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Volumn 3, Issue FEB, 2012, Pages

Post-translational modifications of Kaposi's sarcoma-associated herpesvirus regulatory proteins - SUMO and KSHV

Author keywords

K bZIP; K Rta; KSHV; LANA; Post translational modification; SUMO; Transcription

Indexed keywords


EID: 84875595488     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2012.00031     Document Type: Article
Times cited : (31)

References (107)
  • 1
    • 0035124377 scopus 로고    scopus 로고
    • Epstein-Barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodies
    • Adamson, A. L., and 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
  • 2
    • 13544258096 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus modulates cellular gene expression and protects lymphoid cells from p16 INK4A-induced cell cycle arrest
    • An, F. Q., Compitello, N., Horwitz, E., Sramkoski, M., Knudsen, E. S., and Renne, R. (2005). The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus modulates cellular gene expression and protects lymphoid cells from p16 INK4A-induced cell cycle arrest. J. Biol. Chem. 280, 3862-3874.
    • (2005) J. Biol. Chem , vol.280 , pp. 3862-3874
    • An, F.Q.1    Compitello, N.2    Horwitz, E.3    Sramkoski, M.4    Knudsen, E.S.5    Renne, R.6
  • 4
    • 33745886845 scopus 로고    scopus 로고
    • KSHV encoded LANA upregulates Pim-1 and is a substrate for its kinase activity
    • Bajaj, B. G., Verma, S. C., Lan, K., Cotter, M. A., Woodman, Z. L., and Robertson, E. S. (2006). KSHV encoded LANA upregulates Pim-1 and is a substrate for its kinase activity. Virology 351,18-28.
    • (2006) Virology , vol.351 , pp. 18-28
    • Bajaj, B.G.1    Verma, S.C.2    Lan, K.3    Cotter, M.A.4    Woodman, Z.L.5    Robertson, E.S.6
  • 6
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • Bernardi, R., and Pandolfi, P. P. (2007). Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat. Rev. Mol Cell Biol. 8, 1006-1016.
    • (2007) Nat. Rev. Mol Cell Biol , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 8
    • 34447560073 scopus 로고    scopus 로고
    • Targeting SUMO E1 to ubiquitin ligases: a viral strategy to counteract sumoylation
    • Boggio, R., Passafaro, A., and 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
  • 9
    • 53249134730 scopus 로고    scopus 로고
    • Pondering the puzzle of PML (promye locytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon
    • Borden, K. L. (2008). Pondering the puzzle of PML (promye locytic leukemia) nuclear bodies: can we fit the pieces together using an RNA regulon? Biochim. Biophys. Acta 1783, 2145-2154.
    • (2008) Biochim Biophys. Acta , vol.1783 , pp. 2145-2154
    • Borden, K.L.1
  • 11
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • doi:10.1371/journal.ppat.1002245
    • Boutell, C., Cuchet-Lourenco, D., Vanni, E., Orr, A., Glass, M., McFarlane, S., and Everett, R. D. (2011). A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog. 7, e1002245. doi:10.1371/journal.ppat.1002245
    • (2011) PLoS Pathog , vol.7
    • Boutell, C.1    Cuchet-Lourenco, D.2    Vanni, E.3    Orr, A.4    Glass, M.5    Mcfarlane, S.6    Everett, R.D.7
  • 13
    • 77950864220 scopus 로고    scopus 로고
    • DNA-PK/Ku complex binds to latency-associated nuclear antigen and negatively regulates Kaposi's sarcoma-associated herpesvirus latent replication
    • Cha, S., Lim, C., Lee, J. Y., Song, Y.-J., Park, J., Choe, J., and Seo, T. (2010). DNA-PK/Ku complex binds to latency-associated nuclear antigen and negatively regulates Kaposi's sarcoma-associated herpesvirus latent replication. Biochem. Biophys. Res. Commun. 394, 934-939.
    • (2010) Biochem. Biophys. Res. Commun , vol.394 , pp. 934-939
    • Cha, S.1    Lim, C.2    Lee, J.Y.3    Song, Y.-J.4    Park, J.5    Choe, J.6    Seo, T.7
  • 14
    • 67651007508 scopus 로고    scopus 로고
    • Kruppel-associated box domain-associated protein-1 as a latency regulator for Kaposi's sarcoma-associated herpesvirus and its modulation by the viral protein kinase
    • Chang, P. C., Fitzgerald, L. D., van Geelan, A., Izumiya, Y., Ellison, T. J., Wang, D.-H., Ann, D. K., Luciw, P. A., and Kung, H. J. (2009). Kruppel-associated box domain-associated protein-1 as a latency regulator for Kaposi's sarcoma-associated herpesvirus and its modulation by the viral protein kinase. Cancer Res. 69, 5681-5689.
    • (2009) Cancer Res , vol.69 , pp. 5681-5689
    • Chang, P.C.1    Fitzgerald, L.D.2    van Geelan, 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
  • 15
    • 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, P. C., Izumiya, Y., Wu, C. Y., Fitzgerald, L. D., Campbell, M., Ellison, T. J., Lam, K. S., Luciw, P. A., and Kung, H. J. (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    Izumiya, Y.2    Wu, C.Y.3    Fitzgerald, L.D.4    Campbell, M.5    Ellison, T.J.6    Lam, K.S.7    Luciw, P.A.8    Kung, H.J.9
  • 16
    • 0036121097 scopus 로고    scopus 로고
    • Open reading frame 50 protein of Kaposi's sarcoma-associated herpesvirus directly activates the viral PAN and K12 genes by binding to related response elements
    • Chang, P. J., Shedd, D., Gradoville, L., Cho, M. S., Chen, L. W., Chang, J., and Miller, G. (2002). Open reading frame 50 protein of Kaposi's sarcoma-associated herpesvirus directly activates the viral PAN and K12 genes by binding to related response elements. J. Virol. 76,3168-3178.
    • (2002) J. Virol. , vol.76 , pp. 3168-3178
    • Chang, P.J.1    Shedd, D.2    Gradoville, L.3    Cho, M.S.4    Chen, L.W.5    Chang, J.6    Miller, G.7
  • 17
    • 63449097051 scopus 로고    scopus 로고
    • KSHV reactivation from latency requires Pim-1 and Pim-3 kinases to inactivate the latency-associated nuclear antigen LANA
    • doi:10.1371/journal.ppat.1000324
    • Cheng, F., Weidner-Glunde, M., Varjosalo, M., Rainio, E. M., Lehtonen, A., Schulz, T. F., Koskinen, P. J., Taipale, J., and Ojala, P. M. (2009). KSHV reactivation from latency requires Pim-1 and Pim-3 kinases to inactivate the latency-associated nuclear antigen LANA. PLoS Pathog. 5, e1000324. doi:10.1371/journal.ppat.1000324
    • (2009) PLoS Pathog , vol.5
    • Cheng, F.1    Weidner-Glunde, M.2    Varjosalo, M.3    Rainio, E.M.4    Lehtonen, A.5    Schulz, T.F.6    Koskinen, P.J.7    Taipale, J.8    Ojala, P.M.9
  • 18
    • 0038050244 scopus 로고    scopus 로고
    • The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1
    • Colombo, R., Boggio, R., Seiser, C., Draetta, G. F., and 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
  • 20
    • 36849096094 scopus 로고    scopus 로고
    • Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells
    • Daniel, A. R., Faivre, E. J., and Lange, C. A. (2007). Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells. Mol. Endocrinol. 21, 2890-2906.
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2890-2906
    • Daniel, A.R.1    Faivre, E.J.2    Lange, C.A.3
  • 21
    • 70149092341 scopus 로고    scopus 로고
    • Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells
    • U. S. A
    • Daniel, A. R., and Lange, C. A. (2009). Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells. Proc. Natl Acad. Sci. U.S.A. 106, 14287-14292.
    • (2009) Proc. Natl Acad. Sci , vol.106 , pp. 14287-14292
    • Daniel, A.R.1    Lange, C.A.2
  • 22
    • 0036316347 scopus 로고    scopus 로고
    • Transcriptional regulation of the interleukin-6 gene of human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus)
    • Deng, H., Song, M. J., Chu, J. T., and Sun, R. (2002). Transcriptional regulation of the interleukin-6 gene of human herpesvirus 8 (Kaposi's sarcoma-associated herpesvirus). J. Virol. 76, 8252-8264.
    • (2002) J. Virol. , vol.76 , pp. 8252-8264
    • Deng, H.1    Song, M.J.2    Chu, J.T.3    Sun, R.4
  • 23
    • 16244416873 scopus 로고    scopus 로고
    • Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1
    • Deng, Z., Atanasiu, C., Zhao, K., Marmorstein, R., Sbodio, J. I., Chi, N. W., and Lieberman, P. M. (2005). Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1. J. Virol. 79, 4640-4650.
    • (2005) J. Virol. , vol.79 , pp. 4640-4650
    • Deng, Z.1    Atanasiu, C.2    Zhao, K.3    Marmorstein, R.4    Sbodio, J.I.5    Chi, N.W.6    Lieberman, P.M.7
  • 24
    • 77953955724 scopus 로고    scopus 로고
    • The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3
    • Drane, P., Ouararhni, K., Depaux, A., Shuaib, M., and Hamiche, A. (2010). The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 24, 1253-1265.
    • (2010) 3. Genes Dev. , vol.24 , pp. 1253-1265
    • Drane, P.1    Ouararhni, K.2    Depaux, A.3    Shuaib, M.4    Hamiche, A.5
  • 25
    • 63549108515 scopus 로고    scopus 로고
    • A comprehensive analysis of recruitment and transactivation potential of K-Rta and K-bZIP during reactivation of Kaposi's sarcoma-associated herpesvirus
    • Ellison, T. J., Izumiya, Y., Izumiya, C., Luciw, P. A., and Kung, H. J. (2009). A comprehensive analysis of recruitment and transactivation potential of K-Rta and K-bZIP during reactivation of Kaposi's sarcoma-associated herpesvirus. Virology 387, 76-88.
    • (2009) Virology , vol.387 , pp. 76-88
    • Ellison, T.J.1    Izumiya, Y.2    Izumiya, C.3    Luciw, P.A.4    Kung, H.J.5
  • 26
    • 40149085109 scopus 로고    scopus 로고
    • replication of ICP0-null mutant herpes simplex virus type 1 is restricted by both PML and sp100
    • Everett, R. D., Parada, C., Gripon, P., Sirma, H., and 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
  • 27
    • 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, R. D., Rechter, S., Papior, P., Tavalai, N., Stamminger, T., and Orr, A. (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    Rechter, S.2    Papior, P.3    Tavalai, N.4    Stamminger, T.5    Orr, A.6
  • 28
    • 34447626493 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 a key regulator of cellular fate
    • Forde, J. E., and Dale, T. C. (2007). Glycogen synthase kinase 3: a key regulator of cellular fate. Cell. Mol. LifeSci. 64, 1930-1944.
    • (2007) Cell. Mol. LifeSci , vol.64 , pp. 1930-1944
    • Forde, J.E.1    Dale, T.C.2
  • 29
    • 0033599006 scopus 로고    scopus 로고
    • p53 inhibition by the LANA protein of KSHV protects against cell death
    • Friborg, J., Kong, W., Hottiger, M. O., and Nabel, G. J. (1999). p53 inhibition by the LANA protein of KSHV protects against cell death. Nature 402, 889-894.
    • (1999) Nature , vol.402 , pp. 889-894
    • Friborg, J.1    Kong, W.2    Hottiger, M.O.3    Nabel, G.J.4
  • 31
    • 0038758853 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus manipulates the activity of glycogen synthase kinase-3 beta
    • Fujimuro, M., and Hayward, S. D. (2003). The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus manipulates the activity of glycogen synthase kinase-3 beta. J. Virol. 77, 8019-8030.
    • (2003) J. Virol , vol.77 , pp. 8019-8030
    • Fujimuro, M.1    Hayward, S.D.2
  • 32
    • 23244454478 scopus 로고    scopus 로고
    • Regulation of the interaction between glycogen synthase kinase 3 and the Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen
    • Fujimuro, M., Liu, J., Zhu, J., Yokosawa, H., and Hayward, S. D. (2005). Regulation of the interaction between glycogen synthase kinase 3 and the Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen. J. Virol. 79,10429-10441.
    • (2005) J. Virol. , vol.79 , pp. 10429-10441
    • Fujimuro, M.1    Liu, J.2    Zhu, J.3    Yokosawa, H.4    Hayward, S.D.5
  • 33
    • 77951192990 scopus 로고    scopus 로고
    • KSHV and the pathogenesis of Kaposi sarcoma: listening to human biology and medicine
    • Ganem, D. (2010). KSHV and the pathogenesis of Kaposi sarcoma: listening to human biology and medicine. J. Clin. Invest. 120, 939-949.
    • (2010) J. Clin. Invest , vol.120 , pp. 939-949
    • Ganem, D.1
  • 37
    • 79960055393 scopus 로고    scopus 로고
    • KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during DNA double-strand break response
    • Goodarzi, A. A., Kurka, T., and Jeggo, P. A. (2011). KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during DNA double-strand break response. Nat. Struct. Mol. Biol. 18,831-839.
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 831-839
    • Goodarzi, A.A.1    Kurka, T.2    Jeggo, P.A.3
  • 38
    • 0242412242 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 and Ste20-like kinase hKFC act as transcriptional repressors for gamma-2 herpesvirus lytic replication
    • Gwack, Y., Nakamura, H., Lee, S. W., Souvis, J., Yustein, J. T., Gyri, S., Kung, H. J., and Jung, J. U. (2003). Poly(ADP-ribose) polymerase 1 and Ste20-like kinase hKFC act as transcriptional repressors for gamma-2 herpesvirus lytic replication. Mol. Cell. Biol. 23, 8282-8294.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 8282-8294
    • Gwack, Y.1    Nakamura, H.2    Lee, S.W.3    Souvis, J.4    Yustein, J.T.5    Gyri, S.6    Kung, H.J.7    Jung, J.U.8
  • 39
    • 66149136812 scopus 로고    scopus 로고
    • Characterization of the interaction between latency-associated nuclear antigen and glycogen synthase kinase 3 beta
    • Hagen, T. (2009). Characterization of the interaction between latency-associated nuclear antigen and glycogen synthase kinase 3 beta. J. Virol. 83, 6312-6317.
    • (2009) J. Virol , vol.83 , pp. 6312-6317
    • Hagen, T.1
  • 41
    • 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., and 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
  • 43
    • 0036827642 scopus 로고    scopus 로고
    • The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells
    • Hu, J., Garber, A. C., and Renne, R. (2002). The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells.J. Virol. 76, 11677-11687.
    • (2002) J. Virol. , vol.76 , pp. 11677-11687
    • Hu, J.1    Garber, A.C.2    Renne, R.3
  • 44
    • 0034842669 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus K8 protein interacts with CREB-binding protein (CBP) and represses CBP-mediated transcription
    • Hwang, S., Gwack, Y., Byun, H., Lim, C., and Choe, J. (2001). The Kaposi's sarcoma-associated herpesvirus K8 protein interacts with CREB-binding protein (CBP) and represses CBP-mediated transcription. J. Virol. 75, 9509-9516.
    • (2001) J. Virol. , vol.75 , pp. 9509-9516
    • Hwang, S.1    Gwack, Y.2    Byun, H.3    Lim, C.4    Choe, J.5
  • 45
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1
    • Ishov, A. M., Sotnikov, A. G., Negorev, D., Vladimirova, O. V., Neff, N., Kamitani, T., Yeh, E. T., Strauss, J. F., 3rd, and Maul, G. G. (1999). PML is critical for ND10 formation and recruits the PML-interacting protein Daxx to this nuclear structure when modified by SUMO-1. J. Cell Biol. 147,221-234.
    • (1999) J. Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6    Yeh, E.T.7    Strauss 3rd, J.F.8    Maul, G.G.9
  • 46
    • 22544486295 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-bZIP represses gene transcription via SUMO modification
    • Izumiya, Y., Ellison, T. J., Yeh, E. T., Jung, J. U., Luciw, P. A., and Kung, H. J. (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    Ellison, T.J.2    Yeh, E.T.3    Jung, J.U.4    Luciw, P.A.5    Kung, H.J.6
  • 47
    • 33846629003 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its interaction with K-bZIP
    • Izumiya, Y., Izumiya, C., Van Geelen, A., Wang, D. H., Lam, K. S., Luciw, P. A., and Kung, H. J. (2007). Kaposi's sarcoma-associated herpesvirus-encoded protein kinase and its interaction with K-bZIP. J. Virol. 81,1072-1082.
    • (2007) J. Virol. , vol.81 , pp. 1072-1082
    • Izumiya, Y.1    Izumiya, C.2    Van Geelen, A.3    Wang, D.H.4    Lam, K.S.5    Luciw, P.A.6    Kung, H.J.7
  • 48
    • 0030734037 scopus 로고    scopus 로고
    • Identification of the gene encoding the major latency-associated nuclear antigen of the Kaposi's sarcoma-associated herpesvirus
    • Kedes, D. H., Lagunoff, M., Renne, R., and Ganem, D. (1997). Identification of the gene encoding the major latency-associated nuclear antigen of the Kaposi's sarcoma-associated herpesvirus. J. Clin. Invest. 100, 2606-2610.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2606-2610
    • Kedes, D.H.1    Lagunoff, M.2    Renne, R.3    Ganem, D.4
  • 49
    • 66149113937 scopus 로고    scopus 로고
    • Role of Kaposi's sarcoma-associated herpesvirus C-terminal LANA chromosome binding in episome persistence
    • Kelley-Clarke, B., De Leon-Vazquez, E., Slain, K., Barbera, A. J., and Kaye, K. M. (2009). Role of Kaposi's sarcoma-associated herpesvirus C-terminal LANA chromosome binding in episome persistence. J. Virol. 83,4326-4337.
    • (2009) J. Virol. , vol.83 , pp. 4326-4337
    • Kelley-Clarke, B.1    De Leon-Vazquez, E.2    Slain, K.3    Barbera, A.J.4    Kaye, K.M.5
  • 50
    • 33750023437 scopus 로고    scopus 로고
    • Keeping transcriptional activators under control
    • Kodadek, T., Sikder, D., and Nalley, K. (2006). Keeping transcriptional activators under control. Cell 127, 261-264.
    • (2006) Cell , vol.127 , pp. 261-264
    • Kodadek, T.1    Sikder, D.2    Nalley, K.3
  • 51
    • 1342321886 scopus 로고    scopus 로고
    • KSHV LANA1 binds DNA as an oligmer and residues N-terminal to the oligomerization domain are essential for DNA binding, replication, and episome persistence
    • Komatsu, T., Ballestas, M. E., Barbera, A. J., Kelley-Clarke, B., and Kaye, K. M. (2004). KSHV LANA1 binds DNA as an oligmer and residues N-terminal to the oligomerization domain are essential for DNA binding, replication, and episome persistence. Virology 319, 225-336.
    • (2004) Virology , vol.319 , pp. 225-336
    • Komatsu, T.1    Ballestas, M.E.2    Barbera, A.J.3    Kelley-Clarke, B.4    Kaye, K.M.5
  • 52
    • 77954274504 scopus 로고    scopus 로고
    • The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets
    • Krishnakumar, R., and Kraus, W L. (2010). The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets. Mol. Cell 39, 8-24.
    • (2010) Mol. Cell , vol.39 , pp. 8-24
    • Krishnakumar, R.1    Kraus, W.L.2
  • 53
    • 14744269431 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus reactivation is regulated by interaction of latency-associated nuclear antigen with recombination signal sequence-binding protein J-kappa, the major downstream effector of the Notch signaling pathway
    • Lan, K., Kuppers, D. A., and Robertson, E. S. (2005). Kaposi's sarcoma-associated herpesvirus reactivation is regulated by interaction of latency-associated nuclear antigen with recombination signal sequence-binding protein J-kappa, the major downstream effector of the Notch signaling pathway. J. Virol. 79, 3468-3478.
    • (2005) J. Virol. , vol.79 , pp. 3468-3478
    • Lan, K.1    Kuppers, D.A.2    Robertson, E.S.3
  • 54
    • 19844383887 scopus 로고    scopus 로고
    • Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor
    • Ledl, A., Schmidt, D., and Muller, S. (2005). Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor. Oncogene 24, 3810-3818.
    • (2005) Oncogene , vol.24 , pp. 3810-3818
    • Ledl, A.1    Schmidt, D.2    Muller, S.3
  • 55
    • 78049294658 scopus 로고    scopus 로고
    • Repression of interferon-alpha stimulated genes expression by Kaposi's sarcoma-assocaited herpesvirus K-bZIP protein
    • Lefort, S., Gravel, A., and Flamand, L. (2010). Repression of interferon-alpha stimulated genes expression by Kaposi's sarcoma-assocaited herpesvirus K-bZIP protein. Virology 408, 14-30.
    • (2010) Virology , vol.408 , pp. 14-30
    • Lefort, S.1    Gravel, A.2    Flamand, L.3
  • 56
    • 77956282773 scopus 로고    scopus 로고
    • Daxx is an H3 3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres
    • U. S. A
    • Lewis, P. W., Elsaesser, S. J., Noh, K. M., Stadler, S. C., and Allis, C. D. (2010). Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U.S.A. 107, 14075-14080.
    • (2010) Proc. Natl. Acad. Sci , vol.107 , pp. 14075-14080
    • Lewis, P.W.1    Elsaesser, S.J.2    Noh, K.M.3    Stadler, S.C.4    Allis, C.D.5
  • 57
    • 33847686708 scopus 로고    scopus 로고
    • Using or abusing: viruses and the cellular DNA damage response
    • Lilley, C. E., Schwartz, R. A., and Weitzman, M. D. (2007). Using or abusing: viruses and the cellular DNA damage response. Trends Microbiol. 15, 119-126.
    • (2007) Trends Microbiol , vol.15 , pp. 119-126
    • Lilley, C.E.1    Schwartz, R.A.2    Weitzman, M.D.3
  • 58
    • 0035903219 scopus 로고    scopus 로고
    • The transcriptional activity of cAMP rsponse element-binding protein is modulated by the latency associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus
    • Lim, C., Gwack, Y., Hwang, S., Kim, S., and Choe, J. (2001). The transcriptional activity of cAMP rsponse element-binding protein is modulated by the latency associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus. J. Biol. Chem. 276,31016-31022.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31016-31022
    • Lim, C.1    Gwack, Y.2    Hwang, S.3    Kim, S.4    Choe, J.5
  • 60
    • 0032978479 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus encodes a bZIP protein with homology to BZLF1 of Epstein-Barr virus
    • Lin, S. F., Robinson, D. R., Miller, G., and Kung, H. J. (1999). Kaposi's sarcoma-associated herpesvirus encodes a bZIP protein with homology to BZLF1 of Epstein-Barr virus.J. Virol. 73, 1909-1917.
    • (1999) J. Virol , vol.73 , pp. 1909-1917
    • Lin, S.F.1    Robinson, D.R.2    Miller, G.3    Kung, H.J.4
  • 61
    • 34247613416 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus LANA protein downregulates nuclear glycogen synthase kinase 3 activity and consequently blocks differentiation
    • Liu, J., Martin, H., Shamay, M., Woodard, C., Tang, Q.-Q., and Hayward, S. D. (2007). Kaposi's sarcoma-associated herpesvirus LANA protein downregulates nuclear glycogen synthase kinase 3 activity and consequently blocks differentiation. J. Virol. 81, 4722-4731.
    • (2007) J. Virol. , vol.81 , pp. 4722-4731
    • Liu, J.1    Martin, H.2    Shamay, M.3    Woodard, C.4    Tang, Q.-Q.5    Hayward, S.D.6
  • 62
    • 33646723291 scopus 로고    scopus 로고
    • Acetylation of the latency-associated nuclear antigen regulates repression of Kaposi's sarcoma-associated herpesvirus lytic transcription
    • Lu, F., Day, L., Gao, S. J., and Lieberman, P. M. (2006). Acetylation of the latency-associated nuclear antigen regulates repression of Kaposi's sarcoma-associated herpesvirus lytic transcription. J. Virol. 80,5273-5282.
    • (2006) J. Virol , vol.80 , pp. 5273-5282
    • Lu, F.1    Day, L.2    Gao, S.J.3    Lieberman, P.M.4
  • 63
    • 0032830320 scopus 로고    scopus 로고
    • Transcriptional activation by the product of open reading frame 50 of Kaposi's sarcoma-associated herpesvirus is required for lytic viral reactivation in B cells
    • Lukac, D. M., Kirshner, J. R., and Ganem, D. (1999). Transcriptional activation by the product of open reading frame 50 of Kaposi's sarcoma-associated herpesvirus is required for lytic viral reactivation in B cells. J. Virol. 73, 9348-9361.
    • (1999) J. Virol , vol.73 , pp. 9348-9361
    • Lukac, D.M.1    Kirshner, J.R.2    Ganem, D.3
  • 64
    • 0032567394 scopus 로고    scopus 로고
    • Reactivation of Kaposi's sarcoma-associated herpesvirus infection from latency by expression of the ORF 50 transactivator, a homolog of the EBV R protein
    • Lukac, D. M., Renne, R., Kirshner, J. R., and Ganem, D. (1998). Reactivation of Kaposi's sarcoma-associated herpesvirus infection from latency by expression of the ORF 50 transactivator, a homolog of the EBV R protein. Virology 252, 304-312.
    • (1998) Virology , vol.252 , pp. 304-312
    • Lukac, D.M.1    Renne, R.2    Kirshner, J.R.3    Ganem, D.4
  • 65
    • 57349108706 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection
    • Lukashchuk, V., McFarlane, S., Everett, R. D., and Preston, C. M. (2006). Human cytomegalovirus protein pp71 displaces the chromatin-associated factor ATRX from nuclear domain 10 at early stages of infection. J. Virol. 82, 12543-12554.
    • (2006) J. Virol. , vol.82 , pp. 12543-12554
    • Lukashchuk, V.1    Mcfarlane, S.2    Everett, R.D.3    Preston, C.M.4
  • 67
    • 77957121811 scopus 로고    scopus 로고
    • Kaposi's sarcoma and its associated herpesvirus
    • Mesri, E. A., Cesarman, E., and Boshoff, C. (2010). Kaposi's sarcoma and its associated herpesvirus. Nat. Rev. Cancer 10, 707-719.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 707-719
    • Mesri, E.A.1    Cesarman, E.2    Boshoff, C.3
  • 68
    • 33748779794 scopus 로고    scopus 로고
    • Ets-1-dependent expression of vascular endothelial growth factor receptors is activated by latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus through interaction with Daxx
    • Murakami, Y., Yamagoe, S., Noguchi, K., Takebe, Y., Takahashi, N., Uehara, Y., and Fukazawa, H. (2006). Ets-1-dependent expression of vascular endothelial growth factor receptors is activated by latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus through interaction with Daxx. J. Biol Chem. 281, 28113-28121.
    • (2006) J. Biol Chem. , vol.281 , pp. 28113-28121
    • Murakami, Y.1    Yamagoe, S.2    Noguchi, K.3    Takebe, Y.4    Takahashi, N.5    Uehara, Y.6    Fukazawa, H.7
  • 69
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani, M., and Tansey, W. P. (2003). How the ubiquitin-proteasome system controls transcription. Nat. Rev. Mol Cell Biol. 4, 192-201.
    • (2003) Nat. Rev. Mol Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 70
    • 79952538034 scopus 로고    scopus 로고
    • Nuclear organization in genome stability: SUMO connections
    • Nagai, S., Davoodi, N., and Gasser, S. M. (2011). Nuclear organization in genome stability: SUMO connections. CellRes. 21, 474-485.
    • (2011) CellRes , vol.21 , pp. 474-485
    • Nagai, S.1    Davoodi, N.2    Gasser, S.M.3
  • 71
    • 0037377723 scopus 로고    scopus 로고
    • Global changes in Kaposi's sarcoma-associated virus gene expression patterns following expression of a tetracycline-inducible Rtatransactivator
    • Nakamura, H., Lu, M., Gwack, Y., Souvlis, J., Zeichner, S. L., and Jung, J. U. (2003). Global changes in Kaposi's sarcoma-associated virus gene expression patterns following expression of a tetracycline-inducible Rtatransactivator. J. Virol. 77,4205-4220.
    • (2003) J. Virol. , vol.77 , pp. 4205-4220
    • Nakamura, H.1    Lu, M.2    Gwack, Y.3    Souvlis, J.4    Zeichner, S.L.5    Jung, J.U.6
  • 73
    • 4444294852 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 binds to Kaposi's sarcoma-associated herpesvirus (KSHV) terminal repeat sequence and modulates KSHV replication in latency
    • Ohsaki, E., Ueda, K., Sakakibara, S., Do, E., Yada, K., and Yamanishi, K. (2004). Poly(ADP-ribose) polymerase 1 binds to Kaposi's sarcoma-associated herpesvirus (KSHV) terminal repeat sequence and modulates KSHV replication in latency. J. Virol. 78, 9936-9946.
    • (2004) J. Virol. , vol.78 , pp. 9936-9946
    • Ohsaki, E.1    Ueda, K.2    Sakakibara, S.3    Do, E.4    Yada, K.5    Yamanishi, K.6
  • 74
    • 0032752995 scopus 로고    scopus 로고
    • Latent nuclear antigen of Kaposi's sarcoma-associated herpesvirus interacts with RING3, a homolog of the Drosophila female sterile homeotic (fsh) gene
    • Platt, G. M., Simpson, G. R., Mittnacht, S., and Schulz, T. F. (1999). Latent nuclear antigen of Kaposi's sarcoma-associated herpesvirus interacts with RING3, a homolog of the Drosophila female sterile homeotic (fsh) gene. J. Virol. 73, 9789-9795.
    • (1999) J. Virol. , vol.73 , pp. 9789-9795
    • Platt, G.M.1    Simpson, G.R.2    Mittnacht, S.3    Schulz, T.F.4
  • 75
    • 0035108091 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-bZIP protein is phosphorylated by cyclin-dependent kinases
    • Polson, A. G., Huang, L., Lukac, D. M., Blethrow, J. D., Morgan, D. O., Burlingame, A. L., and Ganem, D. (2001). Kaposi's sarcoma-associated herpesvirus K-bZIP protein is phosphorylated by cyclin-dependent kinases. J. Virol. 75,3175-3184.
    • (2001) J. Virol , vol.75 , pp. 3175-3184
    • Polson, A.G.1    Huang, L.2    Lukac, D.M.3    Blethrow, J.D.4    Morgan, D.O.5    Burlingame, A.L.6    Ganem, D.7
  • 77
    • 0033782793 scopus 로고    scopus 로고
    • The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells
    • Radkov, S. A., Kellam, P., and Boshoff, C. (2000). The latent nuclear antigen of Kaposi sarcoma-associated herpesvirus targets the retinoblastoma-E2F pathway and with the oncogene Hras transforms primary rat cells. Nat.Med.6, 1121-1127.
    • (2000) Nat. Med , vol.6 , pp. 1121-1127
    • Radkov, S.A.1    Kellam, P.2    Boshoff, C.3
  • 78
    • 9944247534 scopus 로고    scopus 로고
    • Proteins of the PIAS family enhance the sumoylation of the papillomavirus E1 protein
    • Rosas-Acosta, G., Langereis, M. A., Deyrieux, A., and Wilson, V G. (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
  • 80
    • 0034971887 scopus 로고    scopus 로고
    • KSHV/HHV8-assoicated lymphoproliferations in the AIDS setting
    • Schulz, T. F. (2001). KSHV/HHV8-assoicated lymphoproliferations in the AIDS setting. Eur. J. Cancer 37, 1217-1226.
    • (2001) Eur. J. Cancer , vol.37 , pp. 1217-1226
    • Schulz, T.F.1
  • 81
    • 0035028618 scopus 로고    scopus 로고
    • Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification
    • Seeler, J. S., Marchio, A., Losson, R., Desterro, J. M., Hay, R. T., Cham-bon, P., and Dejean, A. (2001). Common properties of nuclear body protein SP100 and TIF1alpha chromatin factor: role of SUMO modification. Mol. Cell. Biol. 21, 3314-3324.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3314-3324
    • Seeler, J.S.1    Marchio, A.2    Losson, R.3    Desterro, J.M.4    Hay, R.T.5    Cham-bon, P.6    Dejean, A.7
  • 82
    • 0036241373 scopus 로고    scopus 로고
    • Characterization of interactions between RTA and the promoter of polyadenylated nuclear RNA in Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8
    • Song, M. J., Li, X., Brown, H. J., and Sun, R. (2002). Characterization of interactions between RTA and the promoter of polyadenylated nuclear RNA in Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8. J. Virol. 76, 5000-5013.
    • (2002) J. Virol. , vol.76 , pp. 5000-5013
    • Song, M.J.1    Li, X.2    Brown, H.J.3    Sun, R.4
  • 84
    • 51049083598 scopus 로고    scopus 로고
    • SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing
    • Stielow, B., Sapetschnig, A., Wink, C., Kruger, I., and Suske, G. (2008). SUMO-modified Sp3 represses transcription by provoking local heterochromatic gene silencing. EMBO Rep. 9, 899-906.
    • (2008) EMBO Rep , vol.9 , pp. 899-906
    • Stielow, B.1    Sapetschnig, A.2    Wink, C.3    Kruger, I.4    Suske, G.5
  • 85
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins
    • Sun, H., Leverson, J. D., and 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
  • 86
    • 0032167919 scopus 로고    scopus 로고
    • Aviral gene that activates lytic cycle expression of Kaposi's sarcoma-associated herpesvirus
    • U. S. A
    • Sun, R., Lin, S.F.,Gradoville,L., Yuan, Y., Zhu, F., and Miller, G. (1998). Aviral gene that activates lytic cycle expression of Kaposi's sarcoma-associated herpesvirus. Proc. Natl. Acad. Sci. U.S.A. 95, 10866-10871.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 10866-10871
    • Sun, R.1    Lin, S.F.2    Gradoville, L.3    Yuan, Y.4    Zhu, F.5    Miller, G.6
  • 87
    • 0033584846 scopus 로고    scopus 로고
    • Human JIK, a novel member of the STE20 kinas family that inhibits JNK and is negatively regulated by epidermal growth factor
    • Tassi, E., Biesova, Z., Di Fiore, P. P., Gutkind, J. S., and Wong, W. T. (1999). Human JIK, a novel member of the STE20 kinas family that inhibits JNK and is negatively regulated by epidermal growth factor. J. Biol. Chem. 274, 33287-33295.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33287-33295
    • Tassi, E.1    Biesova, Z.2    Di Fiore, P.P.3    Gutkind, J.S.4    Wong, W.T.5
  • 89
    • 33746840094 scopus 로고    scopus 로고
    • Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections
    • Tavalai, N., Papior, P., Rechter, S., Leis, M., and Stamminger, T. (2006). Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infections. J. Virol. 80,8006-8018.
    • (2006) J. Virol. , vol.80 , pp. 8006-8018
    • Tavalai, N.1    Papior, P.2    Rechter, S.3    Leis, M.4    Stamminger, T.5
  • 90
    • 77951455708 scopus 로고    scopus 로고
    • Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1
    • Tempera, I., Deng, Z., Atanasiu, C., Chen, C.-J., D'Erme, M., and Lieberman, P. (2010). Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1. J. Virol. 84, 4988-4997.
    • (2010) J. Virol. , vol.84 , pp. 4988-4997
    • Tempera, I.1    Deng, Z.2    Atanasiu, C.3    Chen, C.-J.4    D'Erme, M.5    Lieberman, P.6
  • 91
    • 33747373841 scopus 로고    scopus 로고
    • Involvement of SUMO modification in MBD1- and MCAF1-mediated het-erochromatin formation
    • Uchimura, Y., Ichimura, T., Uwada, J., Tachibana, T., Sugahara, S., Nakao, M., and Saitoh, H. (2006). Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation. J. Biol. Chem. 281,23180-23190.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23180-23190
    • Uchimura, Y.1    Ichimura, T.2    Uwada, J.3    Tachibana, T.4    Sugahara, S.5    Nakao, M.6    Saitoh, H.7
  • 94
    • 4544290097 scopus 로고    scopus 로고
    • Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus upregulates transcription of human telomerase reverse transcriptase promoter through interaction with transcription factor Sp1
    • Verma, S. C., Borah, S., and Robertson, E. (2004). Latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus upregulates transcription of human telomerase reverse transcriptase promoter through interaction with transcription factor Sp1. J. Virol. 78, 10348-10359.
    • (2004) J. Virol , vol.78 , pp. 10348-10359
    • Verma, S.C.1    Borah, S.2    Robertson, E.3
  • 95
    • 34247618075 scopus 로고    scopus 로고
    • Structure and function of latency-associated nuclear antigen
    • Verma, S. C., Lan, K., and Robertson, E. (2007). Structure and function of latency-associated nuclear antigen. Curr. Top. Microbiol. Immunol. 312, 101-136.
    • (2007) Curr. Top. Microbiol. Immunol , vol.312 , pp. 101-136
    • Verma, S.C.1    Lan, K.2    Robertson, E.3
  • 96
    • 77957951602 scopus 로고    scopus 로고
    • Genomes in conflict: maintaining genome integrity during virus infection
    • Weitzman, M. D., Lilley, C. E., and Chaurushiya, M. S. (2010). Genomes in conflict: maintaining genome integrity during virus infection. Annu. Rev. Microbiol. 64,61-81.
    • (2010) Annu. Rev. Microbiol , vol.64 , pp. 61-81
    • Weitzman, M.D.1    Lilley, C.E.2    Chaurushiya, M.S.3
  • 97
    • 0042467672 scopus 로고    scopus 로고
    • The role of Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8 regulator of tran scription activation (RTA) in control of gene expression
    • West, J. T., and Wood, C. (2003). The role of Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8 regulator of tran scription activation (RTA) in control of gene expression. Oncogene 22, 5150-5163.
    • (2003) Oncogene , vol.22 , pp. 5150-5163
    • West, J.T.1    Wood, C.2
  • 99
    • 37749005793 scopus 로고    scopus 로고
    • Papillomaviruses and the host SUMOylation system
    • Wu,Y. C., Deyrieux, A. F., and Wilson, V. G. (2007). Papillomaviruses and the host SUMOylation system. Biochem. Soc. Trans. 35,1433-1435.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 1433-1435
    • Wu, Y.C.1    Deyrieux, A.F.2    Wilson, V.G.3
  • 100
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3 Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie, Y., Kerscher, O., Kroetz, M. B., McConchie, H. F., Sung, P., and Hochstrasser, M. (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    Kerscher, O.2    Kroetz, M.B.3    Mcconchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 101
    • 14744270253 scopus 로고    scopus 로고
    • A Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50 deletion mutant is defective for reactivation of latent virus and DNA replication
    • Xu, Y., AuCoin, D. P., Huete, A. R., Cei, S. A., Hanson, L. J., and Pari, G. S. (2005). A Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8 ORF50 deletion mutant is defective for reactivation of latent virus and DNA replication. J. Virol. 79,3479-3487.
    • (2005) J. Virol , vol.79 , pp. 3479-3487
    • Xu, Y.1    Aucoin, D.P.2    Huete, A.R.3    Cei, S.A.4    Hanson, L.J.5    Pari, G.S.6
  • 102
    • 41149167561 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus transactivator RTA promotes degradation of the repressors to regulate viral lytic replication
    • Yang, Z., Yan, Z., and Wood, C. (2008). Kaposi's sarcoma-associated herpesvirus transactivator RTA promotes degradation of the repressors to regulate viral lytic replication. J. Virol. 82, 3590-3603.
    • (2008) J. Virol , vol.82 , pp. 3590-3603
    • Yang, Z.1    Yan, Z.2    Wood, C.3
  • 103
    • 12444275739 scopus 로고    scopus 로고
    • The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteasome-mediated degradation
    • Yu, Y., Wang, S. E., and Hayward, G. S. (2005). The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteasome-mediated degradation. Immunity 22, 59-70.
    • (2005) Immunity , vol.22 , pp. 59-70
    • Yu, Y.1    Wang, S.E.2    Hayward, G.S.3
  • 104
    • 0034598814 scopus 로고    scopus 로고
    • KFC, a Ste20-like kinase with mitogenic potential and capability to activate the SAPK/JNK pathway
    • Yustein, J. T., Li, D., Robinson, D., and Kung, H. J. (2000). KFC, a Ste20-like kinase with mitogenic potential and capability to activate the SAPK/JNK pathway. Oncogene 19,710-718.
    • (2000) Oncogene , vol.19 , pp. 710-718
    • Yustein, J.T.1    Li, D.2    Robinson, D.3    Kung, H.J.4
  • 105
    • 0142057145 scopus 로고    scopus 로고
    • Comparative studies of a new subfamily of human Ste-20-like kinases: homodimerization, subcellular localization, and selective activation of MKK3 and p38
    • Yustein, J. T., Xia, L., Kahlenburg, J. M., Robinson, D., Templeton, D., and Kung, H. J. (2003). Comparative studies of a new subfamily of human Ste-20-like kinases: homodimerization, subcellular localization, and selective activation of MKK3 and p38. Oncogene 22, 6129-6141.
    • (2003) Oncogene , vol.22 , pp. 6129-6141
    • Yustein, J.T.1    Xia, L.2    Kahlenburg, J.M.3    Robinson, D.4    Templeton, D.5    Kung, H.J.6
  • 107
    • 62549105364 scopus 로고    scopus 로고
    • Mutually exclusive STAT1 modifications identified by Ubc9/substrate dimerization-dependent SUMOylation
    • Zimnik, S., Gaestel, M., and Niedenthal, R. (2009). Mutually exclusive STAT1 modifications identified by Ubc9/substrate dimerization-dependent SUMOylation. Nucleic Acids Res. 37, e30.
    • (2009) Nucleic Acids Res , vol.37
    • Zimnik, S.1    Gaestel, M.2    Niedenthal, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.