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Volumn 89, Issue 15, 2015, Pages 7465-7477

LMP1-induced sumoylation influences the maintenance of Epstein-Barr virus latency through KAP1

Author keywords

[No Author keywords available]

Indexed keywords

ANACARDIC ACID; GANCICLOVIR; GINKGOLIC ACID; KRAB ASSOCIATED PROTEIN 1; LATENT MEMBRANE PROTEIN 1; PLANT MEDICINAL PRODUCT; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; EBV-ASSOCIATED MEMBRANE ANTIGEN, EPSTEIN-BARR VIRUS; MATRIX PROTEIN; PROTEIN BINDING; REPRESSOR PROTEIN; TRIM28 PROTEIN, HUMAN;

EID: 84937686570     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00711-15     Document Type: Article
Times cited : (41)

References (105)
  • 2
    • 0037039363 scopus 로고    scopus 로고
    • Control of Epstein-Barr virus reactivation by activated CD40 and viral latent membrane protein 1
    • Adler B, Schaadt E, Kempkes B, Zimber-Strobl U, Baier B, Bornkamm GW. 2002. Control of Epstein-Barr virus reactivation by activated CD40 and viral latent membrane protein 1. Proc Natl Acad Sci USA 99:437-442. http://dx.doi.org/10.1073/pnas.221439999.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 437-442
    • Adler, B.1    Schaadt, E.2    Kempkes, B.3    Zimber-Strobl, U.4    Baier, B.5    Bornkamm, G.W.6
  • 3
    • 15244354778 scopus 로고    scopus 로고
    • Epstein-Barr virus transforming protein LMP1 plays a critical role in virus production
    • Ahsan N, Kanda T, Nagashima K, Takada K. 2005. Epstein-Barr virus transforming protein LMP1 plays a critical role in virus production. J Virol 79:4415-4424. http://dx.doi.org/10.1128/JVI.79.7.4415-4424.2005.
    • (2005) J Virol , vol.79 , pp. 4415-4424
    • Ahsan, N.1    Kanda, T.2    Nagashima, K.3    Takada, K.4
  • 4
    • 0037385685 scopus 로고    scopus 로고
    • Latent membrane protein 1 inhibits Epstein-Barr virus lytic cycle induction and progress via different mechanisms
    • Prince S, Keating S, Fielding C, Brennan P, Floettmann E, Rowe M. 2003. Latent membrane protein 1 inhibits Epstein-Barr virus lytic cycle induction and progress via different mechanisms. J Virol 77:5000-5007. http://dx.doi.org/10.1128/JVI.77.8.5000-5007.2003.
    • (2003) J Virol , vol.77 , pp. 5000-5007
    • Prince, S.1    Keating, S.2    Fielding, C.3    Brennan, P.4    Floettmann, E.5    Rowe, M.6
  • 5
    • 84937719597 scopus 로고    scopus 로고
    • Springer, New York, NY
    • Pagano J. 2009. EBV diseases, p 217-240. Springer, New York, NY.
    • (2009) EBV diseases , pp. 217-240
    • Pagano, J.1
  • 8
    • 0041422143 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1: structure and functions
    • Li HP, Chang YS. 2003. Epstein-Barr virus latent membrane protein 1: structure and functions. J Biomed Sci 10:490-504. http://dx.doi.org/10.1007/BF02256110.
    • (2003) J Biomed Sci , vol.10 , pp. 490-504
    • Li, H.P.1    Chang, Y.S.2
  • 10
    • 0035847087 scopus 로고    scopus 로고
    • Mechanism of action of a novel latent membrane protein-1 dominant negative
    • Brennan P, Floettmann JE, Mehl A, Jones M, Rowe M. 2001. Mechanism of action of a novel latent membrane protein-1 dominant negative. J Biol Chem 276:1195-1203. http://dx.doi.org/10.1074/jbc.M005461200.
    • (2001) J Biol Chem , vol.276 , pp. 1195-1203
    • Brennan, P.1    Floettmann, J.E.2    Mehl, A.3    Jones, M.4    Rowe, M.5
  • 12
    • 0036132839 scopus 로고    scopus 로고
    • The Epstein-Barr virus latent membrane protein 1 putative Janus kinase 3 (JAK3) binding domain does not mediate JAK3 association or activation in B-lymphoma or lymphoblastoid cell lines
    • Higuchi M, Kieff E, Izumi KM. 2002. The Epstein-Barr virus latent membrane protein 1 putative Janus kinase 3 (JAK3) binding domain does not mediate JAK3 association or activation in B-lymphoma or lymphoblastoid cell lines. J Virol 76:455-459. http://dx.doi.org/10.1128/JVI.76.1.455-459.2002.
    • (2002) J Virol , vol.76 , pp. 455-459
    • Higuchi, M.1    Kieff, E.2    Izumi, K.M.3
  • 13
    • 0032750932 scopus 로고    scopus 로고
    • The residues between the two transformation effector sites of Epstein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation
    • Izumi KM, Cahir McFarland ED, Riley EA, Rizzo D, Chen Y, Kieff E. 1999. The residues between the two transformation effector sites of Epstein-Barr virus latent membrane protein 1 are not critical for B-lymphocyte growth transformation. J Virol 73:9908-9916.
    • (1999) J Virol , vol.73 , pp. 9908-9916
    • Izumi, K.M.1    Cahir McFarland, E.D.2    Riley, E.A.3    Rizzo, D.4    Chen, Y.5    Kieff, E.6
  • 14
    • 80054006064 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9
    • Bentz GL, Whitehurst CB, Pagano JS. 2011. Epstein-Barr virus latent membrane protein 1 (LMP1) C-terminal-activating region 3 contributes to LMP1-mediated cellular migration via its interaction with Ubc9. J Virol 85:10144-10153. http://dx.doi.org/10.1128/JVI.05035-11.
    • (2011) J Virol , vol.85 , pp. 10144-10153
    • Bentz, G.L.1    Whitehurst, C.B.2    Pagano, J.S.3
  • 15
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M. 2006. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22:159-180. http://dx.doi.org/10.1146/annurev.cellbio.22.010605.093503.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 16
    • 33745017746 scopus 로고    scopus 로고
    • SUMO: a ubiquitin-like protein modifier
    • Kroetz MB. 2005. SUMO: a ubiquitin-like protein modifier. Yale J Biol Med 78:197-201.
    • (2005) Yale J Biol Med , vol.78 , pp. 197-201
    • Kroetz, M.B.1
  • 17
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher O. 2007. SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBORep 8:550-555. http://dx.doi.org/10.1038/sj.embor.7400980.
    • (2007) EMBORep , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 18
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • Bies J, Markus J, Wolff L. 2002. Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J Biol Chem 277:8999-9009. http://dx.doi.org/10.1074/jbc.M110453200.
    • (2002) J Biol Chem , vol.277 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 19
    • 0034705319 scopus 로고    scopus 로고
    • SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53
    • Buschmann T, Fuchs SY, Lee CG, Pan ZQ, Ronai Z. 2000. SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53. Cell 101:753-762. http://dx.doi.org/10.1016/S0092-8674(00)80887-9.
    • (2000) Cell , vol.101 , pp. 753-762
    • Buschmann, T.1    Fuchs, S.Y.2    Lee, C.G.3    Pan, Z.Q.4    Ronai, Z.5
  • 20
    • 17644407601 scopus 로고    scopus 로고
    • The protein stability and transcriptional activity of p63 alpha are regulated by SUMO-1 conjugation
    • Ghioni P, D'Alessandra Y, Mansueto G, Jaffray E, Hay RT, La Mantia G, Guerrini L. 2005. The protein stability and transcriptional activity of p63 alpha are regulated by SUMO-1 conjugation. Cell Cycle 4:183-190. http://dx.doi.org/10.4161/cc.4.1.1359.
    • (2005) Cell Cycle , vol.4 , pp. 183-190
    • Ghioni, P.1    D'Alessandra, Y.2    Mansueto, G.3    Jaffray, E.4    Hay, R.T.5    La Mantia, G.6    Guerrini, L.7
  • 22
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitinrelated modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller S, Matunis MJ, Dejean A. 1998. Conjugation with the ubiquitinrelated modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J 17:61-70. http://dx.doi.org/10.1093/emboj/17.1.61.
    • (1998) EMBO J , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 23
    • 0037022564 scopus 로고    scopus 로고
    • Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity
    • Schmidt D, Muller S. 2002. Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. Proc Natl Acad Sci USA 99:2872-2877. http://dx.doi.org/10.1073/pnas.052559499.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2872-2877
    • Schmidt, D.1    Muller, S.2
  • 24
    • 0042574401 scopus 로고    scopus 로고
    • SUMO in cancer-wrestlers wanted
    • Alarcon-Vargas D, Ronai Z. 2002. SUMO in cancer-wrestlers wanted. Cancer Biol Ther 1:237-242. http://dx.doi.org/10.4161/cbt.74.
    • (2002) Cancer Biol Ther , vol.1 , pp. 237-242
    • Alarcon-Vargas, D.1    Ronai, Z.2
  • 25
    • 38449103757 scopus 로고    scopus 로고
    • Overexpression of small ubiquitin-related modifier-1 and sumoylated Mdm2 in oral squamous cell carcinoma: possible involvement in tumor proliferation and prognosis
    • Katayama A, Ogino T, Bandoh N, Takahara M, Kishibe K, Nonaka S, Harabuchi Y. 2007. Overexpression of small ubiquitin-related modifier-1 and sumoylated Mdm2 in oral squamous cell carcinoma: possible involvement in tumor proliferation and prognosis. Int J Oncol 31:517-524. http://dx.doi.org/10.3892/ijo.31.3.517.
    • (2007) Int J Oncol , vol.31 , pp. 517-524
    • Katayama, A.1    Ogino, T.2    Bandoh, N.3    Takahara, M.4    Kishibe, K.5    Nonaka, S.6    Harabuchi, Y.7
  • 26
    • 61749102005 scopus 로고    scopus 로고
    • Targeting the SUMO E2 conjugating enzyme Ubc9 interaction for anti-cancer drug design
    • Duan X, Trent JO, Ye H. 2009. Targeting the SUMO E2 conjugating enzyme Ubc9 interaction for anti-cancer drug design. Anticancer Agents Med Chem 9:51-54. http://dx.doi.org/10.2174/187152009787047716.
    • (2009) Anticancer Agents Med Chem , vol.9 , pp. 51-54
    • Duan, X.1    Trent, J.O.2    Ye, H.3
  • 27
    • 13944268693 scopus 로고    scopus 로고
    • Basal and reovirusinduced beta interferon (IFN-beta) and IFN-beta-stimulated gene expression are cell type specific in the cardiac protective response
    • Stewart MJ, Smoak K, Blum MA, Sherry B. 2005. Basal and reovirusinduced beta interferon (IFN-beta) and IFN-beta-stimulated gene expression are cell type specific in the cardiac protective response. J Virol 79:2979-2987. http://dx.doi.org/10.1128/JVI.79.5.2979-2987.2005.
    • (2005) J Virol , vol.79 , pp. 2979-2987
    • Stewart, M.J.1    Smoak, K.2    Blum, M.A.3    Sherry, B.4
  • 28
    • 28844506610 scopus 로고    scopus 로고
    • Targeting Ubc9 for cancer therapy
    • Mo YY, Moschos SJ. 2005. Targeting Ubc9 for cancer therapy. Expert Opin Ther Targets 9:1203-1216. http://dx.doi.org/10.1517/14728222.9.6.1203.
    • (2005) Expert Opin Ther Targets , vol.9 , pp. 1203-1216
    • Mo, Y.Y.1    Moschos, S.J.2
  • 29
    • 0036133284 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2
    • Lin J, Johannsen E, Robertson E, Kieff E. 2002. Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2. J Virol 76:232-242. http://dx.doi.org/10.1128/JVI.76.1.232-242.2002.
    • (2002) J Virol , vol.76 , pp. 232-242
    • Lin, J.1    Johannsen, E.2    Robertson, E.3    Kieff, E.4
  • 30
    • 0347626039 scopus 로고    scopus 로고
    • EBNA3C coactivation with EBNA2 requires aSUMOhomology domain
    • Rosendorff A, Illanes D, David G, Lin J, Kieff E, Johannsen E. 2004. EBNA3C coactivation with EBNA2 requires aSUMOhomology domain. J Virol 78:367-377. http://dx.doi.org/10.1128/JVI.78.1.367-377.2004.
    • (2004) J Virol , vol.78 , pp. 367-377
    • Rosendorff, A.1    Illanes, D.2    David, G.3    Lin, J.4    Kieff, E.5    Johannsen, E.6
  • 31
    • 0036255876 scopus 로고    scopus 로고
    • Lysine residues of Epstein-Barr virus-encoded nuclear antigen 2 do not confer secondary modifications via ubiquitin or SUMO-like proteins but modulate transcriptional activation
    • Hille A, Badu-Antwi A, Holzer D, Grasser FA. 2002. Lysine residues of Epstein-Barr virus-encoded nuclear antigen 2 do not confer secondary modifications via ubiquitin or SUMO-like proteins but modulate transcriptional activation. J Gen Virol 83:1037-1042.
    • (2002) J Gen Virol , vol.83 , pp. 1037-1042
    • Hille, A.1    Badu-Antwi, A.2    Holzer, D.3    Grasser, F.A.4
  • 32
    • 24344466952 scopus 로고    scopus 로고
    • Effects of SUMO-1 upon Epstein-Barr virus BZLF1 function and BMRF1 expression
    • Adamson AL. 2005. Effects of SUMO-1 upon Epstein-Barr virus BZLF1 function and BMRF1 expression. Biochem Biophys Res Commun 336: 22-28. http://dx.doi.org/10.1016/j.bbrc.2005.08.036.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 22-28
    • Adamson, A.L.1
  • 33
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • Adamson AL, Kenney S. 2001. Epstein-Barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies. J Virol 75:2388-2399. http://dx.doi.org/10.1128/JVI.75.5.2388-2399.2001.
    • (2001) J Virol , vol.75 , pp. 2388-2399
    • Adamson, A.L.1    Kenney, S.2
  • 35
    • 43049127401 scopus 로고    scopus 로고
    • Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM
    • Chang LK, Liu ST, Kuo CW, Wang WH, Chuang JY, Bianchi E, Hong YR. 2008. Enhancement of transactivation activity of Rta of Epstein-Barr virus by RanBPM. J Mol Biol 379:231-242. http://dx.doi.org/10.1016/j.jmb.2008.04.011.
    • (2008) J Mol Biol , vol.379 , pp. 231-242
    • Chang, L.K.1    Liu, S.T.2    Kuo, C.W.3    Wang, W.H.4    Chuang, J.Y.5    Bianchi, E.6    Hong, Y.R.7
  • 36
    • 77950811209 scopus 로고    scopus 로고
    • Sumoylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virus-encoded protein kinase
    • Hagemeier SR, Dickerson SJ, Meng Q, Yu X, Mertz JE, Kenney SC. 2010. Sumoylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virus-encoded protein kinase. J Virol 84:4383-4394. http://dx.doi.org/10.1128/JVI.02369-09.
    • (2010) J Virol , vol.84 , pp. 4383-4394
    • Hagemeier, S.R.1    Dickerson, S.J.2    Meng, Q.3    Yu, X.4    Mertz, J.E.5    Kenney, S.C.6
  • 37
    • 33646807840 scopus 로고    scopus 로고
    • Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxbeta
    • Liu ST, Wang WH, Hong YR, Chuang JY, Lu PJ, Chang LK. 2006. Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxbeta. Virus Res 119:163-170. http://dx.doi.org/10.1016/j.virusres.2006.01.004.
    • (2006) Virus Res , vol.119 , pp. 163-170
    • Liu, S.T.1    Wang, W.H.2    Hong, Y.R.3    Chuang, J.Y.4    Lu, P.J.5    Chang, L.K.6
  • 38
    • 53449102964 scopus 로고    scopus 로고
    • TRAF6 and the three C-terminal lysine sites on IRF7 are required for its ubiquitination-mediated activation by the tumor necrosis factor receptor family member latent membrane protein 1
    • Ning S, Campos AD, Darnay BG, Bentz GL, Pagano JS. 2008. TRAF6 and the three C-terminal lysine sites on IRF7 are required for its ubiquitination-mediated activation by the tumor necrosis factor receptor family member latent membrane protein 1. Mol Cell Biol 28:6536-6546. http://dx.doi.org/10.1128/MCB.00785-08.
    • (2008) Mol Cell Biol , vol.28 , pp. 6536-6546
    • Ning, S.1    Campos, A.D.2    Darnay, B.G.3    Bentz, G.L.4    Pagano, J.S.5
  • 39
    • 0041387416 scopus 로고    scopus 로고
    • Interferon regulatory factor 7 regulates expression of Epstein-Barr virus latent membrane protein 1: a regulatory circuit
    • Ning S, Hahn AM, Huye LE, Pagano JS. 2003. Interferon regulatory factor 7 regulates expression of Epstein-Barr virus latent membrane protein 1: a regulatory circuit. J Virol 77:9359-9368. http://dx.doi.org/10.1128/JVI.77.17.9359-9368.2003.
    • (2003) J Virol , vol.77 , pp. 9359-9368
    • Ning, S.1    Hahn, A.M.2    Huye, L.E.3    Pagano, J.S.4
  • 40
    • 22544477984 scopus 로고    scopus 로고
    • Interferon regulatory factor 5 represses expression of the Epstein-Barr virus oncoprotein LMP1: braking of the IRF7/LMP1 regulatory circuit
    • Ning S, Huye LE, Pagano JS. 2005. Interferon regulatory factor 5 represses expression of the Epstein-Barr virus oncoprotein LMP1: braking of the IRF7/LMP1 regulatory circuit. J Virol 79:11671-11676. http://dx.doi.org/10.1128/JVI.79.18.11671-11676.2005.
    • (2005) J Virol , vol.79 , pp. 11671-11676
    • Ning, S.1    Huye, L.E.2    Pagano, J.S.3
  • 41
    • 16844377509 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of the IRF7 promoter by a pathway independent of interferon signaling
    • Ning S, Huye LE, Pagano JS. 2005. Regulation of the transcriptional activity of the IRF7 promoter by a pathway independent of interferon signaling. J Biol Chem 280:12262-12270. http://dx.doi.org/10.1074/jbc.M404260200.
    • (2005) J Biol Chem , vol.280 , pp. 12262-12270
    • Ning, S.1    Huye, L.E.2    Pagano, J.S.3
  • 42
    • 77952716624 scopus 로고    scopus 로고
    • The A20 deubiquitinase activity negatively regulates LMP1 activation of IRF7
    • Ning S, Pagano JS. 2010. The A20 deubiquitinase activity negatively regulates LMP1 activation of IRF7. J Virol 84:6130-6138. http://dx.doi.org/10.1128/JVI.00364-10.
    • (2010) J Virol , vol.84 , pp. 6130-6138
    • Ning, S.1    Pagano, J.S.2
  • 43
    • 80052284504 scopus 로고    scopus 로고
    • IRF7: activation, regulation, modification and function
    • Ning S, Pagano JS, Barber GN. 2011. IRF7: activation, regulation, modification and function. Genes Immun 12:399-414. http://dx.doi.org/10.1038/gene.2011.21.
    • (2011) Genes Immun , vol.12 , pp. 399-414
    • Ning, S.1    Pagano, J.S.2    Barber, G.N.3
  • 44
    • 0035201544 scopus 로고    scopus 로고
    • Interferon regulatory factor 7: a key cellular mediator of LMP-1 in EBV latency and transformation
    • Zhang L, Pagano JS. 2001. Interferon regulatory factor 7: a key cellular mediator of LMP-1 in EBV latency and transformation. Semin Cancer Biol 11:445-453. http://dx.doi.org/10.1006/scbi.2001.0411.
    • (2001) Semin Cancer Biol , vol.11 , pp. 445-453
    • Zhang, L.1    Pagano, J.S.2
  • 45
    • 0035202289 scopus 로고    scopus 로고
    • Intracellular signaling molecules activated by Epstein-Barr virus for induction of interferon regulatory factor 7
    • Zhang L, Wu L, Hong K, Pagano JS. 2001. Intracellular signaling molecules activated by Epstein-Barr virus for induction of interferon regulatory factor 7. J Virol 75:12393-12401. http://dx.doi.org/10.1128/JVI.75.24.12393-12401.2001.
    • (2001) J Virol , vol.75 , pp. 12393-12401
    • Zhang, L.1    Wu, L.2    Hong, K.3    Pagano, J.S.4
  • 46
    • 84869120419 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 regulates the function of interferon regulatory factor 7 by inducing its sumoylation
    • Bentz GL, Shackelford J, Pagano JS. 2012. Epstein-Barr virus latent membrane protein 1 regulates the function of interferon regulatory factor 7 by inducing its sumoylation. J Virol 86:12251-12261. http://dx.doi.org/10.1128/JVI.01407-12.
    • (2012) J Virol , vol.86 , pp. 12251-12261
    • Bentz, G.L.1    Shackelford, J.2    Pagano, J.S.3
  • 47
    • 37749031273 scopus 로고    scopus 로고
    • SUMO: getting it on
    • Anckar J, Sistonen L. 2007. SUMO: getting it on. Biochem Soc Trans 35:1409-1413. http://dx.doi.org/10.1042/BST0351409.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1409-1413
    • Anckar, J.1    Sistonen, L.2
  • 48
    • 73849105365 scopus 로고    scopus 로고
    • SUMOylation and cell signalling
    • Andreou AM, Tavernarakis N. 2009. SUMOylation and cell signalling. Biotechnol J 4:1740-1752. http://dx.doi.org/10.1002/biot.200900219.
    • (2009) Biotechnol J , vol.4 , pp. 1740-1752
    • Andreou, A.M.1    Tavernarakis, N.2
  • 49
    • 34248338373 scopus 로고    scopus 로고
    • SUMO: regulating the regulator
    • Bossis G, Melchior F. 2006. SUMO: regulating the regulator. Cell Div 1:13. http://dx.doi.org/10.1186/1747-1028-1-13.
    • (2006) Cell Div , vol.1 , pp. 13
    • Bossis, G.1    Melchior, F.2
  • 50
    • 84878950821 scopus 로고    scopus 로고
    • TRIM involvement in transcriptional regulation
    • Cammas F, Khetchoumian K, Chambon P, Losson R. 2012. TRIM involvement in transcriptional regulation. Adv Exp Med Biol 770:59-76. http://dx.doi.org/10.1007/978-1-4614-5398-7_5.
    • (2012) Adv Exp Med Biol , vol.770 , pp. 59-76
    • Cammas, F.1    Khetchoumian, K.2    Chambon, P.3    Losson, R.4
  • 51
  • 52
    • 54949126675 scopus 로고    scopus 로고
    • TRIM family proteins and their emerging roles in innate immunity
    • Ozato K, Shin DM, Chang TH, Morse HC, III. 2008. TRIM family proteins and their emerging roles in innate immunity. Nat Rev Immunol 8:849-860. http://dx.doi.org/10.1038/nri2413.
    • (2008) Nat Rev Immunol , vol.8 , pp. 849-860
    • Ozato, K.1    Shin, D.M.2    Chang, T.H.3    Morse, H.C.4
  • 53
    • 79960677839 scopus 로고    scopus 로고
    • KAP1 protein: an enigmatic master regulator of the genome
    • Iyengar S, Farnham PJ. 2011. KAP1 protein: an enigmatic master regulator of the genome. J Biol Chem 286:26267-26276. http://dx.doi.org/10.1074/jbc.R111.252569.
    • (2011) J Biol Chem , vol.286 , pp. 26267-26276
    • Iyengar, S.1    Farnham, P.J.2
  • 54
    • 79551556884 scopus 로고    scopus 로고
    • KAP1 depletion increases PML nuclear body number in concert with ultrastructural changes in chromatin
    • Kepkay R, Attwood KM, Ziv Y, Shiloh Y, Dellaire G. 2011. KAP1 depletion increases PML nuclear body number in concert with ultrastructural changes in chromatin. Cell Cycle 10:308-322. http://dx.doi.org/10.4161/cc.10.2.14551.
    • (2011) Cell Cycle , vol.10 , pp. 308-322
    • Kepkay, R.1    Attwood, K.M.2    Ziv, Y.3    Shiloh, Y.4    Dellaire, G.5
  • 55
    • 0344278906 scopus 로고
    • Epstein-Barr virus (EBV) induces expression of B-cell activation markers on in vitro infection of EBV-negative B-lymphoma cells
    • Calender A, Billaud M, Aubry JP, Banchereau J, Vuillaume M, Lenoir GM. 1987. Epstein-Barr virus (EBV) induces expression of B-cell activation markers on in vitro infection of EBV-negative B-lymphoma cells. Proc Natl Acad Sci USA 84:8060-8064. http://dx.doi.org/10.1073/pnas.84.22.8060.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8060-8064
    • Calender, A.1    Billaud, M.2    Aubry, J.P.3    Banchereau, J.4    Vuillaume, M.5    Lenoir, G.M.6
  • 56
    • 0025038502 scopus 로고
    • Modulation of cellular gene expression in B lymphoma cells following in vitro infection by Epstein-Barr virus (EBV)
    • Calender A, Cordier M, Billaud M, Lenoir GM. 1990. Modulation of cellular gene expression in B lymphoma cells following in vitro infection by Epstein-Barr virus (EBV). Int J Cancer 46:658-663. http://dx.doi.org/10.1002/ijc.2910460418.
    • (1990) Int J Cancer , vol.46 , pp. 658-663
    • Calender, A.1    Cordier, M.2    Billaud, M.3    Lenoir, G.M.4
  • 57
    • 0032055162 scopus 로고    scopus 로고
    • Expression of the Epstein-Barr virus protein LMP1 mediates tumor regression in vivo
    • Cherney BW, Sgadari C, Kanegane C, Wang F, Tosato G. 1998. Expression of the Epstein-Barr virus protein LMP1 mediates tumor regression in vivo. Blood 91:2491-2500.
    • (1998) Blood , vol.91 , pp. 2491-2500
    • Cherney, B.W.1    Sgadari, C.2    Kanegane, C.3    Wang, F.4    Tosato, G.5
  • 58
    • 0038243011 scopus 로고    scopus 로고
    • Latent membrane protein 1 is critical for efficient growth transformation of human B cells by Epstein-Barr virus
    • Dirmeier U, Neuhierl B, Kilger E, Reisbach G, Sandberg ML, Hammerschmidt W. 2003. Latent membrane protein 1 is critical for efficient growth transformation of human B cells by Epstein-Barr virus. Cancer Res 63:2982-2989.
    • (2003) Cancer Res , vol.63 , pp. 2982-2989
    • Dirmeier, U.1    Neuhierl, B.2    Kilger, E.3    Reisbach, G.4    Sandberg, M.L.5    Hammerschmidt, W.6
  • 59
    • 0031060448 scopus 로고    scopus 로고
    • Epstein-Barr virus LMP1 induction of the epidermal growth factor receptor is mediated through a TRAF signaling pathway distinct from NF-kappaB activation
    • Miller WE, Mosialos G, Kieff E, Raab-Traub N. 1997. Epstein-Barr virus LMP1 induction of the epidermal growth factor receptor is mediated through a TRAF signaling pathway distinct from NF-kappaB activation. J Virol 71:586-594.
    • (1997) J Virol , vol.71 , pp. 586-594
    • Miller, W.E.1    Mosialos, G.2    Kieff, E.3    Raab-Traub, N.4
  • 60
    • 34248339596 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus
    • Gershburg E, Raffa S, Torrisi MR, Pagano JS. 2007. Epstein-Barr virus-encoded protein kinase (BGLF4) is involved in production of infectious virus. J Virol 81:5407-5412. http://dx.doi.org/10.1128/JVI.02398-06.
    • (2007) J Virol , vol.81 , pp. 5407-5412
    • Gershburg, E.1    Raffa, S.2    Torrisi, M.R.3    Pagano, J.S.4
  • 61
    • 33845467396 scopus 로고    scopus 로고
    • Epstein-Barr virus selectively deregulates DNA damage responses in normal B cells but has no detectable effect on regulation of the tumor suppressor p53
    • O'Nions J, Turner A, Craig R, Allday MJ. 2006. Epstein-Barr virus selectively deregulates DNA damage responses in normal B cells but has no detectable effect on regulation of the tumor suppressor p53. J Virol 80:12408-12413. http://dx.doi.org/10.1128/JVI.01363-06.
    • (2006) J Virol , vol.80 , pp. 12408-12413
    • O'Nions, J.1    Turner, A.2    Craig, R.3    Allday, M.J.4
  • 62
    • 0027429286 scopus 로고
    • Detection of DNA double-strand breaks through the cell-cycle after exposure to X-rays, bleomycin, etoposide and (125)Idurd
    • Olive PL, Banath JP. 1993. Detection of DNA double-strand breaks through the cell-cycle after exposure to X-rays, bleomycin, etoposide and (125)Idurd. Int J Radiat Biol 64:349-358. http://dx.doi.org/10.1080/09553009314551531.
    • (1993) Int J Radiat Biol , vol.64 , pp. 349-358
    • Olive, P.L.1    Banath, J.P.2
  • 63
    • 84857078927 scopus 로고    scopus 로고
    • Dynamic chromatin environment of key lytic cycle regulatory regions of the Epstein-Barr virus genome
    • Ramasubramanyan S, Osborn K, Flower K, Sinclair AJ. 2012. Dynamic chromatin environment of key lytic cycle regulatory regions of the Epstein-Barr virus genome. J Virol 86:1809-1819. http://dx.doi.org/10.1128/JVI.06334-11.
    • (2012) J Virol , vol.86 , pp. 1809-1819
    • Ramasubramanyan, S.1    Osborn, K.2    Flower, K.3    Sinclair, A.J.4
  • 64
    • 66149133220 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity
    • Whitehurst CB, Ning S, Bentz GL, Dufour F, Gershburg E, Shackelford J, Langelier Y, Pagano JS. 2009. The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity. J Virol 83:4345-4353. http://dx.doi.org/10.1128/JVI.02195-08.
    • (2009) J Virol , vol.83 , pp. 4345-4353
    • Whitehurst, C.B.1    Ning, S.2    Bentz, G.L.3    Dufour, F.4    Gershburg, E.5    Shackelford, J.6    Langelier, Y.7    Pagano, J.S.8
  • 66
    • 0035930517 scopus 로고    scopus 로고
    • Cell cycle-dependent proteolysis and phosphorylation of human Mcm10
    • Izumi M, Yatagai F, Hanaoka F. 2001. Cell cycle-dependent proteolysis and phosphorylation of human Mcm10. J Biol Chem 276:48526-48531.
    • (2001) J Biol Chem , vol.276 , pp. 48526-48531
    • Izumi, M.1    Yatagai, F.2    Hanaoka, F.3
  • 67
    • 79959625605 scopus 로고    scopus 로고
    • PU.1-dependent regulation of UCH L1 expression in B-lymphoma cells
    • Bheda A, Yue W, Gullapalli A, Shackelford J, Pagano JS. 2011. PU.1-dependent regulation of UCH L1 expression in B-lymphoma cells. Leuk Lymphoma 52:1336-1347. http://dx.doi.org/10.3109/10428194.2011.562571.
    • (2011) Leuk Lymphoma , vol.52 , pp. 1336-1347
    • Bheda, A.1    Yue, W.2    Gullapalli, A.3    Shackelford, J.4    Pagano, J.S.5
  • 68
    • 79958067517 scopus 로고    scopus 로고
    • Arsenic mediated disruption of promyelocytic leukemia protein nuclear bodies induces ganciclovir susceptibility in Epstein-Barr positive epithelial cells
    • Sides MD, Block GJ, Shan B, Esteves KC, Lin Z, Flemington EK, Lasky JA. 2011. Arsenic mediated disruption of promyelocytic leukemia protein nuclear bodies induces ganciclovir susceptibility in Epstein-Barr positive epithelial cells. Virology 416:86-97. http://dx.doi.org/10.1016/j.virol.2011.04.005.
    • (2011) Virology , vol.416 , pp. 86-97
    • Sides, M.D.1    Block, G.J.2    Shan, B.3    Esteves, K.C.4    Lin, Z.5    Flemington, E.K.6    Lasky, J.A.7
  • 69
    • 44449109018 scopus 로고    scopus 로고
    • Human CMV infection of endothelial cells induces an angiogenic response through viral binding to EGF receptor and beta1 and beta3 integrins
    • Bentz GL, Yurochko AD. 2008. Human CMV infection of endothelial cells induces an angiogenic response through viral binding to EGF receptor and beta1 and beta3 integrins. Proc Natl Acad Sci USA 105:5531-5536. http://dx.doi.org/10.1073/pnas.0800037105.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5531-5536
    • Bentz, G.L.1    Yurochko, A.D.2
  • 70
    • 84870704593 scopus 로고    scopus 로고
    • The cellular ataxia telangiectasia-mutated kinase promotes Epstein-Barr virus lytic reactivation in response to multiple different types of lytic reactivationinducing stimuli
    • Hagemeier SR, Barlow EA, Meng Q, Kenney SC. 2012. The cellular ataxia telangiectasia-mutated kinase promotes Epstein-Barr virus lytic reactivation in response to multiple different types of lytic reactivationinducing stimuli. J Virol 86:13360-13370. http://dx.doi.org/10.1128/JVI.01850-12.
    • (2012) J Virol , vol.86 , pp. 13360-13370
    • Hagemeier, S.R.1    Barlow, E.A.2    Meng, Q.3    Kenney, S.C.4
  • 71
    • 0037086080 scopus 로고    scopus 로고
    • Chemotherapy induces lytic EBV replication and confers ganciclovir susceptibility to EBV-positive epithelial cell tumors
    • Feng WH, Israel B, Raab-Traub N, Busson P, Kenney SC. 2002. Chemotherapy induces lytic EBV replication and confers ganciclovir susceptibility to EBV-positive epithelial cell tumors. Cancer Res 62:1920-1926.
    • (2002) Cancer Res , vol.62 , pp. 1920-1926
    • Feng, W.H.1    Israel, B.2    Raab-Traub, N.3    Busson, P.4    Kenney, S.C.5
  • 72
    • 0034667460 scopus 로고    scopus 로고
    • Activation of lytic Epstein-Barr virus (EBV) infection by radiation and sodium butyrate in vitro and in vivo: a potential method for treating EBV-positive malignancies
    • Westphal EM, Blackstock W, Feng W, Israel B, Kenney SC. 2000. Activation of lytic Epstein-Barr virus (EBV) infection by radiation and sodium butyrate in vitro and in vivo: a potential method for treating EBV-positive malignancies. Cancer Res 60:5781-5788.
    • (2000) Cancer Res , vol.60 , pp. 5781-5788
    • Westphal, E.M.1    Blackstock, W.2    Feng, W.3    Israel, B.4    Kenney, S.C.5
  • 73
    • 1942535076 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane protein 1 induces micronucleus formation, represses DNA repair and enhances sensitivity to DNA-damaging agents in human epithelial cells
    • Liu MT, Chen YR, Chen SC, Hu CY, Lin CS, Chang YT, Wang WB, Chen JY. 2004. Epstein-Barr virus latent membrane protein 1 induces micronucleus formation, represses DNA repair and enhances sensitivity to DNA-damaging agents in human epithelial cells. Oncogene 23:2531-2539. http://dx.doi.org/10.1038/sj.onc.1207375.
    • (2004) Oncogene , vol.23 , pp. 2531-2539
    • Liu, M.T.1    Chen, Y.R.2    Chen, S.C.3    Hu, C.Y.4    Lin, C.S.5    Chang, Y.T.6    Wang, W.B.7    Chen, J.Y.8
  • 74
    • 60649088334 scopus 로고    scopus 로고
    • Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate
    • Fukuda I, Ito A, Hirai G, Nishimura S, Kawasaki H, Saitoh H, Kimura K, Sodeoka M, Yoshida M. 2009. Ginkgolic acid inhibits protein SUMOylation by blocking formation of the E1-SUMO intermediate. Chem Biol 16:133-140. http://dx.doi.org/10.1016/j.chembiol.2009.01.009.
    • (2009) Chem Biol , vol.16 , pp. 133-140
    • Fukuda, I.1    Ito, A.2    Hirai, G.3    Nishimura, S.4    Kawasaki, H.5    Saitoh, H.6    Kimura, K.7    Sodeoka, M.8    Yoshida, M.9
  • 75
    • 0033967220 scopus 로고    scopus 로고
    • The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells
    • Giorgino F, de Robertis O, Laviola L, Montrone C, Perrini S, McCowen KC, Smith RJ. 2000. The sentrin-conjugating enzyme mUbc9 interacts with GLUT4 and GLUT1 glucose transporters and regulates transporter levels in skeletal muscle cells. Proc Natl Acad Sci USA 97: 1125-1130. http://dx.doi.org/10.1073/pnas.97.3.1125.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1125-1130
    • Giorgino, F.1    de Robertis, O.2    Laviola, L.3    Montrone, C.4    Perrini, S.5    McCowen, K.C.6    Smith, R.J.7
  • 76
    • 0037169534 scopus 로고    scopus 로고
    • Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein
    • Mo YY, Yu Y, Shen Z, Beck WT. 2002. Nucleolar delocalization of human topoisomerase I in response to topotecan correlates with sumoylation of the protein. J Biol Chem 277:2958-2964. http://dx.doi.org/10.1074/jbc.M108263200.
    • (2002) J Biol Chem , vol.277 , pp. 2958-2964
    • Mo, Y.Y.1    Yu, Y.2    Shen, Z.3    Beck, W.T.4
  • 77
    • 20044364558 scopus 로고    scopus 로고
    • Ubc9 and protein inhibitor of activated STAT 1 activate chicken ovalbumin upstream promotertranscription factor I-mediated human CYP11B2 gene transcription
    • Kurihara I, Shibata H, Kobayashi S, Suda N, Ikeda Y, Yokota K, Murai A, Saito I, Rainey WE, Saruta T. 2005. Ubc9 and protein inhibitor of activated STAT 1 activate chicken ovalbumin upstream promotertranscription factor I-mediated human CYP11B2 gene transcription. J Biol Chem 280:6721-6730. http://dx.doi.org/10.1074/jbc.M411820200.
    • (2005) J Biol Chem , vol.280 , pp. 6721-6730
    • Kurihara, I.1    Shibata, H.2    Kobayashi, S.3    Suda, N.4    Ikeda, Y.5    Yokota, K.6    Murai, A.7    Saito, I.8    Rainey, W.E.9    Saruta, T.10
  • 78
    • 0041731797 scopus 로고    scopus 로고
    • SUMO-1/Ubc9 promotes nuclear accumulation and metabolic stability of tumor suppressor Smad4
    • Lin X, Liang M, Liang YY, Brunicardi FC, Feng XH. 2003. SUMO-1/Ubc9 promotes nuclear accumulation and metabolic stability of tumor suppressor Smad4. J Biol Chem 278:31043-31048. http://dx.doi.org/10.1074/jbc.C300112200.
    • (2003) J Biol Chem , vol.278 , pp. 31043-31048
    • Lin, X.1    Liang, M.2    Liang, Y.Y.3    Brunicardi, F.C.4    Feng, X.H.5
  • 79
    • 22244478319 scopus 로고    scopus 로고
    • DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation
    • Wang QE, Zhu Q, Wani G, El-Mahdy MA, Li J, Wani AA. 2005. DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation. Nucleic Acids Res 33:4023-4034. http://dx.doi.org/10.1093/nar/gki684.
    • (2005) Nucleic Acids Res , vol.33 , pp. 4023-4034
    • Wang, Q.E.1    Zhu, Q.2    Wani, G.3    El-Mahdy, M.A.4    Li, J.5    Wani, A.A.6
  • 80
    • 17444411923 scopus 로고    scopus 로고
    • Induction of lytic Epstein-Barr virus (EBV) infection by synergistic action of rituximab and dexamethasone renders EBV-positive lymphoma cells more susceptible to ganciclovir cytotoxicity in vitro and in vivo
    • Daibata M, Bandobashi K, Kuroda M, Imai S, Miyoshi I, Taguchi H. 2005. Induction of lytic Epstein-Barr virus (EBV) infection by synergistic action of rituximab and dexamethasone renders EBV-positive lymphoma cells more susceptible to ganciclovir cytotoxicity in vitro and in vivo. J Virol 79:5875-5879. http://dx.doi.org/10.1128/JVI.79.9.5875-5879.2005.
    • (2005) J Virol , vol.79 , pp. 5875-5879
    • Daibata, M.1    Bandobashi, K.2    Kuroda, M.3    Imai, S.4    Miyoshi, I.5    Taguchi, H.6
  • 82
    • 0842326026 scopus 로고    scopus 로고
    • Lytic induction therapy for Epstein-Barr virus-positive B-cell lymphomas
    • Feng WH, Hong G, Delecluse HJ, Kenney SC. 2004. Lytic induction therapy for Epstein-Barr virus-positive B-cell lymphomas. J Virol 78: 1893-1902. http://dx.doi.org/10.1128/JVI.78.4.1893-1902.2004.
    • (2004) J Virol , vol.78 , pp. 1893-1902
    • Feng, W.H.1    Hong, G.2    Delecluse, H.J.3    Kenney, S.C.4
  • 83
    • 33749031579 scopus 로고    scopus 로고
    • Valproic acid enhances the efficacy of chemotherapy in EBV-positive tumors by increasing lytic viral gene expression
    • Feng WH, Kenney SC. 2006. Valproic acid enhances the efficacy of chemotherapy in EBV-positive tumors by increasing lytic viral gene expression. Cancer Res 66:8762-8769. http://dx.doi.org/10.1158/0008-5472.CAN-06-1006.
    • (2006) Cancer Res , vol.66 , pp. 8762-8769
    • Feng, W.H.1    Kenney, S.C.2
  • 84
    • 84878376672 scopus 로고    scopus 로고
    • Co-treatment with arsenic trioxide and ganciclovir reduces tumor volume in a murine xenograft model of nasopharyngeal carcinoma
    • Sides MD, Sosulski ML, Luo F, Lin Z, Flemington EK, Lasky JA. 2013. Co-treatment with arsenic trioxide and ganciclovir reduces tumor volume in a murine xenograft model of nasopharyngeal carcinoma. Virol J 10:152. http://dx.doi.org/10.1186/1743-422X-10-152.
    • (2013) Virol J , vol.10 , pp. 152
    • Sides, M.D.1    Sosulski, M.L.2    Luo, F.3    Lin, Z.4    Flemington, E.K.5    Lasky, J.A.6
  • 85
    • 77950850768 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV)-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral production
    • Meng Q, Hagemeier SR, Fingeroth JD, Gershburg E, Pagano JS, Kenney SC. 2010. The Epstein-Barr virus (EBV)-encoded protein kinase, EBV-PK, but not the thymidine kinase (EBV-TK), is required for ganciclovir and acyclovir inhibition of lytic viral production. J Virol 84: 4534-4542. http://dx.doi.org/10.1128/JVI.02487-09.
    • (2010) J Virol , vol.84 , pp. 4534-4542
    • Meng, Q.1    Hagemeier, S.R.2    Fingeroth, J.D.3    Gershburg, E.4    Pagano, J.S.5    Kenney, S.C.6
  • 86
    • 0346274978 scopus 로고    scopus 로고
    • KRAB-containing zinc-finger repressor proteins
    • Urrutia R. 2003. KRAB-containing zinc-finger repressor proteins. Genome Biol 4:231. http://dx.doi.org/10.1186/gb-2003-4-10-231.
    • (2003) Genome Biol , vol.4 , pp. 231
    • Urrutia, R.1
  • 87
    • 84920873822 scopus 로고    scopus 로고
    • KAPtain in charge of multiple missions: emerging roles of KAP1
    • Cheng CT, Kuo CY, Ann DK. 2014. KAPtain in charge of multiple missions: emerging roles of KAP1. World J Biol Chem 5:308-320. http://dx.doi.org/10.4331/wjbc.v5.i3.308.
    • (2014) World J Biol Chem , vol.5 , pp. 308-320
    • Cheng, C.T.1    Kuo, C.Y.2    Ann, D.K.3
  • 91
    • 33847270257 scopus 로고    scopus 로고
    • Doxorubicin downregulates Kruppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells
    • Lee YK, Thomas SN, Yang AJ, Ann DK. 2007. Doxorubicin downregulates Kruppel-associated box domain-associated protein 1 sumoylation that relieves its transcription repression on p21WAF1/CIP1 in breast cancer MCF-7 cells. J Biol Chem 282:1595-1606. http://dx.doi.org/10.1074/jbc.M606306200.
    • (2007) J Biol Chem , vol.282 , pp. 1595-1606
    • Lee, Y.K.1    Thomas, S.N.2    Yang, A.J.3    Ann, D.K.4
  • 92
    • 34249853932 scopus 로고    scopus 로고
    • Sumoylation of the transcriptional intermediary factor 1beta (TIF1beta), the co-repressor of the KRAB multifinger proteins, is required for its transcriptional activity and is modulated by the KRAB domain
    • Mascle XH, Germain-Desprez D, Huynh P, Estephan P, Aubry M. 2007. Sumoylation of the transcriptional intermediary factor 1beta (TIF1beta), the co-repressor of the KRAB multifinger proteins, is required for its transcriptional activity and is modulated by the KRAB domain. J Biol Chem 282:10190-10202. http://dx.doi.org/10.1074/jbc.M611429200.
    • (2007) J Biol Chem , vol.282 , pp. 10190-10202
    • Mascle, X.H.1    Germain-Desprez, D.2    Huynh, P.3    Estephan, P.4    Aubry, M.5
  • 93
    • 67651007508 scopus 로고    scopus 로고
    • Kruppel-associated box domain-associated protein-1 as a latency regulator for Kaposi's sarcomaassociated herpesvirus and its modulation by the viral protein kinase
    • Chang PC, Fitzgerald LD, Van Geelen A, Izumiya Y, Ellison TJ, Wang DH, Ann DK, Luciw PA, Kung HJ. 2009. Kruppel-associated box domain-associated protein-1 as a latency regulator for Kaposi's sarcomaassociated herpesvirus and its modulation by the viral protein kinase. Cancer Res 69:5681-5689. http://dx.doi.org/10.1158/0008-5472.CAN-08-4570.
    • (2009) Cancer Res , vol.69 , pp. 5681-5689
    • Chang, P.C.1    Fitzgerald, L.D.2    Van Geelen, A.3    Izumiya, Y.4    Ellison, T.J.5    Wang, D.H.6    Ann, D.K.7    Luciw, P.A.8    Kung, H.J.9
  • 96
    • 80555133291 scopus 로고    scopus 로고
    • Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7
    • Liang QM, Deng HY, Li XJ, Wu XF, Tang QY, Chang TH, Peng HZ, Rauscher FJ, Ozato K, Zhu FX. 2011. Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7. J Immunol 187:4754-4763. http://dx.doi.org/10.4049/jimmunol.1101704.
    • (2011) J Immunol , vol.187 , pp. 4754-4763
    • Liang, Q.M.1    Deng, H.Y.2    Li, X.J.3    Wu, X.F.4    Tang, Q.Y.5    Chang, T.H.6    Peng, H.Z.7    Rauscher, F.J.8    Ozato, K.9    Zhu, F.X.10
  • 97
    • 80052689126 scopus 로고    scopus 로고
    • Kruppel-associated boxassociated protein 1 negatively regulates TNF-alpha-induced NF-kappa B transcriptional activity by influencing the interactions among STAT3, p300, and NF-kappa B/p65
    • Kamitani S, Togi S, Ikeda O, Nakasuji M, Sakauchi A, Sekine Y, Muromoto R, Oritani K, Matsuda T. 2011. Kruppel-associated boxassociated protein 1 negatively regulates TNF-alpha-induced NF-kappa B transcriptional activity by influencing the interactions among STAT3, p300, and NF-kappa B/p65. J Immunol 187:2476-2483. http://dx.doi.org/10.4049/jimmunol.1003243.
    • (2011) J Immunol , vol.187 , pp. 2476-2483
    • Kamitani, S.1    Togi, S.2    Ikeda, O.3    Nakasuji, M.4    Sakauchi, A.5    Sekine, Y.6    Muromoto, R.7    Oritani, K.8    Matsuda, T.9
  • 98
    • 53849101837 scopus 로고    scopus 로고
    • Innate link between NF-kappaB activity and ubiquitin-like modifiers
    • Lang V, Rodriguez MS. 2008. Innate link between NF-kappaB activity and ubiquitin-like modifiers. Biochem Soc Trans 36:853-857. http://dx.doi.org/10.1042/BST0360853.
    • (2008) Biochem Soc Trans , vol.36 , pp. 853-857
    • Lang, V.1    Rodriguez, M.S.2
  • 99
    • 34447617038 scopus 로고    scopus 로고
    • SUMO and NF-kappaB ties
    • Mabb AM, Miyamoto S. 2007. SUMO and NF-kappaB ties. Cell Mol Life Sci 64:1979-1996. http://dx.doi.org/10.1007/s00018-007-7005-2.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1979-1996
    • Mabb, A.M.1    Miyamoto, S.2
  • 100
    • 37749006669 scopus 로고    scopus 로고
    • Signalling pathways and the regulation of SUMO modification
    • Guo B, Yang SH, Witty J, Sharrocks AD. 2007. Signalling pathways and the regulation of SUMO modification. Biochem Soc Trans 35:1414-1418. http://dx.doi.org/10.1042/BST0351414.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1414-1418
    • Guo, B.1    Yang, S.H.2    Witty, J.3    Sharrocks, A.D.4
  • 101
    • 0037044836 scopus 로고    scopus 로고
    • SUMO-1 modification of the C-terminal KVEKVD of axin is required for JNK activation but has no effect on Wnt signaling
    • Rui HL, Fan E, Zhou HM, Xu Z, Zhang Y, Lin SC. 2002. SUMO-1 modification of the C-terminal KVEKVD of axin is required for JNK activation but has no effect on Wnt signaling. J Biol Chem 277:42981-42986. http://dx.doi.org/10.1074/jbc.M208099200.
    • (2002) J Biol Chem , vol.277 , pp. 42981-42986
    • Rui, H.L.1    Fan, E.2    Zhou, H.M.3    Xu, Z.4    Zhang, Y.5    Lin, S.C.6
  • 103
    • 34147208226 scopus 로고    scopus 로고
    • Interferon regulatory factor 7 is activated by a viral oncoprotein through RIP-dependent ubiquitination
    • Huye LE, Ning S, Kelliher M, Pagano JS. 2007. Interferon regulatory factor 7 is activated by a viral oncoprotein through RIP-dependent ubiquitination. Mol Cell Biol 27:2910-2918. http://dx.doi.org/10.1128/MCB.02256-06.
    • (2007) Mol Cell Biol , vol.27 , pp. 2910-2918
    • Huye, L.E.1    Ning, S.2    Kelliher, M.3    Pagano, J.S.4
  • 104
    • 0023698910 scopus 로고
    • Identification and characterization of OriLyt, a lytic origin of DNA replication of Epstein-Barr virus
    • Hammerschmidt W, Sugden B. 1988. Identification and characterization of OriLyt, a lytic origin of DNA replication of Epstein-Barr virus. Cell 55:427-433. http://dx.doi.org/10.1016/0092-8674(88)90028-1.
    • (1988) Cell , vol.55 , pp. 427-433
    • Hammerschmidt, W.1    Sugden, B.2
  • 105
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes
    • Bossis G, Melchior F. 2006. Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol Cell 21:349-357. http://dx.doi.org/10.1016/j.molcel.2005.12.019.
    • (2006) Mol Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2


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