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Volumn 3 MAY, Issue , 2013, Pages

Differential roles of PML isoforms

Author keywords

As2O3; CK2; PML isoforms; PML nomenclature; RNF4; SIM; SUMO; TRIM; Virus

Indexed keywords

ARSENIC TRIOXIDE; CASEIN KINASE II; CULLIN; DEUBIQUITINASE; EPSTEIN BARR VIRUS ANTIGEN 1; GAMMA INTERFERON; HIGH MOBILITY GROUP A2 PROTEIN; HISTONE ACETYLTRANSFERASE; MITOGEN ACTIVATED PROTEIN KINASE; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE PIN1; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN UBC9; RETINOIC ACID RECEPTOR ALPHA; SMAD2 PROTEIN; SMAD3 PROTEIN; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; TELOMERASE REVERSE TRANSCRIPTASE; TELOMERIC REPEAT BINDING FACTOR 1; TRANSFORMING GROWTH FACTOR BETA; TRIPARTITE MOTIF PROTEIN 19; TRIPARTITE MOTIF PROTEIN 5; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84891112860     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2013.00125     Document Type: Review
Times cited : (125)

References (112)
  • 1
    • 54249103056 scopus 로고    scopus 로고
    • Regulation of apoptosis by PML and the PML-NBs
    • Bernardi, R., Papa, A., and Pandolfi, P. P. (2008). Regulation of apoptosis by PML and the PML-NBs. Oncogene 27, 6299-6312.
    • (2008) Oncogene , vol.27 , pp. 6299-6312
    • Bernardi, R.1    Papa, A.2    Pandolfi, P.P.3
  • 3
    • 84871958784 scopus 로고    scopus 로고
    • The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription
    • Berscheminski, J., Groitl, P., Dobner, T., Wimmer, P., and Schreiner, S. (2013). The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription. J. Virol. 87, 965-977.
    • (2013) J. Virol. , vol.87 , pp. 965-977
    • Berscheminski, J.1    Groitl, P.2    Dobner, T.3    Wimmer, P.4    Schreiner, S.5
  • 5
    • 77957192176 scopus 로고    scopus 로고
    • Resistance to rabies virus infection conferred by the PMLIV isoform
    • Blondel, D., Kheddache, S., Lahaye, X., Dianoux, L., and Chelbi-Alix, M. K. (2010). Resistance to rabies virus infection conferred by the PMLIV isoform. J. Virol. 84, 10719-10726.
    • (2010) J. Virol. , vol.84 , pp. 10719-10726
    • Blondel, D.1    Kheddache, S.2    Lahaye, X.3    Dianoux, L.4    Chelbi-Alix, M.K.5
  • 6
    • 18744379736 scopus 로고    scopus 로고
    • Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies
    • Blondel, D., Regad, T., Poisson, N., Pavie, B., Harper, F., Pandolfi, P. P., et al. (2002). Rabies virus P and small P products interact directly with PML and reorganize PML nuclear bodies. Oncogene 21, 7957-7970.
    • (2002) Oncogene , vol.21 , pp. 7957-7970
    • Blondel, D.1    Regad, T.2    Poisson, N.3    Pavie, B.4    Harper, F.5    Pandolfi, P.P.6
  • 8
    • 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., et al. (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
  • 9
    • 84874035038 scopus 로고    scopus 로고
    • Regulation of alphaherpesvirus infections by the ICP0 family of proteins
    • Boutell, C., and Everett, R. D. (2013). Regulation of alphaherpesvirus infections by the ICP0 family of proteins. J. Gen. Virol. 94, 465-481.
    • (2013) J. Gen. Virol. , vol.94 , pp. 465-481
    • Boutell, C.1    Everett, R.D.2
  • 10
    • 77956202370 scopus 로고    scopus 로고
    • Assembly dynamics of PML nuclear bodies in living cells
    • Brand, P., Lenser, T., and Hemmerich, P. (2010). Assembly dynamics of PML nuclear bodies in living cells. PMC Biophys. 3, 3.
    • (2010) PMC Biophys. , vol.3 , pp. 3
    • Brand, P.1    Lenser, T.2    Hemmerich, P.3
  • 12
    • 42249109186 scopus 로고    scopus 로고
    • SUMOylation of HMGA2: selective destabilization of promyelocytic leukemia protein via proteasome
    • Cao, X., Clavijo, C., Li, X., Lin, H. H., Chen, Y., Shih, H. M., et al. (2008). SUMOylation of HMGA2: selective destabilization of promyelocytic leukemia protein via proteasome. Mol. Cancer Ther. 7, 923-934.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 923-934
    • Cao, X.1    Clavijo, C.2    Li, X.3    Lin, H.H.4    Chen, Y.5    Shih, H.M.6
  • 13
    • 79957798908 scopus 로고    scopus 로고
    • The nuclear bodies inside out: PML conquers the cytoplasm
    • Carracedo, A., Ito, K., and Pandolfi, P. P. (2011). The nuclear bodies inside out: PML conquers the cytoplasm. Curr. Opin. Cell Biol. 23, 360-366.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 360-366
    • Carracedo, A.1    Ito, K.2    Pandolfi, P.P.3
  • 14
    • 0033611590 scopus 로고    scopus 로고
    • Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins
    • Chelbi-Alix, M. K., and de The, H. (1999). Herpes virus induced proteasome-dependent 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 The, H.2
  • 15
    • 0030610686 scopus 로고    scopus 로고
    • Use of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia (APL): I. As2O3 exerts dose-dependent dual effects on APL cells
    • Chen, G. Q., Shi, X. G., Tang, W., Xiong, S. M., Zhu, J., Cai, X., et al. (1997). Use of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia (APL): I. As2O3 exerts dose-dependent dual effects on APL cells. Blood 89, 3345-3353.
    • (1997) Blood , vol.89 , pp. 3345-3353
    • Chen, G.Q.1    Shi, X.G.2    Tang, W.3    Xiong, S.M.4    Zhu, J.5    Cai, X.6
  • 16
    • 84865468924 scopus 로고    scopus 로고
    • The role of PML ubiquitination in human malignancies
    • Chen, R. H., Lee, Y. R., and Yuan, W. C. (2012). The role of PML ubiquitination in human malignancies. J. Biomed. Sci. 19, 81.
    • (2012) J. Biomed. Sci. , vol.19 , pp. 81
    • Chen, R.H.1    Lee, Y.R.2    Yuan, W.C.3
  • 17
    • 84885626870 scopus 로고    scopus 로고
    • Post-translational modifications of PML: consequences and implications
    • doi:10.3389/fonc.2012.00210
    • Cheng, X., and Kao, H. Y. (2012). Post-translational modifications of PML: consequences and implications. Front. Oncol. 2:210. doi:10.3389/fonc.2012.00210
    • (2012) Front. Oncol. , vol.2 , pp. 210
    • Cheng, X.1    Kao, H.Y.2
  • 19
    • 84869025216 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation
    • Cuchet-Lourenco, D., Vanni, E., Glass, M., Orr, A., and Everett, R. D. (2012). Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation. J. Virol. 86, 11209-11222.
    • (2012) J. Virol. , vol.86 , pp. 11209-11222
    • Cuchet-Lourenco, D.1    Vanni, E.2    Glass, M.3    Orr, A.4    Everett, R.D.5
  • 21
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The, H., Lavau, C., Marchio, A., Chomienne, C., Degos, L., and Dejean, A. (1991). The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66, 675-684.
    • (1991) Cell , vol.66 , pp. 675-684
    • de The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 22
    • 0034974380 scopus 로고    scopus 로고
    • Role of the promyelocytic leukemia protein PML in the interferon sensitivity of lymphocytic choriomeningitis virus
    • Djavani, M., Rodas, J., Lukashevich, I. S., Horejsh, D., Pandolfi, P. P., Borden, K. L., et al. (2001). Role of the promyelocytic leukemia protein PML in the interferon sensitivity of lymphocytic choriomeningitis virus. J. Virol. 75, 6204-6208.
    • (2001) J. Virol. , vol.75 , pp. 6204-6208
    • Djavani, M.1    Rodas, J.2    Lukashevich, I.S.3    Horejsh, D.4    Pandolfi, P.P.5    Borden, K.L.6
  • 23
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck, J. A., Maul, G. G., Miller, W. H. Jr., Chen, J. D., Kakizuka, A., and Evans, R. M. (1994). A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76, 333-343.
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr., W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 24
    • 79951516890 scopus 로고    scopus 로고
    • PML positively regulates interferon gamma signaling
    • El Bougrini, J., Dianoux, L., and Chelbi-Alix, M. K. (2011). PML positively regulates interferon gamma signaling. Biochimie. 93, 389-398.
    • (2011) Biochimie. , vol.93 , pp. 389-398
    • El Bougrini, J.1    Dianoux, L.2    Chelbi-Alix, M.K.3
  • 25
    • 78049519070 scopus 로고    scopus 로고
    • SUMOylation promotes PML degradation during encephalomyocarditis virus infection
    • El Mchichi, B., Regad, T., Maroui, M. A., Rodriguez, M. S., Aminev, A., Gerbaud, S., et al. (2010). SUMOylation promotes PML degradation during encephalomyocarditis virus infection. J. Virol. 84, 11634-11645.
    • (2010) J. Virol. , vol.84 , pp. 11634-11645
    • El Mchichi, B.1    Regad, T.2    Maroui, M.A.3    Rodriguez, M.S.4    Aminev, A.5    Gerbaud, S.6
  • 26
    • 84878986048 scopus 로고    scopus 로고
    • Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation
    • Erker, Y., Neyret-Kahn, H., Seeler, J. S., Dejean, A., Atfi, A., and Levy, L. (2013). Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML degradation. Mol. Cell. Biol. 33, 2163-2177.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2163-2177
    • Erker, Y.1    Neyret-Kahn, H.2    Seeler, J.S.3    Dejean, A.4    Atfi, A.5    Levy, L.6
  • 27
    • 59349108844 scopus 로고    scopus 로고
    • Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3
    • Evdokimov, E., Sharma, P., Lockett, S. J., Lualdi, M., and Kuehn, M. R. (2008). Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3. J. Cell. Sci. 121, 4106-4113.
    • (2008) J. Cell. Sci. , vol.121 , pp. 4106-4113
    • Evdokimov, E.1    Sharma, P.2    Lockett, S.J.3    Lualdi, M.4    Kuehn, M.R.5
  • 28
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett, R. D., and Chelbi-Alix, M. K. (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
  • 29
    • 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, R. D., Freemont, P., Saitoh, H., Dasso, M., Orr, A., Kathoria, M., 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    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6
  • 30
    • 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, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., and Parkinson, J. (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    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 31
    • 0026578112 scopus 로고
    • Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms
    • Fagioli, M., Alcalay, M., Pandolfi, P. P., Venturini, L., Mencarelli, A., Simeone, A., et al. (1992). Alternative splicing of PML transcripts predicts coexpression of several carboxy-terminally different protein isoforms. Oncogene 7, 1083-1091.
    • (1992) Oncogene , vol.7 , pp. 1083-1091
    • Fagioli, M.1    Alcalay, M.2    Pandolfi, P.P.3    Venturini, L.4    Mencarelli, A.5    Simeone, A.6
  • 32
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of p53 activity in nuclear bodies by a specific PML isoform
    • Fogal, V., Gostissa, M., Sandy, P., Zacchi, P., Sternsdorf, T., Jensen, K., et al. (2000). Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J. 19, 6185-6195.
    • (2000) EMBO J. , vol.19 , pp. 6185-6195
    • Fogal, V.1    Gostissa, M.2    Sandy, P.3    Zacchi, P.4    Sternsdorf, T.5    Jensen, K.6
  • 33
    • 79953187281 scopus 로고    scopus 로고
    • A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells
    • M110004796
    • Galisson, F., Mahrouche, L., Courcelles, M., Bonneil, E., Meloche, S., Chelbi-Alix, M. K., et al. (2011). A novel proteomics approach to identify SUMOylated proteins and their modification sites in human cells. Mol. Cell Proteomics 10, M110004796.
    • (2011) Mol. Cell Proteomics , vol.10
    • Galisson, F.1    Mahrouche, L.2    Courcelles, M.3    Bonneil, E.4    Meloche, S.5    Chelbi-Alix, M.K.6
  • 34
    • 84865749807 scopus 로고    scopus 로고
    • Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation
    • Geng, Y., Monajembashi, S., Shao, A., Cui, D., He, W., Chen, Z., et al. (2012). Contribution of the C-terminal regions of promyelocytic leukemia protein (PML) isoforms II and V to PML nuclear body formation. J. Biol. Chem. 287, 30729-30742.
    • (2012) J. Biol. Chem. , vol.287 , pp. 30729-30742
    • Geng, Y.1    Monajembashi, S.2    Shao, A.3    Cui, D.4    He, W.5    Chen, Z.6
  • 35
    • 78651471295 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia protein in host antiviral defense
    • Geoffroy, M. C., and Chelbi-Alix, M. K. (2011). Role of promyelocytic leukemia protein in host antiviral defense. J. Interferon Cytokine Res. 31, 145-158.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 145-158
    • Geoffroy, M.C.1    Chelbi-Alix, M.K.2
  • 36
    • 78649425814 scopus 로고    scopus 로고
    • PML regulates apoptosis at endoplasmic reticulum by modulating calcium release
    • Giorgi, C., Ito, K., Lin, H. K., Santangelo, C., Wieckowski, M. R., Lebiedzinska, M., et al. (2010). PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 330, 1247-1251.
    • (2010) Science , vol.330 , pp. 1247-1251
    • Giorgi, C.1    Ito, K.2    Lin, H.K.3    Santangelo, C.4    Wieckowski, M.R.5    Lebiedzinska, M.6
  • 39
    • 35948982216 scopus 로고    scopus 로고
    • The mengovirus leader protein blocks interferon-alpha/beta gene transcription and inhibits activation of interferon regulatory factor 3
    • Hato, S. V., Ricour, C., Schulte, B. M., Lanke, K. H., De Bruijni, M., Zoll, J., et al. (2007). The mengovirus leader protein blocks interferon-alpha/beta gene transcription and inhibits activation of interferon regulatory factor 3. Cell. Microbiol. 9, 2921-2930.
    • (2007) Cell. Microbiol. , vol.9 , pp. 2921-2930
    • Hato, S.V.1    Ricour, C.2    Schulte, B.M.3    Lanke, K.H.4    De Bruijni, M.5    Zoll, J.6
  • 40
    • 1842785771 scopus 로고    scopus 로고
    • Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis
    • Hayakawa, F., and Privalsky, M. L. (2004). Phosphorylation of PML by mitogen-activated protein kinases plays a key role in arsenic trioxide-mediated apoptosis. Cancer Cell 5, 389-401.
    • (2004) Cancer Cell , vol.5 , pp. 389-401
    • Hayakawa, F.1    Privalsky, M.L.2
  • 41
    • 0023752982 scopus 로고
    • Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia
    • Huang, M. E., Ye, Y. C., Chen, S. R., Chai, J. R., Lu, J. X., Zhoa, L., et al. (1988). Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia. Blood 72, 567-572.
    • (1988) Blood , vol.72 , pp. 567-572
    • Huang, M.E.1    Ye, Y.C.2    Chen, S.R.3    Chai, J.R.4    Lu, J.X.5    Zhoa, L.6
  • 42
    • 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., et al. (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
  • 44
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen, K., Shiels, C., and Freemont, P. S. (2001). PML protein isoforms and the RBCC/TRIM motif. Oncogene 20, 7223-7233.
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 45
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • Kakizuka, A., Miller, W. H. Jr., Umesono, K., Warrell, R. P. Jr., Frankel, S. R., Murty, V. V., et al. (1991). Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell 66, 663-674.
    • (1991) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller Jr., W.H.2    Umesono, K.3    Warrell Jr., R.P.4    Frankel, S.R.5    Murty, V.V.6
  • 47
    • 0026583943 scopus 로고
    • Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins
    • Kastner, P., Perez, A., Lutz, Y., Rochette-Egly, C., Gaub, M. P., Durand, B., et al. (1992). Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. EMBO J. 11, 629-642.
    • (1992) EMBO J. , vol.11 , pp. 629-642
    • Kastner, P.1    Perez, A.2    Lutz, Y.3    Rochette-Egly, C.4    Gaub, M.P.5    Durand, B.6
  • 48
    • 53449090838 scopus 로고    scopus 로고
    • Role of nuclear bodies in apoptosis signalling
    • Krieghoff-Henning, E., and Hofmann, T. G. (2008). Role of nuclear bodies in apoptosis signalling. Biochim. Biophys. Acta 1783, 2185-2194.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 2185-2194
    • Krieghoff-Henning, E.1    Hofmann, T.G.2
  • 49
    • 66149128368 scopus 로고    scopus 로고
    • Components of nuclear domain 10 bodies regulate varicella-zoster virus replication
    • Kyratsous, C. A., and Silverstein, S. J. (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
  • 50
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • Lallemand-Breitenbach, V., Jeanne, M., Benhenda, S., Nasr, R., Lei, M., Peres, L., et al. (2008). Arsenic degrades PML or PML-RARalpha 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    Jeanne, M.2    Benhenda, S.3    Nasr, R.4    Lei, M.5    Peres, L.6
  • 52
    • 0035908032 scopus 로고    scopus 로고
    • Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation
    • Lallemand-Breitenbach, V., Zhu, J., Puvion, F., Koken, M., Honore, N., Doubeikovsky, A., et al. (2001). Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation. J. Exp. Med. 193, 1361-1371.
    • (2001) J. Exp. Med. , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3    Koken, M.4    Honore, N.5    Doubeikovsky, A.6
  • 53
    • 59849108860 scopus 로고    scopus 로고
    • Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukaemia (PML) protein nuclear domains for disruption via a sequence in PML isoform II that is predicted as a protein interaction site by bioinformatic analysis
    • Leppard, K. N., Emmott, E., Cortese, M. S., and Rich, T. (2009). Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukaemia (PML) protein nuclear domains for disruption via a sequence in PML isoform II that is predicted as a protein interaction site by bioinformatic analysis. J. Gen. Virol. 90, 95-104.
    • (2009) J. Gen. Virol. , vol.90 , pp. 95-104
    • Leppard, K.N.1    Emmott, E.2    Cortese, M.S.3    Rich, T.4
  • 54
    • 34548238145 scopus 로고    scopus 로고
    • Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation
    • Levy, L., Howell, M., Das, D., Harkin, S., Episkopou, V., and Hill, C. S. (2007). Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation. Mol. Cell. Biol. 27, 6068-6083.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6068-6083
    • Levy, L.1    Howell, M.2    Das, D.3    Harkin, S.4    Episkopou, V.5    Hill, C.S.6
  • 55
    • 84455173238 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover
    • Lim, J. H., Liu, Y., Reineke, E., and Kao, H. Y. (2011). Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover. J. Biol. Chem. 286, 44403-44411.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44403-44411
    • Lim, J.H.1    Liu, Y.2    Reineke, E.3    Kao, H.Y.4
  • 56
    • 4544256756 scopus 로고    scopus 로고
    • Cytoplasmic PML function in TGF-beta signalling
    • Lin, H. K., Bergmann, S., and Pandolfi, P. P. (2004). Cytoplasmic PML function in TGF-beta signalling. Nature 431, 205-211.
    • (2004) Nature , vol.431 , pp. 205-211
    • Lin, H.K.1    Bergmann, S.2    Pandolfi, P.P.3
  • 58
    • 84877913024 scopus 로고    scopus 로고
    • Trafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleus
    • doi:10.1074/jbc.M112.437392. [Epub ahead of print].
    • Malloy, M. T., McIntosh, D. J., Walters, T. S., Flores, A., Goodwin, J. S., and Arinze, I. J. (2013). Trafficking of the transcription factor Nrf2 to promyelocytic leukemia-nuclear bodies: implications for degradation of NRF2 in the nucleus. J. Biol. Chem. doi:10.1074/jbc.M112.437392. [Epub ahead of print].
    • (2013) J. Biol. Chem.
    • Malloy, M.T.1    McIntosh, D.J.2    Walters, T.S.3    Flores, A.4    Goodwin, J.S.5    Arinze, I.J.6
  • 59
    • 84866510150 scopus 로고    scopus 로고
    • Requirement of PML SUMO interacting motif for RNF4-or arsenic trioxide-induced degradation of nuclear PML isoforms
    • doi:10.1371/journal.pone.0044949
    • Maroui, M. A., Kheddache-Atmane, S., El Asmi, F., Dianoux, L., Aubry, M., and Chelbi-Alix, M. K. (2012). Requirement of PML SUMO interacting motif for RNF4-or arsenic trioxide-induced degradation of nuclear PML isoforms. PLoS ONE 7:e44949. doi:10.1371/journal.pone.0044949
    • (2012) PLoS ONE , vol.7
    • Maroui, M.A.1    Kheddache-Atmane, S.2    El Asmi, F.3    Dianoux, L.4    Aubry, M.5    Chelbi-Alix, M.K.6
  • 60
    • 84855836014 scopus 로고    scopus 로고
    • Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies
    • Maroui, M. A., Pampin, M., and Chelbi-Alix, M. K. (2011). Promyelocytic leukemia isoform IV confers resistance to encephalomyocarditis virus via the sequestration of 3D polymerase in nuclear bodies. J. Virol. 85, 13164-13173.
    • (2011) J. Virol. , vol.85 , pp. 13164-13173
    • Maroui, M.A.1    Pampin, M.2    Chelbi-Alix, M.K.3
  • 61
    • 77956251955 scopus 로고    scopus 로고
    • Single-agent arsenic trioxide in the treatment of newly diagnosed acute promyelocytic leukemia: long-term follow-up data
    • Mathews, V., George, B., Chendamarai, E., Lakshmi, K. M., Desire, S., Balasubramanian, P., et al. (2010). Single-agent arsenic trioxide in the treatment of newly diagnosed acute promyelocytic leukemia: long-term follow-up data. J. Clin. Oncol. 28, 3866-3871.
    • (2010) J. Clin. Oncol. , vol.28 , pp. 3866-3871
    • Mathews, V.1    George, B.2    Chendamarai, E.3    Lakshmi, K.M.4    Desire, S.5    Balasubramanian, P.6
  • 62
    • 48449083440 scopus 로고    scopus 로고
    • A role for cytoplasmic PML in cellular resistance to viral infection
    • doi:10.1371/journal.pone.0002277
    • McNally, B. A., Trgovcich, J., Maul, G. G., Liu, Y., and Zheng, P. (2008). A role for cytoplasmic PML in cellular resistance to viral infection. PLoS ONE 3:e2277. doi:10.1371/journal.pone.0002277
    • (2008) PLoS ONE , vol.3
    • McNally, B.A.1    Trgovcich, J.2    Maul, G.G.3    Liu, Y.4    Zheng, P.5
  • 63
    • 0037409182 scopus 로고    scopus 로고
    • The molecular pathogenesis of acute promyelocytic leukaemia: implications for the clinical management of the disease
    • Mistry, A. R., Pedersen, E. W., Solomon, E., and Grimwade, D. (2003). The molecular pathogenesis of acute promyelocytic leukaemia: implications for the clinical management of the disease. Blood Rev. 17, 71-97.
    • (2003) Blood Rev. , vol.17 , pp. 71-97
    • Mistry, A.R.1    Pedersen, E.W.2    Solomon, E.3    Grimwade, D.4
  • 64
    • 0027232936 scopus 로고
    • Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA
    • Moriuchi, H., Moriuchi, M., Straus, S. E., and Cohen, J. I. (1993). Varicella-zoster virus (VZV) open reading frame 61 protein transactivates VZV gene promoters and enhances the infectivity of VZV DNA. J. Virol. 67, 4290-4295.
    • (1993) J. Virol. , vol.67 , pp. 4290-4295
    • Moriuchi, H.1    Moriuchi, M.2    Straus, S.E.3    Cohen, J.I.4
  • 65
    • 0033935685 scopus 로고    scopus 로고
    • Herpes simplex virus ICP0 mutants are hypersensitive to interferon
    • Mossman, K. L., Saffran, H. A., and Smiley, J. R. (2000). Herpes simplex virus ICP0 mutants are hypersensitive to interferon. J. Virol. 74, 2052-2056.
    • (2000) J. Virol. , vol.74 , pp. 2052-2056
    • Mossman, K.L.1    Saffran, H.A.2    Smiley, J.R.3
  • 66
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Muller, S., Matunis, M. J., and Dejean, A. (1998). Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J. 17, 61-70.
    • (1998) EMBO J. , vol.17 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 67
    • 28444448039 scopus 로고    scopus 로고
    • The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice
    • Nacerddine, K., Lehembre, F., Bhaumik, M., Artus, J., Cohen-Tannoudji, M., Babinet, C., 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    Lehembre, F.2    Bhaumik, M.3    Artus, J.4    Cohen-Tannoudji, M.5    Babinet, C.6
  • 68
    • 0032497586 scopus 로고    scopus 로고
    • Targeting the PML/RAR alpha translocation product triggers apoptosis in promyelocytic leukemia cells
    • Nason-Burchenal, K., Takle, G., Pace, U., Flynn, S., Allopenna, J., Martin, P., et al. (1998). Targeting the PML/RAR alpha translocation product triggers apoptosis in promyelocytic leukemia cells. Oncogene 17, 1759-1768.
    • (1998) Oncogene , vol.17 , pp. 1759-1768
    • Nason-Burchenal, K.1    Takle, G.2    Pace, U.3    Flynn, S.4    Allopenna, J.5    Martin, P.6
  • 69
    • 11144219997 scopus 로고    scopus 로고
    • Physical and functional link of the leukemia-associated factors AML1 and PML
    • Nguyen, L. A., Pandolfi, P. P., Aikawa, Y., Tagata, Y., Ohki, M., and Kitabayashi, I. (2005). Physical and functional link of the leukemia-associated factors AML1 and PML. Blood 105, 292-300.
    • (2005) Blood , vol.105 , pp. 292-300
    • Nguyen, L.A.1    Pandolfi, P.P.2    Aikawa, Y.3    Tagata, Y.4    Ohki, M.5    Kitabayashi, I.6
  • 70
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: retroviral restriction and antiviral defence
    • Nisole, S., Stoye, J. P., and Saib, A. (2005). TRIM family proteins: retroviral restriction and antiviral defence. Nat. Rev. Microbiol. 3, 799-808.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 71
    • 69549138485 scopus 로고    scopus 로고
    • PML-IV functions as a negative regulator of telomerase by interacting with TERT
    • Oh, W., Ghim, J., Lee, E. W., Yang, M. R., Kim, E. T., Ahn, J. H., et al. (2009). PML-IV functions as a negative regulator of telomerase by interacting with TERT. J. Cell. Sci. 122, 2613-2622.
    • (2009) J. Cell. Sci. , vol.122 , pp. 2613-2622
    • Oh, W.1    Ghim, J.2    Lee, E.W.3    Yang, M.R.4    Kim, E.T.5    Ahn, J.H.6
  • 72
    • 33748636239 scopus 로고    scopus 로고
    • Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense
    • Pampin, M., Simonin, Y., Blondel, B., Percherancier, Y., and Chelbi-Alix, M. K. (2006). Cross talk between PML and p53 during poliovirus infection: implications for antiviral defense. J. Virol. 80, 8582-8592.
    • (2006) J. Virol. , vol.80 , pp. 8582-8592
    • Pampin, M.1    Simonin, Y.2    Blondel, B.3    Percherancier, Y.4    Chelbi-Alix, M.K.5
  • 73
    • 0025917413 scopus 로고
    • Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties
    • Pandolfi, P. P., Grignani, F., Alcalay, M., Mencarelli, A., Biondi, A., Lococo, F., et al. (1991). Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene 6, 1285-1292.
    • (1991) Oncogene , vol.6 , pp. 1285-1292
    • Pandolfi, P.P.1    Grignani, F.2    Alcalay, M.3    Mencarelli, A.4    Biondi, A.5    Lococo, F.6
  • 74
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Pearson, M., Carbone, R., Sebastiani, C., Cioce, M., Fagioli, M., Saito, S., et al. (2000). PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 406, 207-210.
    • (2000) Nature , vol.406 , pp. 207-210
    • Pearson, M.1    Carbone, R.2    Sebastiani, C.3    Cioce, M.4    Fagioli, M.5    Saito, S.6
  • 75
    • 67650239825 scopus 로고    scopus 로고
    • Role of SUMO in RNF4-mediated promyelocytic leukemia protein (PML) degradation: sumoylation of PML and phospho-switch control of its SUMO binding domain dissected in living cells
    • Percherancier, Y., Germain-Desprez, D., Galisson, F., Mascle, X. H., Dianoux, L., Estephan, P., et al. (2009). Role of SUMO in RNF4-mediated promyelocytic leukemia protein (PML) degradation: sumoylation of PML and phospho-switch control of its SUMO binding domain dissected in living cells. J. Biol. Chem. 284, 16595-16608.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16595-16608
    • Percherancier, Y.1    Germain-Desprez, D.2    Galisson, F.3    Mascle, X.H.4    Dianoux, L.5    Estephan, P.6
  • 76
    • 13244249577 scopus 로고    scopus 로고
    • Interferons alpha and gamma induce p53-dependent and p53-independent apoptosis, respectively
    • Porta, C., Hadj-Slimane, R., Nejmeddine, M., Pampin, M., Tovey, M. G., Espert, L., et al. (2005). Interferons alpha and gamma induce p53-dependent and p53-independent apoptosis, respectively. Oncogene 24, 605-615.
    • (2005) Oncogene , vol.24 , pp. 605-615
    • Porta, C.1    Hadj-Slimane, R.2    Nejmeddine, M.3    Pampin, M.4    Tovey, M.G.5    Espert, L.6
  • 77
    • 84860526509 scopus 로고    scopus 로고
    • The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA
    • Rabellino, A., Carter, B., Konstantinidou, G., Wu, S. Y., Rimessi, A., Byers, L. A., et al. (2012). The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA. Cancer Res. 72, 2275-2284.
    • (2012) Cancer Res. , vol.72 , pp. 2275-2284
    • Rabellino, A.1    Carter, B.2    Konstantinidou, G.3    Wu, S.Y.4    Rimessi, A.5    Byers, L.A.6
  • 78
    • 84883290530 scopus 로고    scopus 로고
    • PML degradation: multiple ways to eliminate PML
    • doi:10.3389/fonc.2013.00060
    • Rabellino, A., and Scaglioni, P. P. (2013). PML degradation: multiple ways to eliminate PML. Front. Oncol. 3:60. doi:10.3389/fonc.2013.00060
    • (2013) Front. Oncol. , vol.3 , pp. 60
    • Rabellino, A.1    Scaglioni, P.P.2
  • 79
    • 79952219169 scopus 로고    scopus 로고
    • Entrapment of viral capsids in nuclear PML cages is an intrinsic antiviral host defense against varicella-zoster virus
    • doi:10.1371/journal.ppat.1001266
    • Reichelt, M., Wang, L., Sommer, M., Perrino, J., Nour, A. M., Sen, N., 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. doi:10.1371/journal.ppat.1001266
    • (2011) PLoS Pathog. , vol.7
    • Reichelt, M.1    Wang, L.2    Sommer, M.3    Perrino, J.4    Nour, A.M.5    Sen, N.6
  • 80
    • 38549132438 scopus 로고    scopus 로고
    • Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells
    • Reineke, E. L., Lam, M., Liu, Q., Liu, Y., Stanya, K. J., Chang, K. S., et al. (2008). Degradation of the tumor suppressor PML by Pin1 contributes to the cancer phenotype of breast cancer MDA-MB-231 cells. Mol. Cell. Biol. 28, 997-1006.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 997-1006
    • Reineke, E.L.1    Lam, M.2    Liu, Q.3    Liu, Y.4    Stanya, K.J.5    Chang, K.S.6
  • 81
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • Reymond, A., Meroni, G., Fantozzi, A., Merla, G., Cairo, S., Luzi, L., et al. (2001). The tripartite motif family identifies cell compartments. EMBO J. 20, 2140-2151.
    • (2001) EMBO J. , vol.20 , pp. 2140-2151
    • Reymond, A.1    Meroni, G.2    Fantozzi, A.3    Merla, G.4    Cairo, S.5    Luzi, L.6
  • 82
    • 79551649719 scopus 로고    scopus 로고
    • The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies
    • doi:10.1371/journal.pone.0016598
    • Sarkari, F., Wang, X., Nguyen, T., and Frappier, L. (2011). The herpesvirus associated ubiquitin specific protease, USP7, is a negative regulator of PML proteins and PML nuclear bodies. PLoS ONE 6:e16598. doi:10.1371/journal.pone.0016598
    • (2011) PLoS ONE , vol.6
    • Sarkari, F.1    Wang, X.2    Nguyen, T.3    Frappier, L.4
  • 85
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., Huibregtse, J. M., Vierstra, R. D., and Howley, P. M. (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 86
    • 84888867501 scopus 로고    scopus 로고
    • Regulation of the tumor suppressor PML by sequential post-translational modifications
    • doi:10.3389/fonc.2012.00204
    • Schmitz, M. L., and Grishina, I. (2012). Regulation of the tumor suppressor PML by sequential post-translational modifications. Front. Oncol. 2:204. doi:10.3389/fonc.2012.00204
    • (2012) Front. Oncol. , vol.2 , pp. 204
    • Schmitz, M.L.1    Grishina, I.2
  • 88
    • 77957965855 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 1 hijacks the host kinase CK2 to disrupt PML nuclear bodies
    • Sivachandran, N., Cao, J. Y., and Frappier, L. (2010). Epstein-Barr virus nuclear antigen 1 hijacks the host kinase CK2 to disrupt PML nuclear bodies. J. Virol. 84, 11113-11123.
    • (2010) J. Virol. , vol.84 , pp. 11113-11123
    • Sivachandran, N.1    Cao, J.Y.2    Frappier, L.3
  • 90
    • 55449133376 scopus 로고    scopus 로고
    • Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies
    • doi:10.1371/journal.ppat.1000170
    • Sivachandran, N., Sarkari, F., and Frappier, L. (2008). Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies. PLoS Pathog. 4:e1000170. doi:10.1371/journal.ppat.1000170
    • (2008) PLoS Pathog. , vol.4
    • Sivachandran, N.1    Sarkari, F.2    Frappier, L.3
  • 91
    • 79960441542 scopus 로고    scopus 로고
    • CK2 inhibitors increase the sensitivity of HSV-1 to interferon-beta
    • Smith, M. C., Bayless, A. M., Goddard, E. T., and Davido, D. J. (2011). CK2 inhibitors increase the sensitivity of HSV-1 to interferon-beta. Antiviral Res. 91, 259-266.
    • (2011) Antiviral Res. , vol.91 , pp. 259-266
    • Smith, M.C.1    Bayless, A.M.2    Goddard, E.T.3    Davido, D.J.4
  • 93
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling
    • Stehmeier, P., and Muller, S. (2009). Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol. Cell 33, 400-409.
    • (2009) Mol. Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 94
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham, M. H., Geoffroy, M. C., Shen, L., Plechanovova, A., Hattersley, N., Jaffray, E. G., 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    Geoffroy, M.C.2    Shen, L.3    Plechanovova, A.4    Hattersley, N.5    Jaffray, E.G.6
  • 95
    • 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
  • 96
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai, N., and 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
  • 97
    • 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, T. H., and 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
  • 98
    • 33846019234 scopus 로고    scopus 로고
    • Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics
    • Vertegaal, A. C., Andersen, J. S., Ogg, S. C., Hay, R. T., Mann, M., and Lamond, A. I. (2006). Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol. Cell Proteomics 5, 2298-2310.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2298-2310
    • Vertegaal, A.C.1    Andersen, J.S.2    Ogg, S.C.3    Hay, R.T.4    Mann, M.5    Lamond, A.I.6
  • 99
    • 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
    • doi:10.1371/journal.ppat.1002157
    • Wang, L., Oliver, S. L., Sommer, M., Rajamani, J., Reichelt, M., and Arvin, A. M. (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. doi:10.1371/journal.ppat.1002157
    • (2011) PLoS Pathog. , vol.7
    • Wang, L.1    Oliver, S.L.2    Sommer, M.3    Rajamani, J.4    Reichelt, M.5    Arvin, A.M.6
  • 101
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis, K., Rambaud, S., Lavau, C., Jansen, J., Carvalho, T., Carmo-Fonseca, M., et al. (1994). Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76, 345-356.
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6
  • 102
    • 51249085621 scopus 로고    scopus 로고
    • Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML
    • Weisshaar, S. R., Keusekotten, K., Krause, A., Horst, C., Springer, H. M., Gottsche, K., 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    Keusekotten, K.2    Krause, A.3    Horst, C.4    Springer, H.M.5    Gottsche, K.6
  • 104
    • 67649768532 scopus 로고    scopus 로고
    • PML3 orchestrates the nuclear dynamics and function of TIP60
    • Wu, Q., Hu, H., Lan, J., Emenari, C., Wang, Z., Chang, K. S., et al. (2009). PML3 orchestrates the nuclear dynamics and function of TIP60. J. Biol. Chem. 284, 8747-8759.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8747-8759
    • Wu, Q.1    Hu, H.2    Lan, J.3    Emenari, C.4    Wang, Z.5    Chang, K.S.6
  • 105
    • 14644394332 scopus 로고    scopus 로고
    • A role for PML3 in centrosome duplication and genome stability
    • Xu, Z. X., Zou, W. X., Lin, P., and Chang, K. S. (2005). A role for PML3 in centrosome duplication and genome stability. Mol. Cell 17, 721-732.
    • (2005) Mol. Cell , vol.17 , pp. 721-732
    • Xu, Z.X.1    Zou, W.X.2    Lin, P.3    Chang, K.S.4
  • 106
    • 34547873122 scopus 로고    scopus 로고
    • PML-retinoic acid receptor alpha inhibits PML IV enhancement of PU.1-induced C/EBPepsilon expression in myeloid differentiation
    • Yoshida, H., Ichikawa, H., Tagata, Y., Katsumoto, T., Ohnishi, K., Akao, Y., et al. (2007). PML-retinoic acid receptor alpha inhibits PML IV enhancement of PU.1-induced C/EBPepsilon expression in myeloid differentiation. Mol. Cell. Biol. 27, 5819-5834.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5819-5834
    • Yoshida, H.1    Ichikawa, H.2    Tagata, Y.3    Katsumoto, T.4    Ohnishi, K.5    Akao, Y.6
  • 107
    • 77950021419 scopus 로고    scopus 로고
    • PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells
    • Yu, J., Lan, J., Wang, C., Wu, Q., Zhu, Y., Lai, X., et al. (2010). PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells. Cancer Lett. 291, 177-186.
    • (2010) Cancer Lett. , vol.291 , pp. 177-186
    • Yu, J.1    Lan, J.2    Wang, C.3    Wu, Q.4    Zhu, Y.5    Lai, X.6
  • 108
    • 80051583598 scopus 로고    scopus 로고
    • A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression
    • Yuan, W. C., Lee, Y. R., Huang, S. F., Lin, Y. M., Chen, T. Y., Chung, H. C., et al. (2011). A Cullin3-KLHL20 Ubiquitin ligase-dependent pathway targets PML to potentiate HIF-1 signaling and prostate cancer progression. Cancer Cell 20, 214-228.
    • (2011) Cancer Cell , vol.20 , pp. 214-228
    • Yuan, W.C.1    Lee, Y.R.2    Huang, S.F.3    Lin, Y.M.4    Chen, T.Y.5    Chung, H.C.6
  • 109
    • 0035969115 scopus 로고    scopus 로고
    • Translocations of the RARalpha gene in acute promyelocytic leukemia
    • Zelent, A., Guidez, F., Melnick, A., Waxman, S., and Licht, J. D. (2001). Translocations of the RARalpha gene in acute promyelocytic leukemia. Oncogene 20, 7186-7203.
    • (2001) Oncogene , vol.20 , pp. 7186-7203
    • Zelent, A.1    Guidez, F.2    Melnick, A.3    Waxman, S.4    Licht, J.D.5
  • 110
    • 77950826446 scopus 로고    scopus 로고
    • Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML
    • Zhang, X. W., Yan, X. J., Zhou, Z. R., Yang, F. F., Wu, Z. Y., Sun, H. B., et al. (2010). Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML. Science 328, 240-243.
    • (2010) Science , vol.328 , pp. 240-243
    • Zhang, X.W.1    Yan, X.J.2    Zhou, Z.R.3    Yang, F.F.4    Wu, Z.Y.5    Sun, H.B.6
  • 111
    • 0033592948 scopus 로고    scopus 로고
    • Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARalpha) and oncogenic RARalpha fusion proteins
    • Zhu, J., Gianni, M., Kopf, E., Honore, N., Chelbi-Alix, M., Koken, M., et al. (1999). Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARalpha) and oncogenic RARalpha fusion proteins. Proc. Natl. Acad. Sci. U.S.A. 96, 14807-14812.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14807-14812
    • Zhu, J.1    Gianni, M.2    Kopf, E.3    Honore, N.4    Chelbi-Alix, M.5    Koken, M.6
  • 112
    • 0030890942 scopus 로고    scopus 로고
    • Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia
    • Zhu, J., Koken, M. H., Quignon, F., Chelbi-Alix, M. K., Degos, L., Wang, Z. Y., et al. (1997). Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc. Natl. Acad. Sci. U.S.A. 94, 3978-3983.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3978-3983
    • Zhu, J.1    Koken, M.H.2    Quignon, F.3    Chelbi-Alix, M.K.4    Degos, L.5    Wang, Z.Y.6


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