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Volumn 88, Issue 12, 2014, Pages 6944-6958

Cullin4A and cullin4B are interchangeable for HIV Vpr and Vpx Action through the CRL4 ubiquitin ligase complex

Author keywords

[No Author keywords available]

Indexed keywords

CRL4 UBIQUITIN PROTEIN LIGASE COMPLEX; CULLIN; CULLIN4A; CULLIN4B; GLYCOSIDASE; PROTEASOME; PROTEIN SAMHD1; PROTEIN VPX; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; URACIL N GLYCOSYLASE 2; VIRUS PROTEIN; VPR PROTEIN;

EID: 84901377734     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00241-14     Document Type: Article
Times cited : (12)

References (108)
  • 1
    • 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
  • 2
    • 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 WC. 2003. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12:591-601. http://dx.doi.org/10.1016/S1097-2765(03)00353-8.
    • (2003) Mol. Cell , vol.12 , pp. 591-601
    • Stopak, K.1    de Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 3
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy AM, Gaddis NC, Malim MH. 2003. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9:1404-1407. http://dx.doi.org/10.1038/nm945.
    • (2003) Nat. Med. , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 4
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M, Rose KM, Kozak SL, Kabat D. 2003. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9:1398-1403. http://dx.doi.org/10.1038/nm946.
    • (2003) Nat. Med. , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 5
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • Conticello SG, Harris RS, Neuberger MS. 2003. The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr. Biol. 13:2009-2013. http://dx.doi.org/10.1016/j.cub.2003.10.034.
    • (2003) Curr. Biol. , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 6
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabuzda D. 2004. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279: 7792-7798. 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
  • 8
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells
    • Chiu YL, Soros VB, Kreisberg JF, Stopak K, Yonemoto W, Greene WC. 2005. Cellular APOBEC3G restricts HIV-1 infection in resting CD4+ T cells. Nature 435:108-114. http://dx.doi.org/10.1038/nature 03493.
    • (2005) Nature , vol.435 , pp. 108-114
    • Chiu, Y.L.1    Soros, V.B.2    Kreisberg, J.F.3    Stopak, K.4    Yonemoto, W.5    Greene, W.C.6
  • 10
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L. 2003. The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424:94-98. http://dx.doi.org/10.1038/nature01707.
    • (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
  • 11
    • 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. 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
  • 13
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat B, Gers-Huber G, Lehmann M, Zufferey M, Luban J, Piguet V. 2009. HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog. 5:e1000574. http://dx.doi.org/10.1371/journal.ppat.1000574.
    • (2009) PLoS Pathog. , vol.5
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Piguet, V.6
  • 16
    • 67249100279 scopus 로고    scopus 로고
    • Mutation of a single residue renders human tetherin resistant to HIV-1 Vpu-mediated depletion
    • Gupta RK, Hue S, Schaller T, Verschoor E, Pillay D, Towers GJ. 2009. Mutation of a single residue renders human tetherin resistant to HIV-1 Vpu-mediated depletion. PLoS Pathog. 5:e1000443. http://dx.doi.org/10.1371/journal.ppat.1000443.
    • (2009) PLoS Pathog. , vol.5
    • Gupta, R.K.1    Hue, S.2    Schaller, T.3    Verschoor, E.4    Pillay, D.5    Towers, G.J.6
  • 17
    • 41849116366 scopus 로고    scopus 로고
    • The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein
    • Van Damme N, GoffD, Katsura C, Jorgenson RL, Mitchell R, Johnson MC, Stephens EB, Guatelli J. 2008. The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein. Cell Host Microbe 3:245-252. http://dx.doi.org/10.1016/j.chom.2008.03.001.
    • (2008) Cell Host Microbe , vol.3 , pp. 245-252
    • Van Damme, N.1    Goff, D.2    Katsura, C.3    Jorgenson, R.L.4    Mitchell, R.5    Johnson, M.C.6    Stephens, E.B.7    Guatelli, J.8
  • 18
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJ, Zang T, Bieniasz PD. 2008. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 451:425-430. http://dx.doi.org/10.1038/nature06553.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 20
    • 84859482628 scopus 로고    scopus 로고
    • HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1
    • Ahn J, Hao C, Yan J, DeLucia M, Mehrens J, Wang C, Gronenborn AM, Skowronski J. 2012. HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1. J. Biol. Chem. 287:12550-12558. http://dx.doi.org/10.1074/jbc. M112.340711.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12550-12558
    • Ahn, J.1    Hao, C.2    Yan, J.3    DeLucia, M.4    Mehrens, J.5    Wang, C.6    Gronenborn, A.M.7    Skowronski, J.8
  • 24
    • 0035450254 scopus 로고    scopus 로고
    • HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25
    • Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y. 2001. HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25. Virology 287:359-370. http://dx.doi.org/10.1006/viro.2001.1007.
    • (2001) Virology , vol.287 , pp. 359-370
    • Elder, R.T.1    Yu, M.2    Chen, M.3    Zhu, X.4    Yanagida, M.5    Zhao, Y.6
  • 25
    • 0033059945 scopus 로고    scopus 로고
    • Cell cycle-and Vpr-mediated regulation of human immunodeficiency virus type 1 expression in primary and transformed T-cell lines
    • Gummuluru S, Emerman M. 1999. Cell cycle-and Vpr-mediated regulation of human immunodeficiency virus type 1 expression in primary and transformed T-cell lines. J. Virol. 73:5422-5430.
    • (1999) J. Virol. , vol.73 , pp. 5422-5430
    • Gummuluru, S.1    Emerman, M.2
  • 26
    • 0030960059 scopus 로고    scopus 로고
    • Conservation and host specificity of Vpr-mediated cell cycle arrest suggest a fundamental role in primate lentivirus evolution and biology
    • Stivahtis GL, Soares MA, Vodicka MA, Hahn BH, Emerman M. 1997. Conservation and host specificity of Vpr-mediated cell cycle arrest suggest a fundamental role in primate lentivirus evolution and biology. J. Virol. 71:4331-4338.
    • (1997) J. Virol. , vol.71 , pp. 4331-4338
    • Stivahtis, G.L.1    Soares, M.A.2    Vodicka, M.A.3    Hahn, B.H.4    Emerman, M.5
  • 27
    • 0029843983 scopus 로고    scopus 로고
    • Effect of human immunodeficiency virus type 1 protein R (vpr) gene expression on basic cellular function of fission yeast Schizosaccharomyces pombe
    • Zhao Y, Cao J, O'Gorman MR, Yu M, Yogev R. 1996. Effect of human immunodeficiency virus type 1 protein R (vpr) gene expression on basic cellular function of fission yeast Schizosaccharomyces pombe. J. Virol. 70:5821-5826.
    • (1996) J. Virol. , vol.70 , pp. 5821-5826
    • Zhao, Y.1    Cao, J.2    O'Gorman, M.R.3    Yu, M.4    Yogev, R.5
  • 28
    • 0029869861 scopus 로고    scopus 로고
    • Vprinduced cell cycle arrest is conserved among primate lentiviruses
    • Planelles V, Jowett JB, Li QX, Xie Y, Hahn B, Chen IS. 1996. Vprinduced cell cycle arrest is conserved among primate lentiviruses. J. Virol. 70:2516-2524.
    • (1996) J. Virol. , vol.70 , pp. 2516-2524
    • Planelles, V.1    Jowett, J.B.2    Li, Q.X.3    Xie, Y.4    Hahn, B.5    Chen, I.S.6
  • 29
    • 0028853961 scopus 로고
    • Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity
    • He J, Choe S, Walker R, Di Marzio P, Morgan DO, Landau NR. 1995. Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity. J. Virol. 69:6705-6711.
    • (1995) J. Virol. , vol.69 , pp. 6705-6711
    • He, J.1    Choe, S.2    Walker, R.3    Di Marzio, P.4    Morgan, D.O.5    Landau, N.R.6
  • 30
    • 0028824894 scopus 로고
    • Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr
    • Di Marzio P, Choe S, Ebright M, Knoblauch R, Landau NR. 1995. Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr. J. Virol. 69: 7909-7916.
    • (1995) J. Virol. , vol.69 , pp. 7909-7916
    • Di Marzio, P.1    Choe, S.2    Ebright, M.3    Knoblauch, R.4    Landau, N.R.5
  • 31
    • 34848911347 scopus 로고    scopus 로고
    • The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A-containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor
    • Wen X, Duus KM, Friedrich TD, de Noronha CM. 2007. The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A-containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor. J. Biol. Chem. 282:27046-27057. http://dx.doi.org/10.1074/jbc. M703955200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27046-27057
    • Wen, X.1    Duus, K.M.2    Friedrich, T.D.3    de Noronha, C.M.4
  • 32
    • 34648833229 scopus 로고    scopus 로고
    • DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrest
    • Tan L, Ehrlich E, Yu XF. 2007. DDB1 and Cul4A are required for human immunodeficiency virus type 1 Vpr-induced G2 arrest. J. Virol. 81:10822-10830. http://dx.doi.org/10.1128/JVI.01380-07.
    • (2007) J. Virol. , vol.81 , pp. 10822-10830
    • Tan, L.1    Ehrlich, E.2    Yu, X.F.3
  • 33
    • 33846899500 scopus 로고    scopus 로고
    • HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase
    • Le Rouzic E, Belaidouni N, Estrabaud E, Morel M, Rain JC, Transy C, Margottin-Goguet F. 2007. HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase. Cell Cycle 6:182-188. http://dx.doi.org/10.4161/cc.6.2.3732.
    • (2007) Cell Cycle , vol.6 , pp. 182-188
    • Le Rouzic, E.1    Belaidouni, N.2    Estrabaud, E.3    Morel, M.4    Rain, J.C.5    Transy, C.6    Margottin-Goguet, F.7
  • 35
    • 34347376505 scopus 로고    scopus 로고
    • HIV-1 Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system
    • DeHart JL, Zimmerman ES, Ardon O, Monteiro-Filho CM, Arganaraz ER, Planelles V. 2007. HIV-1 Vpr activates the G2 checkpoint through manipulation of the ubiquitin proteasome system. Virol. J. 4:57. http://dx.doi.org/10.1186/1743-422X-4-57.
    • (2007) Virol. J. , vol.4 , pp. 57
    • DeHart, J.L.1    Zimmerman, E.S.2    Ardon, O.3    Monteiro-Filho, C.M.4    Arganaraz, E.R.5    Planelles, V.6
  • 36
    • 34547639932 scopus 로고    scopus 로고
    • HIV-1 Vpr-mediated G2 arrest involves the DDB1-CUL4A(VPRBP) E3 ubiquitin ligase
    • Belzile JP, Duisit G, Rougeau N, Mercier J, Finzi A, Cohen EA. 2007. HIV-1 Vpr-mediated G2 arrest involves the DDB1-CUL4A(VPRBP) E3 ubiquitin ligase. PLoS Pathog. 3:e85. http://dx.doi.org/10.1371/journal.ppat.0030085.
    • (2007) PLoS Pathog. , vol.3
    • Belzile, J.P.1    Duisit, G.2    Rougeau, N.3    Mercier, J.4    Finzi, A.5    Cohen, E.A.6
  • 38
    • 84856159248 scopus 로고    scopus 로고
    • The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover
    • Wen X, Casey Klockow L, Nekorchuk M, SharifiHJ, de Noronha CM. 2012. The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover. PLoS One 7:e30939. http://dx.doi.org/10.1371/journal.pone.0030939.
    • (2012) PLoS One , vol.7
    • Wen, X.1    Casey Klockow, L.2    Nekorchuk, M.3    Sharifi, H.J.4    de Noronha, C.M.5
  • 39
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
    • Schröfelbauer B, Yu Q, Zeitlin SG, Landau NR. 2005. Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J. Virol. 79:10978-10987. http://dx.doi.org/10.1128/JVI.79.17.10978-10987.2005.
    • (2005) J. Virol. , vol.79 , pp. 10978-10987
    • Schröfelbauer, B.1    Yu, Q.2    Zeitlin, S.G.3    Landau, N.R.4
  • 40
    • 78549238925 scopus 로고    scopus 로고
    • HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation
    • Ahn J, Vu T, Novince Z, Guerrero-Santoro J, Rapic-Otrin V, Gronenborn AM. 2010. HIV-1 Vpr loads uracil DNA glycosylase-2 onto DCAF1, a substrate recognition subunit of a cullin 4A-ring E3 ubiquitin ligase for proteasome-dependent degradation. J. Biol. Chem. 285:37333-37341. http://dx.doi.org/10.1074/jbc. M110.133181.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37333-37341
    • Ahn, J.1    Vu, T.2    Novince, Z.3    Guerrero-Santoro, J.4    Rapic-Otrin, V.5    Gronenborn, A.M.6
  • 41
    • 0003124066 scopus 로고    scopus 로고
    • HIV-1 Vpr increases viral expression by manipulation of the cell cycle: a mechanism for selection of Vpr in vivo
    • Goh WC, Rogel ME, Kinsey CM, Michael SF, Fultz PN, Nowak MA, Hahn BH, Emerman M. 1998. HIV-1 Vpr increases viral expression by manipulation of the cell cycle: a mechanism for selection of Vpr in vivo. Nat. Med. 4:65-71. http://dx.doi.org/10.1038/nm0198-065.
    • (1998) Nat. Med. , vol.4 , pp. 65-71
    • Goh, W.C.1    Rogel, M.E.2    Kinsey, C.M.3    Michael, S.F.4    Fultz, P.N.5    Nowak, M.A.6    Hahn, B.H.7    Emerman, M.8
  • 42
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers S, Li T, Yi X, MacCoss MJ, Moon RT, Zheng N. 2006. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443:590-593. http://dx.doi.org/10.1038/nature 05175.
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    MacCoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 43
    • 33751112293 scopus 로고    scopus 로고
    • DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases
    • He YJ, McCall CM, Hu J, Zeng Y, Xiong Y. 2006. DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases. Genes Dev. 20:2949-2954. http://dx.doi.org/10.1101/gad.1483206.
    • (2006) Genes Dev. , vol.20 , pp. 2949-2954
    • He, Y.J.1    McCall, C.M.2    Hu, J.3    Zeng, Y.4    Xiong, Y.5
  • 44
    • 33747831132 scopus 로고    scopus 로고
    • L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage
    • Higa LA, Banks D, Wu M, Kobayashi R, Sun H, Zhang H. 2006. L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage. Cell Cycle 5:1675-1680. http://dx.doi.org/10.4161/cc.5.15.3149.
    • (2006) Cell Cycle , vol.5 , pp. 1675-1680
    • Higa, L.A.1    Banks, D.2    Wu, M.3    Kobayashi, R.4    Sun, H.5    Zhang, H.6
  • 45
    • 33747873322 scopus 로고    scopus 로고
    • A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1
    • Jin J, Arias EE, Chen J, Harper JW, Walter JC. 2006. A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. Mol. Cell 23:709-721. http://dx.doi.org/10.1016/j.molcel.2006.08.010.
    • (2006) Mol. Cell , vol.23 , pp. 709-721
    • Jin, J.1    Arias, E.E.2    Chen, J.3    Harper, J.W.4    Walter, J.C.5
  • 46
    • 79951913687 scopus 로고    scopus 로고
    • The Cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1
    • Ahn J, Novince Z, Concel J, Byeon CH, Makhov AM, Byeon IJ, Zhang P, Gronenborn AM. 2011. The Cullin-RING E3 ubiquitin ligase CRL4-DCAF1 complex dimerizes via a short helical region in DCAF1. Biochemistry 50:1359-1367. http://dx.doi.org/10.1021/bi101749s.
    • (2011) Biochemistry , vol.50 , pp. 1359-1367
    • Ahn, J.1    Novince, Z.2    Concel, J.3    Byeon, C.H.4    Makhov, A.M.5    Byeon, I.J.6    Zhang, P.7    Gronenborn, A.M.8
  • 47
    • 77953356718 scopus 로고    scopus 로고
    • The functions of the HIV1 protein Vpr and its action through the DCAF1.DDB1.Cullin4 ubiquitin ligase
    • Casey L, Wen X, de Noronha CM. 2010. The functions of the HIV1 protein Vpr and its action through the DCAF1.DDB1.Cullin4 ubiquitin ligase. Cytokine 51:1-9. http://dx.doi.org/10.1016/j.cyto.2010.02.018.
    • (2010) Cytokine , vol.51 , pp. 1-9
    • Casey, L.1    Wen, X.2    de Noronha, C.M.3
  • 49
    • 44449107162 scopus 로고    scopus 로고
    • Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection
    • Srivastava S, Swanson SK, Manel N, Florens L, Washburn MP, Skowronski J. 2008. Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection. PLoS Pathog. 4:e1000059. http://dx.doi.org/10.1371/journal.ppat.1000059.
    • (2008) PLoS Pathog. , vol.4
    • Srivastava, S.1    Swanson, S.K.2    Manel, N.3    Florens, L.4    Washburn, M.P.5    Skowronski, J.6
  • 50
    • 52049095759 scopus 로고    scopus 로고
    • Assembly with the Cul4A-DDB1-DCAF1 ubiquitin ligase protects HIV-1 Vpr from proteasomal degradation
    • Le Rouzic E, Morel M, Ayinde D, Belaidouni N, Letienne J, Transy C, Margottin-Goguet F. 2008. Assembly with the Cul4A-DDB1-DCAF1 ubiquitin ligase protects HIV-1 Vpr from proteasomal degradation. J. Biol. Chem. 283:21686-21692. http://dx.doi.org/10.1074/jbc. M710298200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 21686-21692
    • Le Rouzic, E.1    Morel, M.2    Ayinde, D.3    Belaidouni, N.4    Letienne, J.5    Transy, C.6    Margottin-Goguet, F.7
  • 51
    • 70450225328 scopus 로고    scopus 로고
    • Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression
    • Zou Y, Mi J, Cui J, Lu D, Zhang X, Guo C, Gao G, Liu Q, Chen B, Shao C, Gong Y. 2009. Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression. J. Biol. Chem. 284:33320-33332. http://dx.doi.org/10.1074/jbc. M109.050427.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33320-33332
    • Zou, Y.1    Mi, J.2    Cui, J.3    Lu, D.4    Zhang, X.5    Guo, C.6    Gao, G.7    Liu, Q.8    Chen, B.9    Shao, C.10    Gong, Y.11
  • 54
    • 75149125167 scopus 로고    scopus 로고
    • Deletion of the CUL4B gene in a boy with mental retardation, minor facial anomalies, short stature, hypogonadism, and ataxia
    • Isidor B, Pichon O, Baron S, David A, Le Caignec C. 2010. Deletion of the CUL4B gene in a boy with mental retardation, minor facial anomalies, short stature, hypogonadism, and ataxia. Am. J. Med. Genet. A152A: 175-180. http://dx.doi.org/10.1002/ajmg.a.33152.
    • (2010) Am. J. Med. Genet. , vol.A152A , pp. 175-180
    • Isidor, B.1    Pichon, O.2    Baron, S.3    David, A.4    Le Caignec, C.5
  • 57
    • 79960897683 scopus 로고    scopus 로고
    • X-linked mental retardation gene CUL4B targets ubiquitylation of H3K4 methyltransferase component WDR5 and regulates neuronal gene expression
    • Nakagawa T, Xiong Y. 2011. X-linked mental retardation gene CUL4B targets ubiquitylation of H3K4 methyltransferase component WDR5 and regulates neuronal gene expression. Mol. Cell 43:381-391. http://dx.doi.org/10.1016/j.molcel.2011.05.033.
    • (2011) Mol. Cell , vol.43 , pp. 381-391
    • Nakagawa, T.1    Xiong, Y.2
  • 59
    • 0036614698 scopus 로고    scopus 로고
    • TFDP1, CUL4A, and CDC16 identified as targets for amplification at 13q34 in hepatocellular carcinomas
    • Yasui K, Arii S, Zhao C, Imoto I, Ueda M, Nagai H, Emi M, Inazawa J. 2002. TFDP1, CUL4A, and CDC16 identified as targets for amplification at 13q34 in hepatocellular carcinomas. Hepatology 35:1476-1484. http://dx.doi.org/10.1053/jhep.2002.33683.
    • (2002) Hepatology , vol.35 , pp. 1476-1484
    • Yasui, K.1    Arii, S.2    Zhao, C.3    Imoto, I.4    Ueda, M.5    Nagai, H.6    Emi, M.7    Inazawa, J.8
  • 61
    • 65649105790 scopus 로고    scopus 로고
    • CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis
    • Liu L, Lee S, Zhang J, Peters SB, Hannah J, Zhang Y, Yin Y, KoffA, Ma L, Zhou P. 2009. CUL4A abrogation augments DNA damage response and protection against skin carcinogenesis. Mol. Cell 34:451-460. http://dx.doi.org/10.1016/j.molcel.2009.04.020.
    • (2009) Mol. Cell , vol.34 , pp. 451-460
    • Liu, L.1    Lee, S.2    Zhang, J.3    Peters, S.B.4    Hannah, J.5    Zhang, Y.6    Yin, Y.7    Koff, A.8    Ma, L.9    Zhou, P.10
  • 63
    • 0037830710 scopus 로고    scopus 로고
    • Activation of the ATR-mediated DNA damage response by the HIV-1 viral protein R
    • Roshal M, Kim B, Zhu Y, Nghiem P, Planelles V. 2003. Activation of the ATR-mediated DNA damage response by the HIV-1 viral protein R. J. Biol. Chem. 278:25879-25886. http://dx.doi.org/10.1074/jbc. M30394 8200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25879-25886
    • Roshal, M.1    Kim, B.2    Zhu, Y.3    Nghiem, P.4    Planelles, V.5
  • 65
    • 0035798131 scopus 로고    scopus 로고
    • Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr
    • de Noronha CM, Sherman MP, Lin HW, Cavrois MV, Moir RD, Goldman RD, Greene WC. 2001. Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr. Science 294: 1105-1108. http://dx.doi.org/10.1126/science.1063957.
    • (2001) Science , vol.294 , pp. 1105-1108
    • de Noronha, C.M.1    Sherman, M.P.2    Lin, H.W.3    Cavrois, M.V.4    Moir, R.D.5    Goldman, R.D.6    Greene, W.C.7
  • 66
    • 0034640884 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization blocks the elongation phase of DNA replication
    • Moir RD, Spann TP, Herrmann H, Goldman RD. 2000. Disruption of nuclear lamin organization blocks the elongation phase of DNA replication. J. Cell Biol. 149:1179-1192. http://dx.doi.org/10.1083/jcb.149.6.1179.
    • (2000) J. Cell Biol. , vol.149 , pp. 1179-1192
    • Moir, R.D.1    Spann, T.P.2    Herrmann, H.3    Goldman, R.D.4
  • 67
    • 84867629398 scopus 로고    scopus 로고
    • A novel DCAF1-binding motif required for Vpx-mediated degradation of nuclear SAMHD1 and Vpr-induced G2 arrest
    • Wei W, Guo H, Han X, Liu X, Zhou X, Zhang W, Yu XF. 2012. A novel DCAF1-binding motif required for Vpx-mediated degradation of nuclear SAMHD1 and Vpr-induced G2 arrest. Cell. Microbiol. 14:1745-1756. http://dx.doi.org/10.1111/j.1462-5822.2012.01835.x.
    • (2012) Cell. Microbiol. , vol.14 , pp. 1745-1756
    • Wei, W.1    Guo, H.2    Han, X.3    Liu, X.4    Zhou, X.5    Zhang, W.6    Yu, X.F.7
  • 70
    • 0344766077 scopus 로고    scopus 로고
    • Primary human immunodeficiency virus type 2 (HIV-2) isolates, like HIV-1 isolates, frequently use CCR5 but show promiscuity in coreceptor usage
    • Morner A, Bjorndal A, Albert J, Kewalramani VN, Littman DR, Inoue R, Thorstensson R, Fenyo EM, Bjorling E. 1999. Primary human immunodeficiency virus type 2 (HIV-2) isolates, like HIV-1 isolates, frequently use CCR5 but show promiscuity in coreceptor usage. J. Virol. 73:2343-2349.
    • (1999) J. Virol. , vol.73 , pp. 2343-2349
    • Morner, A.1    Bjorndal, A.2    Albert, J.3    Kewalramani, V.N.4    Littman, D.R.5    Inoue, R.6    Thorstensson, R.7    Fenyo, E.M.8    Bjorling, E.9
  • 71
    • 0024380087 scopus 로고
    • Rapid detec-tion of octamer binding proteins with 'mini-extracts', prepared from a small number of cells
    • Schreiber E, Matthias P, Muller MM, Schaffner W. 1989. Rapid detec-tion of octamer binding proteins with 'mini-extracts', prepared from a small number of cells. Nucleic Acids Res. 17:6419. http://dx.doi.org/10.1093/nar/17.15.6419.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 72
    • 0026672676 scopus 로고
    • Macrophagetropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: definition of critical amino acids involved in cell tropism
    • Chesebro B, Wehrly K, Nishio J, Perryman S. 1992. Macrophagetropic human immunodeficiency virus isolates from different patients exhibit unusual V3 envelope sequence homogeneity in comparison with T-cell-tropic isolates: definition of critical amino acids involved in cell tropism. J. Virol. 66:6547-6554.
    • (1992) J. Virol. , vol.66 , pp. 6547-6554
    • Chesebro, B.1    Wehrly, K.2    Nishio, J.3    Perryman, S.4
  • 73
    • 0028290899 scopus 로고
    • HIV-2 viral protein X association with the GAG p27 capsid protein
    • Horton R, Spearman P, Ratner L. 1994. HIV-2 viral protein X association with the GAG p27 capsid protein. Virology 199:453-457. http://dx.doi.org/10.1006/viro.1994.1144.
    • (1994) Virology , vol.199 , pp. 453-457
    • Horton, R.1    Spearman, P.2    Ratner, L.3
  • 74
    • 0029872245 scopus 로고    scopus 로고
    • High-efficiency gene transfer into CD34+ cells with a human immunodeficiency virus type 1-based retroviral vector pseudotyped with vesicular stomatitis virus envelope glycoprotein G
    • Akkina RK, Walton RM, Chen ML, Li QX, Planelles V, Chen IS. 1996. High-efficiency gene transfer into CD34+ cells with a human immunodeficiency virus type 1-based retroviral vector pseudotyped with vesicular stomatitis virus envelope glycoprotein G. J. Virol. 70:2581-2585.
    • (1996) J. Virol. , vol.70 , pp. 2581-2585
    • Akkina, R.K.1    Walton, R.M.2    Chen, M.L.3    Li, Q.X.4    Planelles, V.5    Chen, I.S.6
  • 75
    • 0028033251 scopus 로고
    • CD4 expressing human 293 cells as a tool for studies in HIV-1 replication: the efficiency of translational frameshifting is not altered by HIV-1 infection
    • Reil H, Hoxter M, Moosmayer D, Pauli G, Hauser H. 1994. CD4 expressing human 293 cells as a tool for studies in HIV-1 replication: the efficiency of translational frameshifting is not altered by HIV-1 infection. Virology 205:371-375. http://dx.doi.org/10.1006/viro.1994.1655.
    • (1994) Virology , vol.205 , pp. 371-375
    • Reil, H.1    Hoxter, M.2    Moosmayer, D.3    Pauli, G.4    Hauser, H.5
  • 76
    • 0028297360 scopus 로고
    • Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: mutational analysis of a primary HIV-1 isolate
    • Balliet JW, Kolson DL, Eiger G, Kim FM, McGann KA, Srinivasan A, Collman R. 1994. Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: mutational analysis of a primary HIV-1 isolate. Virology 200:623-631. http://dx.doi.org/10.1006/viro.1994.1225.
    • (1994) Virology , vol.200 , pp. 623-631
    • Balliet, J.W.1    Kolson, D.L.2    Eiger, G.3    Kim, F.M.4    McGann, K.A.5    Srinivasan, A.6    Collman, R.7
  • 77
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes
    • Connor RI, Chen BK, Choe S, Landau NR. 1995. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology 206:935-944. http://dx.doi.org/10.1006/viro.1995.1016.
    • (1995) Virology , vol.206 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 79
    • 0030009151 scopus 로고    scopus 로고
    • Protein stability influences human immunodeficiency virus type 2 Vpr virion incorporation and cell cycle effect
    • Kewalramani VN, Park CS, Gallombardo PA, Emerman M. 1996. Protein stability influences human immunodeficiency virus type 2 Vpr virion incorporation and cell cycle effect. Virology 218:326-334. http://dx.doi.org/10.1006/viro.1996.0201.
    • (1996) Virology , vol.218 , pp. 326-334
    • Kewalramani, V.N.1    Park, C.S.2    Gallombardo, P.A.3    Emerman, M.4
  • 80
    • 0030958826 scopus 로고    scopus 로고
    • Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest
    • Selig L, Benichou S, Rogel ME, Wu LI, Vodicka MA, Sire J, Benarous R, Emerman M. 1997. Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest. J. Virol. 71:4842-4846.
    • (1997) J. Virol. , vol.71 , pp. 4842-4846
    • Selig, L.1    Benichou, S.2    Rogel, M.E.3    Wu, L.I.4    Vodicka, M.A.5    Sire, J.6    Benarous, R.7    Emerman, M.8
  • 81
    • 70349283033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr modulates cellular expression of UNG2 via a negative transcriptional effect
    • Langevin C, Maidou-Peindara P, Aas PA, Jacquot G, Otterlei M, Slupphaug G, Benichou S. 2009. Human immunodeficiency virus type 1 Vpr modulates cellular expression of UNG2 via a negative transcriptional effect. J. Virol. 83:10256-10263. http://dx.doi.org/10.1128/JVI.02654-08.
    • (2009) J. Virol. , vol.83 , pp. 10256-10263
    • Langevin, C.1    Maidou-Peindara, P.2    Aas, P.A.3    Jacquot, G.4    Otterlei, M.5    Slupphaug, G.6    Benichou, S.7
  • 82
    • 13944277344 scopus 로고    scopus 로고
    • HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle
    • Priet S, Gros N, Navarro JM, Boretto J, Canard B, Querat G, Sire J. 2005. HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle. Mol. Cell 17:479-490. http://dx.doi.org/10.1016/j.molcel.2005.01.016.
    • (2005) Mol. Cell , vol.17 , pp. 479-490
    • Priet, S.1    Gros, N.2    Navarro, J.M.3    Boretto, J.4    Canard, B.5    Querat, G.6    Sire, J.7
  • 83
    • 77953314025 scopus 로고    scopus 로고
    • X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells
    • Jones KL, Roche M, Gantier MP, Begum NA, Honjo T, Caradonna S, Williams BR, Mak J. 2010. X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells. J. Biol. Chem. 285:18603-18614. http://dx.doi.org/10.1074/jbc. M109.090126.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18603-18614
    • Jones, K.L.1    Roche, M.2    Gantier, M.P.3    Begum, N.A.4    Honjo, T.5    Caradonna, S.6    Williams, B.R.7    Mak, J.8
  • 86
    • 30344440118 scopus 로고    scopus 로고
    • Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G
    • Kaiser SM, Emerman M. 2006. Uracil DNA glycosylase is dispensable for human immunodeficiency virus type 1 replication and does not contribute to the antiviral effects of the cytidine deaminase Apobec3G. J. Virol. 80:875-882. http://dx.doi.org/10.1128/JVI.80.2.875-882.2006.
    • (2006) J. Virol. , vol.80 , pp. 875-882
    • Kaiser, S.M.1    Emerman, M.2
  • 87
    • 0032486488 scopus 로고    scopus 로고
    • Differential association of uracil DNA glycosylase with SIVSM Vpr and Vpx proteins
    • Sleigh R, Sharkey M, Newman MA, Hahn B, Stevenson M. 1998. Differential association of uracil DNA glycosylase with SIVSM Vpr and Vpx proteins. Virology 245:338-343. http://dx.doi.org/10.1006/viro.1998.9159.
    • (1998) Virology , vol.245 , pp. 338-343
    • Sleigh, R.1    Sharkey, M.2    Newman, M.A.3    Hahn, B.4    Stevenson, M.5
  • 88
    • 0032478787 scopus 로고    scopus 로고
    • Diversity of HIV-1 Vpr interactions involves usage of the WXXF motif of host cell proteins
    • BouHamdan M, Xue Y, Baudat Y, Hu B, Sire J, Pomerantz RJ, Duan LX. 1998. Diversity of HIV-1 Vpr interactions involves usage of the WXXF motif of host cell proteins. J. Biol. Chem. 273:8009-8016. http://dx.doi.org/10.1074/jbc.273.14.8009.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8009-8016
    • BouHamdan, M.1    Xue, Y.2    Baudat, Y.3    Hu, B.4    Sire, J.5    Pomerantz, R.J.6    Duan, L.X.7
  • 90
    • 34247187942 scopus 로고    scopus 로고
    • HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1
    • Schrofelbauer B, Hakata Y, Landau NR. 2007. HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1. Proc. Natl. Acad. Sci. U. S. A. 104:4130-4135. http://dx.doi.org/10.1073/pnas.0610167104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 4130-4135
    • Schrofelbauer, B.1    Hakata, Y.2    Landau, N.R.3
  • 92
    • 28944448413 scopus 로고    scopus 로고
    • Identification of substrates for F-box proteins
    • Jin J, Ang XL, Shirogane T, Wade Harper J. 2005. Identification of substrates for F-box proteins. Methods Enzymol. 399:287-309. http://dx.doi.org/10.1016/S0076-6879(05)99020-4.
    • (2005) Methods Enzymol. , vol.399 , pp. 287-309
    • Jin, J.1    Ang, X.L.2    Shirogane, T.3    Wade Harper, J.4
  • 93
    • 84871412468 scopus 로고    scopus 로고
    • SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+T-lymphocytes cannot be upregulated by interferons
    • St Gelais C, de Silva S, Amie SM, Coleman CM, Hoy H, Hollenbaugh JA, Kim B, Wu L. 2012. SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+T-lymphocytes cannot be upregulated by interferons. Retrovirology 9:105. http://dx.doi.org/10.1186/1742-4690-9-105.
    • (2012) Retrovirology , vol.9 , pp. 105
    • St Gelais, C.1    de Silva, S.2    Amie, S.M.3    Coleman, C.M.4    Hoy, H.5    Hollenbaugh, J.A.6    Kim, B.7    Wu, L.8
  • 94
    • 84886881354 scopus 로고    scopus 로고
    • Inhibition of CUL4A neddylation causes a reversible block to SAMHD1-mediated restriction of HIV-1
    • Hofmann H, Norton TD, Schultz ML, Polsky SB, Sunseri N, Landau NR. 2013. Inhibition of CUL4A neddylation causes a reversible block to SAMHD1-mediated restriction of HIV-1. J. Virol. 87:11741-11750. http://dx.doi.org/10.1128/JVI.02002-13.
    • (2013) J. Virol. , vol.87 , pp. 11741-11750
    • Hofmann, H.1    Norton, T.D.2    Schultz, M.L.3    Polsky, S.B.4    Sunseri, N.5    Landau, N.R.6
  • 95
    • 84890890219 scopus 로고    scopus 로고
    • A first-in-class NAE inhibitor, MLN4924, blocks lentiviral infection in myeloid cells by disrupting neddylation-dependent Vpxmediated SAMHD1 degradation
    • Wei W, Guo H, Liu X, Zhang H, Qian L, Luo K, Markham RB, Yu XF. 2014. A first-in-class NAE inhibitor, MLN4924, blocks lentiviral infection in myeloid cells by disrupting neddylation-dependent Vpxmediated SAMHD1 degradation. J. Virol. 88:745-751. http://dx.doi.org/10.1128/JVI.02568-13.
    • (2014) J. Virol. , vol.88 , pp. 745-751
    • Wei, W.1    Guo, H.2    Liu, X.3    Zhang, H.4    Qian, L.5    Luo, K.6    Markham, R.B.7    Yu, X.F.8
  • 97
    • 34547101263 scopus 로고    scopus 로고
    • Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracilDNAglycosylases TDG and UNG2
    • Hardeland U, Kunz C, Focke F, Szadkowski M, Schar P. 2007. Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracilDNAglycosylases TDG and UNG2. Nucleic Acids Res. 35:3859-3867. http://dx.doi.org/10.1093/nar/gkm337.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3859-3867
    • Hardeland, U.1    Kunz, C.2    Focke, F.3    Szadkowski, M.4    Schar, P.5
  • 98
    • 81255184464 scopus 로고    scopus 로고
    • Modulation of NKG2D-mediated cytotoxic functions of natural killer cells by viral protein R (Vpr) from HIV-1 primary isolates
    • Pham TN, Richard J, Gerard FC, Power C, Cohen EA. 2011. Modulation of NKG2D-mediated cytotoxic functions of natural killer cells by viral protein R (Vpr) from HIV-1 primary isolates. J. Virol. 85:12254-12261. http://dx.doi.org/10.1128/JVI.05835-11.
    • (2011) J. Virol. , vol.85 , pp. 12254-12261
    • Pham, T.N.1    Richard, J.2    Gerard, F.C.3    Power, C.4    Cohen, E.A.5
  • 99
    • 77949903887 scopus 로고    scopus 로고
    • HIV-1 Vpr up-regulates expression of ligands for the activating NKG2D receptor and promotes NK cell-mediated killing
    • Richard J, Sindhu S, Pham TN, Belzile JP, Cohen EA. 2010. HIV-1 Vpr up-regulates expression of ligands for the activating NKG2D receptor and promotes NK cell-mediated killing. Blood 115:1354-1363. http://dx.doi.org/10.1182/blood-2009-08-237370.
    • (2010) Blood , vol.115 , pp. 1354-1363
    • Richard, J.1    Sindhu, S.2    Pham, T.N.3    Belzile, J.P.4    Cohen, E.A.5
  • 100
    • 73349122322 scopus 로고    scopus 로고
    • HIV-1 Vpr triggers natural killer cell-mediated lysis of infected cells through activation of the ATRmediated DNA damage response
    • Ward J, Davis Z, DeHart J, Zimmerman E, Bosque A, Brunetta E, Mavilio D, Planelles V, Barker E. 2009. HIV-1 Vpr triggers natural killer cell-mediated lysis of infected cells through activation of the ATRmediated DNA damage response. PLoS Pathog. 5:e1000613. http://dx.doi.org/10.1371/journal.ppat.1000613.
    • (2009) PLoS Pathog. , vol.5
    • Ward, J.1    Davis, Z.2    DeHart, J.3    Zimmerman, E.4    Bosque, A.5    Brunetta, E.6    Mavilio, D.7    Planelles, V.8    Barker, E.9
  • 102
    • 84882814047 scopus 로고    scopus 로고
    • The HIV-1 protein Vpr targets the endoribonuclease Dicer for proteasomal degradation to boost macrophage infection
    • Casey Klockow L, SharifiHJ, Wen X, Flagg M, Furuya AK, Nekorchuk M, de Noronha CM. 2013. The HIV-1 protein Vpr targets the endoribonuclease Dicer for proteasomal degradation to boost macrophage infection. Virology 444:191-202. http://dx.doi.org/10.1016/j.virol.2013.06.010.
    • (2013) Virology , vol.444 , pp. 191-202
    • Casey Klockow, L.1    Sharifi, H.J.2    Wen, X.3    Flagg, M.4    Furuya, A.K.5    Nekorchuk, M.6    de Noronha, C.M.7
  • 103
    • 84880063164 scopus 로고    scopus 로고
    • Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradation
    • Guo H, Wei W, Wei Z, Liu X, Evans SL, Yang W, Wang H, Guo Y, Zhao K, Zhou JY, Yu XF. 2013. Identification of critical regions in human SAMHD1 required for nuclear localization and Vpx-mediated degradation. PLoS One 8:e66201. http://dx.doi.org/10.1371/journal.pone.0066201.
    • (2013) PLoS One , vol.8
    • Guo, H.1    Wei, W.2    Wei, Z.3    Liu, X.4    Evans, S.L.5    Yang, W.6    Wang, H.7    Guo, Y.8    Zhao, K.9    Zhou, J.Y.10    Yu, X.F.11
  • 106
    • 79959353247 scopus 로고    scopus 로고
    • Vpx rescues HIV-1 transduction of dendritic cells from the antiviral state established by type 1 interferon
    • Pertel T, Reinhard C, Luban J. 2011. Vpx rescues HIV-1 transduction of dendritic cells from the antiviral state established by type 1 interferon. Retrovirology 8:49. http://dx.doi.org/10.1186/1742-4690-8-49.
    • (2011) Retrovirology , vol.8 , pp. 49
    • Pertel, T.1    Reinhard, C.2    Luban, J.3
  • 107
    • 84893185403 scopus 로고    scopus 로고
    • Vpx rescue of HIV-1 from the antiviral state in mature dendritic cells is independent of the intracellular deoxynucleotide concentration
    • Reinhard C, Bottinelli D, Kim B, Luban J. 2014. Vpx rescue of HIV-1 from the antiviral state in mature dendritic cells is independent of the intracellular deoxynucleotide concentration. Retrovirology 11:12. http://dx.doi.org/10.1186/1742-4690-11-12.
    • (2014) Retrovirology , vol.11 , pp. 12
    • Reinhard, C.1    Bottinelli, D.2    Kim, B.3    Luban, J.4
  • 108
    • 78649974984 scopus 로고    scopus 로고
    • Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics
    • Bennett EJ, Rush J, Gygi SP, Harper JW. 2010. Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 143:951-965. http://dx.doi.org/10.1016/j.cell.2010.11.017.
    • (2010) Cell , vol.143 , pp. 951-965
    • Bennett, E.J.1    Rush, J.2    Gygi, S.P.3    Harper, J.W.4


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