메뉴 건너뛰기




Volumn 40, Issue , 2018, Pages 3-12

Multilayered and versatile inhibition of cellular antiviral factors by HIV and SIV accessory proteins

Author keywords

Accessory proteins; HIV; Immune activation; Restriction factors; SIV

Indexed keywords

ANTIVIRUS AGENT; B LYMPHOCYTE ANTIGEN; HUMAN IMMUNODEFICIENCY VIRUS VACCINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NEF PROTEIN; PROTEASOME; T LYMPHOCYTE ANTIGEN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; VIF PROTEIN; VIRAL PROTEIN; VPR PROTEIN; VPU PROTEIN; VPX PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; NEF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; VPR PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; VPU PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 85043393231     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2018.02.005     Document Type: Review
Times cited : (52)

References (146)
  • 1
    • 0032502748 scopus 로고    scopus 로고
    • Virus-induced host gene shutoff in animals and plants
    • Aranda, M., Maule, A., Virus-induced host gene shutoff in animals and plants. Virology 243 (1998), 261–267, 10.1006/viro.1998.9032.
    • (1998) Virology , vol.243 , pp. 261-267
    • Aranda, M.1    Maule, A.2
  • 2
    • 84956585606 scopus 로고    scopus 로고
    • SnapShot: antiviral restriction factors
    • Kluge, S.F., Sauter, D., Kirchhoff, F., SnapShot: antiviral restriction factors. Cell 163 (2015), 774–774.e1, 10.1016/j.cell.2015.10.019.
    • (2015) Cell , vol.163 , pp. 774-774.e1
    • Kluge, S.F.1    Sauter, D.2    Kirchhoff, F.3
  • 3
    • 0030664277 scopus 로고    scopus 로고
    • PKR-a protein kinase regulated by double-stranded RNA
    • Clemens, M.J., PKR-a protein kinase regulated by double-stranded RNA. Int. J. Biochem. Cell Biol. 29 (1997), 945–949.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 945-949
    • Clemens, M.J.1
  • 4
    • 84974593823 scopus 로고    scopus 로고
    • Alphavirus infection host cell shut-off and inhibition of antiviral responses
    • Fros, J.J., Pijlman, G.P., Alphavirus infection host cell shut-off and inhibition of antiviral responses. Viruses, 8, 2016, 10.3390/v8060166.
    • (2016) Viruses , vol.8
    • Fros, J.J.1    Pijlman, G.P.2
  • 5
    • 84988511942 scopus 로고    scopus 로고
    • Virology Closing in on the causes of host shutoff
    • Mohr, I., Virology Closing in on the causes of host shutoff. ELife, 5, 2016, e20755, 10.7554/eLife.20755.
    • (2016) ELife , vol.5 , pp. e20755
    • Mohr, I.1
  • 7
    • 84930892539 scopus 로고    scopus 로고
    • Timing is everything: coordinated control of host shutoff by influenza a virus NS1 and PA-X proteins
    • Khaperskyy, D.A., McCormick, C., Timing is everything: coordinated control of host shutoff by influenza a virus NS1 and PA-X proteins. J. Virol. 89 (2015), 6528–6531, 10.1128/JVI.00386-15.
    • (2015) J. Virol. , vol.89 , pp. 6528-6531
    • Khaperskyy, D.A.1    McCormick, C.2
  • 8
    • 77953117609 scopus 로고    scopus 로고
    • Inhibition of host translation by virus infection in vivo
    • Toribio, R., Ventoso, I., Inhibition of host translation by virus infection in vivo. Proc. Natl. Acad. Sci. 107 (2010), 9837–9842, 10.1073/pnas.1004110107.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 9837-9842
    • Toribio, R.1    Ventoso, I.2
  • 9
    • 81255160914 scopus 로고    scopus 로고
    • Viral subversion of the host protein synthesis machinery
    • Walsh, D., Mohr, I., Viral subversion of the host protein synthesis machinery. Nat. Rev. Microbiol. 9 (2011), 860–875, 10.1038/nrmicro2655.
    • (2011) Nat. Rev. Microbiol. , vol.9 , pp. 860-875
    • Walsh, D.1    Mohr, I.2
  • 12
    • 84855911746 scopus 로고    scopus 로고
    • Next-generation sequencing reveals HIV-1-mediated suppression of T cell activation and RNA processing and regulation of noncoding RNA expression in a CD4+ T cell line
    • Chang, S.T., Sova, P., Peng, X., Weiss, J., Law, G.L., Palermo, R.E., Katze, M.G., Next-generation sequencing reveals HIV-1-mediated suppression of T cell activation and RNA processing and regulation of noncoding RNA expression in a CD4+ T cell line. MBio, 2, 2011, 10.1128/mBio.00134-11.
    • (2011) MBio , vol.2
    • Chang, S.T.1    Sova, P.2    Peng, X.3    Weiss, J.4    Law, G.L.5    Palermo, R.E.6    Katze, M.G.7
  • 13
    • 84958191271 scopus 로고    scopus 로고
    • Analysis of host gene expression profile in HIV-1 and HIV-2 infected T-cells
    • Devadas, K., Biswas, S., Haleyurgirisetty, M., Wood, O., Ragupathy, V., Lee, S., Hewlett, I., Analysis of host gene expression profile in HIV-1 and HIV-2 infected T-cells. PLoS One, 11, 2016, e0147421, 10.1371/journal.pone.0147421.
    • (2016) PLoS One , vol.11 , pp. e0147421
    • Devadas, K.1    Biswas, S.2    Haleyurgirisetty, M.3    Wood, O.4    Ragupathy, V.5    Lee, S.6    Hewlett, I.7
  • 16
    • 84875430753 scopus 로고    scopus 로고
    • Transcriptome sequencing of gene expression in the brain of the HIV-1 transgenic rat
    • Li, M.D., Cao, J., Wang, S., Wang, J., Sarkar, S., Vigorito, M., Ma, J.Z., Chang, S.L., Transcriptome sequencing of gene expression in the brain of the HIV-1 transgenic rat. PLoS One, 8, 2013, e59582, 10.1371/journal.pone.0059582.
    • (2013) PLoS One , vol.8 , pp. e59582
    • Li, M.D.1    Cao, J.2    Wang, S.3    Wang, J.4    Sarkar, S.5    Vigorito, M.6    Ma, J.Z.7    Chang, S.L.8
  • 17
    • 53249151597 scopus 로고    scopus 로고
    • BCL11 B is a general transcriptional repressor of the HIV-1 long terminal repeat in T lymphocytes through recruitment of the NuRD complex
    • Cismasiu, V.B., Paskaleva, E., Suman Daya, S., Canki, M., Duus, K., Avram, D., BCL11 B is a general transcriptional repressor of the HIV-1 long terminal repeat in T lymphocytes through recruitment of the NuRD complex. Virology 380 (2008), 173–181, 10.1016/j.virol.2008.07.035.
    • (2008) Virology , vol.380 , pp. 173-181
    • Cismasiu, V.B.1    Paskaleva, E.2    Suman Daya, S.3    Canki, M.4    Duus, K.5    Avram, D.6
  • 18
    • 84907029494 scopus 로고    scopus 로고
    • The multifaceted roles of Bcl11b in thymic and peripheral T cells − impact on immune diseases
    • Avram, D., Califano, D., The multifaceted roles of Bcl11b in thymic and peripheral T cells − impact on immune diseases. J. Immunol. 193 (2014), 2059–2065, 10.4049/jimmunol.1400930.
    • (2014) J. Immunol. , vol.193 , pp. 2059-2065
    • Avram, D.1    Califano, D.2
  • 19
    • 85014424945 scopus 로고    scopus 로고
    • Primate lentiviruses modulate NF-κB activity by multiple mechanisms to fine-tune viral and cellular gene expression
    • Heusinger, E., Kirchhoff, F., Primate lentiviruses modulate NF-κB activity by multiple mechanisms to fine-tune viral and cellular gene expression. Front. Microbiol., 8, 2017, 198, 10.3389/fmicb.2017.00198.
    • (2017) Front. Microbiol. , vol.8 , pp. 198
    • Heusinger, E.1    Kirchhoff, F.2
  • 21
    • 80052073169 scopus 로고    scopus 로고
    • NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62
    • Kalveram, B., Lihoradova, O., Ikegami, T., NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62. J. Virol. 85 (2011), 6234–6243, 10.1128/JVI.02255-10.
    • (2011) J. Virol. , vol.85 , pp. 6234-6243
    • Kalveram, B.1    Lihoradova, O.2    Ikegami, T.3
  • 22
    • 22544473919 scopus 로고    scopus 로고
    • Shutoff of RNA polymerase II transcription by poliovirus involves 3C protease-mediated cleavage of the TATA-binding protein at an alternative site: incomplete shutoff of transcription interferes with efficient viral replication
    • Kundu, P., Raychaudhuri, S., Tsai, W., Dasgupta, A., Shutoff of RNA polymerase II transcription by poliovirus involves 3C protease-mediated cleavage of the TATA-binding protein at an alternative site: incomplete shutoff of transcription interferes with efficient viral replication. J. Virol. 79 (2005), 9702–9713, 10.1128/JVI.79.15.9702-9713.2005.
    • (2005) J. Virol. , vol.79 , pp. 9702-9713
    • Kundu, P.1    Raychaudhuri, S.2    Tsai, W.3    Dasgupta, A.4
  • 23
    • 78349236605 scopus 로고    scopus 로고
    • The role of the influenza virus RNA polymerase in host shut-off
    • Vreede, F.T., Fodor, E., The role of the influenza virus RNA polymerase in host shut-off. Virulence 1 (2010), 436–439, 10.4161/viru.1.5.12967.
    • (2010) Virulence , vol.1 , pp. 436-439
    • Vreede, F.T.1    Fodor, E.2
  • 24
    • 34248339180 scopus 로고    scopus 로고
    • Herpes simplex virus immediate-early protein ICP22 triggers loss of serine 2-phosphorylated RNA polymerase II
    • Fraser, K.A., Rice, S.A., Herpes simplex virus immediate-early protein ICP22 triggers loss of serine 2-phosphorylated RNA polymerase II. J. Virol. 81 (2007), 5091–5101, 10.1128/JVI. 00184-07.
    • (2007) J. Virol. , vol.81 , pp. 5091-5101
    • Fraser, K.A.1    Rice, S.A.2
  • 25
    • 84858714200 scopus 로고    scopus 로고
    • Dynamic roles for NF-κB in HTLV-I and HIV-1 retroviral pathogenesis
    • Chan, J.K., Greene, W.C., Dynamic roles for NF-κB in HTLV-I and HIV-1 retroviral pathogenesis. Immunol. Rev. 246 (2012), 286–310, 10.1111/j.1600-065X.2012.01094.x.
    • (2012) Immunol. Rev. , vol.246 , pp. 286-310
    • Chan, J.K.1    Greene, W.C.2
  • 28
    • 84857300414 scopus 로고    scopus 로고
    • The cytoplasmic domain of the HIV-1 glycoprotein gp41 induces NF-κB activation through TGF-β-activated kinase 1
    • Postler, T.S., Desrosiers, R.C., The cytoplasmic domain of the HIV-1 glycoprotein gp41 induces NF-κB activation through TGF-β-activated kinase 1. Cell Host Microbe. 11 (2012), 181–193, 10.1016/j.chom.2011.12.005.
    • (2012) Cell Host Microbe. , vol.11 , pp. 181-193
    • Postler, T.S.1    Desrosiers, R.C.2
  • 29
    • 0035163739 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors
    • Akari, H., Bour, S., Kao, S., Adachi, A., Strebel, K., The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors. J. Exp. Med. 194 (2001), 1299–1311.
    • (2001) J. Exp. Med. , vol.194 , pp. 1299-1311
    • Akari, H.1    Bour, S.2    Kao, S.3    Adachi, A.4    Strebel, K.5
  • 30
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B
    • Bour, S., Perrin, C., Akari, H., Strebel, K., The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B. J. Biol. Chem. 276 (2001), 15920–15928, 10.1074/jbc.M010533200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 31
    • 0242439335 scopus 로고    scopus 로고
    • Directed expression of the HIV-1 accessory protein Vpu in drosophila fat-body cells inhibits toll-dependent immune responses
    • Leulier, F., Marchal, C., Miletich, I., Limbourg-Bouchon, B., Benarous, R., Lemaitre, B., Directed expression of the HIV-1 accessory protein Vpu in drosophila fat-body cells inhibits toll-dependent immune responses. EMBO Rep. 4 (2003), 976–981, 10.1038/sj.embor.embor936.
    • (2003) EMBO Rep. , vol.4 , pp. 976-981
    • Leulier, F.1    Marchal, C.2    Miletich, I.3    Limbourg-Bouchon, B.4    Benarous, R.5    Lemaitre, B.6
  • 32
    • 84869194198 scopus 로고    scopus 로고
    • Innate sensing of HIV-1 assembly by tetherin induces NFκB-dependent proinflammatory responses
    • Galão, R.P., Le Tortorec, A., Pickering, S., Kueck, T., Neil, S.J.D., Innate sensing of HIV-1 assembly by tetherin induces NFκB-dependent proinflammatory responses. Cell Host Microbe 12 (2012), 633–644, 10.1016/j.chom.2012.10.007.
    • (2012) Cell Host Microbe , vol.12 , pp. 633-644
    • Galão, R.P.1    Le Tortorec, A.2    Pickering, S.3    Kueck, T.4    Neil, S.J.D.5
  • 35
    • 85047153419 scopus 로고    scopus 로고
    • PKCθ is a key regulator of T-cell behavior and a drug target for t cell-mediated diseases
    • Isakov, N., PKCθ is a key regulator of T-cell behavior and a drug target for t cell-mediated diseases. J. Clin. Cell. Immunol. 0 (2012), 1–7, 10.4172/2155-9899.S12-008.
    • (2012) J. Clin. Cell. Immunol. , pp. 1-7
    • Isakov, N.1
  • 36
    • 67349166158 scopus 로고    scopus 로고
    • Is the high virulence of HIV-1 an unfortunate coincidence of primate lentiviral evolution?
    • Kirchhoff, F., Is the high virulence of HIV-1 an unfortunate coincidence of primate lentiviral evolution?. Nat. Rev. Microbiol. 7 (2009), 467–476, 10.1038/nrmicro2111.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 467-476
    • Kirchhoff, F.1
  • 40
    • 84871699358 scopus 로고    scopus 로고
    • Inhibition of NF-κB activity by HIV-1 Vpr is dependent on Vpr binding protein
    • Kogan, M., Deshmane, S., Sawaya, B.E., Gracely, E.J., Khalili, K., Rappaport, J., Inhibition of NF-κB activity by HIV-1 Vpr is dependent on Vpr binding protein. J. Cell. Physiol. 228 (2013), 781–790, 10.1002/jcp.24226.
    • (2013) J. Cell. Physiol. , vol.228 , pp. 781-790
    • Kogan, M.1    Deshmane, S.2    Sawaya, B.E.3    Gracely, E.J.4    Khalili, K.5    Rappaport, J.6
  • 42
    • 0036730820 scopus 로고    scopus 로고
    • The HIV-1 accessory gene vpr can inhibit antigen-specific immune function
    • Muthumani, K., Hwang, D.S., Dayes, N.S., Kim, J.J., Weiner, D.B., The HIV-1 accessory gene vpr can inhibit antigen-specific immune function. DNA Cell Biol. 21 (2002), 689–695, 10.1089/104454902760330237.
    • (2002) DNA Cell Biol. , vol.21 , pp. 689-695
    • Muthumani, K.1    Hwang, D.S.2    Dayes, N.S.3    Kim, J.J.4    Weiner, D.B.5
  • 43
    • 33846382998 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) type 1 Vpr induces differential regulation of T cell costimulatory molecules: direct effect of Vpr on T cell activation and immune function
    • Venkatachari, N.J., Majumder, B., Ayyavoo, V., Human immunodeficiency virus (HIV) type 1 Vpr induces differential regulation of T cell costimulatory molecules: direct effect of Vpr on T cell activation and immune function. Virology 358 (2007), 347–356, 10.1016/j.virol.2006.08.030.
    • (2007) Virology , vol.358 , pp. 347-356
    • Venkatachari, N.J.1    Majumder, B.2    Ayyavoo, V.3
  • 45
    • 0034002849 scopus 로고    scopus 로고
    • Activation of transcription factors NF-kappaB and NF-IL-6 by human immunodeficiency virus type 1 protein R (Vpr) induces interleukin-8 expression
    • Roux, P., Alfieri, C., Hrimech, M., Cohen, E.A., Tanner, J.E., Activation of transcription factors NF-kappaB and NF-IL-6 by human immunodeficiency virus type 1 protein R (Vpr) induces interleukin-8 expression. J. Virol. 74 (2000), 4658–4665.
    • (2000) J. Virol. , vol.74 , pp. 4658-4665
    • Roux, P.1    Alfieri, C.2    Hrimech, M.3    Cohen, E.A.4    Tanner, J.E.5
  • 46
    • 84952636638 scopus 로고    scopus 로고
    • HIV-1 Vpr protein activates the NF-κB pathway to promote G2/M cell cycle arrest
    • Liang, Z., Liu, R., Lin, Y., Liang, C., Tan, J., Qiao, W., HIV-1 Vpr protein activates the NF-κB pathway to promote G2/M cell cycle arrest. Virol. Sin. 30 (2015), 441–448, 10.1007/s12250-015-3654-8.
    • (2015) Virol. Sin. , vol.30 , pp. 441-448
    • Liang, Z.1    Liu, R.2    Lin, Y.3    Liang, C.4    Tan, J.5    Qiao, W.6
  • 47
    • 84902496017 scopus 로고    scopus 로고
    • HIV-1 vpr stimulates NF-κB and AP-1 signaling by activating TAK1
    • Liu, R., Lin, Y., Jia, R., Geng, Y., Liang, C., Tan, J., Qiao, W., HIV-1 vpr stimulates NF-κB and AP-1 signaling by activating TAK1. Retrovirology, 11, 2014, 45, 10.1186/1742-4690-11-45.
    • (2014) Retrovirology , vol.11 , pp. 45
    • Liu, R.1    Lin, Y.2    Jia, R.3    Geng, Y.4    Liang, C.5    Tan, J.6    Qiao, W.7
  • 48
    • 84874996875 scopus 로고    scopus 로고
    • HIV-1 Vpr activates both canonical and noncanonical NF-κB pathway by enhancing the phosphorylation of IKKα/β
    • Liu, R., Tan, J., Lin, Y., Jia, R., Yang, W., Liang, C., Geng, Y., Qiao, W., HIV-1 Vpr activates both canonical and noncanonical NF-κB pathway by enhancing the phosphorylation of IKKα/β. Virology 439 (2013), 47–56, 10.1016/j.virol.2013.01.020.
    • (2013) Virology , vol.439 , pp. 47-56
    • Liu, R.1    Tan, J.2    Lin, Y.3    Jia, R.4    Yang, W.5    Liang, C.6    Geng, Y.7    Qiao, W.8
  • 49
    • 84943143765 scopus 로고    scopus 로고
    • Multiple protein kinases via activation of transcription factors NF-κB, AP-1 and C/EBP-δ regulate the IL-6/IL-8 production by HIV-1 vpr in astrocytes
    • Gangwani, M.R., Kumar, A., Multiple protein kinases via activation of transcription factors NF-κB, AP-1 and C/EBP-δ regulate the IL-6/IL-8 production by HIV-1 vpr in astrocytes. PLoS One, 10, 2015, e0135633, 10.1371/journal.pone.0135633.
    • (2015) PLoS One , vol.10 , pp. e0135633
    • Gangwani, M.R.1    Kumar, A.2
  • 50
    • 30044438704 scopus 로고    scopus 로고
    • Synthetic Vpr protein activates activator protein-1, c-Jun N-terminal kinase, and NF-kappaB and stimulates HIV-1 transcription in promonocytic cells and primary macrophages
    • Varin, A., Decrion, A.-Z., Sabbah, E., Quivy, V., Sire, J., Van Lint, C., Roques, B.P., Aggarwal, B.B., Herbein, G., Synthetic Vpr protein activates activator protein-1, c-Jun N-terminal kinase, and NF-kappaB and stimulates HIV-1 transcription in promonocytic cells and primary macrophages. J. Biol. Chem. 280 (2005), 42557–42567, 10.1074/jbc.M502211200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42557-42567
    • Varin, A.1    Decrion, A.-Z.2    Sabbah, E.3    Quivy, V.4    Sire, J.5    Van Lint, C.6    Roques, B.P.7    Aggarwal, B.B.8    Herbein, G.9
  • 51
    • 84865106370 scopus 로고    scopus 로고
    • Vpu mediates depletion of interferon regulatory factor 3 during HIV infection by a lysosome-dependent mechanism
    • Doehle, B.P., Chang, K., Rustagi, A., McNevin, J., McElrath, M.J., Gale, M., Vpu mediates depletion of interferon regulatory factor 3 during HIV infection by a lysosome-dependent mechanism. J. Virol. 86 (2012), 8367–8374, 10.1128/JVI.00423-12.
    • (2012) J. Virol. , vol.86 , pp. 8367-8374
    • Doehle, B.P.1    Chang, K.2    Rustagi, A.3    McNevin, J.4    McElrath, M.J.5    Gale, M.6
  • 52
    • 84919388383 scopus 로고    scopus 로고
    • HIV-1 vpu accessory protein induces caspase-mediated cleavage of IRF3 transcription factor
    • Park, S.Y., Waheed, A.A., Zhang, Z.-R., Freed, E.O., Bonifacino, J.S., HIV-1 vpu accessory protein induces caspase-mediated cleavage of IRF3 transcription factor. J. Biol. Chem. 289 (2014), 35102–35110, 10.1074/jbc.M114.597062.
    • (2014) J. Biol. Chem. , vol.289 , pp. 35102-35110
    • Park, S.Y.1    Waheed, A.A.2    Zhang, Z.-R.3    Freed, E.O.4    Bonifacino, J.S.5
  • 54
    • 84878553328 scopus 로고    scopus 로고
    • HIV-1 vpu does not degrade interferon regulatory factor 3
    • Hotter, D., Kirchhoff, F., Sauter, D., HIV-1 vpu does not degrade interferon regulatory factor 3. J. Virol. 87 (2013), 7160–7165, 10.1128/JVI.00526-13.
    • (2013) J. Virol. , vol.87 , pp. 7160-7165
    • Hotter, D.1    Kirchhoff, F.2    Sauter, D.3
  • 55
    • 24944498529 scopus 로고    scopus 로고
    • A novel role for Vpr of human immunodeficiency virus type 1 as a regulator of the splicing of cellular pre-mRNA
    • Kuramitsu, M., Hashizume, C., Yamamoto, N., Azuma, A., Kamata, M., Yamamoto, N., Tanaka, Y., Aida, Y., A novel role for Vpr of human immunodeficiency virus type 1 as a regulator of the splicing of cellular pre-mRNA. Microbes Infect. 7 (2005), 1150–1160, 10.1016/j.micinf.2005.03.022.
    • (2005) Microbes Infect. , vol.7 , pp. 1150-1160
    • Kuramitsu, M.1    Hashizume, C.2    Yamamoto, N.3    Azuma, A.4    Kamata, M.5    Yamamoto, N.6    Tanaka, Y.7    Aida, Y.8
  • 56
    • 33947194178 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr interacts with spliceosomal protein SAP145 to mediate cellular pre-mRNA splicing inhibition
    • Hashizume, C., Kuramitsu, M., Zhang, X., Kurosawa, T., Kamata, M., Aida, Y., Human immunodeficiency virus type 1 Vpr interacts with spliceosomal protein SAP145 to mediate cellular pre-mRNA splicing inhibition. Microbes Infect. 9 (2007), 490–497, 10.1016/j.micinf.2007.01.013.
    • (2007) Microbes Infect. , vol.9 , pp. 490-497
    • Hashizume, C.1    Kuramitsu, M.2    Zhang, X.3    Kurosawa, T.4    Kamata, M.5    Aida, Y.6
  • 57
    • 33750378322 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145
    • Terada, Y., Yasuda, Y., Human immunodeficiency virus type 1 vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145. Mol. Cell. Biol. 26 (2006), 8149–8158, 10.1128/MCB.01170-06.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8149-8158
    • Terada, Y.1    Yasuda, Y.2
  • 58
    • 84862642115 scopus 로고    scopus 로고
    • Non-canonical translation in RNA viruses
    • Firth, A.E., Brierley, I., Non-canonical translation in RNA viruses. J. Gen. Virol. 93 (2012), 1385–1409, 10.1099/vir.0.042499-0.
    • (2012) J. Gen. Virol. , vol.93 , pp. 1385-1409
    • Firth, A.E.1    Brierley, I.2
  • 59
    • 84943338797 scopus 로고    scopus 로고
    • Retrospective, eIF4F: A
    • Merrick, W.C., Retrospective, eIF4F: A, J. Biol. Chem. 290 (2015), 24091–24099, 10.1074/jbc.R115.675280.
    • (2015) J. Biol. Chem. , vol.290 , pp. 24091-24099
    • Merrick, W.C.1
  • 60
    • 0842347402 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by poliovirus 3C protease inhibits host cell translation: a novel mechanism for host translation shutoff
    • Kuyumcu-Martinez, N.M., Van Eden, M.E., Younan, P., Lloyd, R.E., Cleavage of poly(A)-binding protein by poliovirus 3C protease inhibits host cell translation: a novel mechanism for host translation shutoff. Mol. Cell. Biol. 24 (2004), 1779–1790.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1779-1790
    • Kuyumcu-Martinez, N.M.1    Van Eden, M.E.2    Younan, P.3    Lloyd, R.E.4
  • 61
    • 0036171240 scopus 로고    scopus 로고
    • Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease
    • Kuyumcu-Martinez, N.M., Joachims, M., Lloyd, R.E., Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease. J.Virol 76 (2002), 2062–2074.
    • (2002) J.Virol , vol.76 , pp. 2062-2074
    • Kuyumcu-Martinez, N.M.1    Joachims, M.2    Lloyd, R.E.3
  • 62
    • 3242702220 scopus 로고    scopus 로고
    • Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein
    • Kuyumcu-Martinez, M., Belliot, G., Sosnovtsev, S.V., Chang, K.-O., Green, K.Y., Lloyd, R.E., Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein. J. Virol. 78 (2004), 8172–8182, 10.1128/JVI.78.15.8172-8182.2004.
    • (2004) J. Virol. , vol.78 , pp. 8172-8182
    • Kuyumcu-Martinez, M.1    Belliot, G.2    Sosnovtsev, S.V.3    Chang, K.-O.4    Green, K.Y.5    Lloyd, R.E.6
  • 63
    • 0032530480 scopus 로고    scopus 로고
    • Proteolysis of human eukaryotic translation initiation factor eIF4GII but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection
    • Gradi, A., Svitkin, Y.V., Imataka, H., Sonenberg, N., Proteolysis of human eukaryotic translation initiation factor eIF4GII but not eIF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection. Proc. Natl. Acad. Sci. U. S. A. 95 (1998), 11089–11094.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11089-11094
    • Gradi, A.1    Svitkin, Y.V.2    Imataka, H.3    Sonenberg, N.4
  • 65
    • 0032889326 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff?
    • Kerekatte, V., Keiper, B.D., Badorff, C., Cai, A., Knowlton, K.U., Rhoads, R.E., Cleavage of poly(A)-binding protein by coxsackievirus 2A protease in vitro and in vivo: another mechanism for host protein synthesis shutoff?. J.Virol 73 (1999), 709–717.
    • (1999) J.Virol , vol.73 , pp. 709-717
    • Kerekatte, V.1    Keiper, B.D.2    Badorff, C.3    Cai, A.4    Knowlton, K.U.5    Rhoads, R.E.6
  • 66
    • 0242661870 scopus 로고    scopus 로고
    • The eukaryotic translation initiation factor 4GI is cleaved by different retroviral proteases
    • Alvarez, E., Menéndez-Arias, L., Carrasco, L., The eukaryotic translation initiation factor 4GI is cleaved by different retroviral proteases. J.Virol 77 (2003), 12392–12400.
    • (2003) J.Virol , vol.77 , pp. 12392-12400
    • Alvarez, E.1    Menéndez-Arias, L.2    Carrasco, L.3
  • 67
    • 71049190550 scopus 로고    scopus 로고
    • HIV- 1 protease inhibits Cap- and poly(A)-dependent translation upon eIF4GI and PABP cleavage
    • Castelló A., Franco, D., Moral-López, P., Berlanga, J.J., Alvarez, E., Wimmer, E., Carrasco, L., HIV- 1 protease inhibits Cap- and poly(A)-dependent translation upon eIF4GI and PABP cleavage. PLoS One, 4, 2009, e7997, 10.1371/journal.pone.0007997.
    • (2009) PLoS One , vol.4 , pp. e7997
    • Castelló, A.1    Franco, D.2    Moral-López, P.3    Berlanga, J.J.4    Alvarez, E.5    Wimmer, E.6    Carrasco, L.7
  • 68
    • 0037413865 scopus 로고    scopus 로고
    • Cleavage of eIF4G by HIV-1 protease: effects on translation
    • Perales, C., Carrasco, L., Ventoso, I., Cleavage of eIF4G by HIV-1 protease: effects on translation. FEBS Lett. 533 (2003), 89–94.
    • (2003) FEBS Lett. , vol.533 , pp. 89-94
    • Perales, C.1    Carrasco, L.2    Ventoso, I.3
  • 69
    • 84875678997 scopus 로고    scopus 로고
    • IRES-dependent translational control during virus-induced endoplasmic reticulum stress and apoptosis
    • Hanson, P.J., Zhang, H.M., Hemida, M.G., Ye, X., Qiu, Y., Yang, D., IRES-dependent translational control during virus-induced endoplasmic reticulum stress and apoptosis. Front. Microbiol., 3, 2012, 92, 10.3389/fmicb.2012.00092.
    • (2012) Front. Microbiol. , vol.3 , pp. 92
    • Hanson, P.J.1    Zhang, H.M.2    Hemida, M.G.3    Ye, X.4    Qiu, Y.5    Yang, D.6
  • 70
    • 84893810605 scopus 로고    scopus 로고
    • HIV-1 accessory proteins adapt cellular adaptors to facilitate immune evasion
    • Collins, D.R., Collins, K.L., HIV-1 accessory proteins adapt cellular adaptors to facilitate immune evasion. PLoS Pathog., 10, 2014, e1003851, 10.1371/journal.ppat.1003851.
    • (2014) PLoS Pathog. , vol.10 , pp. e1003851
    • Collins, D.R.1    Collins, K.L.2
  • 71
    • 85033451147 scopus 로고    scopus 로고
    • Hijacking of the ubiquitin/proteasome pathway by the HIV auxiliary proteins
    • Seissler, T., Marquet, R., Paillart, J.C., Hijacking of the ubiquitin/proteasome pathway by the HIV auxiliary proteins. Viruses, 9, 2017, E322, 10.3390/v9110322.
    • (2017) Viruses , vol.9 , pp. E322
    • Seissler, T.1    Marquet, R.2    Paillart, J.C.3
  • 72
    • 84944755225 scopus 로고    scopus 로고
    • HIV-1 Nef hijacks clathrin coats by stabilizing AP-1:Arf1 polygons
    • Shen, Q.T., Ren, X., Zhang, R., Lee, I.H., Hurley, J.H., HIV-1 Nef hijacks clathrin coats by stabilizing AP-1:Arf1 polygons. Science, 350, 2015, aac5137, 10.1126/science.aac5137.
    • (2015) Science , vol.350 , pp. aac5137
    • Shen, Q.T.1    Ren, X.2    Zhang, R.3    Lee, I.H.4    Hurley, J.H.5
  • 73
    • 84898733948 scopus 로고    scopus 로고
    • How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4
    • Ren, X., Park, S.Y., Bonifacino, J.S., Hurley, J.H., How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4. Elife, 3, 2014, e01754, 10.7554/eLife.01754.
    • (2014) Elife , vol.3 , pp. e01754
    • Ren, X.1    Park, S.Y.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 74
    • 84899819636 scopus 로고    scopus 로고
    • Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1
    • Jia, X., Weber, E., Tokarev, A., Lewinski, M., Rizk, M., Suarez, M., Guatelli, J., Xiong, Y., Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1. Elife, 3, 2014, e02362, 10.7554/eLife.02362.
    • (2014) Elife , vol.3 , pp. e02362
    • Jia, X.1    Weber, E.2    Tokarev, A.3    Lewinski, M.4    Rizk, M.5    Suarez, M.6    Guatelli, J.7    Xiong, Y.8
  • 76
    • 84890125460 scopus 로고    scopus 로고
    • HIV accessory proteins versus host restriction factors
    • Strebel, K., HIV accessory proteins versus host restriction factors. Curr. Opin. Virol. 3 (2013), 692–699.
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 692-699
    • Strebel, K.1
  • 77
    • 84960129732 scopus 로고    scopus 로고
    • Remodeling of the host cell plasma membrane by HIV-1 nef and vpu: a strategy to ensure viral fitness and persistence
    • Sugden, S.M., Bego, M.G., Pham, T.N., Cohen, É.A., Remodeling of the host cell plasma membrane by HIV-1 nef and vpu: a strategy to ensure viral fitness and persistence. Viruses, 8, 2016, 67.
    • (2016) Viruses , vol.8 , pp. 67
    • Sugden, S.M.1    Bego, M.G.2    Pham, T.N.3    Cohen, É.A.4
  • 78
    • 84929907228 scopus 로고    scopus 로고
    • Intrinsic host restrictions to HIV-1 and mechanisms of viral escape
    • Simon, V., Bloch, N., Landau, N.R., Intrinsic host restrictions to HIV-1 and mechanisms of viral escape. Nat. Immunol. 16 (2015), 546–553.
    • (2015) Nat. Immunol. , vol.16 , pp. 546-553
    • Simon, V.1    Bloch, N.2    Landau, N.R.3
  • 79
    • 84981271675 scopus 로고    scopus 로고
    • HIV-1 nef: taking control of protein trafficking
    • Pereira, E.A., daSilva, L.L., HIV-1 nef: taking control of protein trafficking. Traffic 17 (2016), 976–996.
    • (2016) Traffic , vol.17 , pp. 976-996
    • Pereira, E.A.1    daSilva, L.L.2
  • 81
    • 10344258588 scopus 로고    scopus 로고
    • HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail
    • Roeth, J.F., Williams, M., Kasper, M.R., Filzen, T.M., Collins, K.L., HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J. Cell Biol. 167 (2004), 903–913.
    • (2004) J. Cell Biol. , vol.167 , pp. 903-913
    • Roeth, J.F.1    Williams, M.2    Kasper, M.R.3    Filzen, T.M.4    Collins, K.L.5
  • 82
    • 0032055774 scopus 로고    scopus 로고
    • Nef interacts with mu subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC I molecules
    • Le Gall, S., Erdtmann, L., Benichou, S., Berlloz-Torrent, C., Liu, L., Benarous, R., Heard, J.M., Schwartz, O., Nef interacts with mu subunit of clathrin adaptor complexes and reveals a cryptic sorting signal in MHC I molecules. Immunity 8 (1998), 483–495.
    • (1998) Immunity , vol.8 , pp. 483-495
    • Le Gall, S.1    Erdtmann, L.2    Benichou, S.3    Berlloz-Torrent, C.4    Liu, L.5    Benarous, R.6    Heard, J.M.7    Schwartz, O.8
  • 83
    • 85021368920 scopus 로고    scopus 로고
    • Endocytic activity of HIV-1 Vpu: phosphoserine-dependent interactions with clathrin adaptors
    • Stoneham, C.A., Singh, R., Jia, X., Xiong, Y., Guatelli, J., Endocytic activity of HIV-1 Vpu: phosphoserine-dependent interactions with clathrin adaptors. Traffic 18 (2017), 545–561.
    • (2017) Traffic , vol.18 , pp. 545-561
    • Stoneham, C.A.1    Singh, R.2    Jia, X.3    Xiong, Y.4    Guatelli, J.5
  • 84
    • 0346601814 scopus 로고    scopus 로고
    • The physiological relevance of CD4 receptor down-modulation during HIV infection
    • Lama, J., The physiological relevance of CD4 receptor down-modulation during HIV infection. Curr. HIV Res. 1 (2003), 167–184.
    • (2003) Curr. HIV Res. , vol.1 , pp. 167-184
    • Lama, J.1
  • 86
    • 84944110470 scopus 로고    scopus 로고
    • SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef
    • Usami, Y., Wu, Y., Gottlinger, H.G., SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef. Nature 526 (2015), 218–223.
    • (2015) Nature , vol.526 , pp. 218-223
    • Usami, Y.1    Wu, Y.2    Gottlinger, H.G.3
  • 87
    • 0035794535 scopus 로고    scopus 로고
    • Mechanism for down-regulation of CD28 by Nef
    • Swigut, T., Shohdy, N., Skowronski, J., Mechanism for down-regulation of CD28 by Nef. EMBO J. 20 (2001), 1593–1604.
    • (2001) EMBO J. , vol.20 , pp. 1593-1604
    • Swigut, T.1    Shohdy, N.2    Skowronski, J.3
  • 88
    • 23244459907 scopus 로고    scopus 로고
    • Nef proteins from diverse groups of primate lentiviruses downmodulate CXCR4 to inhibit migration to the chemokine stromal derived factor 1
    • Hrecka, K., Swigut, T., Schindler, M., Kirchhoff, F., Skowronski, J., Nef proteins from diverse groups of primate lentiviruses downmodulate CXCR4 to inhibit migration to the chemokine stromal derived factor 1. J. Virol. 79 (2005), 10650–10659.
    • (2005) J. Virol. , vol.79 , pp. 10650-10659
    • Hrecka, K.1    Swigut, T.2    Schindler, M.3    Kirchhoff, F.4    Skowronski, J.5
  • 89
    • 23844471509 scopus 로고    scopus 로고
    • Human immunodeficiency virus Nef induces rapid internalization of the T-cell coreceptor CD8alphabeta
    • Stove, V., Van de Walle, I., Naessens, E., Coene, E., Stove, C., Plum, J., Verhasselt, B., Human immunodeficiency virus Nef induces rapid internalization of the T-cell coreceptor CD8alphabeta. J. Virol. 79 (2005), 11422–11433.
    • (2005) J. Virol. , vol.79 , pp. 11422-11433
    • Stove, V.1    Van de Walle, I.2    Naessens, E.3    Coene, E.4    Stove, C.5    Plum, J.6    Verhasselt, B.7
  • 91
    • 0038758782 scopus 로고    scopus 로고
    • Cooperative interactions of simian immunodeficiency virus Nef, AP-2, and CD3-zeta mediate the selective induction of T-cell receptor-CD3 endocytosis
    • Swigut, T., Greenberg, M., Skowronski, J., Cooperative interactions of simian immunodeficiency virus Nef, AP-2, and CD3-zeta mediate the selective induction of T-cell receptor-CD3 endocytosis. J. Virol. 77 (2003), 8116–8126.
    • (2003) J. Virol. , vol.77 , pp. 8116-8126
    • Swigut, T.1    Greenberg, M.2    Skowronski, J.3
  • 94
    • 0141521574 scopus 로고    scopus 로고
    • Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles
    • Schindler, M., Würfl, S., Benaroch, P., Greenough, T.C., Daniels, R., Easterbrook, P., Brenner, M., Münch, J., Kirchhoff, F., Down-modulation of mature major histocompatibility complex class II and up-regulation of invariant chain cell surface expression are well-conserved functions of human and simian immunodeficiency virus nef alleles. J. Virol. 77 (2003), 10548–10556.
    • (2003) J. Virol. , vol.77 , pp. 10548-10556
    • Schindler, M.1    Würfl, S.2    Benaroch, P.3    Greenough, T.C.4    Daniels, R.5    Easterbrook, P.6    Brenner, M.7    Münch, J.8    Kirchhoff, F.9
  • 95
    • 50149094043 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nef expression prevents AP-2-mediated internalization of the major histocompatibility complex class II-associated invariant chain
    • Toussaint, H., Gobert, F.X., Schindler, M., Banning, C., Kozik, P., Jouve, M., Kirchhoff, F., Benaroch, P., Human immunodeficiency virus type 1 nef expression prevents AP-2-mediated internalization of the major histocompatibility complex class II-associated invariant chain. J. Virol. 82 (2008), 8373–8382.
    • (2008) J. Virol. , vol.82 , pp. 8373-8382
    • Toussaint, H.1    Gobert, F.X.2    Schindler, M.3    Banning, C.4    Kozik, P.5    Jouve, M.6    Kirchhoff, F.7    Benaroch, P.8
  • 96
    • 49149110847 scopus 로고    scopus 로고
    • Competition model for upregulation of the major histocompatibility complex class II-associated invariant chain by human immunodeficiency virus type 1 Nef
    • Mitchell, R.S., Chaudhuri, R., Lindwasser, O.W., Tanaka, K.A., Lau, D., Murillo, R., Bonifacino, J.S., Guatelli, J.C., Competition model for upregulation of the major histocompatibility complex class II-associated invariant chain by human immunodeficiency virus type 1 Nef. J. Virol. 82 (2008), 7758–7767.
    • (2008) J. Virol. , vol.82 , pp. 7758-7767
    • Mitchell, R.S.1    Chaudhuri, R.2    Lindwasser, O.W.3    Tanaka, K.A.4    Lau, D.5    Murillo, R.6    Bonifacino, J.S.7    Guatelli, J.C.8
  • 97
    • 37849053288 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation
    • Hussain, A., Wesley, C., Khalid, M., Chaudhry, A., Jameel, S., Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation. J. Virol. 82 (2008), 893–902.
    • (2008) J. Virol. , vol.82 , pp. 893-902
    • Hussain, A.1    Wesley, C.2    Khalid, M.3    Chaudhry, A.4    Jameel, S.5
  • 99
  • 100
    • 34247129671 scopus 로고    scopus 로고
    • Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor
    • Chaudhuri, R., Lindwasser, O.W., Smith, W.J., Hurley, J.H., Bonifacino, J.S., Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor. J. Virol. 81 (2007), 3877–3890.
    • (2007) J. Virol. , vol.81 , pp. 3877-3890
    • Chaudhuri, R.1    Lindwasser, O.W.2    Smith, W.J.3    Hurley, J.H.4    Bonifacino, J.S.5
  • 101
    • 34548510349 scopus 로고    scopus 로고
    • HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2
    • Lubben, N.B., Sahlender, D.A., Motley, A.M., Lehner, P.J., Benaroch, P., Robinson, M.S., HIV-1 Nef-induced down-regulation of MHC class I requires AP-1 and clathrin but not PACS-1 and is impeded by AP-2. Mol. Biol. Cell 18 (2007), 3351–3365.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3351-3365
    • Lubben, N.B.1    Sahlender, D.A.2    Motley, A.M.3    Lehner, P.J.4    Benaroch, P.5    Robinson, M.S.6
  • 102
    • 0034713437 scopus 로고    scopus 로고
    • Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif
    • Craig, H.M., Reddy, T.R., Riggs, N.L., Dao, P.P., Guatelli, J.C., Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif. Virology 271 (2000), 9–17.
    • (2000) Virology , vol.271 , pp. 9-17
    • Craig, H.M.1    Reddy, T.R.2    Riggs, N.L.3    Dao, P.P.4    Guatelli, J.C.5
  • 104
    • 13444291133 scopus 로고    scopus 로고
    • Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes
    • Coleman, S.H., Van Damme, N., Day, J.R., Noviello, C.M., Hitchin, D., Madrid, R., Benichou, S., Guatelli, J.C., Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes. J. Virol. 79 (2005), 2066–2078.
    • (2005) J. Virol. , vol.79 , pp. 2066-2078
    • Coleman, S.H.1    Van Damme, N.2    Day, J.R.3    Noviello, C.M.4    Hitchin, D.5    Madrid, R.6    Benichou, S.7    Guatelli, J.C.8
  • 105
    • 84942814148 scopus 로고    scopus 로고
    • Interplay between the virus and the ubiquitin-proteasome system: molecular mechanism of viral pathogenesis
    • Luo, H., Interplay between the virus and the ubiquitin-proteasome system: molecular mechanism of viral pathogenesis. Curr. Opin. Virol. 17 (2016), 1–10.
    • (2016) Curr. Opin. Virol. , vol.17 , pp. 1-10
    • Luo, H.1
  • 106
    • 84987850271 scopus 로고    scopus 로고
    • Suppression of APOBEC3-mediated restriction of HIV-1 by vif
    • Feng, Y., Baig, T.T., Love, R.P., Chelico, L., Suppression of APOBEC3-mediated restriction of HIV-1 by vif. Front. Microbiol., 5, 2014, 450.
    • (2014) Front. Microbiol. , vol.5 , pp. 450
    • Feng, Y.1    Baig, T.T.2    Love, R.P.3    Chelico, L.4
  • 107
    • 85034439997 scopus 로고    scopus 로고
    • APOBEC enzymes as targets for virus and cancer therapy
    • Olson, M.E., Harris, R.S., Harki, D.A., APOBEC enzymes as targets for virus and cancer therapy. Cell Chem. Biol. 25 (2018), 36–49.
    • (2018) Cell Chem. Biol. , vol.25 , pp. 36-49
    • Olson, M.E.1    Harris, R.S.2    Harki, D.A.3
  • 110
    • 0033798414 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription
    • Dettenhofer, M., Cen, S., Carlson, B.A., Kleiman, L., Yu, X.F., Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription. J. Virol. 74 (2000), 8938–8945.
    • (2000) J. Virol. , vol.74 , pp. 8938-8945
    • Dettenhofer, M.1    Cen, S.2    Carlson, B.A.3    Kleiman, L.4    Yu, X.F.5
  • 111
    • 84866740475 scopus 로고    scopus 로고
    • Evolutionary conflicts between viruses and restriction factors shape immunity
    • Duggal, N.K., Emerman, M., Evolutionary conflicts between viruses and restriction factors shape immunity. Nat. Rev. Immunol. 12 (2012), 687–695.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 687-695
    • Duggal, N.K.1    Emerman, M.2
  • 112
    • 84982994774 scopus 로고    scopus 로고
    • Conservation and innovation of APOBEC3A restriction functions during primate evolution
    • McLaughlin, R.N. Jr, Gable, J.T., Wittkopp, C.J., Emerman, M., Malik, H.S., Conservation and innovation of APOBEC3A restriction functions during primate evolution. Mol. Biol. Evol. 33 (2016), 1889–1901.
    • (2016) Mol. Biol. Evol. , vol.33 , pp. 1889-1901
    • McLaughlin, R.N.1    Gable, J.T.2    Wittkopp, C.J.3    Emerman, M.4    Malik, H.S.5
  • 113
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • Schubert, U., Antón, L.C., Bacík, I., Cox, J.H., Bour, S., Bennink, J.R., Orlowski, M., Strebel, K., Yewdell, J.W., CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72 (1998), 2280–2288.
    • (1998) J. Virol. , vol.72 , pp. 2280-2288
    • Schubert, U.1    Antón, L.C.2    Bacík, I.3    Cox, J.H.4    Bour, S.5    Bennink, J.R.6    Orlowski, M.7    Strebel, K.8    Yewdell, J.W.9
  • 114
    • 0032012456 scopus 로고    scopus 로고
    • A novel human WD protein h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif
    • Margottin, F., Bour, S.P., Durand, H., Selig, L., Benichou, S., Richard, V., Thomas, D., Strebel, K., Benarous, R., A novel human WD protein h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol. Cell 1 (1998), 565–574.
    • (1998) Mol. Cell , vol.1 , pp. 565-574
    • Margottin, F.1    Bour, S.P.2    Durand, H.3    Selig, L.4    Benichou, S.5    Richard, V.6    Thomas, D.7    Strebel, K.8    Benarous, R.9
  • 115
    • 77954047969 scopus 로고    scopus 로고
    • Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps
    • Magadán, J.G., Pérez-Victoria, F.J., Sougrat, R., Ye, Y., Strebel, K., Bonifacino, J.S., Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathog., 6, 2010, e1000869.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000869
    • Magadán, J.G.1    Pérez-Victoria, F.J.2    Sougrat, R.3    Ye, Y.4    Strebel, K.5    Bonifacino, J.S.6
  • 116
    • 84855187526 scopus 로고    scopus 로고
    • HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/tetherin to overcome the virion release restriction
    • (e00036-11)
    • Schmidt, S., Fritz, J.V., Bitzegeio, J., Fackler, O.T., Keppler, O.T., HIV-1 Vpu blocks recycling and biosynthetic transport of the intrinsic immunity factor CD317/tetherin to overcome the virion release restriction. MBio, 2, 2011, 10.1128/mBio.00036-11 (e00036-11).
    • (2011) MBio , vol.2
    • Schmidt, S.1    Fritz, J.V.2    Bitzegeio, J.3    Fackler, O.T.4    Keppler, O.T.5
  • 117
    • 84937903128 scopus 로고    scopus 로고
    • HIV-1 Vpu utilizes both cullin-RING ligase (CRL) dependent and independent mechanisms to downmodulate host proteins
    • Ramirez, P.W., DePaula-Silva, A.B., Szaniawski, M., Barker, E., Bosque, A., Planelles, V., HIV-1 Vpu utilizes both cullin-RING ligase (CRL) dependent and independent mechanisms to downmodulate host proteins. Retrovirology, 12, 2015, 65.
    • (2015) Retrovirology , vol.12 , pp. 65
    • Ramirez, P.W.1    DePaula-Silva, A.B.2    Szaniawski, M.3    Barker, E.4    Bosque, A.5    Planelles, V.6
  • 118
    • 78650038839 scopus 로고    scopus 로고
    • Serine-threonine ubiquitination mediates downregulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu
    • Tokarev, A.A., Munguia, J., Guatelli, J.C., Serine-threonine ubiquitination mediates downregulation of BST-2/tetherin and relief of restricted virion release by HIV-1 Vpu. J. Virol. 85 (2011), 51–63.
    • (2011) J. Virol. , vol.85 , pp. 51-63
    • Tokarev, A.A.1    Munguia, J.2    Guatelli, J.C.3
  • 119
    • 84869194198 scopus 로고    scopus 로고
    • Innate sensing of HIV-1 assembly by Tetherin induces NFκB-dependent proinflammatory responses
    • Galão, R.P., Le Tortorec, A., Pickering, S., Kueck, T., Neil, S.J., Innate sensing of HIV-1 assembly by Tetherin induces NFκB-dependent proinflammatory responses. Cell Host Microbe 12 (2012), 633–644.
    • (2012) Cell Host Microbe , vol.12 , pp. 633-644
    • Galão, R.P.1    Le Tortorec, A.2    Pickering, S.3    Kueck, T.4    Neil, S.J.5
  • 120
    • 77956939580 scopus 로고    scopus 로고
    • Inhibition of lipid antigen presentation in dendritic cells by HIV-1 Vpu interference with CD1d recycling from endosomal compartments
    • Moll, M., Andersson, S.K., Smed-Sörensen, A., Sandberg, J.K., Inhibition of lipid antigen presentation in dendritic cells by HIV-1 Vpu interference with CD1d recycling from endosomal compartments. Blood 116 (2010), 1876–1884.
    • (2010) Blood , vol.116 , pp. 1876-1884
    • Moll, M.1    Andersson, S.K.2    Smed-Sörensen, A.3    Sandberg, J.K.4
  • 121
    • 78349264184 scopus 로고    scopus 로고
    • Degranulation of natural killer cells following interaction with HIV-1-infected cells is hindered by downmodulation of NTB-A by Vpu
    • Shah, A.H., Sowrirajan, B., Davis, Z.B., Ward, J.P., Campbell, E.M., Planelles, V., Barker, E., Degranulation of natural killer cells following interaction with HIV-1-infected cells is hindered by downmodulation of NTB-A by Vpu. Cell Host Microbe 8 (2010), 397–409.
    • (2010) Cell Host Microbe , vol.8 , pp. 397-409
    • Shah, A.H.1    Sowrirajan, B.2    Davis, Z.B.3    Ward, J.P.4    Campbell, E.M.5    Planelles, V.6    Barker, E.7
  • 122
    • 84861391185 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Nef and Vpu proteins downregulate the natural killer cell-activating ligand PVR
    • Matusali, G., Potestà M., Santoni, A., Cerboni, C., Doria, M., The human immunodeficiency virus type 1 Nef and Vpu proteins downregulate the natural killer cell-activating ligand PVR. J. Virol. 86 (2012), 4496–4504.
    • (2012) J. Virol. , vol.86 , pp. 4496-4504
    • Matusali, G.1    Potestà, M.2    Santoni, A.3    Cerboni, C.4    Doria, M.5
  • 124
    • 85030323086 scopus 로고    scopus 로고
    • Making sense of multifunctional proteins: human immunodeficiency virus type 1 accessory and regulatory proteins and connections to transcription
    • Faust, T.B., Binning, J.M., Gross, J.D., Frankel, A.D., Making sense of multifunctional proteins: human immunodeficiency virus type 1 accessory and regulatory proteins and connections to transcription. Annu. Rev. Virol. 4 (2017), 241–260.
    • (2017) Annu. Rev. Virol. , vol.4 , pp. 241-260
    • Faust, T.B.1    Binning, J.M.2    Gross, J.D.3    Frankel, A.D.4
  • 125
    • 85009513519 scopus 로고    scopus 로고
    • The HIV-1 vpr protein: a multifaceted target for therapeutic intervention
    • González, M.E., The HIV-1 vpr protein: a multifaceted target for therapeutic intervention. Int. J. Mol. Sci., 18, 2017, E126.
    • (2017) Int. J. Mol. Sci. , vol.18 , pp. E126
    • González, M.E.1
  • 129
    • 85039432245 scopus 로고    scopus 로고
    • HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase
    • Zhou, X., DeLucia, M., Hao, C., Hrecka, K., Monnie, C., Skowronski, J., Ahn, J., HIV-1 Vpr protein directly loads helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase. J. Biol. Chem. 292 (2017), 21117–21127.
    • (2017) J. Biol. Chem. , vol.292 , pp. 21117-21127
    • Zhou, X.1    DeLucia, M.2    Hao, C.3    Hrecka, K.4    Monnie, C.5    Skowronski, J.6    Ahn, J.7
  • 131
    • 84994434538 scopus 로고    scopus 로고
    • Activation of the DNA damage response is a conserved function of HIV-1 and HIV-2 vpr that is independent of SLX4 recruitment
    • Fregoso, O.I., Emerman, M., Activation of the DNA damage response is a conserved function of HIV-1 and HIV-2 vpr that is independent of SLX4 recruitment. MBio 7 (2016), e01433–16.
    • (2016) MBio , vol.7 , pp. e01433-16
    • Fregoso, O.I.1    Emerman, M.2
  • 133
    • 84857347109 scopus 로고    scopus 로고
    • The ability of primate lentiviruses to degrade the monocyte restriction factor SAMHD1 preceded the birth of the viral accessory protein Vpx
    • Lim, E.S., Fregoso, O.I., McCoy, C.O., Matsen, F.A., Malik, H.S., Emerman, M., The ability of primate lentiviruses to degrade the monocyte restriction factor SAMHD1 preceded the birth of the viral accessory protein Vpx. Cell Host Microbe 11 (2012), 194–204.
    • (2012) Cell Host Microbe , vol.11 , pp. 194-204
    • Lim, E.S.1    Fregoso, O.I.2    McCoy, C.O.3    Matsen, F.A.4    Malik, H.S.5    Emerman, M.6
  • 134
    • 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, X.F., A novel DCAF1-binding motif required for Vpx-mediated degradation of nuclear SAMHD1 and Vpr-induced G2 arrest. Cell. Microbiol. 14 (2012), 1745–1756.
    • (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
  • 138
    • 84884745681 scopus 로고    scopus 로고
    • Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1
    • Fregoso, O.I., Ahn, J., Wang, C., Mehrens, J., Skowronski, J., Emerman, M., Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1. PLoS Pathog., 9, 2013, e1003496.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003496
    • Fregoso, O.I.1    Ahn, J.2    Wang, C.3    Mehrens, J.4    Skowronski, J.5    Emerman, M.6
  • 139
    • 84891358983 scopus 로고    scopus 로고
    • Antagonism of SAMHD1 is actively maintained in natural infections of simian immunodeficiency virus
    • Spragg, C.J., Emerman, M., Antagonism of SAMHD1 is actively maintained in natural infections of simian immunodeficiency virus. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 21136–21141.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 21136-21141
    • Spragg, C.J.1    Emerman, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.