메뉴 건너뛰기




Volumn 5, Issue 6, 2010, Pages

HIV-1 replication through hHR23A-mediated interaction of Vpr with 26S proteasome

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PROTEASOME; PROTEIN HHR23A; PROTEIN MTS2; PROTEIN MTS4; PROTEIN S5A; PROTEINASE; UNCLASSIFIED DRUG; VPR PROTEIN;

EID: 77956221542     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0011371     Document Type: Article
Times cited : (10)

References (59)
  • 1
    • 0028239060 scopus 로고
    • The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells
    • USA
    • Heinzinger N, Bukinsky M, Haggerty S, Ragland A, Kewalramani V, et al. (1994) The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells. Proc Nat Acad Sci USA 91(15): 7311-5.
    • (1994) Proc Nat Acad Sci , vol.91 , Issue.15 , pp. 7311-7315
    • Heinzinger, N.1    Bukinsky, M.2    Haggerty, S.3    Ragland, A.4    Kewalramani, V.5
  • 2
    • 0028853961 scopus 로고
    • Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity
    • He J, Choe S, Walker R, Di Marzio PD, Morgan DO, et al. (1995) Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity. J Virol 69(11): 6705-11.
    • (1995) J Virol , vol.69 , Issue.11 , pp. 6705-6711
    • He, J.1    Choe, S.2    Walker, R.3    Di Marzio, P.D.4    Morgan, D.O.5
  • 3
    • 0030920243 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest
    • Stewart SA, Poon B, Jowett JB, Chen IS (1997) Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest. J Virol 71(7): 5579-92.
    • (1997) J Virol , Issue.7 , pp. 5579-5592
    • Stewart, S.A.1    Poon, B.2    Jowett, J.B.3    Chen, I.S.4
  • 4
    • 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 ISY (1998) Cell cycle arrest by Vpr in HIV-1 virions and insensitivity to antiretroviral agents. Science 281(5374): 266-9.
    • (1998) Science , vol.281 , Issue.5374 , pp. 266-269
    • Poon, B.1    Grovit-Ferbas, K.2    Stewart, S.A.3    Chen, I.S.Y.4
  • 5
    • 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(1): 65-71.
    • (1998) Nat Med , vol.4 , Issue.1 , pp. 65-71
    • Goh, W.C.1    Rogel, M.E.2    Kinsey, C.M.3    Michael, S.F.4    Fultz, P.N.5
  • 6
    • 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(10): 1547-54.
    • (2003) J Clin Invest , vol.111 , Issue.10 , pp. 1547-1554
    • Lum, J.J.1    Cohen, O.J.2    Nie, Z.3    Weaver, J.G.4    Gomez, T.S.5
  • 7
    • 0032557445 scopus 로고    scopus 로고
    • Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex
    • Popov S, Rexach M, Ratner L, Blobel G, Bukrinsky M (1998) Viral protein R regulates docking of the HIV-1 preintegration complex to the nuclear pore complex. J Biol Chem 273(21): 13347-52.
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 13347-13352
    • Popov, S.1    Rexach, M.2    Ratner, L.3    Blobel, G.4    Bukrinsky, M.5
  • 8
    • 0028842207 scopus 로고
    • Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phago- cytes
    • Connor RI, Chen BK, Choe S, Landau NR (1995) Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phago- cytes. Virology 206(2): 935-44.
    • (1995) Virology , vol.206 , Issue.2 , pp. 935-944
    • Connor, R.I.1    Chen, B.K.2    Choe, S.3    Landau, N.R.4
  • 9
    • 36049004869 scopus 로고    scopus 로고
    • Evidence for direct involvement of the capsid protein in HIV infection of nondividing cells
    • Yamashita M, Perez O, Hope TJ, Emerman M (2007) Evidence for direct involvement of the capsid protein in HIV infection of nondividing cells. PLoS Pathog 3(10): 1502-10.
    • (2007) PLoS Pathog , vol.3 , Issue.10 , pp. 1502-1510
    • Yamashita, M.1    Perez, O.2    Hope, T.J.3    Emerman, M.4
  • 10
    • 0000087784 scopus 로고    scopus 로고
    • HIV-1 nuclear import: In search of a leader
    • Bukrinsky MI, Haffar OK (1997) HIV-1 nuclear import: in search of a leader. Front Biosci 2(d578-87.
    • (1997) Front Biosci , vol.2
    • Bukrinsky, M.I.1    Haffar, O.K.2
  • 11
    • 44449129551 scopus 로고    scopus 로고
    • Primate lentiviral Vpx commandeers DDB1 to counteract a macrophage restriction
    • Sharova N, Wu Y, Zhu X, Stranska R, Kaushik R, et al. (2008) Primate lentiviral Vpx commandeers DDB1 to counteract a macrophage restriction. PLoS Pathog 4(5): e1000057.
    • (2008) PLoS Pathog , vol.4 , Issue.5
    • Sharova, N.1    Wu, Y.2    Zhu, X.3    Stranska, R.4    Kaushik, R.5
  • 12
    • 73949153266 scopus 로고    scopus 로고
    • Evidence for an activation domain at the amino terminus of simian immunodeficiency virus Vpx
    • Gramberg T, Sunseri N, Landau NR Evidence for an activation domain at the amino terminus of simian immunodeficiency virus Vpx. J Virol 84(3): 1387-96.
    • J Virol , vol.84 , Issue.3 , pp. 1387-1396
    • Gramberg, T.1    Sunseri, N.2    Landau, N.R.3
  • 13
    • 67651092299 scopus 로고    scopus 로고
    • A cellular restriction dictates the permissivity of nondividing monocytes/macrophages to lentivirus and gammaretrovirus infection
    • Kaushik R, Zhu X, Stranska R, Wu Y, Stevenson M (2009) A cellular restriction dictates the permissivity of nondividing monocytes/macrophages to lentivirus and gammaretrovirus infection. Cell Host Microbe 6(1): 68-80.
    • (2009) Cell Host Microbe , vol.6 , Issue.1 , pp. 68-80
    • Kaushik, R.1    Zhu, X.2    Stranska, R.3    Wu, Y.4    Stevenson, M.5
  • 15
    • 0037079693 scopus 로고    scopus 로고
    • Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination
    • Elder RT, Song XQ, Chen M, Hopkins KM, Lieberman HB, et al. (2002) Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination. Nucleic Acids Res 30(2): 581-91.
    • (2002) Nucleic Acids Res , vol.30 , Issue.2 , pp. 581-591
    • Elder, R.T.1    Song, X.Q.2    Chen, M.3    Hopkins, K.M.4    Lieberman, H.B.5
  • 16
    • 1342300578 scopus 로고    scopus 로고
    • Integral UBL domain proteins: A family of proteasome interacting proteins
    • Hartmann-Petersen R, Gordon C (2004) Integral UBL domain proteins: a family of proteasome interacting proteins. Semin Cell Dev Biol 15(2): 247-59.
    • (2004) Semin Cell Dev Biol , vol.15 , Issue.2 , pp. 247-259
    • Hartmann-Petersen, R.1    Gordon, C.2
  • 17
    • 0034762028 scopus 로고    scopus 로고
    • Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
    • Chen L, Shinde U, Ortolan TG, Madura K (2001) Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly. EMBO Rep 2(10): 933-8.
    • (2001) EMBO Rep , vol.2 , Issue.10 , pp. 933-938
    • Chen, L.1    Shinde, U.2    Ortolan, T.G.3    Madura, K.4
  • 18
    • 64749088422 scopus 로고    scopus 로고
    • HIV-1 viral protein R (Vpr) and its interactions with host cell
    • Li G, Bukrinsky M, Zhao RY (2009) HIV-1 viral protein R (Vpr) and its interactions with host cell. Curr HIV Res 7(2): 178-83.
    • (2009) Curr HIV Res , vol.7 , Issue.2 , pp. 178-183
    • Li, G.1    Bukrinsky, M.2    Zhao, R.Y.3
  • 19
    • 18844393683 scopus 로고    scopus 로고
    • HIV-1 viral protein R (Vpr) & host cellular responses
    • Zhao RY, Bukrinsky M, Elder RT (2005) HIV-1 viral protein R (Vpr) & host cellular responses. Indian J Med Res 121(4): 270-86.
    • (2005) Indian J Med Res , vol.121 , Issue.4 , pp. 270-286
    • Zhao, R.Y.1    Bukrinsky, M.2    Elder, R.T.3
  • 20
    • 4644251531 scopus 로고    scopus 로고
    • Anti-Vpr activity of a yeast chaperone protein
    • Benko Z, Liang D, Agbottah E, Hou J, Chiu K, et al. (2004) Anti-Vpr activity of a yeast chaperone protein. J Virol 78(20): 11016-29.
    • (2004) J Virol , vol.78 , Issue.20 , pp. 11016-11029
    • Benko, Z.1    Liang, D.2    Agbottah, E.3    Hou, J.4    Chiu, K.5
  • 21
    • 33947503465 scopus 로고    scopus 로고
    • Antagonistic interaction of HIV-1 Vpr with Hsf-mediated cellular heat shock response and Hsp16 in fission yeast (Schizosaccharomyces pombe)
    • Benko Z, Liang D, Agbottah E, Hou J, Taricani L, et al. (2007) Antagonistic interaction of HIV-1 Vpr with Hsf-mediated cellular heat shock response and Hsp16 in fission yeast (Schizosaccharomyces pombe). Retrovirology 4(16.
    • (2007) Retrovirology , vol.4 , pp. 16
    • Benko, Z.1    Liang, D.2    Agbottah, E.3    Hou, J.4    Taricani, L.5    Et al.6
  • 23
    • 0035798131 scopus 로고    scopus 로고
    • Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr
    • de Noronha CM, Sherman MP, Lin HW, Cavrois MV, Moir RD, et al. (2001) Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr. Science 294(5544): 1105-8.
    • (2001) Science , vol.294 , Issue.5544 , pp. 1105-1108
    • de Noronha, C.M.1    Sherman, M.P.2    Lin, H.W.3    Cavrois, M.V.4    Moir, R.D.5
  • 24
    • 0041474703 scopus 로고    scopus 로고
    • Studies with GFP-Vpr fusion proteins: Induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization
    • Waldhuber MG, Bateson M, Tan J, Greenway AL, McPhee DA (2003) Studies with GFP-Vpr fusion proteins: induction of apoptosis but ablation of cell-cycle arrest despite nuclear membrane or nuclear localization. Virology 313(1): 91-104.
    • (2003) Virology , vol.313 , Issue.1 , pp. 91-104
    • Waldhuber, M.G.1    Bateson, M.2    Tan, J.3    Greenway, A.L.4    McPhee, D.A.5
  • 25
    • 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(47): 45091-8.
    • (2002) J Biol Chem , vol.277 , Issue.47 , pp. 45091-45098
    • Le Rouzic, E.1    Mousnier, A.2    Rustum, C.3    Stutz, F.4    Hallberg, E.5
  • 26
    • 0031713206 scopus 로고    scopus 로고
    • Fission yeast expression vectors adapted for positive identification of gene insertion and GFP fusion
    • Zhao Y, Elder RT, Chen MZ, Cao J (1998) Fission yeast expression vectors adapted for positive identification of gene insertion and GFP fusion. BioTechniques 25(3): 2-4.
    • (1998) BioTechniques , vol.25 , Issue.3 , pp. 2-4
    • Zhao, Y.1    Elder, R.T.2    Chen, M.Z.3    Cao, J.4
  • 27
    • 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(4): 3236-45.
    • (1999) J Virol , vol.73 , Issue.4 , pp. 3236-3245
    • Chen, M.1    Elder, R.T.2    Yu, M.3    O'Gorman, M.G.4    Selig, L.5
  • 28
    • 0038805579 scopus 로고    scopus 로고
    • Nuclear export of Vpr is required for efficient replication of human immunodeficiency virus type 1 in tissue macrophages
    • Sherman MP, de Noronha CM, Eckstein LA, Hataye J, Mundt P, et al. (2003) Nuclear export of Vpr is required for efficient replication of human immunodeficiency virus type 1 in tissue macrophages. J Virol 77(13): 7582-9.
    • (2003) J Virol , vol.77 , Issue.13 , pp. 7582-7589
    • Sherman, M.P.1    de Noronha, C.M.2    Eckstein, L.A.3    Hataye, J.4    Mundt, P.5
  • 29
    • 0035450254 scopus 로고    scopus 로고
    • HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25
    • Elder RT, Yu M, Chen M, Zhu X, Yanagida M, et al. (2001) HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25. Virology 287(2): 359-70.
    • (2001) Virology , vol.287 , Issue.2 , pp. 359-370
    • Elder, R.T.1    Yu, M.2    Chen, M.3    Zhu, X.4    Yanagida, M.5
  • 30
    • 0034720458 scopus 로고    scopus 로고
    • Identification of a 26S proteasome- associated UCH in fission yeast
    • Li T, Naqvi NI, Yang H, Teo TS (2000) Identification of a 26S proteasome- associated UCH in fission yeast. Biochem Biophys Res Commun 272(1): 270-5.
    • (2000) Biochem Biophys Res Commun , vol.272 , Issue.1 , pp. 270-275
    • Li, T.1    Naqvi, N.I.2    Yang, H.3    Teo, T.S.4
  • 31
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma R, Chen S, Feldman R, Schieltz D, Yates J, et al. (2000) Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell 11(10): 3425-39.
    • (2000) Mol Biol Cell , vol.11 , Issue.10 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5
  • 32
    • 0032486606 scopus 로고    scopus 로고
    • Pleiotropic effects of HIV-1 protein R (Vpr) on morphogenesis and cell survival in fission yeast and antagonism by pentoxifylline
    • Zhao Y, Yu M, Chen M, Elder RT, Yamamoto A, et al. (1998) Pleiotropic effects of HIV-1 protein R (Vpr) on morphogenesis and cell survival in fission yeast and antagonism by pentoxifylline. Virol 246(266-276.
    • (1998) Virol , vol.246 , pp. 266-276
    • Zhao, Y.1    Yu, M.2    Chen, M.3    Elder, R.T.4    Yamamoto, A.5    Et al.6
  • 33
    • 0034597619 scopus 로고    scopus 로고
    • Cut8, essential for anaphase, controls localization of 26S proteasome, facilitating destruction of cyclin and Cut2
    • Tatebe H, Yanagida M (2000) Cut8, essential for anaphase, controls localization of 26S proteasome, facilitating destruction of cyclin and Cut2. Curr Biol 10(21): 1329-38.
    • (2000) Curr Biol , vol.10 , Issue.21 , pp. 1329-1338
    • Tatebe, H.1    Yanagida, M.2
  • 34
    • 0032538881 scopus 로고    scopus 로고
    • Localization of the 26S proteasome during mitosis and meiosis in fission yeast
    • Wilkinson CR, Wallace M, Morphew M, Perry P, Allshire R, et al. (1998) Localization of the 26S proteasome during mitosis and meiosis in fission yeast. EMBO J 17(22): 6465-76.
    • (1998) EMBO J , vol.17 , Issue.22 , pp. 6465-6476
    • Wilkinson, C.R.1    Wallace, M.2    Morphew, M.3    Perry, P.4    Allshire, R.5
  • 35
    • 0030808452 scopus 로고    scopus 로고
    • Mts4, a non- ATPase subunit of the 26 S protease in fission yeast is essential for mitosis and interacts directly with the ATPase subunit Mts2
    • Wilkinson CR, Wallace M, Seeger M, Dubiel W, Gordon C (1997) Mts4, a non- ATPase subunit of the 26 S protease in fission yeast is essential for mitosis and interacts directly with the ATPase subunit Mts2. J Biol Chem 272(41): 25768-77.
    • (1997) J Biol Chem , vol.272 , Issue.41 , pp. 25768-25777
    • Wilkinson, C.R.1    Wallace, M.2    Seeger, M.3    Dubiel, W.4    Gordon, C.5
  • 36
    • 23744466996 scopus 로고    scopus 로고
    • Regulation of nuclear proteasome by Rhp6/ Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8
    • Takeda K, Yanagida M (2005) Regulation of nuclear proteasome by Rhp6/ Ubc2 through ubiquitination and destruction of the sensor and anchor Cut8. Cell 122(3): 393-405.
    • (2005) Cell , vol.122 , Issue.3 , pp. 393-405
    • Takeda, K.1    Yanagida, M.2
  • 37
    • 0030730822 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair
    • Withers-Ward ES, Jowett JB, Stewart SA, Xie YM, Garfinkel A, et al. (1997) Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair. J Virol 71(12): 9732-42.
    • (1997) J Virol , vol.71 , Issue.12 , pp. 9732-9742
    • Withers-Ward, E.S.1    Jowett, J.B.2    Stewart, S.A.3    Xie, Y.M.4    Garfinkel, A.5
  • 38
    • 34548566134 scopus 로고    scopus 로고
    • Intermediate- type 20 S proteasomes in HeLa cells: ''asymmetric'' subunit composition, diversity and adaptation
    • Klare N, Seeger M, Janek K, Jungblut PR, Dahlmann B (2007) Intermediate- type 20 S proteasomes in HeLa cells: ''asymmetric'' subunit composition, diversity and adaptation. J Mol Biol 373(1): 1-10.
    • (2007) J Mol Biol , vol.373 , Issue.1 , pp. 1-10
    • Klare, N.1    Seeger, M.2    Janek, K.3    Jungblut, P.R.4    Dahlmann, B.5
  • 39
    • 0032486250 scopus 로고    scopus 로고
    • HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr
    • Gragerov A, Kino T, Ilyina-Gragerova G, Chrousos GP, Pavlakis GN (1998) HHR23A, the human homologue of the yeast repair protein RAD23, interacts specifically with Vpr protein and prevents cell cycle arrest but not the transcriptional effects of Vpr. Virology 245(2): 323-30.
    • (1998) Virology , vol.245 , Issue.2 , pp. 323-330
    • Gragerov, A.1    Kino, T.2    Ilyina-Gragerova, G.3    Chrousos, G.P.4    Pavlakis, G.N.5
  • 40
    • 0031730342 scopus 로고    scopus 로고
    • Structure of a human DNA repair protein UBA domain that interacts with HIV- 1 Vpr
    • Dieckmann T, Withers-Ward ES, Jarosinski MA, Liu CF, Chen IS, et al. (1998) Structure of a human DNA repair protein UBA domain that interacts with HIV- 1 Vpr. Nat Struct Biol 5(12): 1042-7.
    • (1998) Nat Struct Biol , vol.5 , Issue.12 , pp. 1042-1047
    • Dieckmann, T.1    Withers-Ward, E.S.2    Jarosinski, M.A.3    Liu, C.F.4    Chen, I.S.5
  • 41
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    • Hiyama H, Yokoi M, Masutani C, Sugasawa K, Maekawa T, et al. (1999) Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome. J Biol Chem 274(39): 28019-25.
    • (1999) J Biol Chem , vol.274 , Issue.39 , pp. 28019-28025
    • Hiyama, H.1    Yokoi, M.2    Masutani, C.3    Sugasawa, K.4    Maekawa, T.5
  • 42
    • 0032510057 scopus 로고    scopus 로고
    • Rad23 links DNA repair to the ubiquitin/proteasome pathway
    • Schauber C, Chen L, Tongaonkar P, Vega I, Lambertson D, et al. (1998) Rad23 links DNA repair to the ubiquitin/proteasome pathway. Nature 391(6668): 715-8.
    • (1998) Nature , vol.391 , Issue.6668 , pp. 715-718
    • Schauber, C.1    Chen, L.2    Tongaonkar, P.3    Vega, I.4    Lambertson, D.5
  • 43
    • 0035138170 scopus 로고    scopus 로고
    • Human homologue of yeast Rad23 protein A interacts with p300/cyclic AMP-responsive element binding (CREB)- binding protein to down-regulate transcriptional activity of p53
    • Zhu Q, Wani G, Wani MA, Wani AA (2001) Human homologue of yeast Rad23 protein A interacts with p300/cyclic AMP-responsive element binding (CREB)- binding protein to down-regulate transcriptional activity of p53. Cancer Res 61(1): 64-70.
    • (2001) Cancer Res , vol.61 , Issue.1 , pp. 64-70
    • Zhu, Q.1    Wani, G.2    Wani, M.A.3    Wani, A.A.4
  • 44
    • 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(4): 909-17.
    • (1998) EMBO J , vol.17 , Issue.4 , pp. 909-917
    • Popov, S.1    Rexach, M.2    Zybarth, G.3    Reiling, N.4    Lee, M.A.5
  • 45
    • 34250851699 scopus 로고    scopus 로고
    • Depletion of mitochondrial DNA by down-regulation of deoxyguanosine kinase expression in non-proliferating HeLa cells
    • Franco M, Johansson M, Karlsson A (2007) Depletion of mitochondrial DNA by down-regulation of deoxyguanosine kinase expression in non-proliferating HeLa cells. Exp Cell Res 313(12): 2687-94.
    • (2007) Exp Cell Res , vol.313 , Issue.12 , pp. 2687-2694
    • Franco, M.1    Johansson, M.2    Karlsson, A.3
  • 46
    • 0141682702 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits
    • Apcher GS, Heink S, Zantopf D, Kloetzel PM, Schmid HP, et al. (2003) Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits. FEBS Lett 553(1-2): 200-4.
    • (2003) FEBS Lett , vol.553 , Issue.1-2 , pp. 200-204
    • Apcher, G.S.1    Heink, S.2    Zantopf, D.3    Kloetzel, P.M.4    Schmid, H.P.5
  • 47
    • 33846701783 scopus 로고    scopus 로고
    • SIVSM/HIV-2 Vpx proteins promote retroviral escape from a proteasome- dependent restriction pathway present in human dendritic cells
    • Goujon C, Riviere L, Jarrosson-Wuilleme L, Bernaud J, Rigal D, et al. (2007) SIVSM/HIV-2 Vpx proteins promote retroviral escape from a proteasome- dependent restriction pathway present in human dendritic cells. Retrovirology 4(2.
    • (2007) Retrovirology , vol.4 , pp. 2
    • Goujon, C.1    Riviere, L.2    Jarrosson-Wuilleme, L.3    Bernaud, J.4    Rigal, D.5    Et al.6
  • 48
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X, Yu Y, Liu B, Luo K, Kong W, et al. (2003) Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302(5647): 1056-60.
    • (2003) Science , vol.302 , Issue.5647 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5
  • 49
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • Sheehy AM, Gaddis NC, Malim MH (2003) The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med 9(11): 1404-7.
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 50
    • 34848911347 scopus 로고    scopus 로고
    • The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A- containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor
    • Wen X, Duus KM, Friedrich TD, de Noronha CM (2007) The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A- containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor. J Biol Chem 282(37): 27046-57.
    • (2007) J Biol Chem , vol.282 , Issue.37 , pp. 27046-27057
    • Wen, X.1    Duus, K.M.2    Friedrich, T.D.3    de Noronha, C.M.4
  • 51
    • 34547639932 scopus 로고    scopus 로고
    • HIV-1 Vpr- mediated G2 arrest involves the DDB1-CUL4AVPRBP E3 ubiquitin ligase
    • Belzile JP, Duisit G, Rougeau N, Mercier J, Finzi A, et al. (2007) HIV-1 Vpr- mediated G2 arrest involves the DDB1-CUL4AVPRBP E3 ubiquitin ligase. PLoS Pathog 3(7): e85.
    • (2007) PLoS Pathog , vol.3 , Issue.7
    • Belzile, J.P.1    Duisit, G.2    Rougeau, N.3    Mercier, J.4    Finzi, A.5
  • 52
    • 0035970307 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 Vpr with the HHR23A DNA repair protein does not correlate with multiple biological functions of Vpr
    • Mansky LM, Preveral S, Le Rouzic E, Bernard LC, Selig L, et al. (2001) Interaction of human immunodeficiency virus type 1 Vpr with the HHR23A DNA repair protein does not correlate with multiple biological functions of Vpr. Virology 282(1): 176-85.
    • (2001) Virology , vol.282 , Issue.1 , pp. 176-185
    • Mansky, L.M.1    Preveral, S.2    Le Rouzic, E.3    Bernard, L.C.4    Selig, L.5
  • 53
    • 77949392988 scopus 로고    scopus 로고
    • HIV-1 Vpr induces the K48-linked polyubiquitination and proteasomal degradation of target cellular proteins to activate ATR and promote G2 arrest
    • Belzile JP, Richard J, Rougeau N, Xiao Y, Cohen EA (2010) HIV-1 Vpr induces the K48-linked polyubiquitination and proteasomal degradation of target cellular proteins to activate ATR and promote G2 arrest. J Virol 84(7): 3320-30.
    • (2010) J Virol , vol.84 , Issue.7 , pp. 3320-3330
    • Belzile, J.P.1    Richard, J.2    Rougeau, N.3    Xiao, Y.4    Cohen, E.A.5
  • 54
    • 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. Exp Cell Res 259(2): 398-403.
    • (2000) Exp Cell Res , vol.259 , Issue.2 , pp. 398-403
    • Agostini, I.1    Popov, S.2    Li, J.3    Dubrovsky, L.4    Hao, T.5
  • 55
    • 44449107162 scopus 로고    scopus 로고
    • Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection
    • Srivastava S, Swanson SK, Manel N, Florens L, Washburn MP, et al. (2008) Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection. PLoS Pathog 4(5): e1000059.
    • (2008) PLoS Pathog 4(5) , vol.e1000059
    • Srivastava, S.1    Swanson, S.K.2    Manel, N.3    Florens, L.4    Washburn, M.P.5
  • 56
    • 0029843983 scopus 로고    scopus 로고
    • Effect of human immunodeficiency virus type 1 protein R (vpr) gene expression on basic cellular function of fission yeast Schizosaccharomyces pombe
    • Zhao Y, Cao J, O'Gorman MR, Yu M, Yogev R (1996) Effect of human immunodeficiency virus type 1 protein R (vpr) gene expression on basic cellular function of fission yeast Schizosaccharomyces pombe. J Virol 70(9): 5821-6.
    • (1996) J Virol , vol.70 , Issue.9 , pp. 5821-5826
    • Zhao, Y.1    Cao, J.2    O'Gorman, M.R.3    Yu, M.4    Yogev, R.5
  • 57
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S, Song O (1989) A novel genetic system to detect protein-protein interactions. Nature 340(6230): 245-6.
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 58
    • 0027379925 scopus 로고
    • Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit
    • Gordon C, McGurk G, Dillon P, Rosen C, Hastie ND (1993) Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit. Nature 366(6453): 355-7.
    • (1993) Nature , vol.366 , Issue.6453 , pp. 355-357
    • Gordon, C.1    McGurk, G.2    Dillon, P.3    Rosen, C.4    Hastie, N.D.5
  • 59
    • 40149104238 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces cell cycle G2 arrest through Srk1/MK2-mediated phosphorylation of Cdc25
    • Huard S, Elder RT, Liang D, Li G, Zhao RY (2008) Human immunodeficiency virus type 1 Vpr induces cell cycle G2 arrest through Srk1/MK2-mediated phosphorylation of Cdc25. J Virol 82(6): 2904-17.
    • (2008) J Virol , vol.82 , Issue.6 , pp. 2904-2917
    • Huard, S.1    Elder, R.T.2    Liang, D.3    Li, G.4    Zhao, R.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.