ehrlich, X. Yu, and X. F. Yu. 2004. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev. 18:2867-2872.
    • (2004) Genes Dev , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 61
    • 58049217469 scopus 로고    scopus 로고
    • Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host antiviral proteins
    • Zhang, W., G. Chen, A. M. Niewiadomska, R. Xu, and X. F. Yu. 2008. Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host antiviral proteins. PLoS One 3:e3963.
    • (2008) PLoS One , vol.3
    • Zhang, W.1    Chen, G.2    Niewiadomska, A.M.3    Xu, R.4    Yu, X.F.5
  • 62
    • 47549104961 scopus 로고    scopus 로고
    • Conserved and non-conserved features of HIV-1 and SIVagm Vif mediated suppression of APOBEC3 cytidine deaminases
    • Zhang, W., et al. 2008. Conserved and non-conserved features of HIV-1 and SIVagm Vif mediated suppression of APOBEC3 cytidine deaminases. Cell Microbiol. 10:1662-1675.
    • (2008) Cell Microbiol , vol.10 , pp. 1662-1675
    • Zhang, W.1
  • 63
    • 77953770502 scopus 로고    scopus 로고
    • Vif of feline immunodeficiency virus from domestic cats protects against APOBEC3 restriction factors from many felids
    • Zielonka, J., et al. 2010. Vif of feline immunodeficiency virus from domestic cats protects against APOBEC3 restriction factors from many felids. J. Virol. 84:7312-7324.
    • (2010) J. Virol. , vol.84 , pp. 7312-7324
    • Zielonka, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.