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Volumn 195, Issue , 2015, Pages 25-34

The HIV-1 accessory protein Vpr induces the degradation of the anti-HIV-1 agent APOBEC3G through a VprBP-mediated proteasomal pathway

Author keywords

APOBEC3G (A3G); Degradation; Encapsidation; HIV 1; Vpr; VprBP

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; PROTEASOME; VPR PROTEIN; APOBEC3G PROTEIN, HUMAN; CARRIER PROTEIN; CYTIDINE DEAMINASE; PROTEIN BINDING; VPR PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; VPRBP PROTEIN, HUMAN;

EID: 84919389946     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2014.08.021     Document Type: Article
Times cited : (21)

References (60)
  • 1
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • Adachi A., Gendelman H.E., Koenig S., Folks T., Willey R., Rabson A., Martin M.A. Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone. J. Virol. 1986, 59(2):284-291.
    • (1986) J. Virol. , vol.59 , Issue.2 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 2
    • 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 A.M. 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. 2010, 285(48):37333-37341.
    • (2010) J. Biol. Chem. , vol.285 , Issue.48 , pp. 37333-37341
    • Ahn, J.1    Vu, T.2    Novince, Z.3    Guerrero-Santoro, J.4    Rapic-Otrin, V.5    Gronenborn, A.M.6
  • 3
    • 84861369218 scopus 로고    scopus 로고
    • HIV-1, ubiquitin and ubiquitin-like proteins: the dialectic interactions of a virus with a sophisticated network of post-translational modifications
    • Biard-Piechaczyk M., Borel S., Espert L., de Bettignies G., Coux O. HIV-1, ubiquitin and ubiquitin-like proteins: the dialectic interactions of a virus with a sophisticated network of post-translational modifications. Biol. Cell 2012, 104(3):165-187.
    • (2012) Biol. Cell , vol.104 , Issue.3 , pp. 165-187
    • Biard-Piechaczyk, M.1    Borel, S.2    Espert, L.3    de Bettignies, G.4    Coux, O.5
  • 4
    • 37749032764 scopus 로고    scopus 로고
    • Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type I Vpu protein in the endoplasmic reticulum
    • Binette J., Dube M., Mercier J., Halawani D., Latterich M., Cohen E.A. Requirements for the selective degradation of CD4 receptor molecules by the human immunodeficiency virus type I Vpu protein in the endoplasmic reticulum. Retrovirology 2007, 4:75.
    • (2007) Retrovirology , vol.4 , pp. 75
    • Binette, J.1    Dube, M.2    Mercier, J.3    Halawani, D.4    Latterich, M.5    Cohen, E.A.6
  • 5
  • 6
    • 84863099257 scopus 로고    scopus 로고
    • (-)-Epigallocatechin-3-gallate inhibits the replication cycle of hepatitis C virus
    • Chen C., Qiu H., Gong J., Liu Q., Xiao H., Chen X.W., Sun B.L., Yang R.G. (-)-Epigallocatechin-3-gallate inhibits the replication cycle of hepatitis C virus. Arch. Virol. 2012, 157(7):1301-1312.
    • (2012) Arch. Virol. , vol.157 , Issue.7 , pp. 1301-1312
    • Chen, C.1    Qiu, H.2    Gong, J.3    Liu, Q.4    Xiao, H.5    Chen, X.W.6    Sun, B.L.7    Yang, R.G.8
  • 7
    • 33746190700 scopus 로고    scopus 로고
    • Alpha interferon potently enhances the anti-human immunodeficiency virus type 1 activity of APOBEC3G in resting primary CD4T cells
    • Chen K., Huang J., Zhang C., Huang S., Nunnari G., Wang F.X., Tong X., Gao L., Nikisher K., Zhang H. Alpha interferon potently enhances the anti-human immunodeficiency virus type 1 activity of APOBEC3G in resting primary CD4T cells. J. Virol. 2006, 80(15):7645-7657.
    • (2006) J. Virol. , vol.80 , Issue.15 , pp. 7645-7657
    • Chen, K.1    Huang, J.2    Zhang, C.3    Huang, S.4    Nunnari, G.5    Wang, F.X.6    Tong, X.7    Gao, L.8    Nikisher, K.9    Zhang, H.10
  • 8
    • 3142651460 scopus 로고    scopus 로고
    • Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages
    • Chen R.X., Le Rouzic E., Kearney J.A., Mansky L.M., Benichou S. Vpr-mediated incorporation of UNG2 into HIV-1 particles is required to modulate the virus mutation rate and for replication in macrophages. J. Biol. Chem. 2004, 279(27):28419-28425.
    • (2004) J. Biol. Chem. , vol.279 , Issue.27 , pp. 28419-28425
    • Chen, R.X.1    Le Rouzic, E.2    Kearney, J.A.3    Mansky, L.M.4    Benichou, S.5
  • 9
    • 42649120310 scopus 로고    scopus 로고
    • The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements
    • Chiu Y.L., Greene W.C. The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu. Rev. Immunol. 2008, 26:317-353.
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 317-353
    • Chiu, Y.L.1    Greene, W.C.2
  • 10
    • 18344372631 scopus 로고    scopus 로고
    • Cellular APOBEC3G restricts HIV-1 infection in resting CD4(+) T cells (Retracted Article. See vol. 466, pg 276, 2010)
    • Chiu Y.L., Soros V.B., Kreisberg J.F., Stopak K., Yonemoto W., Greene W.C. Cellular APOBEC3G restricts HIV-1 infection in resting CD4(+) T cells (Retracted Article. See vol. 466, pg 276, 2010). Nature 2005, 435(7038):108-114.
    • (2005) Nature , vol.435 , Issue.7038 , 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
  • 11
    • 38349136841 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 vpr links proteasomal degradation and checkpoint activation
    • DeHart J.L., Planelles V. Human immunodeficiency virus type 1 vpr links proteasomal degradation and checkpoint activation. J. Virol. 2008, 82(3):1066-1072.
    • (2008) J. Virol. , vol.82 , Issue.3 , pp. 1066-1072
    • DeHart, J.L.1    Planelles, V.2
  • 13
    • 84874759842 scopus 로고    scopus 로고
    • HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G
    • Feng Y.Q., Love R.P., Chelico L. HIV-1 viral infectivity factor (Vif) alters processive single-stranded DNA scanning of the retroviral restriction factor APOBEC3G. J. Biol. Chem. 2013, 288(9):6083-6094.
    • (2013) J. Biol. Chem. , vol.288 , Issue.9 , pp. 6083-6094
    • Feng, Y.Q.1    Love, R.P.2    Chelico, L.3
  • 14
    • 48949118733 scopus 로고    scopus 로고
    • HIV-1 Vif, APOBEC, and intrinsic immunity
    • Goila-Gaur R., Strebel K. HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 2008, 5:51.
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 15
    • 84857854783 scopus 로고    scopus 로고
    • Recruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1
    • Guenzel C.A., Herate C., Le Rouzic E., Maidou-Peindara P., Sadler H.A., Rouyez M.C., Mansky L.M., Benichou S. Recruitment of the nuclear form of uracil DNA glycosylase into virus particles participates in the full infectivity of HIV-1. J. Virol. 2012, 86(5):2533-2544.
    • (2012) J. Virol. , vol.86 , Issue.5 , pp. 2533-2544
    • Guenzel, C.A.1    Herate, C.2    Le Rouzic, E.3    Maidou-Peindara, P.4    Sadler, H.A.5    Rouyez, M.C.6    Mansky, L.M.7    Benichou, S.8
  • 19
    • 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 K.L., Roche M., Gantier M.P., Begum N.A., Honjo T., Caradonna S., Williams B.R.G., Mak J. X4 and R5 HIV-1 have distinct post-entry requirements for uracil DNA glycosylase during infection of primary cells. J. Biol. Chem. 2010, 285(24):18603-18614.
    • (2010) J. Biol. Chem. , vol.285 , Issue.24 , 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.G.7    Mak, J.8
  • 20
    • 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 S.M., Emerman M. 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. 2006, 80(2):875-882.
    • (2006) J. Virol. , vol.80 , Issue.2 , pp. 875-882
    • Kaiser, S.M.1    Emerman, M.2
  • 22
    • 84882814047 scopus 로고    scopus 로고
    • The HIV-1 protein Vpr targets the endoribonuclease Dicer for proteasomal degradation to boost macrophage infection
    • Klockow L.C., Sharifi H.J., Wen X.Y., Flagg M., Furuya A.K.M., Nekorchuk M., de Noronha C.M.C. The HIV-1 protein Vpr targets the endoribonuclease Dicer for proteasomal degradation to boost macrophage infection. Virology 2013, 444(1-2):191-202.
    • (2013) Virology , vol.444 , Issue.1-2 , pp. 191-202
    • Klockow, L.C.1    Sharifi, H.J.2    Wen, X.Y.3    Flagg, M.4    Furuya, A.K.M.5    Nekorchuk, M.6    de Noronha, C.M.C.7
  • 23
    • 79953848334 scopus 로고    scopus 로고
    • HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention
    • Kogan M., Rappaport J. HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention. Retrovirology 2011, 8:25.
    • (2011) Retrovirology , vol.8 , pp. 25
    • Kogan, M.1    Rappaport, J.2
  • 24
    • 84874005275 scopus 로고    scopus 로고
    • DNA damage enhances integration of HIV-1 into macrophages by overcoming integrase inhibition
    • Koyama T., Sun B.L., Tokunaga K., Tatsumi M., Ishizaka Y. DNA damage enhances integration of HIV-1 into macrophages by overcoming integrase inhibition. Retrovirology 2013, 10:21.
    • (2013) Retrovirology , vol.10 , pp. 21
    • Koyama, T.1    Sun, B.L.2    Tokunaga, K.3    Tatsumi, M.4    Ishizaka, Y.5
  • 25
    • 33645862586 scopus 로고    scopus 로고
    • Endogenous factors enhance HIV infection of tissue naive CD4T cells by stimulating high molecular mass APOBEC3G complex formation
    • Kreisberg J.F., Yonemoto W., Greene W.C. Endogenous factors enhance HIV infection of tissue naive CD4T cells by stimulating high molecular mass APOBEC3G complex formation. J. Exp. Med. 2006, 203(4):865-870.
    • (2006) J. Exp. Med. , vol.203 , Issue.4 , pp. 865-870
    • Kreisberg, J.F.1    Yonemoto, W.2    Greene, W.C.3
  • 27
    • 42449109442 scopus 로고    scopus 로고
    • Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1
    • Langlois M.A., Neuberger M.S. Human APOBEC3G can restrict retroviral infection in avian cells and acts independently of both UNG and SMUG1. J. Virol. 2008, 82(9):4660-4664.
    • (2008) J. Virol. , vol.82 , Issue.9 , pp. 4660-4664
    • Langlois, M.A.1    Neuberger, M.S.2
  • 28
  • 29
    • 18144379557 scopus 로고    scopus 로고
    • The Vpr protein from HIV-1: distinct roles along the viral life cycle
    • Le Rouzic E., Benichou S. The Vpr protein from HIV-1: distinct roles along the viral life cycle. Retrovirology 2005, 2:11.
    • (2005) Retrovirology , vol.2 , pp. 11
    • Le Rouzic, E.1    Benichou, S.2
  • 30
    • 77954047969 scopus 로고    scopus 로고
    • Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps
    • Magadan J.G., Perez-Victoria F.J., Sougrat R., Ye Y.H., Strebel K., Bonifacino J.S. Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathog. 2010, 6(4):e1000869.
    • (2010) PLoS Pathog. , vol.6 , Issue.4 , pp. e1000869
    • Magadan, J.G.1    Perez-Victoria, F.J.2    Sougrat, R.3    Ye, Y.H.4    Strebel, K.5    Bonifacino, J.S.6
  • 32
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • Marin M., Rose K.M., Kozak S.L., Kabat D. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 2003, 9(11):1398-1403.
    • (2003) Nat. Med. , vol.9 , Issue.11 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 33
    • 77951232176 scopus 로고    scopus 로고
    • Fiber Dock: flexible induced-fit backbone refinement in molecular docking
    • Mashiach E., Nussinov R., Wolfson H.J. Fiber Dock: flexible induced-fit backbone refinement in molecular docking. Proteins 2010, 78(6):1503-1519.
    • (2010) Proteins , vol.78 , Issue.6 , pp. 1503-1519
    • Mashiach, E.1    Nussinov, R.2    Wolfson, H.J.3
  • 34
    • 84885128030 scopus 로고    scopus 로고
    • HIV-1 Vpr induces the degradation of ZIP and sZIP, adaptors of the NuRD chromatin remodeling complex, by hijacking DCAF1/VprBP
    • Maudet C., Sourisce A., Dragin L., Lahouassa H., Rain J.C., Bouaziz S., Ramirez B.C., Margottin-Goguet F. HIV-1 Vpr induces the degradation of ZIP and sZIP, adaptors of the NuRD chromatin remodeling complex, by hijacking DCAF1/VprBP. PLoS One 2013, 8(10):e77320.
    • (2013) PLoS One , vol.8 , Issue.10 , pp. e77320
    • Maudet, C.1    Sourisce, A.2    Dragin, L.3    Lahouassa, H.4    Rain, J.C.5    Bouaziz, S.6    Ramirez, B.C.7    Margottin-Goguet, F.8
  • 36
    • 84883687665 scopus 로고    scopus 로고
    • VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases
    • Nakagawa T., Mondal K., Swanson P.C. VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases. BMC Mol. Biol. 2013, 14:22.
    • (2013) BMC Mol. Biol. , vol.14 , pp. 22
    • Nakagawa, T.1    Mondal, K.2    Swanson, P.C.3
  • 38
    • 80052966856 scopus 로고    scopus 로고
    • The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells
    • Norman J.M., Mashiba M., McNamara L.A., Onafuwa-Nuga A., Chiari-Fort E., Shen W.W., Collins K.L. The antiviral factor APOBEC3G enhances the recognition of HIV-infected primary T cells by natural killer cells. Nat. Immunol. 2011, 12(10):975-983.
    • (2011) Nat. Immunol. , vol.12 , Issue.10 , pp. 975-983
    • Norman, J.M.1    Mashiba, M.2    McNamara, L.A.3    Onafuwa-Nuga, A.4    Chiari-Fort, E.5    Shen, W.W.6    Collins, K.L.7
  • 39
    • 40649114040 scopus 로고    scopus 로고
    • HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradation
    • Okumura A., Alce T., Lubyova B., Ezelle H., Strebel K., Pitha P.M. HIV-1 accessory proteins VPR and Vif modulate antiviral response by targeting IRF-3 for degradation. Virology 2008, 373(1):85-97.
    • (2008) Virology , vol.373 , Issue.1 , pp. 85-97
    • Okumura, A.1    Alce, T.2    Lubyova, B.3    Ezelle, H.4    Strebel, K.5    Pitha, P.M.6
  • 40
    • 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 J.M., Boretto J., Canard B., Querat G., Sire J. HIV-1-associated uracil DNA glycosylase activity controls dUTP misincorporation in viral DNA and is essential to the HIV-1 life cycle. Mol. Cell 2005, 17(4):479-490.
    • (2005) Mol. Cell , vol.17 , Issue.4 , 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
  • 41
    • 84876443721 scopus 로고    scopus 로고
    • Lentivirus Vpr and Vpx accessory proteins usurp the cullin4-DDB1 (DCAF1) E3 ubiquitin ligase
    • Romani B., Cohen E.A. Lentivirus Vpr and Vpx accessory proteins usurp the cullin4-DDB1 (DCAF1) E3 ubiquitin ligase. Curr. Opin. Virol. 2012, 2(6):755-763.
    • (2012) Curr. Opin. Virol. , vol.2 , Issue.6 , pp. 755-763
    • Romani, B.1    Cohen, E.A.2
  • 43
    • 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 N.R. HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1. Proc. Natl. Acad. Sci. U.S.A. 2007, 104(10):4130-4135.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , Issue.10 , pp. 4130-4135
    • Schrofelbauer, B.1    Hakata, Y.2    Landau, N.R.3
  • 44
    • 23844471513 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases
    • Schrofelbauer B., Yu Q., Zeitlin S.G., Landau N.R. Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. J. Virol. 2005, 79(17):10978-10987.
    • (2005) J. Virol. , vol.79 , Issue.17 , pp. 10978-10987
    • Schrofelbauer, B.1    Yu, Q.2    Zeitlin, S.G.3    Landau, N.R.4
  • 45
    • 2442456104 scopus 로고    scopus 로고
    • A method for simultaneous alignment of multiple protein structures
    • Shatsky M., Nussinov R., Wolfson H.J. A method for simultaneous alignment of multiple protein structures. Proteins 2004, 56(1):143-156.
    • (2004) Proteins , vol.56 , Issue.1 , pp. 143-156
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 46
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002, 418(6898):646-650.
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 47
    • 0034960174 scopus 로고    scopus 로고
    • Molecular basis for cell tropism of CXCR4-dependent human immunodeficiency virus type 1 isolates
    • Tokunaga K., Greenberg M.L., Morse M.A., Cumming R.I., Lyerly H.K., Cullen B.R. Molecular basis for cell tropism of CXCR4-dependent human immunodeficiency virus type 1 isolates. J. Virol. 2001, 75(15):6776-6785.
    • (2001) J. Virol. , vol.75 , Issue.15 , pp. 6776-6785
    • Tokunaga, K.1    Greenberg, M.L.2    Morse, M.A.3    Cumming, R.I.4    Lyerly, H.K.5    Cullen, B.R.6
  • 48
    • 0026739866 scopus 로고
    • Evolution of the primate lentiviruses - evidence from Vpx and Vpr
    • Tristem M., Marshall C., Karpas A., Hill F. Evolution of the primate lentiviruses - evidence from Vpx and Vpr. EMBO J. 1992, 11(9):3405-3412.
    • (1992) EMBO J. , vol.11 , Issue.9 , pp. 3405-3412
    • Tristem, M.1    Marshall, C.2    Karpas, A.3    Hill, F.4
  • 49
    • 80052411919 scopus 로고    scopus 로고
    • Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM
    • Tuncbag N., Gursoy A., Nussinov R., Keskin O. Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM. Nat. Protoc. 2011, 6(9):1341-1354.
    • (2011) Nat. Protoc. , vol.6 , Issue.9 , pp. 1341-1354
    • Tuncbag, N.1    Gursoy, A.2    Nussinov, R.3    Keskin, O.4
  • 50
    • 72949088633 scopus 로고    scopus 로고
    • Towards inferring time dimensionality in protein-protein interaction networks by integrating structures: the p53 example
    • Tuncbag N., Kar G., Gursoy A., Keskin O., Nussinov R. Towards inferring time dimensionality in protein-protein interaction networks by integrating structures: the p53 example. Mol. Biosyst. 2009, 5(12):1770-1778.
    • (2009) Mol. Biosyst. , vol.5 , Issue.12 , pp. 1770-1778
    • Tuncbag, N.1    Kar, G.2    Gursoy, A.3    Keskin, O.4    Nussinov, R.5
  • 51
    • 84878386878 scopus 로고    scopus 로고
    • HIV-1 Vpr protein inhibits telomerase activity via the EDD-DDB1-VPRBP E3 ligase complex
    • Wang X., Singh S., Jung H.Y., Yang G.J., Jun S., Sastry K.J., Park J.I. HIV-1 Vpr protein inhibits telomerase activity via the EDD-DDB1-VPRBP E3 ligase complex. J. Biol. Chem. 2013, 288(22):15474-15480.
    • (2013) J. Biol. Chem. , vol.288 , Issue.22 , pp. 15474-15480
    • Wang, X.1    Singh, S.2    Jung, H.Y.3    Yang, G.J.4    Jun, S.5    Sastry, K.J.6    Park, J.I.7
  • 52
    • 73349122322 scopus 로고    scopus 로고
    • HIV-1 Vpr triggers natural killer cell-mediated lysis of infected cells through activation of the ATR-mediated DNA damage response
    • Ward J., Davis Z., DeHart J., Zimmerman E., Bosque A., Brunetta E., Mavilio D., Planelles V., Barker E. HIV-1 Vpr triggers natural killer cell-mediated lysis of infected cells through activation of the ATR-mediated DNA damage response. PLoS Pathog. 2009, 5(10):e1000613.
    • (2009) PLoS Pathog. , vol.5 , Issue.10 , pp. e1000613
    • 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
  • 54
    • 84856159248 scopus 로고    scopus 로고
    • The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover
    • Wen X.Y., Klockow L.C., Nekorchuk M., Sharifi H.J., de Noronha C.M.C. The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover. PLoS One 2012, 7(1):e30939.
    • (2012) PLoS One , vol.7 , Issue.1 , pp. e30939
    • Wen, X.Y.1    Klockow, L.C.2    Nekorchuk, M.3    Sharifi, H.J.4    de Noronha, C.M.C.5
  • 57
    • 34249671724 scopus 로고    scopus 로고
    • Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA
    • Yang B., Chen K.Y., Zhang C., Huang S., Zhang H. Virion-associated uracil DNA glycosylase-2 and apurinic/apyrimidinic endonuclease are involved in the degradation of APOBEC3G-edited nascent HIV-1 DNA. J. Biol. Chem. 2007, 282(16):11667-11675.
    • (2007) J. Biol. Chem. , vol.282 , Issue.16 , pp. 11667-11675
    • Yang, B.1    Chen, K.Y.2    Zhang, C.3    Huang, S.4    Zhang, H.5
  • 58
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X.H., Yu Y.K., Liu B.D., Luo K., Kong W., Mao P.Y., Yu X.F. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003, 302(5647):1056-1060.
    • (2003) Science , vol.302 , Issue.5647 , pp. 1056-1060
    • Yu, X.H.1    Yu, Y.K.2    Liu, B.D.3    Luo, K.4    Kong, W.5    Mao, P.Y.6    Yu, X.F.7
  • 59
    • 79957477586 scopus 로고    scopus 로고
    • Vpr-host interactions during HIV-1 viral life cycle
    • Zhao R.Y., Li G., Bukrinsky M.I. Vpr-host interactions during HIV-1 viral life cycle. J. Neuroimmune Pharmacol. 2011, 6(2):216-229.
    • (2011) J. Neuroimmune Pharmacol. , vol.6 , Issue.2 , pp. 216-229
    • Zhao, R.Y.1    Li, G.2    Bukrinsky, M.I.3
  • 60
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • Zheng Y.H., Irwin D., Kurosu T., Tokunaga K., Sata T., Peterlin B.M. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J. Virol. 2004, 78(11):6073-6076.
    • (2004) J. Virol. , vol.78 , Issue.11 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6


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