메뉴 건너뛰기




Volumn 19, Issue 3, 2006, Pages 349-362

Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN E1; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; VIRUS PROTEIN;

EID: 33750959438     PISSN: 08828245     EISSN: None     Source Type: Journal    
DOI: 10.1089/vim.2006.19.349     Document Type: Conference Paper
Times cited : (29)

References (130)
  • 2
    • 32944462309 scopus 로고    scopus 로고
    • Anti-immunology: Evasion of the host immune system by bacterial and viral pathogens
    • Finlay BB and McFadden G: Anti-immunology: Evasion of the host immune system by bacterial and viral pathogens. Cell 2006;124:767-782.
    • (2006) Cell , vol.124 , pp. 767-782
    • Finlay, B.B.1    McFadden, G.2
  • 5
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson KD: Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome. Semin Cell Dev Biol 2000;11:141-148.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 6
    • 2142663061 scopus 로고    scopus 로고
    • Ubiquitin as a central cellular regulator
    • 2 p following S32
    • Finley D, Ciechanover A, and Varshavsky A: Ubiquitin as a central cellular regulator. Cell 2004;116:S29-S32, 2 p following S32.
    • (2004) Cell , vol.116
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 8
    • 0042157103 scopus 로고    scopus 로고
    • Viruses and the 26S proteasome: Hacking into destruction
    • Banks L, Pim D, and Thomas M: Viruses and the 26S proteasome: Hacking into destruction. Trends Biochem Sci 2003;28:452-459.
    • (2003) Trends Biochem Sci , vol.28 , pp. 452-459
    • Banks, L.1    Pim, D.2    Thomas, M.3
  • 9
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • Ciechanover A and Ben-Saadon R: N-terminal ubiquitination: More protein substrates join in. Trends Cell Biol 2004;14:103-106.
    • (2004) Trends Cell Biol , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 10
    • 1842591240 scopus 로고    scopus 로고
    • The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture
    • Ingham RJ, Gish G, and Pawson T: The Nedd4 family of E3 ubiquitin ligases: Functional diversity within a common modular architecture. Oncogene 2004;23:1972-1984.
    • (2004) Oncogene , vol.23 , pp. 1972-1984
    • Ingham, R.J.1    Gish, G.2    Pawson, T.3
  • 11
    • 0037683361 scopus 로고    scopus 로고
    • No evidence for PHD fingers as ubiquitin ligases
    • author reply 287-288
    • Scheel H and Hofmann K: No evidence for PHD fingers as ubiquitin ligases. Trends Cell Biol 2003;13:285-287; author reply 287-288.
    • (2003) Trends Cell Biol , vol.13 , pp. 285-287
    • Scheel, H.1    Hofmann, K.2
  • 12
    • 0037459172 scopus 로고    scopus 로고
    • U-box proteins as a new family of ubiquitin ligases
    • Hatakeyama S and Nakayama KI: U-box proteins as a new family of ubiquitin ligases. Biochem Biophys Res Commun 2003;302:635-645.
    • (2003) Biochem Biophys Res Commun , vol.302 , pp. 635-645
    • Hatakeyama, S.1    Nakayama, K.I.2
  • 13
    • 18344386695 scopus 로고    scopus 로고
    • SCF-mediated protein degradation and cell cycle control
    • Ang XL and Wade Harper J: SCF-mediated protein degradation and cell cycle control. Oncogene 2005;24:2860-2870.
    • (2005) Oncogene , vol.24 , pp. 2860-2870
    • Ang, X.L.1    Wade Harper, J.2
  • 14
    • 13244283007 scopus 로고    scopus 로고
    • The anaphase-promoting complex: A key factor in the regulation of cell cycle
    • Castro A, Bernis C, Vigneron S, Labbe JC, and Lorca T: The anaphase-promoting complex: A key factor in the regulation of cell cycle. Oncogene 2005;24:314-325.
    • (2005) Oncogene , vol.24 , pp. 314-325
    • Castro, A.1    Bernis, C.2    Vigneron, S.3    Labbe, J.C.4    Lorca, T.5
  • 15
    • 2542501657 scopus 로고    scopus 로고
    • Ubiquitin ligases and the immune response
    • Liu YC: Ubiquitin ligases and the immune response. Annu Rev Immunol 2004;22:81-127.
    • (2004) Annu Rev Immunol , vol.22 , pp. 81-127
    • Liu, Y.C.1
  • 16
    • 0032167919 scopus 로고    scopus 로고
    • A viral gene that activates lytic cycle expression of Kaposi's sarcoma-associated herpesvirus
    • Sun R, Lin SF, Gradoville L, Yuan Y, Zhu F, and Miller G: A viral gene that activates lytic cycle expression of Kaposi's sarcoma-associated herpesvirus. Proc Natl Acad Sci USA 1998;95:10866-10871.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10866-10871
    • Sun, R.1    Lin, S.F.2    Gradoville, L.3    Yuan, Y.4    Zhu, F.5    Miller, G.6
  • 17
    • 12444275739 scopus 로고    scopus 로고
    • The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteosome-mediated degradation
    • Yu Y, Wang SE, and Hayward GS: The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteosome-mediated degradation. Immunity 2005;22:59-70.
    • (2005) Immunity , vol.22 , pp. 59-70
    • Yu, Y.1    Wang, S.E.2    Hayward, G.S.3
  • 18
    • 23944516870 scopus 로고    scopus 로고
    • The host type I interferon response to viral and bacterial infections
    • Perry AK, Chen G, Zheng D, Tang H, and Cheng G: The host type I interferon response to viral and bacterial infections. Cell Res 2005;15:407-422.
    • (2005) Cell Res , vol.15 , pp. 407-422
    • Perry, A.K.1    Chen, G.2    Zheng, D.3    Tang, H.4    Cheng, G.5
  • 19
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • Coscoy L, Sanchez DJ, and Ganem D: A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol 2001;155:1265-1273.
    • (2001) J Cell Biol , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 20
    • 0024535228 scopus 로고
    • The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product
    • Dyson N, Howley PM, Munger K, and Harlow E: The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product. Science 1989;243:934-937.
    • (1989) Science , vol.243 , pp. 934-937
    • Dyson, N.1    Howley, P.M.2    Munger, K.3    Harlow, E.4
  • 21
    • 0037325976 scopus 로고    scopus 로고
    • Human papillomavirus-induced carcinogenesis and the ubiquitin-proteasome system
    • Scheffner M and Whitaker NJ: Human papillomavirus-induced carcinogenesis and the ubiquitin-proteasome system. Semin Cancer Biol 2003;13:59-67.
    • (2003) Semin Cancer Biol , vol.13 , pp. 59-67
    • Scheffner, M.1    Whitaker, N.J.2
  • 22
    • 0025271203 scopus 로고
    • Association of human papillomavirus types 16 and 18 E6 proteins with p53
    • Werness BA, Levine AJ, and Howley PM: Association of human papillomavirus types 16 and 18 E6 proteins with p53. Science 1990;248:76-79.
    • (1990) Science , vol.248 , pp. 76-79
    • Werness, B.A.1    Levine, A.J.2    Howley, P.M.3
  • 24
    • 0028347587 scopus 로고
    • Modulation of transcriptional regulatory properties of p53 by HPV E6
    • Crook T, Fisher C, Masterson PJ, and Vousden KH: Modulation of transcriptional regulatory properties of p53 by HPV E6. Oncogene 1994;9:1225-1230.
    • (1994) Oncogene , vol.9 , pp. 1225-1230
    • Crook, T.1    Fisher, C.2    Masterson, P.J.3    Vousden, K.H.4
  • 25
    • 0025129211 scopus 로고
    • The E7 proteins of the nononcogenic human papillomavirus type 6b (HPV-6b) and of the oncogenic HPV-16 differ in retinoblastoma protein binding and other properties
    • Gage JR, Meyers C, and Wettstein FO: The E7 proteins of the nononcogenic human papillomavirus type 6b (HPV-6b) and of the oncogenic HPV-16 differ in retinoblastoma protein binding and other properties. J Virol 1990;64:723-730.
    • (1990) J Virol , vol.64 , pp. 723-730
    • Gage, J.R.1    Meyers, C.2    Wettstein, F.O.3
  • 26
    • 0026778731 scopus 로고
    • Single amino acid substitutions in "low-risk" human papillomavirus (HPV) type 6 E7 protein enhance features characteristic of the "high-risk" HPV E7 oncoproteins
    • Sang BC and Barbosa MS: Single amino acid substitutions in "low-risk" human papillomavirus (HPV) type 6 E7 protein enhance features characteristic of the "high-risk" HPV E7 oncoproteins. Proc Natl Acad Sci USA 1992;89:8063-8067.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8063-8067
    • Sang, B.C.1    Barbosa, M.S.2
  • 27
    • 0027396829 scopus 로고
    • Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53
    • Huibregtse JM, Scheffner M, and Howley PM: Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53. Mol Cell Biol 1993;13:775-784.
    • (1993) Mol Cell Biol , vol.13 , pp. 775-784
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 28
    • 0032513114 scopus 로고    scopus 로고
    • The role of E6AP in the regulation of p53 protein levels in human papillomavirus (HPV)-positive and HPV-negative cells
    • Talis AL, Huibregtse JM, and Howley PM: The role of E6AP in the regulation of p53 protein levels in human papillomavirus (HPV)-positive and HPV-negative cells. J Biol Chem 1998;273:6439-6445.
    • (1998) J Biol Chem , vol.273 , pp. 6439-6445
    • Talis, A.L.1    Huibregtse, J.M.2    Howley, P.M.3
  • 29
    • 0027169680 scopus 로고
    • Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins
    • Huibregtse JM, Scheffner M, and Howley PM: Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins. Mol Cell Biol 1993;13:4918-4927.
    • (1993) Mol Cell Biol , vol.13 , pp. 4918-4927
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 30
    • 0035859005 scopus 로고    scopus 로고
    • A sequence element of p53 that determines its susceptibility to viral oncoprotein-targeted degradation
    • Gu J, Rubin RM, and Yuan ZM: A sequence element of p53 that determines its susceptibility to viral oncoprotein-targeted degradation. Oncogene 2001;20:3519-3527.
    • (2001) Oncogene , vol.20 , pp. 3519-3527
    • Gu, J.1    Rubin, R.M.2    Yuan, Z.M.3
  • 31
    • 0028358885 scopus 로고
    • Mutational analysis of HPV-18 E6 identifies domains required for p53 degradation in vitro, abolition of p53 transactivation in vivo and immortalisation of primary BMK cells
    • Pim D, Storey A, Thomas M, Massimi P, and Banks L: Mutational analysis of HPV-18 E6 identifies domains required for p53 degradation in vitro, abolition of p53 transactivation in vivo and immortalisation of primary BMK cells. Oncogene 1994;9:1869-1876.
    • (1994) Oncogene , vol.9 , pp. 1869-1876
    • Pim, D.1    Storey, A.2    Thomas, M.3    Massimi, P.4    Banks, L.5
  • 32
    • 0037432164 scopus 로고    scopus 로고
    • Differences in the ubiquitination of p53 by Mdm2 and the HPV protein E6
    • Camus S, Higgins M, Lane DP, and Lain S: Differences in the ubiquitination of p53 by Mdm2 and the HPV protein E6. FEBS Lett 2003;536:220-224.
    • (2003) FEBS Lett , vol.536 , pp. 220-224
    • Camus, S.1    Higgins, M.2    Lane, D.P.3    Lain, S.4
  • 33
    • 0041967157 scopus 로고    scopus 로고
    • Human papillomaviruses: Targeting differentiating epithelial cells for malignant transformation
    • Fehrmann F and Laimins LA: Human papillomaviruses: Targeting differentiating epithelial cells for malignant transformation. Oncogene 2003;22:5201-5207.
    • (2003) Oncogene , vol.22 , pp. 5201-5207
    • Fehrmann, F.1    Laimins, L.A.2
  • 34
    • 0033919402 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase
    • Kao WH, Beaudenon SL, Talis AL, Huibregtse JM, and Howley PM: Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase. J Virol 2000;74:6408-6417.
    • (2000) J Virol , vol.74 , pp. 6408-6417
    • Kao, W.H.1    Beaudenon, S.L.2    Talis, A.L.3    Huibregtse, J.M.4    Howley, P.M.5
  • 35
    • 15244360247 scopus 로고    scopus 로고
    • Human papillomavirus type 18 E6 protein binds the cellular PDZ protein TIP-2/GIPC, which is involved in transforming growth factor β signaling and triggers its degradation by the proteasome
    • Favre-Bonvin A, Reynaud C, Kretz-Remy C, and Jalinot P: Human papillomavirus type 18 E6 protein binds the cellular PDZ protein TIP-2/GIPC, which is involved in transforming growth factor β signaling and triggers its degradation by the proteasome. J Virol 2005;79:4229-4237.
    • (2005) J Virol , vol.79 , pp. 4229-4237
    • Favre-Bonvin, A.1    Reynaud, C.2    Kretz-Remy, C.3    Jalinot, P.4
  • 38
    • 0037478697 scopus 로고    scopus 로고
    • Human papillomavirus E6 and Myc proteins associate in vivo and bind to and cooperatively activate the telomerase reverse transcriptase promoter
    • Veldman T, Liu X, Yuan H, and Schlegel R: Human papillomavirus E6 and Myc proteins associate in vivo and bind to and cooperatively activate the telomerase reverse transcriptase promoter. Proc Natl Acad Sci USA 2003;100:8211-8216.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8211-8216
    • Veldman, T.1    Liu, X.2    Yuan, H.3    Schlegel, R.4
  • 39
    • 0029048405 scopus 로고
    • Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein
    • Chen JJ, Reid CE, Band V, and Androphy EJ: Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein. Science 1995;269:529-531.
    • (1995) Science , vol.269 , pp. 529-531
    • Chen, J.J.1    Reid, C.E.2    Band, V.3    Androphy, E.J.4
  • 40
    • 0033568491 scopus 로고    scopus 로고
    • The E6 protein of human papillomavirus type 16 binds to and inhibits co-activation by CBP and p300
    • Patel D, Huang SM, Baglia LA, and McCance DJ: The E6 protein of human papillomavirus type 16 binds to and inhibits co-activation by CBP and p300. EMBO J 1999;18:5061-5072.
    • (1999) EMBO J , vol.18 , pp. 5061-5072
    • Patel, D.1    Huang, S.M.2    Baglia, L.A.3    McCance, D.J.4
  • 42
    • 0033554631 scopus 로고    scopus 로고
    • The human papilloma virus (HPV)-18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-α
    • Li S, Labrecque S, Gauzzi MC, Cuddihy AR, Wong AH, Pellegrini S, Matlashewski GJ, and Koromilas AE: The human papilloma virus (HPV)-18 E6 oncoprotein physically associates with Tyk2 and impairs Jak-STAT activation by interferon-α. Oncogene 1999;18:5727-5737.
    • (1999) Oncogene , vol.18 , pp. 5727-5737
    • Li, S.1    Labrecque, S.2    Gauzzi, M.C.3    Cuddihy, A.R.4    Wong, A.H.5    Pellegrini, S.6    Matlashewski, G.J.7    Koromilas, A.E.8
  • 44
    • 0032128003 scopus 로고    scopus 로고
    • Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity
    • Ronco LV, Karpova AY, Vidal M, and Howley PM: Human papillomavirus 16 E6 oncoprotein binds to interferon regulatory factor-3 and inhibits its transcriptional activity. Genes Dev 1998;12:2061-2072.
    • (1998) Genes Dev , vol.12 , pp. 2061-2072
    • Ronco, L.V.1    Karpova, A.Y.2    Vidal, M.3    Howley, P.M.4
  • 45
    • 2342591439 scopus 로고    scopus 로고
    • The papillomavirus E7 oncoprotein is ubiquitinated by UbcH7 and Cullin 1- and Skp2-containing E3 ligase
    • Oh KJ, Kalinina A, Wang J, Nakayama K, Nakayama KI, and Bagchi S: The papillomavirus E7 oncoprotein is ubiquitinated by UbcH7 and Cullin 1- and Skp2-containing E3 ligase. J Virol 2004;78:5338-5346.
    • (2004) J Virol , vol.78 , pp. 5338-5346
    • Oh, K.J.1    Kalinina, A.2    Wang, J.3    Nakayama, K.4    Nakayama, K.I.5    Bagchi, S.6
  • 46
    • 0034954453 scopus 로고    scopus 로고
    • Control of interferon signaling in human papillomavirus infection
    • Koromilas AE, Li S, and Matlashewski G: Control of interferon signaling in human papillomavirus infection. Cytokine Growth Factor Rev 2001;12:157-170.
    • (2001) Cytokine Growth Factor Rev , vol.12 , pp. 157-170
    • Koromilas, A.E.1    Li, S.2    Matlashewski, G.3
  • 47
    • 0033526860 scopus 로고    scopus 로고
    • The human papillomavirus E7 oncoprotein abrogates signaling mediated by interferon-α
    • Barnard P and McMillan NA: The human papillomavirus E7 oncoprotein abrogates signaling mediated by interferon-α. Virology 1999;259:305-313.
    • (1999) Virology , vol.259 , pp. 305-313
    • Barnard, P.1    McMillan, N.A.2
  • 48
    • 0034715829 scopus 로고    scopus 로고
    • The human papillomavirus E7 protein is able to inhibit the antiviral and anti-growth functions of interferon-α
    • Barnard P, Payne E, and McMillan NA: The human papillomavirus E7 protein is able to inhibit the antiviral and anti-growth functions of interferon-α. Virology 2000;277:411-419.
    • (2000) Virology , vol.277 , pp. 411-419
    • Barnard, P.1    Payne, E.2    McMillan, N.A.3
  • 49
    • 0035047160 scopus 로고    scopus 로고
    • Papillomavirus type 16 oncogenes downregulate expression of interferon-responsive genes and upregulate proliferation-associated and NF-κB-responsive genes in cervical keratinocytes
    • Nees M, Geoghegan JM, Hyman T, Frank S, Miller L, and Woodworm CD: Papillomavirus type 16 oncogenes downregulate expression of interferon- responsive genes and upregulate proliferation-associated and NF-κB-responsive genes in cervical keratinocytes. J Virol 2001;75:4283-4296.
    • (2001) J Virol , vol.75 , pp. 4283-4296
    • Nees, M.1    Geoghegan, J.M.2    Hyman, T.3    Frank, S.4    Miller, L.5    Woodworm, C.D.6
  • 51
    • 1242342140 scopus 로고    scopus 로고
    • Role of ICPO in the strategy of conquest of the host cell by herpes simplex virus 1
    • Hagglund R and Roizman B: Role of ICPO in the strategy of conquest of the host cell by herpes simplex virus 1. J Virol 2004;78:2169-2178.
    • (2004) J Virol , vol.78 , pp. 2169-2178
    • Hagglund, R.1    Roizman, B.2
  • 52
    • 0035902533 scopus 로고    scopus 로고
    • The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity
    • Van Sant C, Hagglund R, Lopez P, and Roizman B: The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity. Proc Natl Acad Sci USA 2001;98:8815-8820.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8815-8820
    • Van Sant, C.1    Hagglund, R.2    Lopez, P.3    Roizman, B.4
  • 53
    • 0037154225 scopus 로고    scopus 로고
    • Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes
    • Hagglund R, Van Sant C, Lopez P, and Roizman B: Herpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymes. Proc Natl Acad Sci USA 2002;99:631-636.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 631-636
    • Hagglund, R.1    Van Sant, C.2    Lopez, P.3    Roizman, B.4
  • 54
    • 0036138854 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein ICPO and its isolated RING finger domain act as ubiquitin E3 ligases in vitro
    • Boutell C, Sadis S, and Everett RD: Herpes simplex virus type 1 immediate-early protein ICPO and its isolated RING finger domain act as ubiquitin E3 ligases in vitro. J Virol 2002;76:841-850.
    • (2002) J Virol , vol.76 , pp. 841-850
    • Boutell, C.1    Sadis, S.2    Everett, R.D.3
  • 55
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett RD, Meredith M, Orr A, Cross A, Kathoria M, and Parkinson J: A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J 1997;16:1519-1530.
    • (1997) EMBO J , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 56
    • 4644352805 scopus 로고    scopus 로고
    • A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
    • Canning M, Boutell C, Parkinson J, and Everett RD: A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7. J Biol Chem 2004;279:38160- 38168.
    • (2004) J Biol Chem , vol.279 , pp. 38160-38168
    • Canning, M.1    Boutell, C.2    Parkinson, J.3    Everett, R.D.4
  • 57
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M, Brooks CL, Kon N, and Gu W: A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 2004;13:879-886.
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 58
    • 25144467949 scopus 로고    scopus 로고
    • Reciprocal activities between herpes simplex virus type 1 regulatory protein ICPO, a ubiquitin E3 ligase, and ubiquitin-specific protease USP7
    • Boutell C, Canning M, Orr A, and Everett RD: Reciprocal activities between herpes simplex virus type 1 regulatory protein ICPO, a ubiquitin E3 ligase, and ubiquitin-specific protease USP7. J Virol 2005;79:12342-12354.
    • (2005) J Virol , vol.79 , pp. 12342-12354
    • Boutell, C.1    Canning, M.2    Orr, A.3    Everett, R.D.4
  • 59
    • 0141704201 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53
    • Boutell C and Everett RD: The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53. J Biol Chem 2003;278:36596-36602.
    • (2003) J Biol Chem , vol.278 , pp. 36596-36602
    • Boutell, C.1    Everett, R.D.2
  • 60
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase
    • Parkinson J, Lees-Miller SP, and Everett RD: Herpes simplex virus type 1 immediate-early protein vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J Virol 1999;73:650-657.
    • (1999) J Virol , vol.73 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 61
    • 0033559253 scopus 로고    scopus 로고
    • Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110
    • Everett RD, Earnshaw WC, Findlay J, and Lomonte P: Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. EMBO J 1999;18:1526-1538.
    • (1999) EMBO J , vol.18 , pp. 1526-1538
    • Everett, R.D.1    Earnshaw, W.C.2    Findlay, J.3    Lomonte, P.4
  • 62
    • 0035937114 scopus 로고    scopus 로고
    • Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0
    • Lomonte P, Sullivan KF, and Everett RD: Degradation of nucleosome-associated centromeric histone H3-like protein CENP-A induced by herpes simplex virus type 1 protein ICP0. J Biol Chem 2001;276:5829-5835.
    • (2001) J Biol Chem , vol.276 , pp. 5829-5835
    • Lomonte, P.1    Sullivan, K.F.2    Everett, R.D.3
  • 63
    • 0042709466 scopus 로고    scopus 로고
    • PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0
    • Boutell C, Orr A, and Everett RD: PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0. J Virol 2003;77:8686-8694.
    • (2003) J Virol , vol.77 , pp. 8686-8694
    • Boutell, C.1    Orr, A.2    Everett, R.D.3
  • 64
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix MK and de The H: Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 1999;18:935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    De The, H.2
  • 65
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICPO affect cellular structures and proteins
    • Parkinson J and Everett RD: Alphaherpesvirus proteins related to herpes simplex virus type 1 ICPO affect cellular structures and proteins. J Virol 2000;74:10006-10017.
    • (2000) J Virol , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 66
    • 0042808481 scopus 로고    scopus 로고
    • The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a
    • Gu H and Roizman B: The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proc Natl Acad Sci USA 2003;100:8963-8968.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8963-8968
    • Gu, H.1    Roizman, B.2
  • 67
    • 0032860066 scopus 로고    scopus 로고
    • The F-box: A new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction
    • Craig KL and Tyers M: The F-box: A new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction. Prog Biophys Mol Biol 1999;72:299-328.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 299-328
    • Craig, K.L.1    Tyers, M.2
  • 68
    • 0035106881 scopus 로고    scopus 로고
    • Efficient activation of viral genomes by levels of herpes simplex virus ICPO insufficient to affect cellular gene expression or cell survival
    • Hobbs WE, Brough DE, Kovesdi I, and DeLuca NA: Efficient activation of viral genomes by levels of herpes simplex virus ICPO insufficient to affect cellular gene expression or cell survival. J Virol 2001;75:3391-3403.
    • (2001) J Virol , vol.75 , pp. 3391-3403
    • Hobbs, W.E.1    Brough, D.E.2    Kovesdi, I.3    Deluca, N.A.4
  • 69
    • 0032863957 scopus 로고    scopus 로고
    • 1 into S phase of the cell cycle
    • 1 into S phase of the cell cycle. J Virol 1999;73:9456-9467.
    • (1999) J Virol , vol.73 , pp. 9456-9467
    • Lomonte, P.1    Everett, R.D.2
  • 70
    • 4444329792 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 regulatory protein ICPO does not protect cyclins D1 and D3 from degradation during infection
    • Everett RD: Herpes simplex virus type 1 regulatory protein ICPO does not protect cyclins D1 and D3 from degradation during infection. J Virol 2004;78:9599-9604.
    • (2004) J Virol , vol.78 , pp. 9599-9604
    • Everett, R.D.1
  • 71
    • 0036174361 scopus 로고    scopus 로고
    • Expression of herpes simplex virus ICPO inhibits the induction of interferon-stimulated genes by viral infection
    • Eidson KM, Hobbs WE, Manning BJ, Carlson P, and DeLuca NA: Expression of herpes simplex virus ICPO inhibits the induction of interferon-stimulated genes by viral infection. J Virol 2002;76:2180-2191.
    • (2002) J Virol , vol.76 , pp. 2180-2191
    • Eidson, K.M.1    Hobbs, W.E.2    Manning, B.J.3    Carlson, P.4    DeLuca, N.A.5
  • 73
    • 0033833398 scopus 로고    scopus 로고
    • Activation of cellular interferon-responsive genes after infection of human cells with herpes simplex virus type 1
    • Nicholl MJ, Robinson LH, and Preston CM: Activation of cellular interferon-responsive genes after infection of human cells with herpes simplex virus type 1. J Gen Virol 2000;81:2215-2218.
    • (2000) J Gen Virol , vol.81 , pp. 2215-2218
    • Nicholl, M.J.1    Robinson, L.H.2    Preston, C.M.3
  • 74
    • 0034844014 scopus 로고    scopus 로고
    • Activation of interferon response factor-3 in human cells infected with herpes simplex virus type 1 or human cytomegalovirus
    • Preston CM, Harman AN, and Nicholl MJ: Activation of interferon response factor-3 in human cells infected with herpes simplex virus type 1 or human cytomegalovirus. J Virol 2001;75:8909-8916.
    • (2001) J Virol , vol.75 , pp. 8909-8916
    • Preston, C.M.1    Harman, A.N.2    Nicholl, M.J.3
  • 75
    • 0842326034 scopus 로고    scopus 로고
    • The herpes simplex virus ICPO RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes
    • Lin R, Noyce RS, Collins SE, Everett RD, and Mossman KL: The herpes simplex virus ICPO RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genes. J Virol 2004;78:1675-1684.
    • (2004) J Virol , vol.78 , pp. 1675-1684
    • Lin, R.1    Noyce, R.S.2    Collins, S.E.3    Everett, R.D.4    Mossman, K.L.5
  • 76
    • 3543054546 scopus 로고    scopus 로고
    • Herpes simplex virus 1 has multiple mechanisms for blocking virus-induced interferon production
    • Melroe GT, DeLuca NA, and Knipe DM: Herpes simplex virus 1 has multiple mechanisms for blocking virus-induced interferon production. J Virol 2004;78:8411-8420.
    • (2004) J Virol , vol.78 , pp. 8411-8420
    • Melroe, G.T.1    Deluca, N.A.2    Knipe, D.M.3
  • 77
    • 0036057893 scopus 로고    scopus 로고
    • The immediate-early protein, ICP0, is essential for the resistance of herpes simplex virus to interferon-α/β
    • Harle P, Sainz B Jr, Carr DJ, and Halford WP: The immediate-early protein, ICP0, is essential for the resistance of herpes simplex virus to interferon-α/β. Virology 2002;293:295-304.
    • (2002) Virology , vol.293 , pp. 295-304
    • Harle, P.1    Sainz Jr., B.2    Carr, D.J.3    Halford, W.P.4
  • 78
    • 0033935685 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 mutants are hypersensitive to interferon
    • Mossman KL, Saffran HA, and Smiley JR: Herpes simplex virus ICP0 mutants are hypersensitive to interferon. J Virol 2000;74:2052-2056.
    • (2000) J Virol , vol.74 , pp. 2052-2056
    • Mossman, K.L.1    Saffran, H.A.2    Smiley, J.R.3
  • 79
    • 0036150004 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication
    • Mossman KL and Smiley JR: Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication. J Virol 2002;76:1995-1998.
    • (2002) J Virol , vol.76 , pp. 1995-1998
    • Mossman, K.L.1    Smiley, J.R.2
  • 81
    • 0037941647 scopus 로고    scopus 로고
    • Promyelocytic leukemia protein mediates interferon-based antiherpes simplex virus 1 effects
    • Chee AV, Lopez P, Pandolfi PP, and Roizman B: Promyelocytic leukemia protein mediates interferon-based antiherpes simplex virus 1 effects. J Virol 2003;77:7101-7105.
    • (2003) J Virol , vol.77 , pp. 7101-7105
    • Chee, A.V.1    Lopez, P.2    Pandolfi, P.P.3    Roizman, B.4
  • 82
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P and Pandolfi PP: The role of PML in tumor suppression. Cell 2002;108:165-170.
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 84
    • 33645979012 scopus 로고    scopus 로고
    • ICPO prevents RNase L-independent rRNA cleavage in herpes simplex virus type 1-infected cells
    • Sobol PT and Mossman KL: ICPO prevents RNase L-independent rRNA cleavage in herpes simplex virus type 1-infected cells. J Virol 2006;80:218-225.
    • (2006) J Virol , vol.80 , pp. 218-225
    • Sobol, P.T.1    Mossman, K.L.2
  • 85
    • 1542317755 scopus 로고    scopus 로고
    • Cu17/p185/p193 binding to simian virus 40 large T antigen has a role in cellular transformation
    • Ali SH, Kasper JS, Arai T, and DeCaprio JA: Cu17/p185/p193 binding to simian virus 40 large T antigen has a role in cellular transformation. J Virol 2004;78:2749-2757.
    • (2004) J Virol , vol.78 , pp. 2749-2757
    • Ali, S.H.1    Kasper, J.S.2    Arai, T.3    Decaprio, J.A.4
  • 86
    • 0034468690 scopus 로고    scopus 로고
    • A functional complex of adenovirus proteins E1B-55kDa and E4orf6 is necessary to modulate the expression level of p53 but not its transcriptional activity
    • Cathomen T and Weitzman MD: A functional complex of adenovirus proteins E1B-55kDa and E4orf6 is necessary to modulate the expression level of p53 but not its transcriptional activity. J Virol 2000;74:11407-11412.
    • (2000) J Virol , vol.74 , pp. 11407-11412
    • Cathomen, T.1    Weitzman, M.D.2
  • 87
    • 0036720983 scopus 로고    scopus 로고
    • Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery
    • Harada JN, Shevchenko A, Shevchenko A, Pallas DC, and Berk AJ: Analysis of the adenovirus E1B-55K-anchored proteome reveals its link to ubiquitination machinery. J Virol 2002;76:9194-9206.
    • (2002) J Virol , vol.76 , pp. 9194-9206
    • Harada, J.N.1    Shevchenko, A.2    Shevchenko, A.3    Pallas, D.C.4    Berk, A.J.5
  • 90
    • 0035158586 scopus 로고    scopus 로고
    • Identification of three functions of the adenovirus e4orf6 protein that mediate p53 degradation by the E4orf6-ElB55K complex
    • Querido E, Morrison MR, Chu-Pham-Dang H, Thirlwell SW, Boivin D, and Branton PE: Identification of three functions of the adenovirus e4orf6 protein that mediate p53 degradation by the E4orf6-ElB55K complex. J Virol 2001;75:699-709.
    • (2001) J Virol , vol.75 , pp. 699-709
    • Querido, E.1    Morrison, M.R.2    Chu-Pham-Dang, H.3    Thirlwell, S.W.4    Boivin, D.5    Branton, P.E.6
  • 91
    • 0032556920 scopus 로고    scopus 로고
    • The large E1B protein together with the E4orf6 protein target p53 for active degradation in adenovirus infected cells
    • Steegenga WT, Riteco N, Jochemsen AG, Fallaux FJ, and Bos JL: The large E1B protein together with the E4orf6 protein target p53 for active degradation in adenovirus infected cells. Oncogene 1998;16:349-357.
    • (1998) Oncogene , vol.16 , pp. 349-357
    • Steegenga, W.T.1    Riteco, N.2    Jochemsen, A.G.3    Fallaux, F.J.4    Bos, J.L.5
  • 92
    • 27944464545 scopus 로고    scopus 로고
    • Recent lessons in gene expression, cell cycle control, and cell biology from adenovirus
    • Berk AJ: Recent lessons in gene expression, cell cycle control, and cell biology from adenovirus. Oncogene 2005;24:7673-7685.
    • (2005) Oncogene , vol.24 , pp. 7673-7685
    • Berk, A.J.1
  • 93
    • 2142748036 scopus 로고    scopus 로고
    • Interaction of p53 with the adenovirus E1B-55 kDa protein
    • Roth J and Dobbelstein M: Interaction of p53 with the adenovirus E1B-55 kDa protein. Methods Mol Biol 2003;234:135-149.
    • (2003) Methods Mol Biol , vol.234 , pp. 135-149
    • Roth, J.1    Dobbelstein, M.2
  • 95
    • 0036195134 scopus 로고    scopus 로고
    • An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammaliar cells
    • Ohh M, Kim WY, Moslehi JJ, Chen Y, Chau V, Reac MA, and Kaelin WG Jr: An intact NEDD8 pathway is required for Cullin-dependent ubiquitylation in mammaliar cells. EMBO Rep 2002;3:177-182.
    • (2002) EMBO Rep , vol.3 , pp. 177-182
    • Ohh, M.1    Kim, W.Y.2    Moslehi, J.J.3    Chen, Y.4    Chau, V.5    Reac, M.A.6    Kaelin Jr., W.G.7
  • 96
    • 0037130170 scopus 로고    scopus 로고
    • Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex
    • Stracker TH, Carson CT, and Weitzman MD: Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex. Nature 2002;418:348-352.
    • (2002) Nature , vol.418 , pp. 348-352
    • Stracker, T.H.1    Carson, C.T.2    Weitzman, M.D.3
  • 97
    • 27644504904 scopus 로고    scopus 로고
    • Adenovirus exploits the cellular aggresome response to accelerate inactivation of the MRN complex
    • Liu Y, Shevchenko A, Shevchenko A, and Berk AJ: Adenovirus exploits the cellular aggresome response to accelerate inactivation of the MRN complex. J Virol 2005;79:14004-14016.
    • (2005) J Virol , vol.79 , pp. 14004-14016
    • Liu, Y.1    Shevchenko, A.2    Shevchenko, A.3    Berk, A.J.4
  • 98
    • 0030001373 scopus 로고    scopus 로고
    • Blockage by adenovirus E4orf6 of transcriptional activation by the p53 tumor suppressor
    • Dobner T, Horikoshi N, Rubenwolf S, and Shenk T. Blockage by adenovirus E4orf6 of transcriptional activation by the p53 tumor suppressor. Science 1996;272 1470-1473.
    • (1996) Science , vol.272 , pp. 1470-1473
    • Dobner, T.1    Horikoshi, N.2    Rubenwolf, S.3    Shenk, T.4
  • 99
    • 0031901638 scopus 로고    scopus 로고
    • Adenovirus E1B 55K represses p53 activation in vitro
    • Martin ME and Berk AJ: Adenovirus E1B 55K represses p53 activation in vitro. J Virol 1998;72:3146-3154.
    • (1998) J Virol , vol.72 , pp. 3146-3154
    • Martin, M.E.1    Berk, A.J.2
  • 100
    • 0033912223 scopus 로고    scopus 로고
    • Adenovirus E1B 55-kilodalton oncoprotein inhibits p53 acetylation by PCAF
    • Liu Y, Colosimo AL, Yang XJ, and Liao D: Adenovirus E1B 55-kilodalton oncoprotein inhibits p53 acetylation by PCAF. Mol Cell Biol 2000;20:5540-5553.
    • (2000) Mol Cell Biol , vol.20 , pp. 5540-5553
    • Liu, Y.1    Colosimo, A.L.2    Yang, X.J.3    Liao, D.4
  • 102
    • 2642511413 scopus 로고    scopus 로고
    • The viral infectivity factor (Vif) of HIV-1 unveiled
    • Rose KM, Marin M, Kozak SL, and Rabat D: The viral infectivity factor (Vif) of HIV-1 unveiled. Trends Mol Med 2004;10:291-297.
    • (2004) Trends Mol Med , vol.10 , pp. 291-297
    • Rose, K.M.1    Marin, M.2    Kozak, S.L.3    Rabat, D.4
  • 103
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu X, Yu Y, Liu B, Luo K, Kong W, Mao P, and Yu XF: Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003;302:1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 104
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • Yu Y, Xiao Z, Ehrlich ES, Yu X, and Yu XF: Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev 2004;18:2867-2872.
    • (2004) Genes Dev , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 105
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • Mehle A, Goncalves J, Santa-Marta M, McPike M, and Gabuzda D: Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev 2004;18:2861-2866.
    • (2004) Genes Dev , vol.18 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 106
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, and Yu XF: Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci USA 2005;102:11444-11449.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11444-11449
    • Luo, K.1    Xiao, Z.2    Ehrlich, E.3    Yu, Y.4    Liu, B.5    Zheng, S.6    Yu, X.F.7
  • 107
    • 22544465590 scopus 로고    scopus 로고
    • Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase
    • Liu B, Sarkis PT, Luo K, Yu Y, and Yu XF: Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol 2005;79:9579-9587.
    • (2005) J Virol , vol.79 , pp. 9579-9587
    • Liu, B.1    Sarkis, P.T.2    Luo, K.3    Yu, Y.4    Yu, X.F.5
  • 108
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function
    • Kobayashi M, Takaori-Kondo A, Miyauchi Y, Iwai K, and Uchiyama T: Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. J Biol Chem 2005;280:18573-18578.
    • (2005) J Biol Chem , vol.280 , pp. 18573-18578
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3    Iwai, K.4    Uchiyama, T.5
  • 109
    • 3242702452 scopus 로고    scopus 로고
    • Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation
    • Fujita M, Akari H, Sakurai A, Yoshida A, Chiba T, Tanaka K, Strebel K, and Adachi A: Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation. Microbes Infect 2004;6:791-798.
    • (2004) Microbes Infect , vol.6 , pp. 791-798
    • Fujita, M.1    Akari, H.2    Sakurai, A.3    Yoshida, A.4    Chiba, T.5    Tanaka, K.6    Strebel, K.7    Adachi, A.8
  • 110
    • 9644252776 scopus 로고    scopus 로고
    • APOBEC3G ubiquitination by Nedd4-1 favors its packaging into HIV-1 particles
    • Dussart S, Douaisi M, Courcoul M, Bessou G, Vigne R, and Decroly E: APOBEC3G ubiquitination by Nedd4-1 favors its packaging into HIV-1 particles. J Mol Biol 2005;345:547-558.
    • (2005) J Mol Biol , vol.345 , pp. 547-558
    • Dussart, S.1    Douaisi, M.2    Courcoul, M.3    Bessou, G.4    Vigne, R.5    Decroly, E.6
  • 111
    • 15744387175 scopus 로고    scopus 로고
    • HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation
    • Santa-Marta M, da Silva FA, Fonseca AM, and Goncalves J: HIV-1 Vif can directly inhibit apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G-mediated cytidine deamination by using a single amino acid interaction and without protein degradation. J Biol Chem 2005;280:8765-8775.
    • (2005) J Biol Chem , vol.280 , pp. 8765-8775
    • Santa-Marta, M.1    Da Silva, F.A.2    Fonseca, A.M.3    Goncalves, J.4
  • 114
    • 30344460705 scopus 로고    scopus 로고
    • Structure of DDB1 in complex with a paramyxovirus V protein: Viral hijack of a propeller cluster in ubiquitin ligase
    • Li T, Chen X, Garbutt KC, Zhou P, and Zheng N: Structure of DDB1 in complex with a paramyxovirus V protein: Viral hijack of a propeller cluster in ubiquitin ligase. Cell 2006;124:105-117.
    • (2006) Cell , vol.124 , pp. 105-117
    • Li, T.1    Chen, X.2    Garbutt, K.C.3    Zhou, P.4    Zheng, N.5
  • 115
    • 0032530431 scopus 로고    scopus 로고
    • The V protein of the paramyxovirus SV5 interacts with damage-specific DNA binding protein
    • Lin GY, Paterson RG, Richardson CD, and Lamb RA: The V protein of the paramyxovirus SV5 interacts with damage-specific DNA binding protein. Virology 1998;249:189-200.
    • (1998) Virology , vol.249 , pp. 189-200
    • Lin, G.Y.1    Paterson, R.G.2    Richardson, C.D.3    Lamb, R.A.4
  • 116
    • 23244438013 scopus 로고    scopus 로고
    • Composition and assembly of STAT-targeting ubiquitin ligase complexes: Paramyxovirus V protein carboxyl terminus is an oligomerization domain
    • Ulane CM, Kentsis A, Cruz CD, Parisien JP, Schneider KL, and Horvath CM: Composition and assembly of STAT-targeting ubiquitin ligase complexes: Paramyxovirus V protein carboxyl terminus is an oligomerization domain. J Virol 2005;79:10180-10189.
    • (2005) J Virol , vol.79 , pp. 10180-10189
    • Ulane, C.M.1    Kentsis, A.2    Cruz, C.D.3    Parisien, J.P.4    Schneider, K.L.5    Horvath, C.M.6
  • 117
    • 0035100737 scopus 로고    scopus 로고
    • Single amino acid substitution in the V protein of simian virus 5 differentiates its ability to block interferon signaling in human and murine cells
    • Young DF, Chatziandreou N, He B, Goodbourn S, Lamb RA, and Randall RE: Single amino acid substitution in the V protein of simian virus 5 differentiates its ability to block interferon signaling in human and murine cells. J Virol 2001;75:3363-3370.
    • (2001) J Virol , vol.75 , pp. 3363-3370
    • Young, D.F.1    Chatziandreou, N.2    He, B.3    Goodbourn, S.4    Lamb, R.A.5    Randall, R.E.6
  • 118
    • 27144433162 scopus 로고    scopus 로고
    • Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1
    • Precious B, Childs K, Fitzpatrick-Swallow V, Goodbourn S, and Randall RE: Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1. J Virol 2005;79:13434-13441.
    • (2005) J Virol , vol.79 , pp. 13434-13441
    • Precious, B.1    Childs, K.2    Fitzpatrick-Swallow, V.3    Goodbourn, S.4    Randall, R.E.5
  • 119
    • 0036168735 scopus 로고    scopus 로고
    • Degradation of STAT1 and STAT2 by the V proteins of simian virus 5 and human parainfluenza virus type 2, respectively: Consequences for virus replication in the presence of α/β and γ interferons
    • Andrejeva J, Young DF, Goodbourn S, and Randall RE: Degradation of STAT1 and STAT2 by the V proteins of simian virus 5 and human parainfluenza virus type 2, respectively: Consequences for virus replication in the presence of α/β and γ interferons. J Virol 2002;76:2159-2167.
    • (2002) J Virol , vol.76 , pp. 2159-2167
    • Andrejeva, J.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 120
    • 0032731094 scopus 로고    scopus 로고
    • The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation
    • Didcock L, Young DF, Goodbourn S, and Randall RE: The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation. J Virol 1999;73:9928-9933.
    • (1999) J Virol , vol.73 , pp. 9928-9933
    • Didcock, L.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 121
    • 0036942290 scopus 로고    scopus 로고
    • Paramyxoviruses SV5 and HPIV2 assemble STAT protein ubiquitin ligase complexes from cellular components
    • Ulane CM and Horvath CM: Paramyxoviruses SV5 and HPIV2 assemble STAT protein ubiquitin ligase complexes from cellular components. Virology 2002;304:160-166.
    • (2002) Virology , vol.304 , pp. 160-166
    • Ulane, C.M.1    Horvath, C.M.2
  • 122
    • 0036924472 scopus 로고    scopus 로고
    • Recovery of paramyxovirus simian virus 5 with a V protein lacking the conserved cysteine-rich domain: The multifunctional V protein blocks both interferon-β induction and interferon signaling
    • He B, Paterson RG, Stock N, Durbin JE, Durbin RK, Goodbourn S, Randall RE, and Lamb RA: Recovery of paramyxovirus simian virus 5 with a V protein lacking the conserved cysteine-rich domain: The multifunctional V protein blocks both interferon-β induction and interferon signaling. Virology 2002;303:15-32.
    • (2002) Virology , vol.303 , pp. 15-32
    • He, B.1    Paterson, R.G.2    Stock, N.3    Durbin, J.E.4    Durbin, R.K.5    Goodbourn, S.6    Randall, R.E.7    Lamb, R.A.8
  • 123
    • 10344259136 scopus 로고    scopus 로고
    • The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-β promoter
    • Andrejeva J, Childs KS, Young DF, Carlos TS, Stock N, Goodbourn S, and Randall RE: The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-β promoter. Proc Natl Acad Sci USA 2004;101:17264-17269.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17264-17269
    • Andrejeva, J.1    Childs, K.S.2    Young, D.F.3    Carlos, T.S.4    Stock, N.5    Goodbourn, S.6    Randall, R.E.7
  • 124
    • 2342457141 scopus 로고    scopus 로고
    • Conserved cysteine-rich domain of paramyxovirus simian virus 5 V protein plays an important role in blocking apoptosis
    • Sun M, Rothermel TA, Shuman L, Aligo JA, Xu S, Lin Y, Lamb RA, and He B: Conserved cysteine-rich domain of paramyxovirus simian virus 5 V protein plays an important role in blocking apoptosis. J Virol 2004;78:5068-5078.
    • (2004) J Virol , vol.78 , pp. 5068-5078
    • Sun, M.1    Rothermel, T.A.2    Shuman, L.3    Aligo, J.A.4    Xu, S.5    Lin, Y.6    Lamb, R.A.7    He, B.8
  • 125
    • 22544435201 scopus 로고    scopus 로고
    • The role of simian virus 5 V protein on viral RNA synthesis
    • Lin Y, Horvath F, Aligo JA, Wilson R, and He B: The role of simian virus 5 V protein on viral RNA synthesis. Virology 2005;338:270-280.
    • (2005) Virology , vol.338 , pp. 270-280
    • Lin, Y.1    Horvath, F.2    Aligo, J.A.3    Wilson, R.4    He, B.5
  • 126
    • 32144463144 scopus 로고    scopus 로고
    • Opposing actions of STAT-1 and STAT-3
    • Stephanou, A and Latchman DS: Opposing actions of STAT-1 and STAT-3. Growth Factors 2005;23:177-182.
    • (2005) Growth Factors , vol.23 , pp. 177-182
    • Stephanou, A.1    Latchman, D.S.2
  • 127
    • 24644433742 scopus 로고    scopus 로고
    • Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein
    • Chen M, Cortay JC, Logan IR, Sapountzi V, Robson CN, and Gerlier D: Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein. J Virol 2005;79:11824-11836.
    • (2005) J Virol , vol.79 , pp. 11824-11836
    • Chen, M.1    Cortay, J.C.2    Logan, I.R.3    Sapountzi, V.4    Robson, C.N.5    Gerlier, D.6
  • 128
    • 0033946833 scopus 로고    scopus 로고
    • Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-α-regulated genes
    • Nyman TA, Matikainen S, Sareneva T, Julkunen I, and Kalkkinen N: Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-α-regulated genes. Eur J Biochem 2000;267:4011-4019.
    • (2000) Eur J Biochem , vol.267 , pp. 4011-4019
    • Nyman, T.A.1    Matikainen, S.2    Sareneva, T.3    Julkunen, I.4    Kalkkinen, N.5
  • 129
    • 31944435603 scopus 로고    scopus 로고
    • Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15
    • Okumura A, Lu G, Pitha-Rowe I, and Pitha PM: Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15. Proc Natl Acad Sci USA 2006;103:1440-1445.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1440-1445
    • Okumura, A.1    Lu, G.2    Pitha-Rowe, I.3    Pitha, P.M.4
  • 130
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan W and Krug RM: Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J 2001;20:362-371.
    • (2001) EMBO J , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.