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Volumn 6, Issue 11, 2011, Pages

Nuclear exportin receptor cas regulates the NPI-1-mediated nuclear import of HIV-1 vpr

Author keywords

[No Author keywords available]

Indexed keywords

ARMADILLO DOMAIN PROTEIN; CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN; HUMAN IMMUNODEFICIENCY VIRUS PROTEIN; ISOPROTEIN; NUCLEAR PROTEIN; PROTEIN NPI 1; PROTEIN QIP1; PROTEIN RCH1; UNCLASSIFIED DRUG; VPR PROTEIN; DIGITONIN; GLUTATHIONE TRANSFERASE; KARYOPHERIN ALPHA; KARYOPHERIN ALPHA 2; KPNA1 PROTEIN, HUMAN; KPNA4 PROTEIN, HUMAN; VPR PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 81155131430     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0027815     Document Type: Article
Times cited : (15)

References (52)
  • 1
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich D, Mattaj IW, (1996) Nucleocytoplasmic transport. Science 271: 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 3
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: taking an inventory
    • Fried H, Kutay U, (2003) Nucleocytoplasmic transport: taking an inventory. Cell Mol Life Sci 60: 1659-1688.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 4
    • 0036846540 scopus 로고    scopus 로고
    • Importin alpha can migrate into the nucleus in an importin beta- and Ran-independent manner
    • Miyamoto Y, Hieda M, Harreman MT, Fukumoto M, Saiwaki T, et al. (2002) Importin alpha can migrate into the nucleus in an importin beta- and Ran-independent manner. EMBO J 21: 5833-5842.
    • (2002) EMBO J , vol.21 , pp. 5833-5842
    • Miyamoto, Y.1    Hieda, M.2    Harreman, M.T.3    Fukumoto, M.4    Saiwaki, T.5
  • 5
    • 14744267687 scopus 로고    scopus 로고
    • Importin-alpha promotes passage through the nuclear pore complex of human immunodeficiency virus type 1 Vpr
    • Kamata M, Nitahara-Kasahara Y, Miyamoto Y, Yoneda Y, Aida Y, (2005) Importin-alpha promotes passage through the nuclear pore complex of human immunodeficiency virus type 1 Vpr. J Virol 79: 3557-3564.
    • (2005) J Virol , vol.79 , pp. 3557-3564
    • Kamata, M.1    Nitahara-Kasahara, Y.2    Miyamoto, Y.3    Yoneda, Y.4    Aida, Y.5
  • 6
    • 34248403282 scopus 로고    scopus 로고
    • Novel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages
    • Nitahara-Kasahara Y, Kamata M, Yamamoto T, Zhang X, Miyamoto Y, et al. (2007) Novel nuclear import of Vpr promoted by importin alpha is crucial for human immunodeficiency virus type 1 replication in macrophages. J Virol 81: 5284-5293.
    • (2007) J Virol , vol.81 , pp. 5284-5293
    • Nitahara-Kasahara, Y.1    Kamata, M.2    Yamamoto, T.3    Zhang, X.4    Miyamoto, Y.5
  • 7
    • 16344379538 scopus 로고    scopus 로고
    • Importin alpha transports CaMKIV to the nucleus without utilizing importin beta
    • Kotera I, Sekimoto T, Miyamoto Y, Saiwaki T, Nagoshi E, et al. (2005) Importin alpha transports CaMKIV to the nucleus without utilizing importin beta. EMBO J 24: 942-951.
    • (2005) EMBO J , vol.24 , pp. 942-951
    • Kotera, I.1    Sekimoto, T.2    Miyamoto, Y.3    Saiwaki, T.4    Nagoshi, E.5
  • 8
    • 0032547742 scopus 로고    scopus 로고
    • Determination of the functional domain organization of the importin alpha nuclear import factor
    • Herold A, Truant R, Wiegand H, Cullen BR, (1998) Determination of the functional domain organization of the importin alpha nuclear import factor. J Cell Biol 143: 309-318.
    • (1998) J Cell Biol , vol.143 , pp. 309-318
    • Herold, A.1    Truant, R.2    Wiegand, H.3    Cullen, B.R.4
  • 9
    • 76649143068 scopus 로고    scopus 로고
    • Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import
    • Ogawa Y, Miyamoto Y, Asally M, Oka M, Yasuda Y, et al. (2010) Two isoforms of Npap60 (Nup50) differentially regulate nuclear protein import. Mol Biol Cell 21: 630-638.
    • (2010) Mol Biol Cell , vol.21 , pp. 630-638
    • Ogawa, Y.1    Miyamoto, Y.2    Asally, M.3    Oka, M.4    Yasuda, Y.5
  • 10
    • 77958515324 scopus 로고    scopus 로고
    • Novel importin-alpha family member Kpna7 is required for normal fertility and fecundity in the mouse
    • Hu J, Wang F, Yuan Y, Zhu X, Wang Y, et al. (2010) Novel importin-alpha family member Kpna7 is required for normal fertility and fecundity in the mouse. J Biol Chem 285: 33113-33122.
    • (2010) J Biol Chem , vol.285 , pp. 33113-33122
    • Hu, J.1    Wang, F.2    Yuan, Y.3    Zhu, X.4    Wang, Y.5
  • 11
    • 77955375151 scopus 로고    scopus 로고
    • Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha family of nuclear import receptors
    • Kelley JB, Talley AM, Spencer A, Gioeli D, Paschal BM, (2010) Karyopherin alpha7 (KPNA7), a divergent member of the importin alpha family of nuclear import receptors. BMC Cell Biol 11: 63.
    • (2010) BMC Cell Biol , vol.11 , pp. 63
    • Kelley, J.B.1    Talley, A.M.2    Spencer, A.3    Gioeli, D.4    Paschal, B.M.5
  • 12
    • 67649452381 scopus 로고    scopus 로고
    • The role of the nuclear transport system in cell differentiation
    • Yasuhara N, Oka M, Yoneda Y, (2009) The role of the nuclear transport system in cell differentiation. Semin Cell Dev Biol 20: 590-599.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 590-599
    • Yasuhara, N.1    Oka, M.2    Yoneda, Y.3
  • 13
    • 33845888271 scopus 로고    scopus 로고
    • Triggering neural differentiation of ES cells by subtype switching of importin-alpha
    • Yasuhara N, Shibazaki N, Tanaka S, Nagai M, Kamikawa Y, et al. (2007) Triggering neural differentiation of ES cells by subtype switching of importin-alpha. Nat Cell Biol 9: 72-79.
    • (2007) Nat Cell Biol , vol.9 , pp. 72-79
    • Yasuhara, N.1    Shibazaki, N.2    Tanaka, S.3    Nagai, M.4    Kamikawa, Y.5
  • 15
    • 0031975959 scopus 로고    scopus 로고
    • HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection
    • Vodicka MA, Koepp DM, Silver PA, Emerman M, (1998) HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection. Genes Dev 12: 175-185.
    • (1998) Genes Dev , vol.12 , pp. 175-185
    • Vodicka, M.A.1    Koepp, D.M.2    Silver, P.A.3    Emerman, M.4
  • 16
    • 18844468523 scopus 로고    scopus 로고
    • Viral protein R regulates nuclear import of the HIV-1 pre-integration complex
    • Popov S, Rexach M, Zybarth G, Reiling N, Lee MA, et al. (1998) Viral protein R regulates nuclear import of the HIV-1 pre-integration complex. EMBO J 17: 909-917.
    • (1998) EMBO J , vol.17 , pp. 909-917
    • Popov, S.1    Rexach, M.2    Zybarth, G.3    Reiling, N.4    Lee, M.A.5
  • 17
    • 0030250588 scopus 로고    scopus 로고
    • HIV-1, Vpr and the cell cycle
    • Emerman M, (1996) HIV-1, Vpr and the cell cycle. Curr Biol 6: 1096-1103.
    • (1996) Curr Biol , vol.6 , pp. 1096-1103
    • Emerman, M.1
  • 18
    • 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, et al. (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.
    • (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
  • 19
    • 0032504065 scopus 로고    scopus 로고
    • Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents
    • Poon B, Grovit-Ferbas K, Stewart SA, Chen IS, (1998) Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents. Science 281: 266-269.
    • (1998) Science , vol.281 , pp. 266-269
    • Poon, B.1    Grovit-Ferbas, K.2    Stewart, S.A.3    Chen, I.S.4
  • 20
    • 0036776455 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 (HIV-1) accessory protein Vpr induces transcription of the HIV-1 and glucocorticoid-responsive promoters by binding directly to p300/CBP coactivators
    • Kino T, Gragerov A, Slobodskaya O, Tsopanomichalou M, Chrousos GP, et al. (2002) Human immunodeficiency virus type 1 (HIV-1) accessory protein Vpr induces transcription of the HIV-1 and glucocorticoid-responsive promoters by binding directly to p300/CBP coactivators. J Virol 76: 9724-9734.
    • (2002) J Virol , vol.76 , pp. 9724-9734
    • Kino, T.1    Gragerov, A.2    Slobodskaya, O.3    Tsopanomichalou, M.4    Chrousos, G.P.5
  • 21
    • 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, et al. (2007) Human immunodeficiency virus type 1 Vpr interacts with spliceosomal protein SAP145 to mediate cellular pre-mRNA splicing inhibition. Microbes Infect 9: 490-497.
    • (2007) Microbes Infect , vol.9 , pp. 490-497
    • Hashizume, C.1    Kuramitsu, M.2    Zhang, X.3    Kurosawa, T.4    Kamata, M.5
  • 22
    • 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, et al. (2005) A novel role for Vpr of human immunodeficiency virus type 1 as a regulator of the splicing of cellular pre-mRNA. Microbes Infect 7: 1150-1160.
    • (2005) Microbes Infect , vol.7 , pp. 1150-1160
    • Kuramitsu, M.1    Hashizume, C.2    Yamamoto, N.3    Azuma, A.4    Kamata, M.5
  • 24
    • 77956221542 scopus 로고    scopus 로고
    • HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome
    • Li G, Elder RT, Dubrovsky L, Liang D, Pushkarsky T, et al. (2010) HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome. PLoS One 5: e11371.
    • (2010) PLoS One , vol.5
    • Li, G.1    Elder, R.T.2    Dubrovsky, L.3    Liang, D.4    Pushkarsky, T.5
  • 25
    • 0033942182 scopus 로고    scopus 로고
    • Two putative alpha-helical domains of human immunodeficiency virus type 1 Vpr mediate nuclear localization by at least two mechanisms
    • Kamata M, Aida Y, (2000) Two putative alpha-helical domains of human immunodeficiency virus type 1 Vpr mediate nuclear localization by at least two mechanisms. J Virol 74: 7179-7186.
    • (2000) J Virol , vol.74 , pp. 7179-7186
    • Kamata, M.1    Aida, Y.2
  • 26
    • 0031902773 scopus 로고    scopus 로고
    • HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr
    • Bukrinsky MI, Haffar OK, (1998) HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr. Mol Med 4: 138-143.
    • (1998) Mol Med , vol.4 , pp. 138-143
    • Bukrinsky, M.I.1    Haffar, O.K.2
  • 27
    • 0031799691 scopus 로고    scopus 로고
    • Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex
    • Fouchier RA, Meyer BE, Simon JH, Fischer U, Albright AV, et al. (1998) Interaction of the human immunodeficiency virus type 1 Vpr protein with the nuclear pore complex. J Virol 72: 6004-6013.
    • (1998) J Virol , vol.72 , pp. 6004-6013
    • Fouchier, R.A.1    Meyer, B.E.2    Simon, J.H.3    Fischer, U.4    Albright, A.V.5
  • 28
    • 0347298811 scopus 로고    scopus 로고
    • Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1
    • Le Rouzic E, Mousnier A, Rustum C, Stutz F, Hallberg E, et al. (2002) Docking of HIV-1 Vpr to the nuclear envelope is mediated by the interaction with the nucleoporin hCG1. J Biol Chem 277: 45091-45098.
    • (2002) J Biol Chem , vol.277 , pp. 45091-45098
    • Le Rouzic, E.1    Mousnier, A.2    Rustum, C.3    Stutz, F.4    Hallberg, E.5
  • 29
    • 60849111935 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 (HIV-1) nuclear import via Vpr-Importin alpha interactions as a novel HIV-1 therapy
    • Suzuki T, Yamamoto N, Nonaka M, Hashimoto Y, Matsuda G, et al. (2009) Inhibition of human immunodeficiency virus type 1 (HIV-1) nuclear import via Vpr-Importin alpha interactions as a novel HIV-1 therapy. Biochem Biophys Res Commun 380: 838-843.
    • (2009) Biochem Biophys Res Commun , vol.380 , pp. 838-843
    • Suzuki, T.1    Yamamoto, N.2    Nonaka, M.3    Hashimoto, Y.4    Matsuda, G.5
  • 31
    • 69449108433 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr: functions and molecular interactions
    • Romani B, Engelbrecht S, (2009) Human immunodeficiency virus type 1 Vpr: functions and molecular interactions. J Gen Virol 90: 1795-1805.
    • (2009) J Gen Virol , vol.90 , pp. 1795-1805
    • Romani, B.1    Engelbrecht, S.2
  • 32
    • 33044503759 scopus 로고    scopus 로고
    • Vpr R77Q is associated with long-term nonprogressive HIV infection and impaired induction of apoptosis
    • Lum JJ, Cohen OJ, Nie Z, Weaver JG, Gomez TS, et al. (2003) Vpr R77Q is associated with long-term nonprogressive HIV infection and impaired induction of apoptosis. J Clin Invest 111: 1547-1554.
    • (2003) J Clin Invest , vol.111 , pp. 1547-1554
    • Lum, J.J.1    Cohen, O.J.2    Nie, Z.3    Weaver, J.G.4    Gomez, T.S.5
  • 33
    • 0033604307 scopus 로고    scopus 로고
    • A carboxy-terminally truncated form of the Vpr protein of human immunodeficiency virus type 1 retards cell proliferation independently of G(2) arrest of the cell cycle
    • Nishizawa M, Myojin T, Nishino Y, Nakai Y, Kamata M, et al. (1999) A carboxy-terminally truncated form of the Vpr protein of human immunodeficiency virus type 1 retards cell proliferation independently of G(2) arrest of the cell cycle. Virology 263: 313-322.
    • (1999) Virology , vol.263 , pp. 313-322
    • Nishizawa, M.1    Myojin, T.2    Nishino, Y.3    Nakai, Y.4    Kamata, M.5
  • 34
    • 0033050673 scopus 로고    scopus 로고
    • Mutational analysis of Vpr-induced G2 arrest, nuclear localization, and cell death in fission yeast
    • Chen M, Elder RT, Yu M, O'Gorman MG, Selig L, et al. (1999) Mutational analysis of Vpr-induced G2 arrest, nuclear localization, and cell death in fission yeast. J Virol 73: 3236-3245.
    • (1999) J Virol , vol.73 , pp. 3236-3245
    • Chen, M.1    Elder, R.T.2    Yu, M.3    O'Gorman, M.G.4    Selig, L.5
  • 35
    • 77956621342 scopus 로고    scopus 로고
    • Importin {alpha}3 Interacts with HIV-1 Integrase and Contributes to HIV-1 Nuclear Import and Replication
    • Ao Z, Danappa Jayappa K, Wang B, Zheng Y, Kung S, et al. (2010) Importin {alpha}3 Interacts with HIV-1 Integrase and Contributes to HIV-1 Nuclear Import and Replication. J Virol 84: 8650-8663.
    • (2010) J Virol , vol.84 , pp. 8650-8663
    • Ao, Z.1    Danappa Jayappa, K.2    Wang, B.3    Zheng, Y.4    Kung, S.5
  • 36
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang P, Palese P, O'Neill RE, (1997) The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J Virol 71: 1850-1856.
    • (1997) J Virol , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 37
    • 20844458749 scopus 로고    scopus 로고
    • The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding
    • Cook A, Fernandez E, Lindner D, Ebert J, Schlenstedt G, et al. (2005) The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Mol Cell 18: 355-367.
    • (2005) Mol Cell , vol.18 , pp. 355-367
    • Cook, A.1    Fernandez, E.2    Lindner, D.3    Ebert, J.4    Schlenstedt, G.5
  • 38
    • 49649128856 scopus 로고    scopus 로고
    • Single-molecule measurements of importin alpha/cargo complex dissociation at the nuclear pore
    • Sun C, Yang W, Tu LC, Musser SM, (2008) Single-molecule measurements of importin alpha/cargo complex dissociation at the nuclear pore. Proc Natl Acad Sci U S A 105: 8613-8618.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8613-8618
    • Sun, C.1    Yang, W.2    Tu, L.C.3    Musser, S.M.4
  • 39
    • 0032520546 scopus 로고    scopus 로고
    • Arginine residues in the C-terminus of HIV-1 Vpr are important for nuclear localization and cell cycle arrest
    • Zhou Y, Lu Y, Ratner L, (1998) Arginine residues in the C-terminus of HIV-1 Vpr are important for nuclear localization and cell cycle arrest. Virology 242: 414-424.
    • (1998) Virology , vol.242 , pp. 414-424
    • Zhou, Y.1    Lu, Y.2    Ratner, L.3
  • 40
    • 0032538829 scopus 로고    scopus 로고
    • Characterization of HIV-1 vpr nuclear import: analysis of signals and pathways
    • Jenkins Y, McEntee M, Weis K, Greene WC, (1998) Characterization of HIV-1 vpr nuclear import: analysis of signals and pathways. J Cell Biol 143: 875-885.
    • (1998) J Cell Biol , vol.143 , pp. 875-885
    • Jenkins, Y.1    McEntee, M.2    Weis, K.3    Greene, W.C.4
  • 41
    • 38649100975 scopus 로고    scopus 로고
    • Localization of HIV-1 Vpr to the nuclear envelope: impact on Vpr functions and virus replication in macrophages
    • Jacquot G, Le Rouzic E, David A, Mazzolini J, Bouchet J, et al. (2007) Localization of HIV-1 Vpr to the nuclear envelope: impact on Vpr functions and virus replication in macrophages. Retrovirology 4: 84.
    • (2007) Retrovirology , vol.4 , pp. 84
    • Jacquot, G.1    Le Rouzic, E.2    David, A.3    Mazzolini, J.4    Bouchet, J.5
  • 42
    • 0032950628 scopus 로고    scopus 로고
    • Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha
    • Kobe B, (1999) Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin alpha. Nat Struct Biol 6: 388-397.
    • (1999) Nat Struct Biol , vol.6 , pp. 388-397
    • Kobe, B.1
  • 43
    • 0034666051 scopus 로고    scopus 로고
    • Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex
    • Agostini I, Popov S, Li J, Dubrovsky L, Hao T, et al. (2000) Heat-shock protein 70 can replace viral protein R of HIV-1 during nuclear import of the viral preintegration complex. Experimental cell research 259: 398-403.
    • (2000) Experimental Cell Research , vol.259 , pp. 398-403
    • Agostini, I.1    Popov, S.2    Li, J.3    Dubrovsky, L.4    Hao, T.5
  • 44
    • 0035827596 scopus 로고    scopus 로고
    • A gamma-2 herpesvirus nucleocytoplasmic shuttle protein interacts with importin alpha 1 and alpha 5
    • Goodwin DJ, Whitehouse A, (2001) A gamma-2 herpesvirus nucleocytoplasmic shuttle protein interacts with importin alpha 1 and alpha 5. J Biol Chem 276: 19905-19912.
    • (2001) J Biol Chem , vol.276 , pp. 19905-19912
    • Goodwin, D.J.1    Whitehouse, A.2
  • 45
    • 19044367766 scopus 로고    scopus 로고
    • Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5
    • Fagerlund R, Melen K, Kinnunen L, Julkunen I, (2002) Arginine/lysine-rich nuclear localization signals mediate interactions between dimeric STATs and importin alpha 5. J Biol Chem 277: 30072-30078.
    • (2002) J Biol Chem , vol.277 , pp. 30072-30078
    • Fagerlund, R.1    Melen, K.2    Kinnunen, L.3    Julkunen, I.4
  • 46
    • 0041344551 scopus 로고    scopus 로고
    • Importin alpha nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein
    • Melen K, Fagerlund R, Franke J, Kohler M, Kinnunen L, et al. (2003) Importin alpha nuclear localization signal binding sites for STAT1, STAT2, and influenza A virus nucleoprotein. J Biol Chem 278: 28193-28200.
    • (2003) J Biol Chem , vol.278 , pp. 28193-28200
    • Melen, K.1    Fagerlund, R.2    Franke, J.3    Kohler, M.4    Kinnunen, L.5
  • 47
    • 33847624936 scopus 로고    scopus 로고
    • Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit
    • Tarendeau F, Boudet J, Guilligay D, Mas PJ, Bougault CM, et al. (2007) Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit. Nat Struct Mol Biol 14: 229-233.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 229-233
    • Tarendeau, F.1    Boudet, J.2    Guilligay, D.3    Mas, P.J.4    Bougault, C.M.5
  • 48
    • 64749102559 scopus 로고    scopus 로고
    • Role of Vpr in HIV-1 nuclear import: therapeutic implications
    • Aida Y, Matsuda G, (2009) Role of Vpr in HIV-1 nuclear import: therapeutic implications. Curr HIV Res 7: 136-143.
    • (2009) Curr HIV Res , vol.7 , pp. 136-143
    • Aida, Y.1    Matsuda, G.2
  • 49
    • 77950659445 scopus 로고    scopus 로고
    • The macrophage in HIV-1 infection: from activation to deactivation?
    • Herbein G, Varin A, (2010) The macrophage in HIV-1 infection: from activation to deactivation? Retrovirology 7: 33.
    • (2010) Retrovirology , vol.7 , pp. 33
    • Herbein, G.1    Varin, A.2
  • 50
    • 78649710011 scopus 로고    scopus 로고
    • Identification of a novel Vpr-binding compound that inhibits HIV-1 multiplication in macrophages by chemical array
    • Hagiwara K, Murakami T, Xue G, Shimizu Y, Takeda E, et al. (2010) Identification of a novel Vpr-binding compound that inhibits HIV-1 multiplication in macrophages by chemical array. Biochem Biophys Res Commun.
    • (2010) Biochem Biophys Res Commun
    • Hagiwara, K.1    Murakami, T.2    Xue, G.3    Shimizu, Y.4    Takeda, E.5
  • 51
    • 0031575854 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr gene product prevents cell proliferation on mouse NIH3T3 cells without the G2 arrest of the cell cycle
    • Nishino Y, Myojin T, Kamata M, Aida Y, (1997) Human immunodeficiency virus type 1 Vpr gene product prevents cell proliferation on mouse NIH3T3 cells without the G2 arrest of the cell cycle. Biochem Biophys Res Commun 232: 550-554.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 550-554
    • Nishino, Y.1    Myojin, T.2    Kamata, M.3    Aida, Y.4
  • 52
    • 39749184106 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr inhibits axonal outgrowth through induction of mitochondrial dysfunction
    • Kitayama H, Miura Y, Ando Y, Hoshino S, Ishizaka Y, et al. (2008) Human immunodeficiency virus type 1 Vpr inhibits axonal outgrowth through induction of mitochondrial dysfunction. J Virol 82: 2528-2542.
    • (2008) J Virol , vol.82 , pp. 2528-2542
    • Kitayama, H.1    Miura, Y.2    Ando, Y.3    Hoshino, S.4    Ishizaka, Y.5


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