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Volumn 86, Issue 2, 2012, Pages 642-654

Human pathogens and the host cell sumoylation system

Author keywords

[No Author keywords available]

Indexed keywords

CELO GAM 1 PROTEIN; IE1 PROTEIN; IE2 PROTEIN; IMMEDIATE EARLY PROTEIN BZLF1; INFECTED CELL PROTEIN 0; LANA2 PROTEIN; ORF61 PROTEIN; PROTEIN UBC9; REGULATOR PROTEIN; RTA PROTEIN; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; TAX PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84856862707     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.06227-11     Document Type: Article
Times cited : (104)

References (203)
  • 1
    • 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.
    • (2005) Biochem. Biophys. Res. Commun. , vol.336 , pp. 22-28
    • Adamson, A.L.1
  • 2
    • 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.
    • (2001) J. Virol. , vol.75 , pp. 2388-2399
    • Adamson, A.L.1    Kenney, S.2
  • 3
    • 0030912888 scopus 로고    scopus 로고
    • The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PMLassociated nuclear bodies at very early times in infected permissive cells
    • Ahn JH, Hayward GS. 1997. The major immediate-early proteins IE1 and IE2 of human cytomegalovirus colocalize with and disrupt PMLassociated nuclear bodies at very early times in infected permissive cells. J. Virol. 71:4599-4613.
    • (1997) J. Virol. , vol.71 , pp. 4599-4613
    • Ahn, J.H.1    Hayward, G.S.2
  • 4
    • 0035082279 scopus 로고    scopus 로고
    • Evaluation of interactions of human cytomegalovirus immediate-early IE2 regulatory protein with small ubiquitin-like modifiers and their conjugation enzyme Ubc9
    • Ahn JH, Xu Y, Jang WJ, Matunis MJ, Hayward GS. 2001. Evaluation of interactions of human cytomegalovirus immediate-early IE2 regulatory protein with small ubiquitin-like modifiers and their conjugation enzyme Ubc9. J. Virol. 75:3859-3872.
    • (2001) J. Virol. , vol.75 , pp. 3859-3872
    • Ahn, J.H.1    Xu, Y.2    Jang, W.J.3    Matunis, M.J.4    Hayward, G.S.5
  • 5
    • 33749069523 scopus 로고    scopus 로고
    • SUMO1 haploinsufficiency leads to cleft lip and palate
    • Alkuraya FS, et al. 2006. SUMO1 haploinsufficiency leads to cleft lip and palate. Science 313:1751.
    • (2006) Science , vol.313 , pp. 1751
    • Alkuraya, F.S.1
  • 6
    • 48749132434 scopus 로고    scopus 로고
    • Candidate genes implicated in type 1 diabetes susceptibility
    • Aribi M. 2008. Candidate genes implicated in type 1 diabetes susceptibility. Curr. Diabetes Rev. 4:110-121.
    • (2008) Curr. Diabetes Rev. , vol.4 , pp. 110-121
    • Aribi, M.1
  • 7
    • 0020602962 scopus 로고
    • Effect of adenovirus on metabolism of specific host mRNAs: transport control and specific translation discrimination
    • Babich A, Feldman LT, Nevins JR, Darnell JE, Weinberger C. 1983. Effect of adenovirus on metabolism of specific host mRNAs: transport control and specific translation discrimination. Mol. Cell. Biol. 3:1212-1221.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 1212-1221
    • Babich, A.1    Feldman, L.T.2    Nevins, J.R.3    Darnell, J.E.4    Weinberger, C.5
  • 8
    • 0036939820 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease
    • Bailey D, O'Hare P. 2002. Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease. J. Gen. Virol. 83:2951-2964.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2951-2964
    • Bailey, D.1    O'Hare, P.2
  • 9
    • 0037383491 scopus 로고    scopus 로고
    • Strain variations in single amino acids of the 86-kilodalton human cytomegalovirus major immediate-early protein (IE2) affect its functional and biochemical properties: implications of dynamic protein conformation
    • Barrasa MI, Harel N, Yu Y, Alwine JC. 2003. Strain variations in single amino acids of the 86-kilodalton human cytomegalovirus major immediate-early protein (IE2) affect its functional and biochemical properties: implications of dynamic protein conformation. J. Virol. 77: 4760-4772.
    • (2003) J. Virol. , vol.77 , pp. 4760-4772
    • Barrasa, M.I.1    Harel, N.2    Yu, Y.3    Alwine, J.C.4
  • 10
    • 77955505569 scopus 로고    scopus 로고
    • SENP1 induces prostatic intraepithelial neoplasia through multiple mechanisms
    • Bawa-Khalfe T, Cheng J, Lin SH, Ittmann MM, Yeh ET. 2010. SENP1 induces prostatic intraepithelial neoplasia through multiple mechanisms. J. Biol. Chem. 285:25859-25866.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25859-25866
    • Bawa-Khalfe, T.1    Cheng, J.2    Lin, S.H.3    Ittmann, M.M.4    Yeh, E.T.5
  • 11
    • 0032504021 scopus 로고    scopus 로고
    • Structure determination of the small ubiquitinrelated modifier SUMO-1
    • Bayer P, et al. 1998. Structure determination of the small ubiquitinrelated modifier SUMO-1. J. Mol. Biol. 280:275-286.
    • (1998) J. Mol. Biol. , vol.280 , pp. 275-286
    • Bayer, P.1
  • 12
    • 72849135764 scopus 로고    scopus 로고
    • Importance of covalent and noncovalent SUMO interactions with the major human cytomegalovirus transactivator IE2p86 for viral infection
    • Berndt A, Hofmann-Winkler H, Tavalai N, Hahn G, Stamminger T. 2009. Importance of covalent and noncovalent SUMO interactions with the major human cytomegalovirus transactivator IE2p86 for viral infection. J. Virol. 83:12881-12894.
    • (2009) J. Virol. , vol.83 , pp. 12881-12894
    • Berndt, A.1    Hofmann-Winkler, H.2    Tavalai, N.3    Hahn, G.4    Stamminger, T.5
  • 13
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy MN, Howe K, Etkin LD, Solomon E, Freemont PS. 1996. PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13:971-982.
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 14
    • 25444521827 scopus 로고    scopus 로고
    • Gam1 and the SUMO pathway
    • Boggio R, Chiocca S. 2005. Gam1 and the SUMO pathway. Cell Cycle 4:533-535.
    • (2005) Cell Cycle , vol.4 , pp. 533-535
    • Boggio, R.1    Chiocca, S.2
  • 15
    • 33746305530 scopus 로고    scopus 로고
    • Viruses and sumoylation: recent highlights
    • Boggio R, Chiocca S. 2006. Viruses and sumoylation: recent highlights. Curr. Opin. Microbiol. 9:430-436.
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 430-436
    • Boggio, R.1    Chiocca, S.2
  • 17
    • 34447560073 scopus 로고    scopus 로고
    • Targeting SUMO E1 to ubiquitin ligases: a viral strategy to counteract sumoylation
    • Boggio R, Passafaro A, Chiocca S. 2007. Targeting SUMO E1 to ubiquitin ligases: a viral strategy to counteract sumoylation. J. Biol. Chem. 282:15376-15382.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15376-15382
    • Boggio, R.1    Passafaro, A.2    Chiocca, S.3
  • 18
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus
    • Bohren KM, Nadkarni V, Song JH, Gabbay KH, Owerbach D. 2004. A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. J. Biol. Chem. 279:27233-27238.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 19
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • Boutell C, et al. 2011. A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog. 7:e1002245.
    • (2011) PLoS Pathog , vol.7
    • Boutell, C.1
  • 20
    • 70350681056 scopus 로고    scopus 로고
    • Mechanisms of HTLV-1 persistence and transformation
    • Boxus M, Willems L. 2009. Mechanisms of HTLV-1 persistence and transformation. Br. J. Cancer 101:1497-1501.
    • (2009) Br. J. Cancer , vol.101 , pp. 1497-1501
    • Boxus, M.1    Willems, L.2
  • 21
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • Brass AL, et al. 2008. Identification of host proteins required for HIV infection through a functional genomic screen. Science 319:921-926.
    • (2008) Science , vol.319 , pp. 921-926
    • Brass, A.L.1
  • 22
    • 0035121442 scopus 로고    scopus 로고
    • Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments
    • Burkham J, Coen DM, Hwang CB, Weller SK. 2001. Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments. J. Virol. 75:2353-2367.
    • (2001) J. Virol. , vol.75 , pp. 2353-2367
    • Burkham, J.1    Coen, D.M.2    Hwang, C.B.3    Weller, S.K.4
  • 23
    • 0031743484 scopus 로고    scopus 로고
    • ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase
    • Burkham J, Coen DM, Weller SK. 1998. ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase. J. Virol. 72: 10100-10107.
    • (1998) J. Virol. , vol.72 , pp. 10100-10107
    • Burkham, J.1    Coen, D.M.2    Weller, S.K.3
  • 24
    • 0029100611 scopus 로고
    • Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies
    • Carvalho T, et al. 1995. Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies. J. Cell Biol. 131: 45-56.
    • (1995) J. Cell Biol. , vol.131 , pp. 45-56
    • Carvalho, T.1
  • 25
    • 4644281387 scopus 로고    scopus 로고
    • Post-translational modification of Rta of Epstein-Barr virus by SUMO-1
    • Chang LK, et al. 2004. Post-translational modification of Rta of Epstein-Barr virus by SUMO-1. J. Biol. Chem. 279:38803-38812.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38803-38812
    • Chang, L.K.1
  • 26
    • 77949329517 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific
    • Chang PC, et al. 2010. Kaposi's sarcoma-associated herpesvirus (KSHV) encodes a SUMO E3 ligase that is SIM-dependent and SUMO-2/3-specific. J. Biol. Chem. 285:5266-5273.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5266-5273
    • Chang, P.C.1
  • 27
    • 67650866693 scopus 로고    scopus 로고
    • Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery
    • Chang TH, et al. 2009. Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PLoS Pathog. 5:e1000493.
    • (2009) PLoS Pathog , vol.5
    • Chang, T.H.1
  • 28
    • 34147109827 scopus 로고    scopus 로고
    • Regulation of nuclear receptor and coactivator functions by the carboxyl terminus of ubiquitin-conjugating enzyme 9
    • Chang YL, et al. 2007. Regulation of nuclear receptor and coactivator functions by the carboxyl terminus of ubiquitin-conjugating enzyme 9. Int. J. Biochem. Cell Biol. 39:1035-1046.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1035-1046
    • Chang, Y.L.1
  • 29
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasomedependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix MK, de Thé H. 1999. Herpes virus induced proteasomedependent degradation of the nuclear bodies-associated PML and Sp100 proteins. Oncogene 18:935-941.
    • (1999) Oncogene , vol.18 , pp. 935-941
    • Chelbi-Alix, M.K.1    de Thé, H.2
  • 30
    • 80052413411 scopus 로고    scopus 로고
    • Sumoylation-promoted enterovirus 71 3C degradation correlates with a reduction in viral replication and cell apoptosis
    • Chen SC, et al. 2011. Sumoylation-promoted enterovirus 71 3C degradation correlates with a reduction in viral replication and cell apoptosis. J. Biol. Chem. 286:31373-31384.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31373-31384
    • Chen, S.C.1
  • 31
    • 37749041985 scopus 로고    scopus 로고
    • Viral control of the SUMO pathway: Gam1, a model system
    • Chiocca S. 2007. Viral control of the SUMO pathway: Gam1, a model system. Biochem. Soc. Trans. 35:1419-1421.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1419-1421
    • Chiocca, S.1
  • 32
    • 0030895130 scopus 로고    scopus 로고
    • Identification of a novel antiapoptotic protein, GAM-1, encoded by the CELO adenovirus
    • Chiocca S, Baker A, Cotten M. 1997. Identification of a novel antiapoptotic protein, GAM-1, encoded by the CELO adenovirus. J. Virol. 71:3168-3177.
    • (1997) J. Virol. , vol.71 , pp. 3168-3177
    • Chiocca, S.1    Baker, A.2    Cotten, M.3
  • 33
    • 0037006797 scopus 로고    scopus 로고
    • Histone deacetylase 1 inactivation by an adenovirus early gene product
    • Chiocca S, et al. 2002. Histone deacetylase 1 inactivation by an adenovirus early gene product. Current Biol. 12:594-598.
    • (2002) Current Biol , vol.12 , pp. 594-598
    • Chiocca, S.1
  • 34
    • 34648828978 scopus 로고    scopus 로고
    • The type 2 dengue virus envelope protein interacts with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9)
    • Chiu MW, Shih HM, Yang TH, Yang YL. 2007. The type 2 dengue virus envelope protein interacts with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9). J. Biomed. Sci. 14:429-444.
    • (2007) J. Biomed. Sci. , vol.14 , pp. 429-444
    • Chiu, M.W.1    Shih, H.M.2    Yang, T.H.3    Yang, Y.L.4
  • 35
    • 77955717602 scopus 로고    scopus 로고
    • Listeria monocytogenes: a bacterial pathogen to hit on the SUMO pathway
    • Citro S, Chiocca S. 2010. Listeria monocytogenes: a bacterial pathogen to hit on the SUMO pathway. Cell Res. 20:738-740.
    • (2010) Cell Res , vol.20 , pp. 738-740
    • Citro, S.1    Chiocca, S.2
  • 36
    • 0038050244 scopus 로고    scopus 로고
    • The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1
    • Colombo R, Boggio R, Seiser C, Draetta GF, Chiocca S. 2002. The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1. EMBO Rep. 3:1062-1068.
    • (2002) EMBO Rep , vol.3 , pp. 1062-1068
    • Colombo, R.1    Boggio, R.2    Seiser, C.3    Draetta, G.F.4    Chiocca, S.5
  • 37
    • 0036192725 scopus 로고    scopus 로고
    • The Yersinia Ysc-Yop virulence apparatus
    • Cornelis GR. 2002. The Yersinia Ysc-Yop virulence apparatus. Int. J. Med. Microbiol. 291:455-462.
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 455-462
    • Cornelis, G.R.1
  • 39
    • 79960942804 scopus 로고    scopus 로고
    • SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes
    • Cuchet-Lourenço D, et al. 2011. SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes. PLoS Pathog. 7:e1002123.
    • (2011) PLoS Pathog , vol.7
    • Cuchet-Lourenço, D.1
  • 40
    • 78651364746 scopus 로고    scopus 로고
    • Over-accumulation of nuclear Igf-1 receptor in tumor cells requires elevated expression of the receptor and the SUMOconjugating enzyme Ubc9
    • Deng H, et al. Over-accumulation of nuclear IGF-1 receptor in tumor cells requires elevated expression of the receptor and the SUMOconjugating enzyme Ubc9. 2011. Biochem. Biophys. Res. Commun. 404: 667-671.
    • (2011) Biochem. Biophys. Res. Commun , vol.404 , pp. 667-671
    • Deng, H.1
  • 42
    • 0030052130 scopus 로고    scopus 로고
    • Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure
    • Doucas V, et al. 1996. Adenovirus replication is coupled with the dynamic properties of the PML nuclear structure. Genes Dev. 10:196-207.
    • (1996) Genes Dev , vol.10 , pp. 196-207
    • Doucas, V.1
  • 43
    • 77951297101 scopus 로고    scopus 로고
    • Polymorphisms in the UBC9 and PIAS3 genes of the Sumo-conjugating system and breast cancer risk
    • Dunnebier T, et al. 2010. Polymorphisms in the UBC9 and PIAS3 genes of the SUMO-conjugating system and breast cancer risk. Breast Cancer Res. Treat 121:185-194.
    • (2010) Breast Cancer Res. Treat , vol.121 , pp. 185-194
    • Dunnebier, T.1
  • 44
    • 12444320379 scopus 로고    scopus 로고
    • Blockage of CRM1-dependent nuclear export of the adenovirus type 5 early region 1B 55-kDa protein augments oncogenic transformation of primary rat cells
    • Endter C, Hartl B, Spruss T, Hauber J, Dobner T. 2005. Blockage of CRM1-dependent nuclear export of the adenovirus type 5 early region 1B 55-kDa protein augments oncogenic transformation of primary rat cells. Oncogene 24:55-64.
    • (2005) Oncogene , vol.24 , pp. 55-64
    • Endter, C.1    Hartl, B.2    Spruss, T.3    Hauber, J.4    Dobner, T.5
  • 45
    • 0035949590 scopus 로고    scopus 로고
    • SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein
    • Endter C, Kzhyshkowska J, Stauber R, Dobner T. 2001. SUMO-1 modification required for transformation by adenovirus type 5 early region 1B 55-kDa oncoprotein. Proc. Natl. Acad. Sci. U. S. A. 98: 11312-11317.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11312-11317
    • Endter, C.1    Kzhyshkowska, J.2    Stauber, R.3    Dobner, T.4
  • 46
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett RD. 2001. DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 20:7266-7273.
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 47
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK. 2007. PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89:819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 48
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110-and proteasome-dependent loss of several PML isoforms
    • Everett RD, et al. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1
  • 49
    • 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, et al. 1997. A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16:1519-1530.
    • (1997) EMBO J , vol.16 , pp. 1519-1530
    • Everett, R.D.1
  • 50
    • 16244422998 scopus 로고    scopus 로고
    • ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection
    • Everett RD, Murray J. 2005. ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection. J. Virol. 79:5078-5089.
    • (2005) J. Virol. , vol.79 , pp. 5078-5089
    • Everett, R.D.1    Murray, J.2
  • 51
    • 35148893559 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts
    • Everett RD, Murray J, Orr A, Preston CM. 2007. Herpes simplex virus type 1 genomes are associated with ND10 nuclear substructures in quiescently infected human fibroblasts. J. Virol. 81:10991-11004.
    • (2007) J. Virol. , vol.81 , pp. 10991-11004
    • Everett, R.D.1    Murray, J.2    Orr, A.3    Preston, C.M.4
  • 52
    • 40149085109 scopus 로고    scopus 로고
    • Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100
    • Everett RD, Parada C, Gripon P, Sirma H, Orr A. 2008. Replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and Sp100. J. Virol. 82:2661-2672.
    • (2008) J. Virol. , vol.82 , pp. 2661-2672
    • Everett, R.D.1    Parada, C.2    Gripon, P.3    Sirma, H.4    Orr, A.5
  • 53
    • 33746827706 scopus 로고    scopus 로고
    • PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
    • Everett RD, et al. 2006. PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0. J. Virol. 80:7995-8005.
    • (2006) J. Virol. , vol.80 , pp. 7995-8005
    • Everett, R.D.1
  • 54
    • 0842304512 scopus 로고    scopus 로고
    • Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes
    • Everett RD, Sourvinos G, Leiper C, Clements JB, Orr A. 2004. Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes. J. Virol. 78:1903-1917.
    • (2004) J. Virol. , vol.78 , pp. 1903-1917
    • Everett, R.D.1    Sourvinos, G.2    Leiper, C.3    Clements, J.B.4    Orr, A.5
  • 55
    • 33749550928 scopus 로고    scopus 로고
    • SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system
    • Fan Z, et al. 2006. SARS-CoV nucleocapsid protein binds to hUbc9, a ubiquitin conjugating enzyme of the sumoylation system. J. Med. Virol. 78:1365-1373.
    • (2006) J. Med. Virol. , vol.78 , pp. 1365-1373
    • Fan, Z.1
  • 56
    • 70450221504 scopus 로고    scopus 로고
    • Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9
    • Fradet-Turcotte A, Brault K, Titolo S, Howley PM, Archambault J. 2009. Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9. Virology 395: 190-201.
    • (2009) Virology , vol.395 , pp. 190-201
    • Fradet-Turcotte, A.1    Brault, K.2    Titolo, S.3    Howley, P.M.4    Archambault, J.5
  • 57
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed EO. 2002. Viral late domains. J. Virol. 76:4679-4687.
    • (2002) J. Virol. , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 60
    • 78650109515 scopus 로고    scopus 로고
    • Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies
    • Geoffroy MC, Jaffray EG, Walker KJ, Hay RT. 2010. Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies. Mol. Biol. Cell 21:4227-4239.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4227-4239
    • Geoffroy, M.C.1    Jaffray, E.G.2    Walker, K.J.3    Hay, R.T.4
  • 61
    • 70749151578 scopus 로고    scopus 로고
    • Coxsackievirus B5 induced apoptosis of HeLa cells: effects on p53 and SUMO
    • Gomes R, Guerra-Sa R, Arruda E. 2010. Coxsackievirus B5 induced apoptosis of HeLa cells: effects on p53 and SUMO. Virology 396: 256-263.
    • (2010) Virology , vol.396 , pp. 256-263
    • Gomes, R.1    Guerra-Sa, R.2    Arruda, E.3
  • 62
    • 84855823939 scopus 로고    scopus 로고
    • Regulation of vaccinia virus E3 protein by small ubiquitin-like modifier proteins
    • González-Santamaría J, et al. 2011. Regulation of vaccinia virus E3 protein by small ubiquitin-like modifier proteins. J. Virol. 85: 12890-12900.
    • (2011) J. Virol. , vol.85 , pp. 12890-12900
    • González-Santamaría, J.1
  • 63
    • 2442700146 scopus 로고    scopus 로고
    • Characterization of human herpesvirus 6 variant B immediate-early 1 protein modifications by small ubiquitin-related modifiers
    • Gravel A, Dion V, Cloutier N, Gosselin J, Flamand L. 2004. Characterization of human herpesvirus 6 variant B immediate-early 1 protein modifications by small ubiquitin-related modifiers. J. Gen. Virol. 85: 1319-1328.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1319-1328
    • Gravel, A.1    Dion, V.2    Cloutier, N.3    Gosselin, J.4    Flamand, L.5
  • 64
    • 0037205469 scopus 로고    scopus 로고
    • Human herpesvirus 6 immediate-early 1 protein is a sumoylated nuclear phosphoprotein colocalizing with promyelocytic leukemia protein-associated nuclear bodies
    • Gravel A, Gosselin J, Flamand L. 2002. Human herpesvirus 6 immediate-early 1 protein is a sumoylated nuclear phosphoprotein colocalizing with promyelocytic leukemia protein-associated nuclear bodies. J. Biol. Chem. 277:19679-19687.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19679-19687
    • Gravel, A.1    Gosselin, J.2    Flamand, L.3
  • 65
    • 11144231031 scopus 로고    scopus 로고
    • Covalent modification of human immunodeficiency virus type 1 p6 by SUMO-1
    • Gurer C, Berthoux L, Luban J. 2005. Covalent modification of human immunodeficiency virus type 1 p6 by SUMO-1. J. Virol. 79:910-917.
    • (2005) J. Virol. , vol.79 , pp. 910-917
    • Gurer, C.1    Berthoux, L.2    Luban, J.3
  • 66
    • 0026644129 scopus 로고
    • The 72K IE1 and 80K IE2 proteins of human cytomegalovirus independently transactivate the c-fos, c-myc and hsp70 promoters via basal promoter elements
    • Hagemeier C, Walker SM, Sissons PJ, Sinclair JH. 1992. The 72K IE1 and 80K IE2 proteins of human cytomegalovirus independently transactivate the c-fos, c-myc and hsp70 promoters via basal promoter elements. J. Gen. Virol. 73:2385-2393.
    • (1992) J. Gen. Virol. , vol.73 , pp. 2385-2393
    • Hagemeier, C.1    Walker, S.M.2    Sissons, P.J.3    Sinclair, J.H.4
  • 67
    • 77950811209 scopus 로고    scopus 로고
    • Sumoylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virusencoded protein kinase
    • Hagemeier SR, et al. 2010. Sumoylation of the Epstein-Barr virus BZLF1 protein inhibits its transcriptional activity and is regulated by the virusencoded protein kinase. J. Virol. 84:4383-4394.
    • (2010) J. Virol. , vol.84 , pp. 4383-4394
    • Hagemeier, S.R.1
  • 68
    • 77951235215 scopus 로고    scopus 로고
    • SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress
    • Han Y, et al. 2010. SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress. J. Biol. Chem. 285:12906-12915.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12906-12915
    • Han, Y.1
  • 70
    • 0029957644 scopus 로고    scopus 로고
    • mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect
    • Hateboer G, et al. 1996. mUBC9, a novel adenovirus E1A-interacting protein that complements a yeast cell cycle defect. J. Biol. Chem. 271: 25906-25911.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25906-25911
    • Hateboer, G.1
  • 71
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: a history of modification
    • Hay RT. 2005. SUMO: a history of modification. Mol. Cell 18:1-12.
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 72
    • 0036430683 scopus 로고    scopus 로고
    • Ubc9 is essential for viability of higher eukaryotic cells
    • Hayashi T, et al. 2002. Ubc9 is essential for viability of higher eukaryotic cells. Exp. Cell Res. 280:212-221.
    • (2002) Exp. Cell Res. , vol.280 , pp. 212-221
    • Hayashi, T.1
  • 73
    • 0025281335 scopus 로고
    • Human cytomegalovirus immediate-early two protein region involved in negative regulation of the major immediate-early promoter
    • Hermiston TW, Malone CL, Stinski MF. 1990. Human cytomegalovirus immediate-early two protein region involved in negative regulation of the major immediate-early promoter. J. Virol. 64:3532-3536.
    • (1990) J. Virol. , vol.64 , pp. 3532-3536
    • Hermiston, T.W.1    Malone, C.L.2    Stinski, M.F.3
  • 74
    • 30444440554 scopus 로고    scopus 로고
    • PDSM, a motif for phosphorylationdependent SUMO modification
    • Hietakangas V, et al. 2006. PDSM, a motif for phosphorylationdependent SUMO modification. Proc. Natl. Acad. Sci. U. S. A. 103: 45-50.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 45-50
    • Hietakangas, V.1
  • 75
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M. 2009. Origin and function of ubiquitin-like proteins. Nature 458:422-429.
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 76
    • 0343340071 scopus 로고    scopus 로고
    • Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b
    • Hofmann H, Floss S, Stamminger T. 2000. Covalent modification of the transactivator protein IE2-p86 of human cytomegalovirus by conjugation to the ubiquitin-homologous proteins SUMO-1 and hSMT3b. J. Virol. 74:2510-2524.
    • (2000) J. Virol. , vol.74 , pp. 2510-2524
    • Hofmann, H.1    Floss, S.2    Stamminger, T.3
  • 77
    • 55249109587 scopus 로고    scopus 로고
    • Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO
    • Huh YH, et al. 2008. Binding STAT2 by the acidic domain of human cytomegalovirus IE1 promotes viral growth and is negatively regulated by SUMO. J. Virol. 82:10444-10454.
    • (2008) J. Virol. , vol.82 , pp. 10444-10454
    • Huh, Y.H.1
  • 78
    • 22544486295 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification
    • Izumiya Y, et al. 2005. Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification. J. Virol. 79: 9912-9925.
    • (2005) J. Virol. , vol.79 , pp. 9912-9925
    • Izumiya, Y.1
  • 79
    • 70349737881 scopus 로고    scopus 로고
    • Human Ubc9 contributes to production of fully infectious human immunodeficiency virus type 1 virions
    • Jaber T, et al. 2009. Human Ubc9 contributes to production of fully infectious human immunodeficiency virus type 1 virions. J. Virol. 83: 10448-10459.
    • (2009) J. Virol. , vol.83 , pp. 10448-10459
    • Jaber, T.1
  • 80
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson ES. 2004. Protein modification by SUMO. Annu. Rev. Biochem. 73:355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 81
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson ES, Gupta AA. 2001. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106:735-744.
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 82
    • 61449247171 scopus 로고    scopus 로고
    • SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells
    • Kaikkonen S, et al. 2009. SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells. Mol. Endocrinol. 23: 292-307.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 292-307
    • Kaikkonen, S.1
  • 83
    • 33746824547 scopus 로고    scopus 로고
    • Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein
    • Kang H, et al. 2006. Inhibition of SUMO-independent PML oligomerization by the human cytomegalovirus IE1 protein. J. Gen. Virol. 87: 2181-2190.
    • (2006) J. Gen. Virol. , vol.87 , pp. 2181-2190
    • Kang, H.1
  • 84
    • 0037370962 scopus 로고    scopus 로고
    • Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitinrelated modifier-1, SUMO-1
    • Kaukinen P, Vaheri A, Plyusnin A. 2003. Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitinrelated modifier-1, SUMO-1. Virus Res. 92:37-45.
    • (2003) Virus Res , vol.92 , pp. 37-45
    • Kaukinen, P.1    Vaheri, A.2    Plyusnin, A.3
  • 85
    • 0037066790 scopus 로고    scopus 로고
    • Ubc9 is a novel modulator of the induction properties of glucocorticoid receptors
    • Kaul S, Blackford JA Jr, Cho S, Simons SS Jr. 2002. Ubc9 is a novel modulator of the induction properties of glucocorticoid receptors. J. Biol. Chem. 277:12541-12549.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12541-12549
    • Kaul, S.1    Blackford Jr., J.A.2    Cho, S.3    Simons Jr., S.S.4
  • 86
    • 26444561651 scopus 로고    scopus 로고
    • Mechanisms of HTLV-1 transformation
    • Kehn K, et al. 2004. Mechanisms of HTLV-1 transformation. Front. Biosci. 9:2347-2372.
    • (2004) Front. Biosci. , vol.9 , pp. 2347-2372
    • Kehn, K.1
  • 87
    • 0028972538 scopus 로고
    • Disruption of PMLassociated nuclear bodies during human cytomegalovirus infection
    • Kelly C, Van Driel R, Wilkinson GW. 1995. Disruption of PMLassociated nuclear bodies during human cytomegalovirus infection. J. Gen. Virol. 76:2887-2893.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2887-2893
    • Kelly, C.1    Van Driel, R.2    Wilkinson, G.W.3
  • 88
    • 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. EMBO Rep. 8:550-555.
    • (2007) EMBO Rep , vol.8 , pp. 550-555
    • Kerscher, O.1
  • 90
    • 78650985961 scopus 로고    scopus 로고
    • Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome
    • Kfoury Y, et al. 2011. Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome. Blood 117:190-199.
    • (2011) Blood , vol.117 , pp. 190-199
    • Kfoury, Y.1
  • 91
    • 77954982420 scopus 로고    scopus 로고
    • Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth
    • Kim ET, Kim YE, Huh YH, Ahn JH. 2010. Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth. J. Virol. 84:8111-8123.
    • (2010) J. Virol. , vol.84 , pp. 8111-8123
    • Kim, E.T.1    Kim, Y.E.2    Huh, Y.H.3    Ahn, J.H.4
  • 92
    • 34249852362 scopus 로고    scopus 로고
    • Intranuclear targeting and nuclear export of the adenovirus E1B-55K protein are regulated by SUMO1 conjugation
    • Kindsmüller K, et al. 2007. Intranuclear targeting and nuclear export of the adenovirus E1B-55K protein are regulated by SUMO1 conjugation. Proc. Natl. Acad. Sci. U. S. A. 104:6684-6689.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6684-6689
    • Kindsmüller, K.1
  • 93
    • 1542360838 scopus 로고    scopus 로고
    • Ubc9 interacts with chicken ovalbumin upstream promoter-transcription factor I and represses receptordependent transcription
    • Kobayashi S, et al. 2004. Ubc9 interacts with chicken ovalbumin upstream promoter-transcription factor I and represses receptordependent transcription. J. Mol. Endocrinol. 32:69-86.
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 69-86
    • Kobayashi, S.1
  • 94
    • 76749108989 scopus 로고    scopus 로고
    • Human host factors required for influenza virus replication
    • König R, et al. 2010. Human host factors required for influenza virus replication. Nature 463:813-817.
    • (2010) Nature , vol.463 , pp. 813-817
    • König, R.1
  • 95
    • 52949130695 scopus 로고    scopus 로고
    • Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication
    • König R, et al. 2008. Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication. Cell 135:49-60.
    • (2008) Cell , vol.135 , pp. 49-60
    • König, R.1
  • 96
    • 54449099430 scopus 로고    scopus 로고
    • Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression
    • Kubota T, et al. 2008. Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression. J. Biol. Chem. 283:25660-25670.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25660-25670
    • Kubota, T.1
  • 97
    • 0035826705 scopus 로고    scopus 로고
    • Ubc9 interacts with a nuclear localization signal and mediates nuclear localization of the paired-like homeobox protein Vsx-1 independent of SUMO-1 modification
    • Kurtzman AL, Schechter N. 2001. Ubc9 interacts with a nuclear localization signal and mediates nuclear localization of the paired-like homeobox protein Vsx-1 independent of SUMO-1 modification. Proc. Natl. Acad. Sci. U. S. A. 98:5602-5607.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5602-5607
    • Kurtzman, A.L.1    Schechter, N.2
  • 98
    • 66149128368 scopus 로고    scopus 로고
    • Components of nuclear domain 10 bodies regulate varicella-zoster virus replication
    • Kyratsous CA, Silverstein SJ. 2009. Components of nuclear domain 10 bodies regulate varicella-zoster virus replication. J. Virol. 83:4262-4274.
    • (2009) J. Virol. , vol.83 , pp. 4262-4274
    • Kyratsous, C.A.1    Silverstein, S.J.2
  • 99
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PMLRARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • Lallemand-Breitenbach V, et al. 2008. Arsenic degrades PML or PMLRARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat. Cell Biol. 10:547-555.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 547-555
    • Lallemand-Breitenbach, V.1
  • 100
    • 27944431565 scopus 로고    scopus 로고
    • Exclusive ubiquitination and sumoylation on overlapping lysine residues mediate NF-kappaB activation by the human T-cell leukemia virus tax oncoprotein
    • Lamsoul I, et al. 2005. Exclusive ubiquitination and sumoylation on overlapping lysine residues mediate NF-kappaB activation by the human T-cell leukemia virus tax oncoprotein. Mol. Cell. Biol. 25:10391-10406.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10391-10406
    • Lamsoul, I.1
  • 101
    • 76649083577 scopus 로고    scopus 로고
    • Three-dimensional organization of promyelocytic leukemia nuclear bodies
    • Lang M, et al. 2010. Three-dimensional organization of promyelocytic leukemia nuclear bodies. J. Cell Sci. 123:392-400.
    • (2010) J. Cell Sci. , vol.123 , pp. 392-400
    • Lang, M.1
  • 102
    • 0242552701 scopus 로고    scopus 로고
    • Association of the nucleocapsid protein of the Seoul and Hantaan hantaviruses with small ubiquitin-like modifier-1-related molecules
    • Lee BH, et al. 2003. Association of the nucleocapsid protein of the Seoul and Hantaan hantaviruses with small ubiquitin-like modifier-1-related molecules. Virus Res. 98:83-91.
    • (2003) Virus Res , vol.98 , pp. 83-91
    • Lee, B.H.1
  • 103
    • 4043163436 scopus 로고    scopus 로고
    • Sumoylation of the major immediate-early IE2 protein of human cytomegalovirus Towne strain is not required for virus growth in cultured human fibroblasts
    • Lee HR, Ahn JH. 2004. Sumoylation of the major immediate-early IE2 protein of human cytomegalovirus Towne strain is not required for virus growth in cultured human fibroblasts. J. Gen. Virol. 85:2149-2154.
    • (2004) J. Gen. Virol. , vol.85 , pp. 2149-2154
    • Lee, H.R.1    Ahn, J.H.2
  • 104
    • 2642574870 scopus 로고    scopus 로고
    • Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells
    • Lee HR, et al. 2004. Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J. Virol. 78:6527-6542.
    • (2004) J. Virol. , vol.78 , pp. 6527-6542
    • Lee, H.R.1
  • 105
    • 0344872513 scopus 로고    scopus 로고
    • PIAS1 enhances SUMO-1 modification and the transactivation activity of the major immediate-early IE2 protein of human cytomegalovirus
    • Lee JM, et al. 2003. PIAS1 enhances SUMO-1 modification and the transactivation activity of the major immediate-early IE2 protein of human cytomegalovirus. FEBS Lett. 555:322-328.
    • (2003) FEBS Lett , vol.555 , pp. 322-328
    • Lee, J.M.1
  • 106
    • 0028279779 scopus 로고
    • Proteolytic cleavage of vaccinia virus virion proteins: mutational analysis of the specificity determinants
    • Lee P, Hruby DE. 1994. Proteolytic cleavage of vaccinia virus virion proteins: mutational analysis of the specificity determinants. J. Biol. Chem. 269:8616-8622.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8616-8622
    • Lee, P.1    Hruby, D.E.2
  • 107
    • 0037311411 scopus 로고    scopus 로고
    • Nuclear matrix localization and SUMO-1 modification of adenovirus type 5 E1b 55K protein are controlled by E4 Orf6 protein
    • Lethbridge KJ, Scott GE, Leppard KN. 2003. Nuclear matrix localization and SUMO-1 modification of adenovirus type 5 E1b 55K protein are controlled by E4 Orf6 protein. J. Gen. Virol. 84:259-268.
    • (2003) J. Gen. Virol. , vol.84 , pp. 259-268
    • Lethbridge, K.J.1    Scott, G.E.2    Leppard, K.N.3
  • 108
    • 17644426001 scopus 로고    scopus 로고
    • Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus
    • Li FQ, Xiao H, Tam JP, Liu DX. 2005. Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus. FEBS Lett. 579:2387-2396.
    • (2005) FEBS Lett , vol.579 , pp. 2387-2396
    • Li, F.Q.1    Xiao, H.2    Tam, J.P.3    Liu, D.X.4
  • 109
    • 84934436346 scopus 로고    scopus 로고
    • Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus by interaction with Ubc9
    • Li Q, Xiao H, Tam JP, Liu DX. 2006. Sumoylation of the nucleocapsid protein of severe acute respiratory syndrome coronavirus by interaction with Ubc9. Adv. Exp. Med. Biol. 581:121-126.
    • (2006) Adv. Exp. Med. Biol. , vol.581 , pp. 121-126
    • Li, Q.1    Xiao, H.2    Tam, J.P.3    Liu, D.X.4
  • 110
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li SJ, Hochstrasser M. 1999. A new protease required for cell-cycle progression in yeast. Nature 398:246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 111
    • 0034310736 scopus 로고    scopus 로고
    • Mechanisms of NF-kappaB activation by the HTLV type 1 tax protein
    • Li XH, Gaynor RB. 2000. Mechanisms of NF-kappaB activation by the HTLV type 1 tax protein. AIDS Res. Hum. Retroviruses 16:1583-1590.
    • (2000) AIDS Res. Hum. Retroviruses , vol.16 , pp. 1583-1590
    • Li, X.H.1    Gaynor, R.B.2
  • 112
    • 33646807840 scopus 로고    scopus 로고
    • Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxbeta
    • Liu ST, et al. 2006. Sumoylation of Rta of Epstein-Barr virus is preferentially enhanced by PIASxbeta. Virus Res. 119:163-170.
    • (2006) Virus Res , vol.119 , pp. 163-170
    • Liu, S.T.1
  • 113
    • 0024383385 scopus 로고
    • Gly-Gly-X, a novel consensus sequence for the proteolytic processing of viral and cellular proteins
    • López-Otín C, Simon-Mateo C, Martinez L, Vinuela E. 1989. Gly-Gly-X, a novel consensus sequence for the proteolytic processing of viral and cellular proteins. J. Biol. Chem. 264:9107-9110.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9107-9110
    • López-Otín, C.1    Simon-Mateo, C.2    Martinez, L.3    Vinuela, E.4
  • 114
    • 77950515413 scopus 로고    scopus 로고
    • Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx
    • Lukashchuk V, Everett RD. 2010. Regulation of ICP0-null mutant herpes simplex virus type 1 infection by ND10 components ATRX and hDaxx. J. Virol. 84:4026-4040.
    • (2010) J. Virol. , vol.84 , pp. 4026-4040
    • Lukashchuk, V.1    Everett, R.D.2
  • 115
    • 0037455554 scopus 로고    scopus 로고
    • The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9)
    • Maeda A, et al. 2003. The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating enzyme 9 (Ubc9). Virology 305: 288-297.
    • (2003) Virology , vol.305 , pp. 288-297
    • Maeda, A.1
  • 116
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R, Delphin C, Guan T, Gerace L, Melchior F. 1997. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88:97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 117
    • 0025260745 scopus 로고
    • Transactivation of a human cytomegalovirus early promoter by gene products from the immediateearly gene IE2 and augmentation by IE1: mutational analysis of the viral proteins
    • Malone CL, Vesole DH, Stinski MF. 1990. Transactivation of a human cytomegalovirus early promoter by gene products from the immediateearly gene IE2 and augmentation by IE1: mutational analysis of the viral proteins. J. Virol. 64:1498-1506.
    • (1990) J. Virol. , vol.64 , pp. 1498-1506
    • Malone, C.L.1    Vesole, D.H.2    Stinski, M.F.3
  • 118
    • 78651233952 scopus 로고    scopus 로고
    • Covalent modification by SUMO is required for efficient disruption of PML oncogenic domains by Kaposi's sarcoma-associated herpesvirus latent protein LANA2
    • Marcos-Villar L, et al. 2011. Covalent modification by SUMO is required for efficient disruption of PML oncogenic domains by Kaposi's sarcoma-associated herpesvirus latent protein LANA2. J. Gen. Virol. 92: 188-194.
    • (2011) J. Gen. Virol. , vol.92 , pp. 188-194
    • Marcos-Villar, L.1
  • 119
    • 69249206864 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus protein LANA2 disrupts PML oncogenic domains and inhibits PMLmediated transcriptional repression of the survivin gene
    • Marcos-Villar L, et al. 2009. Kaposi's sarcoma-associated herpesvirus protein LANA2 disrupts PML oncogenic domains and inhibits PMLmediated transcriptional repression of the survivin gene. J. Virol. 83: 8849-8858.
    • (2009) J. Virol. , vol.83 , pp. 8849-8858
    • Marcos-Villar, L.1
  • 120
    • 77957959661 scopus 로고    scopus 로고
    • Modification of human papillomavirus minor capsid protein L2 by sumoylation
    • Marusic MB, Mencin N, Licen M, Banks L, Grm HS. 2010. Modification of human papillomavirus minor capsid protein L2 by sumoylation. J. Virol. 84:11585-11589.
    • (2010) J. Virol. , vol.84 , pp. 11585-11589
    • Marusic, M.B.1    Mencin, N.2    Licen, M.3    Banks, L.4    Grm, H.S.5
  • 121
    • 77955999636 scopus 로고    scopus 로고
    • Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif
    • Matic I, et al. 2010. Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif. Mol. Cell 39:641-652.
    • (2010) Mol. Cell , vol.39 , pp. 641-652
    • Matic, I.1
  • 122
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis MJ, Coutavas E, Blobel G. 1996. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 123
    • 0028352769 scopus 로고
    • The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0
    • Maul GG, Everett RD. 1994. The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. J. Gen. Virol. 75:1223-1233.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1223-1233
    • Maul, G.G.1    Everett, R.D.2
  • 124
    • 0027769358 scopus 로고
    • Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0)
    • Maul GG, Guldner HH, Spivack JG. 1993. Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). J. Gen. Virol. 74:2679-2690.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2679-2690
    • Maul, G.G.1    Guldner, H.H.2    Spivack, J.G.3
  • 125
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh PB, Koshland D. 1995. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 6:793-807.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 127
    • 77955924786 scopus 로고    scopus 로고
    • Expression analysis of Ubc9, the single small ubiquitin-like modifier (SUMO) E2 conjugating enzyme, in normal and malignant tissues
    • Moschos S. J, et al. 2010. Expression analysis of Ubc9, the single small ubiquitin-like modifier (SUMO) E2 conjugating enzyme, in normal and malignant tissues. Hum. Pathol. 41:1286-1298.
    • (2010) Hum. Pathol. , vol.41 , pp. 1286-1298
    • Moschos, S.J.1
  • 128
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova E, Lima CD. 2000. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5:865-876.
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 129
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: the SUMO proteases
    • Mukhopadhyay D, Dasso M. 2007. Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 32:286-295.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 130
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Muller S, Dejean A. 1999. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J. Virol. 73:5137-5143.
    • (1999) J. Virol. , vol.73 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 131
    • 77954950105 scopus 로고    scopus 로고
    • Transcriptional repression by sumoylation of Epstein-Barr virus BZLF1 protein correlates with association of histone deacetylase
    • Murata T, et al. 2010. Transcriptional repression by sumoylation of Epstein-Barr virus BZLF1 protein correlates with association of histone deacetylase. J. Biol. Chem. 285:23925-23935.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23925-23935
    • Murata, T.1
  • 132
    • 28444448039 scopus 로고    scopus 로고
    • The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice
    • Nacerddine K, et al. 2005. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev. Cell 9:769-779.
    • (2005) Dev. Cell , vol.9 , pp. 769-779
    • Nacerddine, K.1
  • 133
    • 3142732205 scopus 로고    scopus 로고
    • SUMOylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replication
    • Nevels M, Brune W, Shenk T. 2004. SUMOylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replication. J. Virol. 78: 7803-7812.
    • (2004) J. Virol. , vol.78 , pp. 7803-7812
    • Nevels, M.1    Brune, W.2    Shenk, T.3
  • 134
    • 33845421737 scopus 로고    scopus 로고
    • Ubc9 regulates mitosis and cell survival during zebrafish development
    • Nowak M, Hammerschmidt M. 2006. Ubc9 regulates mitosis and cell survival during zebrafish development. Mol. Biol. Cell 17:5324-5336.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5324-5336
    • Nowak, M.1    Hammerschmidt, M.2
  • 135
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • Okura T, et al. 1996. Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J. Immunol. 157: 4277-4281.
    • (1996) J. Immunol. , vol.157 , pp. 4277-4281
    • Okura, T.1
  • 136
    • 0036162971 scopus 로고    scopus 로고
    • Function of the Yersinia effector YopJ
    • Orth K. 2002. Function of the Yersinia effector YopJ. Curr. Opin. Microbiol. 5:38-43.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 38-43
    • Orth, K.1
  • 137
    • 84856856859 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 138
    • 0034711403 scopus 로고    scopus 로고
    • Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease
    • Orth K, et al. 2000. Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease. Science 290:1594-1597.
    • (2000) Science , vol.290 , pp. 1594-1597
    • Orth, K.1
  • 141
    • 73049115776 scopus 로고    scopus 로고
    • Identification of the nonstructural influenza A viral protein NS1A as a bona fide target of the Small Ubiquitin-like MOdifier by the use of dicistronic expression constructs
    • Pal S, Rosas JM, Rosas-Acosta G. 2010. Identification of the nonstructural influenza A viral protein NS1A as a bona fide target of the Small Ubiquitin-like MOdifier by the use of dicistronic expression constructs. J. Virol. Methods 163:498-504.
    • (2010) J. Virol. Methods , vol.163 , pp. 498-504
    • Pal, S.1    Rosas, J.M.2    Rosas-Acosta, G.3
  • 142
    • 79956303456 scopus 로고    scopus 로고
    • Influenza A virus interacts extensively with the cellular SUMOylation system during infection
    • Pal S, Santos A, Rosas JM, Ortiz-Guzman J, Rosas-Acosta G. 2011. Influenza A virus interacts extensively with the cellular SUMOylation system during infection. Virus Res. 158:12-27.
    • (2011) Virus Res , vol.158 , pp. 12-27
    • Pal, S.1    Santos, A.2    Rosas, J.M.3    Ortiz-Guzman, J.4    Rosas-Acosta, G.5
  • 143
    • 19644396270 scopus 로고    scopus 로고
    • Quantitative SUMO-1 modification of a vaccinia virus protein is required for its specific localization and prevents its selfassociation
    • Palacios S, et al. 2005. Quantitative SUMO-1 modification of a vaccinia virus protein is required for its specific localization and prevents its selfassociation. Mol. Biol. Cell 16:2822-2835.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2822-2835
    • Palacios, S.1
  • 144
    • 33646148721 scopus 로고    scopus 로고
    • Ubc9 interacts with SOX4 and represses its transcriptional activity
    • Pan X, et al. 2006. Ubc9 interacts with SOX4 and represses its transcriptional activity. Biochem. Biophys. Res. Commun. 344:727-734.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 727-734
    • Pan, X.1
  • 145
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Parkinson J, Everett RD. 2000. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J. Virol. 74:10006-10017.
    • (2000) J. Virol. , vol.74 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 146
    • 34548749786 scopus 로고    scopus 로고
    • Human T-cell leukemia virus type 1 Tax and cellular transformation
    • Peloponese JM Jr, Kinjo T, Jeang KT. 2007. Human T-cell leukemia virus type 1 Tax and cellular transformation. Int. J. Hematol. 86:101-106.
    • (2007) Int. J. Hematol. , vol.86 , pp. 101-106
    • Peloponese Jr., J.M.1    Kinjo, T.2    Jeang, K.T.3
  • 147
    • 78049525016 scopus 로고    scopus 로고
    • Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that represses p53 and stimulates its nuclear export through interactions with promyelocytic leukemia nuclear bodies
    • Pennella MA, Liu Y, Woo JL, Kim CA, Berk AJ. 2010. Adenovirus E1B 55-kilodalton protein is a p53-SUMO1 E3 ligase that represses p53 and stimulates its nuclear export through interactions with promyelocytic leukemia nuclear bodies. J. Virol. 84:12210-12225.
    • (2010) J. Virol. , vol.84 , pp. 12210-12225
    • Pennella, M.A.1    Liu, Y.2    Woo, J.L.3    Kim, C.A.4    Berk, A.J.5
  • 149
    • 0023849393 scopus 로고
    • trans-Activation and autoregulation of gene expression by the immediate-early region 2 gene products of human cytomegalovirus
    • Pizzorno MC, O'Hare P, Sha L, LaFemina RL, Hayward GS. 1988. trans-Activation and autoregulation of gene expression by the immediate-early region 2 gene products of human cytomegalovirus. J. Virol. 62:1167-1179.
    • (1988) J. Virol. , vol.62 , pp. 1167-1179
    • Pizzorno, M.C.1    O'Hare, P.2    Sha, L.3    LaFemina, R.L.4    Hayward, G.S.5
  • 150
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O, Alam SL, Davis DR, Sundquist WI. 2002. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat. Struct. Biol. 9:812-817.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 151
    • 0037093316 scopus 로고    scopus 로고
    • Structure and functional interactions of the Tsg101 UEV domain
    • Pornillos O, et al. 2002. Structure and functional interactions of the Tsg101 UEV domain. EMBO J. 21:2397-2406.
    • (2002) EMBO J , vol.21 , pp. 2397-2406
    • Pornillos, O.1
  • 153
    • 34648840192 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin ligases in genome stability
    • Prudden J, et al. 2007. SUMO-targeted ubiquitin ligases in genome stability. EMBO J. 26:4089-4101.
    • (2007) EMBO J , vol.26 , pp. 4089-4101
    • Prudden, J.1
  • 154
    • 0029032354 scopus 로고
    • Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body-associated PML protein
    • Puvion-Dutilleul F, et al. 1995. Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body-associated PML protein. Exp. Cell Res. 218:9-16.
    • (1995) Exp. Cell Res. , vol.218 , pp. 9-16
    • Puvion-Dutilleul, F.1
  • 155
    • 0034730653 scopus 로고    scopus 로고
    • Bovine papillomavirus E1 protein is sumoylated by the host cell Ubc9 protein
    • Rangasamy D, Wilson VG. 2000. Bovine papillomavirus E1 protein is sumoylated by the host cell Ubc9 protein. J. Biol. Chem. 275: 30487-30495.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30487-30495
    • Rangasamy, D.1    Wilson, V.G.2
  • 156
    • 0034532450 scopus 로고    scopus 로고
    • SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation
    • Rangasamy D, Woytek K, Khan SA, Wilson VG. 2000. SUMO-1 modification of bovine papillomavirus E1 protein is required for intranuclear accumulation. J. Biol. Chem. 275:37999-38004.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37999-38004
    • Rangasamy, D.1    Woytek, K.2    Khan, S.A.3    Wilson, V.G.4
  • 157
    • 79952219169 scopus 로고    scopus 로고
    • Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus
    • Reichelt M, et al. 2011. Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus. PLoS Pathog. 7:e1001266.
    • (2011) PLoS Pathog , vol.7
    • Reichelt, M.1
  • 158
    • 77951535793 scopus 로고    scopus 로고
    • Listeria monocytogenes impairs SUMOylation for efficient infection
    • Ribet D, et al. 2010. Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 464:1192-1195.
    • (2010) Nature , vol.464 , pp. 1192-1195
    • Ribet, D.1
  • 159
    • 0033661892 scopus 로고    scopus 로고
    • The vaccinia virus E3L protein interacts with SUMO-1 and ribosomal protein L23a in a yeast two hybrid assay
    • Rogan S, Heaphy S. 2000. The vaccinia virus E3L protein interacts with SUMO-1 and ribosomal protein L23a in a yeast two hybrid assay. Virus Genes 21:193-195.
    • (2000) Virus Genes , vol.21 , pp. 193-195
    • Rogan, S.1    Heaphy, S.2
  • 160
    • 9944247534 scopus 로고    scopus 로고
    • Proteins of the PIAS family enhance the sumoylation of the papillomavirus E1 protein
    • Rosas-Acosta G, Langereis MA, Deyrieux A, Wilson VG. 2005. Proteins of the PIAS family enhance the sumoylation of the papillomavirus E1 protein. Virology 331:190-203.
    • (2005) Virology , vol.331 , pp. 190-203
    • Rosas-Acosta, G.1    Langereis, M.A.2    Deyrieux, A.3    Wilson, V.G.4
  • 161
    • 0347626039 scopus 로고    scopus 로고
    • EBNA3C coactivation with EBNA2 requires a SUMO homology domain
    • Rosendorff A, et al. 2004. EBNA3C coactivation with EBNA2 requires a SUMO homology domain. J. Virol. 78:367-377.
    • (2004) J. Virol. , vol.78 , pp. 367-377
    • Rosendorff, A.1
  • 162
    • 23844545176 scopus 로고    scopus 로고
    • SUMO-1 modification of the major immediate-early (IE) 1 and 2 proteins of human cytomegalovirus is regulated by different mechanisms and modulates the intracellular localization of the IE1, but not IE2, protein
    • Sadanari H, Yamada R, Ohnishi K, Matsubara K, Tanaka J. 2005. SUMO-1 modification of the major immediate-early (IE) 1 and 2 proteins of human cytomegalovirus is regulated by different mechanisms and modulates the intracellular localization of the IE1, but not IE2, protein. Arch. Virol. 150:1763-1782.
    • (2005) Arch. Virol. , vol.150 , pp. 1763-1782
    • Sadanari, H.1    Yamada, R.2    Ohnishi, K.3    Matsubara, K.4    Tanaka, J.5
  • 163
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitinrelated protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh H, Hinchey J. 2000. Functional heterogeneity of small ubiquitinrelated protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275:6252-6258.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 164
    • 0032478572 scopus 로고    scopus 로고
    • hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity
    • Saltzman A, et al. 1998. hUBC9 associates with MEKK1 and type I TNF-alpha receptor and stimulates NFkappaB activity. FEBS Lett. 425: 431-435.
    • (1998) FEBS Lett , vol.425 , pp. 431-435
    • Saltzman, A.1
  • 165
    • 71949096137 scopus 로고    scopus 로고
    • Viral entry mechanisms: human papillomavirus and a long journey from extracellular matrix to the nucleus
    • Sapp M, Bienkowska-Haba M. 2009. Viral entry mechanisms: human papillomavirus and a long journey from extracellular matrix to the nucleus. FEBS J. 276:7206-7216.
    • (2009) FEBS J , vol.276 , pp. 7206-7216
    • Sapp, M.1    Bienkowska-Haba, M.2
  • 166
    • 63549136610 scopus 로고    scopus 로고
    • Sumoylation and human disease pathogenesis
    • Sarge KD, Park-Sarge OK. 2009. Sumoylation and human disease pathogenesis. Trends Biochem. Sci. 34:200-205.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 200-205
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 167
    • 80052299981 scopus 로고    scopus 로고
    • Adenovirus type 5 early region 1B 55K oncoprotein dependent degradation of cellular factor Daxx is required for efficient transformation of primary rodent cells
    • Schreiner S, et al. 2011. Adenovirus type 5 early region 1B 55K oncoprotein dependent degradation of cellular factor Daxx is required for efficient transformation of primary rodent cells. J. Virol. 85:8752-8765.
    • (2011) J. Virol. , vol.85 , pp. 8752-8765
    • Schreiner, S.1
  • 168
    • 77953736164 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells
    • Schreiner S, et al. 2010. Proteasome-dependent degradation of Daxx by the viral E1B-55K protein in human adenovirus-infected cells. J. Virol. 84:7029-7038.
    • (2010) J. Virol. , vol.84 , pp. 7029-7038
    • Schreiner, S.1
  • 169
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: ubiquitin, SUMO and related modifiers
    • Schwartz DC, Hochstrasser M. 2003. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem. Sci. 28: 321-328.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 170
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira SD, et al. 2009. A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 139:1255-1267.
    • (2009) Cell , vol.139 , pp. 1255-1267
    • Shapira, S.D.1
  • 172
    • 85056057529 scopus 로고    scopus 로고
    • Is a new immune response mediator in the NF-kappaB pathway-SUMO-4-related to type 1 diabetes
    • Sia C. 2005. Is a new immune response mediator in the NF-kappaB pathway-SUMO-4-related to type 1 diabetes? Rev. Diabet. Stud. 2:58-60.
    • (2005) Rev Diabet. Stud. , vol.2 , pp. 58-60
    • Sia, C.1
  • 175
    • 80053991406 scopus 로고    scopus 로고
    • Sumoylation of the P protein at K254 plays an important role in growth of parainfluenza virus 5
    • Sun D, Xu P, He B. 2011. Sumoylation of the P protein at K254 plays an important role in growth of parainfluenza virus 5. J. Virol. 85: 10261-10268.
    • (2011) J. Virol. , vol.85 , pp. 10261-10268
    • Sun, D.1    Xu, P.2    He, B.3
  • 176
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins
    • Sun H, Leverson JD, Hunter T. 2007. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 26:4102-4112.
    • (2007) EMBO J , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 177
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham MH, et al. 2008. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell Biol. 10: 538-546.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 538-546
    • Tatham, M.H.1
  • 178
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai N, Stamminger T. 2008. New insights into the role of the subnuclear structure ND10 for viral infection. Biochim. Biophys. Acta 1783: 2207-2221.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 179
    • 33749473048 scopus 로고    scopus 로고
    • Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation
    • Tomoiu A, Gravel A, Tanguay RM, Flamand L. 2006. Functional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation. J. Virol. 80:10218-10228.
    • (2006) J. Virol. , vol.80 , pp. 10218-10228
    • Tomoiu, A.1    Gravel, A.2    Tanguay, R.M.3    Flamand, L.4
  • 180
    • 59149107480 scopus 로고    scopus 로고
    • The SUMO system: an overview
    • Ulrich HD. 2009. The SUMO system: an overview. Methods Mol. Biol. 497:3-16.
    • (2009) Methods Mol. Biol. , vol.497 , pp. 3-16
    • Ulrich, H.D.1
  • 181
    • 36348977099 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolytic control of SUMO conjugates
    • Uzunova K, et al. 2007. Ubiquitin-dependent proteolytic control of SUMO conjugates. J. Biol. Chem. 282:34167-34175.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34167-34175
    • Uzunova, K.1
  • 182
    • 77449089538 scopus 로고    scopus 로고
    • A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics
    • Van Damme E, Laukens K, Dang TH, Van Ostade X. 2010. A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics. Int. J. Biol. Sci. 6:51-67.
    • (2010) Int. J. Biol. Sci. , vol.6 , pp. 51-67
    • Van Damme, E.1    Laukens, K.2    Dang, T.H.3    Van Ostade, X.4
  • 183
    • 79959553618 scopus 로고    scopus 로고
    • Crosstalk between viruses and PML nuclear bodies: a network-based approach
    • Van Damme E, Van Ostade X. 2011. Crosstalk between viruses and PML nuclear bodies: a network-based approach. Front. Biosci. 17: 2910-2920.
    • (2011) Front. Biosci. , vol.17 , pp. 2910-2920
    • Van Damme, E.1    Van Ostade, X.2
  • 184
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO: a role in transcriptional regulation
    • Verger A, Perdomo J, Crossley M. 2003. Modification with SUMO: a role in transcriptional regulation. EMBO Rep. 4:137-142.
    • (2003) EMBO Rep , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 185
    • 0034940214 scopus 로고    scopus 로고
    • Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)
    • VerPlank L, et al. 2001. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proc. Natl. Acad. Sci. U. S. A. 98:7724-7729.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7724-7729
    • VerPlank, L.1
  • 186
    • 80052341054 scopus 로고    scopus 로고
    • Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin
    • Wang L, et al. 2011. Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin. PLoS Pathog. 7:e1002157.
    • (2011) PLoS Pathog , vol.7
    • Wang, L.1
  • 187
    • 52649120917 scopus 로고    scopus 로고
    • Dynamics of component exchange at PML nuclear bodies
    • Weidtkamp-Peters S, et al. 2008. Dynamics of component exchange at PML nuclear bodies. J. Cell Sci. 121:2731-2743.
    • (2008) J. Cell Sci. , vol.121 , pp. 2731-2743
    • Weidtkamp-Peters, S.1
  • 188
    • 51249085621 scopus 로고    scopus 로고
    • Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML
    • Weisshaar SR, et al. 2008. Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML. FEBS Lett. 582:3174-3178.
    • (2008) FEBS Lett , vol.582 , pp. 3174-3178
    • Weisshaar, S.R.1
  • 189
    • 0141829740 scopus 로고    scopus 로고
    • Mason-Pfizer monkey virus Gag proteins interact with the human sumo conjugating enzyme, hUbc9
    • Weldon RA Jr, Sarkar P, Brown SM, Weldon SK. 2003. Mason-Pfizer monkey virus Gag proteins interact with the human sumo conjugating enzyme, hUbc9. Virology 314:62-73.
    • (2003) Virology , vol.314 , pp. 62-73
    • Weldon Jr., R.A.1    Sarkar, P.2    Brown, S.M.3    Weldon, S.K.4
  • 190
    • 0035807718 scopus 로고    scopus 로고
    • Viral interaction with the host cell sumoylation system
    • Wilson VG, Rangasamy D. 2001. Viral interaction with the host cell sumoylation system. Virus Res. 81:17-27.
    • (2001) Virus Res , vol.81 , pp. 17-27
    • Wilson, V.G.1    Rangasamy, D.2
  • 191
    • 77957808656 scopus 로고    scopus 로고
    • SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML
    • Wimmer P, et al. 2010. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene 29:5511-5522.
    • (2010) Oncogene , vol.29 , pp. 5511-5522
    • Wimmer, P.1
  • 192
    • 80052051986 scopus 로고    scopus 로고
    • The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus
    • Wu CY, Jeng KS, Lai MM. 2011. The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus. J. Virol. 85:6618-6628.
    • (2011) J. Virol. , vol.85 , pp. 6618-6628
    • Wu, C.Y.1    Jeng, K.S.2    Lai, M.M.3
  • 193
    • 63549116482 scopus 로고    scopus 로고
    • Host cell sumoylation level influences papillomavirus E2 protein stability
    • Wu YC, Bian XL, Heaton PR, Deyrieux AF, Wilson VG. 2009. Host cell sumoylation level influences papillomavirus E2 protein stability. Virology 387:176-183.
    • (2009) Virology , vol.387 , pp. 176-183
    • Wu, Y.C.1    Bian, X.L.2    Heaton, P.R.3    Deyrieux, A.F.4    Wilson, V.G.5
  • 194
  • 195
    • 49049092114 scopus 로고    scopus 로고
    • Modification of papillomavirus E2 proteins by the small ubiquitin-like modifier family members (SUMOs)
    • Wu YC, Roark AA, Bian XL, Wilson VG. 2008. Modification of papillomavirus E2 proteins by the small ubiquitin-like modifier family members (SUMOs). Virology 378:329-338.
    • (2008) Virology , vol.378 , pp. 329-338
    • Wu, Y.C.1    Roark, A.A.2    Bian, X.L.3    Wilson, V.G.4
  • 196
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie Y, et al. 2007. The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J. Biol. Chem. 282:34176-34184.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34176-34184
    • Xie, Y.1
  • 197
    • 78650673299 scopus 로고    scopus 로고
    • Modification of nonstructural protein 1 of influenza A virus by SUMO1
    • Xu K, et al. 2011. Modification of nonstructural protein 1 of influenza A virus by SUMO1. J. Virol. 85:1086-1098.
    • (2011) J. Virol. , vol.85 , pp. 1086-1098
    • Xu, K.1
  • 198
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • Yang SH, Galanis A, Witty J, Sharrocks AD. 2006. An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J. 25:5083-5093.
    • (2006) EMBO J , vol.25 , pp. 5083-5093
    • Yang, S.H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 199
    • 0030745291 scopus 로고    scopus 로고
    • Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteins
    • Yasugi T, Vidal M, Sakai H, Howley PM, Benson JD. 1997. Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteins. J. Virol. 71:5942-5951.
    • (1997) J. Virol. , vol.71 , pp. 5942-5951
    • Yasugi, T.1    Vidal, M.2    Sakai, H.3    Howley, P.M.4    Benson, J.D.5
  • 200
    • 77955922552 scopus 로고    scopus 로고
    • Identification of a molecular recognition feature in the E1A oncoprotein that binds theSUMOconjugase UBC9 and likely interferes with polySUMOylation
    • Yousef AF, et al. 2010. Identification of a molecular recognition feature in the E1A oncoprotein that binds theSUMOconjugase UBC9 and likely interferes with polySUMOylation. Oncogene 29:4693-4704.
    • (2010) Oncogene , vol.29 , pp. 4693-4704
    • Yousef, A.F.1
  • 201
    • 33645966803 scopus 로고    scopus 로고
    • Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection
    • Yueh A, et al. 2006. Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection. J. Virol. 80:342-352.
    • (2006) J. Virol. , vol.80 , pp. 342-352
    • Yueh, A.1
  • 202
    • 79958018867 scopus 로고    scopus 로고
    • Impairment of human immunodeficiency virus type-1 integrase SUMOylation correlates with an early replication defect
    • Zamborlini A, et al. 2011. Impairment of human immunodeficiency virus type-1 integrase SUMOylation correlates with an early replication defect. J. Biol. Chem. 286:21013-21022.
    • (2011) J. Biol. Chem. , vol.286 , pp. 21013-21022
    • Zamborlini, A.1
  • 203
    • 77950067176 scopus 로고    scopus 로고
    • Ubc9 promotes breast cell invasion and metastasis in a sumoylation-independent manner
    • Zhu S, Sachdeva M, Wu F, Lu Z, Mo YY. 2010. Ubc9 promotes breast cell invasion and metastasis in a sumoylation-independent manner. Oncogene 29:1763-1772.
    • (2010) Oncogene , vol.29 , pp. 1763-1772
    • Zhu, S.1    Sachdeva, M.2    Wu, F.3    Lu, Z.4    Mo, Y.Y.5


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