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Volumn 6, Issue 1, 2010, Pages 51-67

A manually curated network of the pml nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics

Author keywords

Cytoscape; Network; PML NB; Protein protein interaction; SUMOylation

Indexed keywords

NUCLEAR PROTEIN; PML PROTEIN, HUMAN; SUMO PROTEIN; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN;

EID: 77449089538     PISSN: 14492288     EISSN: None     Source Type: Journal    
DOI: 10.7150/ijbs.6.51     Document Type: Article
Times cited : (166)

References (152)
  • 1
    • 84961052513 scopus 로고
    • BERNHARD W. [Examination by electron microscope of the VX2 tumor of the domestic rabbit derived from the Shope papilloma.]
    • Oct
    • de THE H, RIVIERE M, BERNHARD W. [Examination by electron microscope of the VX2 tumor of the domestic rabbit derived from the Shope papilloma.]. Bull Assoc Fr Etud Cancer 1960 Oct;47:570-84.
    • (1960) Bull Assoc Fr Etud Cancer , vol.47 , pp. 570-584
    • de The, H.1    Riviere, M.2
  • 2
    • 0010981661 scopus 로고
    • Ultrastructure of invasive pavement-cell cancers of the uterine cervix in women
    • Apr
    • HINGLAIS-GUILLAUD N, MORICARD R, BERNHARD W. [Ultrastructure of invasive pavement-cell cancers of the uterine cervix in women.]. Bull Assoc Fr Etud Cancer 1961 Apr;48:283-316.
    • (1961) Bull Assoc Fr Etud Cancer , vol.48 , pp. 283-316
    • Hinglais-Guillaud, N.1    Moricard, R.2    Bernhard, W.3
  • 3
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Oct 29
    • Jensen K, Shiels C, Freemont PS. PML protein isoforms and the RBCC/TRIM motif. Oncogene 2001 Oct 29;20(49):7223-33.
    • (2001) Oncogene , vol.20 , Issue.49 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 4
    • 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
    • Oct 18
    • Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, Kamitani T, et al. 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 1999 Oct 18;147(2):221-34.
    • (1999) J Cell Biol , vol.147 , Issue.2 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5    Kamitani, T.6
  • 5
    • 0032463343 scopus 로고    scopus 로고
    • RING fingers and B-boxes: Zinc-binding protein-protein interaction domains
    • Borden KL. RING fingers and B-boxes: zinc-binding protein-protein interaction domains. Biochem Cell Biol 1998;76(2-3):351-8.
    • (1998) Biochem Cell Biol , vol.76 , Issue.2-3 , pp. 351-358
    • Borden, K.L.1
  • 6
    • 0035965139 scopus 로고    scopus 로고
    • The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor eIF4E
    • Sep 28
    • Kentsis A, Dwyer EC, Perez JM, Sharma M, Chen A, Pan ZQ, et al. The RING domains of the promyelocytic leukemia protein PML and the arenaviral protein Z repress translation by directly inhibiting translation initiation factor eIF4E. J Mol Biol 2001 Sep 28;312(4):609-23.
    • (2001) J Mol Biol , vol.312 , Issue.4 , pp. 609-623
    • Kentsis, A.1    Dwyer, E.C.2    Perez, J.M.3    Sharma, M.4    Chen, A.5    Pan, Z.Q.6
  • 7
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • May 1
    • Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, et al. The tripartite motif family identifies cell compartments. EMBO J 2001 May 1;20(9):2140-51.
    • (2001) Embo J , vol.20 , Issue.9 , pp. 2140-2151
    • Reymond, A.1    Meroni, G.2    Fantozzi, A.3    Merla, G.4    Cairo, S.5    Luzi, L.6
  • 8
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • Mar 5
    • Boisvert FM, Kruhlak MJ, Box AK, Hendzel MJ, Bazett-Jones DP. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J Cell Biol 2001 Mar 5;152(5):1099-106.
    • (2001) J Cell Biol , vol.152 , Issue.5 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3    Hendzel, M.J.4    Bazett-Jones, D.P.5
  • 10
    • 24644522876 scopus 로고    scopus 로고
    • Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3
    • Aug 18
    • Fu C, Ahmed K, Ding H, Ding X, Lan J, Yang Z, et al. Stabilization of PML nuclear localization by conjugation and oligomerization of SUMO-3. Oncogene 2005 Aug 18;24(35):5401-13.
    • (2005) Oncogene , vol.24 , Issue.35 , pp. 5401-5413
    • Fu, C.1    Ahmed, K.2    Ding, H.3    Ding, X.4    Lan, J.5    Yang, Z.6
  • 11
    • 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
    • Jun 18
    • Lallemand-Breitenbach V, Zhu J, Puvion F, Koken M, Honore N, Doubeikovsky A, et al. 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 2001 Jun 18;193(12):1361-71.
    • (2001) J Exp Med , vol.193 , Issue.12 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1    Zhu, J.2    Puvion, F.3    Koken, M.4    Honore, N.5    Doubeikovsky, A.6
  • 12
    • 43049096803 scopus 로고    scopus 로고
    • Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway
    • May
    • Lallemand-Breitenbach V, Jeanne M, Benhenda S, Nasr R, Lei M, Peres L, et al. Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway. Nat Cell Biol 2008 May;10(5):547-55.
    • (2008) Nat Cell Biol , vol.10 , Issue.5 , pp. 547-555
    • Lallemand-Breitenbach, V.1    Jeanne, M.2    Benhenda, S.3    Nasr, R.4    Lei, M.5    Peres, L.6
  • 13
    • 37749020681 scopus 로고    scopus 로고
    • Small ubiquitin-related modifiers in chains
    • Dec
    • Vertegaal AC. Small ubiquitin-related modifiers in chains. Biochem Soc Trans 2007 Dec;35(Pt 6):1422-3.
    • (2007) Biochem Soc Trans , vol.35 , Issue.Pt 6 , pp. 1422-1423
    • Vertegaal, A.C.1
  • 14
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Apr 1
    • Hay RT. SUMO: a history of modification. Mol Cell 2005 Apr 1;18(1):1-12.
    • (2005) Mol Cell , vol.18 , Issue.1 , pp. 1-12
    • Hay, R.T.1
  • 15
    • 1542501958 scopus 로고    scopus 로고
    • SUMO: Ligases, isopeptidases and nuclear pores
    • Nov
    • Melchior F, Schergaut M, Pichler A. SUMO: ligases, isopeptidases and nuclear pores. Trends Biochem Sci 2003 Nov;28(11):612-8.
    • (2003) Trends Biochem Sci , vol.28 , Issue.11 , pp. 612-618
    • Melchior, F.1    Schergaut, M.2    Pichler, A.3
  • 16
    • 34047127403 scopus 로고    scopus 로고
    • Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity
    • Hamard PJ, Boyer-Guittaut M, Camuzeaux B, Dujardin D, Hauss C, Oelgeschlager T, et al. Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity. Nucleic Acids Res 2007;35(4):1134-44.
    • (2007) Nucleic Acids Res , vol.35 , Issue.4 , pp. 1134-1144
    • Hamard, P.J.1    Boyer-Guittaut, M.2    Camuzeaux, B.3    Dujardin, D.4    Hauss, C.5    Oelgeschlager, T.6
  • 17
    • 38049150586 scopus 로고    scopus 로고
    • The DNA damage response pathways: At the crossroad of protein modifications
    • Jan
    • Huen MS, Chen J. The DNA damage response pathways: at the crossroad of protein modifications. Cell Res 2008 Jan;18(1):8-16.
    • (2008) Cell Res , vol.18 , Issue.1 , pp. 8-16
    • Huen, M.S.1    Chen, J.2
  • 18
    • 33845989925 scopus 로고    scopus 로고
    • Expression of SUMO-2/3 induced senescence through p53- and pRB-mediated pathways
    • Nov 24
    • Li T, Santockyte R, Shen RF, Tekle E, Wang G, Yang DC, et al. Expression of SUMO-2/3 induced senescence through p53- and pRB-mediated pathways. J Biol Chem 2006 Nov 24;281(47):36221-7.
    • (2006) J Biol Chem , vol.281 , Issue.47 , pp. 36221-36227
    • Li, T.1    Santockyte, R.2    Shen, R.F.3    Tekle, E.4    Wang, G.5    Yang, D.C.6
  • 19
    • 0035890322 scopus 로고    scopus 로고
    • Intracellular targeting of proteins by sumoylation
    • Nov 15
    • Wilson VG, Rangasamy D. Intracellular targeting of proteins by sumoylation. Exp Cell Res 2001 Nov 15;271(1):57-65.
    • (2001) Exp Cell Res , vol.271 , Issue.1 , pp. 57-65
    • Wilson, V.G.1    Rangasamy, D.2
  • 20
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: The SUMO proteases
    • Jun
    • Mukhopadhyay D, Dasso M. Modification in reverse: the SUMO proteases. Trends Biochem Sci 2007 Jun;32(6):286-95.
    • (2007) Trends Biochem Sci , vol.32 , Issue.6 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 21
    • 14844299866 scopus 로고    scopus 로고
    • Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
    • Mar 1
    • Xu Z, Au SW. Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. Biochem J 2005 Mar 1;386(Pt 2):325-30.
    • (2005) Biochem J , vol.386 , Issue.Pt 2 , pp. 325-330
    • Xu, Z.1    Au, S.W.2
  • 22
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
    • Jul 15
    • Shen LN, Dong C, Liu H, Naismith JH, Hay RT. The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing. Biochem J 2006 Jul 15;397(2):279-88.
    • (2006) Biochem J , vol.397 , Issue.2 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5
  • 24
    • 4143083663 scopus 로고    scopus 로고
    • A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
    • Aug
    • Reverter D, Lima CD. A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. Structure 2004 Aug;12(8):1519-31.
    • (2004) Structure , vol.12 , Issue.8 , pp. 1519-1531
    • Reverter, D.1    Lima, C.D.2
  • 25
    • 33845370047 scopus 로고    scopus 로고
    • Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
    • Dec
    • Reverter D, Lima CD. Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nat Struct Mol Biol 2006 Dec;13(12):1060-8.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.12 , pp. 1060-1068
    • Reverter, D.1    Lima, C.D.2
  • 26
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • Jun 9
    • Gong L, Yeh ET. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J Biol Chem 2006 Jun 9;281(23):15869-77.
    • (2006) J Biol Chem , vol.281 , Issue.23 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.2
  • 27
    • 28044437730 scopus 로고    scopus 로고
    • SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx
    • Nov 22
    • Kuo HY, Chang CC, Jeng JC, Hu HM, Lin DY, Maul GG, et al. SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx. Proc Natl Acad Sci U S A 2005 Nov 22;102(47):16973-8.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.47 , pp. 16973-16978
    • Kuo, H.Y.1    Chang, C.C.2    Jeng, J.C.3    Hu, H.M.4    Lin, D.Y.5    Maul, G.G.6
  • 28
    • 67650911884 scopus 로고    scopus 로고
    • Characterization of SENP7, a SUMO-2/3-specific isopeptidase
    • Jul 15
    • Shen LN, Geoffroy MC, Jaffray EG, Hay RT. Characterization of SENP7, a SUMO-2/3-specific isopeptidase. Biochem J 2009 Jul 15;421(2):223-30.
    • (2009) Biochem J , vol.421 , Issue.2 , pp. 223-230
    • Shen, L.N.1    Geoffroy, M.C.2    Jaffray, E.G.3    Hay, R.T.4
  • 29
    • 33748990136 scopus 로고    scopus 로고
    • SUSP1 antagonizes formation of highly SUMO2/3-conjugated species
    • Sep 25
    • Mukhopadhyay D, Ayaydin F, Kolli N, Tan SH, Anan T, Kametaka A, et al. SUSP1 antagonizes formation of highly SUMO2/3-conjugated species. J Cell Biol 2006 Sep 25;174(7):939-49.
    • (2006) J Cell Biol , vol.174 , Issue.7 , pp. 939-949
    • Mukhopadhyay, D.1    Ayaydin, F.2    Kolli, N.3    Tan, S.H.4    Anan, T.5    Kametaka, A.6
  • 30
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Sep 15
    • Johnson ES, Schwienhorst I, Dohmen RJ, Blobel G. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO J 1997 Sep 15;16(18):5509-19.
    • (1997) Embo J , vol.16 , Issue.18 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 32
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Nov 17
    • Desterro JM, Thomson J, Hay RT. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett 1997 Nov 17;417(3):297-300.
    • (1997) Febs Lett , vol.417 , Issue.3 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 33
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Apr 20
    • Rodriguez MS, Dargemont C, Hay RT. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem 2001 Apr 20;276(16):12654-9.
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 34
    • 0030657575 scopus 로고    scopus 로고
    • Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9
    • Nov 7
    • Gong L, Kamitani T, Fujise K, Caskey LS, Yeh ET. Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9. J Biol Chem 1997 Nov 7;272(45):28198-201.
    • (1997) J Biol Chem , vol.272 , Issue.45 , pp. 28198-28201
    • Gong, L.1    Kamitani, T.2    Fujise, K.3    Caskey, L.S.4    Yeh, E.T.5
  • 35
    • 25444505677 scopus 로고    scopus 로고
    • p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners
    • Apr
    • Rizos H, Woodruff S, Kefford RF. p14ARF interacts with the SUMO-conjugating enzyme Ubc9 and promotes the sumoylation of its binding partners. Cell Cycle 2005 Apr;4(4):597-603.
    • (2005) Cell Cycle , vol.4 , Issue.4 , pp. 597-603
    • Rizos, H.1    Woodruff, S.2    Kefford, R.F.3
  • 36
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Jan 11
    • Pichler A, Gast A, Seeler JS, Dejean A, Melchior F. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 2002 Jan 11;108(1):109-20.
    • (2002) Cell , vol.108 , Issue.1 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 37
    • 24144483441 scopus 로고    scopus 로고
    • Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo
    • Sep 12
    • Weger S, Hammer E, Heilbronn R. Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett 2005 Sep 12;579(22):5007-12.
    • (2005) Febs Lett , vol.579 , Issue.22 , pp. 5007-5012
    • Weger, S.1    Hammer, E.2    Heilbronn, R.3
  • 39
    • 0038558190 scopus 로고    scopus 로고
    • Sumoylation is involved in beta-catenin-dependent activation of Tcf-4
    • May 1
    • Yamamoto H, Ihara M, Matsuura Y, Kikuchi A. Sumoylation is involved in beta-catenin-dependent activation of Tcf-4. EMBO J 2003 May 1;22(9):2047-59.
    • (2003) Embo J , vol.22 , Issue.9 , pp. 2047-2059
    • Yamamoto, H.1    Ihara, M.2    Matsuura, Y.3    Kikuchi, A.4
  • 40
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • Dec 1
    • Sachdev S, Bruhn L, Sieber H, Pichler A, Melchior F, Grosschedl R. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev 2001 Dec 1;15(23):3088-103.
    • (2001) Genes Dev , vol.15 , Issue.23 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 41
    • 17644365783 scopus 로고    scopus 로고
    • SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4
    • May
    • Ihara M, Yamamoto H, Kikuchi A. SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4. Mol Cell Biol 2005 May;25(9):3506-18.
    • (2005) Mol Cell Biol , vol.25 , Issue.9 , pp. 3506-3518
    • Ihara, M.1    Yamamoto, H.2    Kikuchi, A.3
  • 42
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Apr 4
    • Kagey MH, Melhuish TA, Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell 2003 Apr 4;113(1):127-37.
    • (2003) Cell , vol.113 , Issue.1 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 43
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • May
    • Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, et al. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 2008 May;10(5):538-46.
    • (2008) Nat Cell Biol , vol.10 , Issue.5 , pp. 538-546
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3    Plechanovova, A.4    Hattersley, N.5    Jaffray, E.G.6
  • 44
    • 43149121351 scopus 로고    scopus 로고
    • MEL-18 interacts with HSF2 and the SUMO E2 UBC9 to inhibit HSF2 sumoylation
    • Mar 21
    • Zhang J, Goodson ML, Hong Y, Sarge KD. MEL-18 interacts with HSF2 and the SUMO E2 UBC9 to inhibit HSF2 sumoylation. J Biol Chem 2008 Mar 21;283(12):7464-9.
    • (2008) J Biol Chem , vol.283 , Issue.12 , pp. 7464-7469
    • Zhang, J.1    Goodson, M.L.2    Hong, Y.3    Sarge, K.D.4
  • 45
    • 0942290414 scopus 로고    scopus 로고
    • Proteasome-dependent dispersal of PML nuclear bodies in response to alkylating DNA damage
    • Jan 8
    • Conlan LA, McNees CJ, Heierhorst J. Proteasome-dependent dispersal of PML nuclear bodies in response to alkylating DNA damage. Oncogene 2004 Jan 8;23(1):307-10.
    • (2004) Oncogene , vol.23 , Issue.1 , pp. 307-310
    • Conlan, L.A.1    McNees, C.J.2    Heierhorst, J.3
  • 46
    • 4644345015 scopus 로고    scopus 로고
    • The Nijmegen breakage syndrome gene and its role in genome stability
    • Sep
    • Lijima K, Komatsu K, Matsuura S, Tauchi H. The Nijmegen breakage syndrome gene and its role in genome stability. Chromosoma 2004 Sep;113(2):53-61.
    • (2004) Chromosoma , vol.113 , Issue.2 , pp. 53-61
    • Lijima, K.1    Komatsu, K.2    Matsuura, S.3    Tauchi, H.4
  • 47
    • 54249103056 scopus 로고    scopus 로고
    • Regulation of apoptosis by PML and the PML-NBs
    • Oct 20
    • Bernardi R, Papa A, Pandolfi PP. Regulation of apoptosis by PML and the PML-NBs. Oncogene 2008 Oct 20;27(48):6299-312.
    • (2008) Oncogene , vol.27 , Issue.48 , pp. 6299-6312
    • Bernardi, R.1    Papa, A.2    Pandolfi, P.P.3
  • 48
    • 53449090838 scopus 로고    scopus 로고
    • Role of nuclear bodies in apoptosis signalling
    • Nov
    • Krieghoff-Henning E, Hofmann TG. Role of nuclear bodies in apoptosis signalling. Biochim Biophys Acta 2008 Nov;1783(11):2185-94.
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.11 , pp. 2185-2194
    • Krieghoff-Henning, E.1    Hofmann, T.G.2
  • 50
    • 0036771840 scopus 로고    scopus 로고
    • PML a target of translocations in APL is a regulator of cellular senescence
    • Oct
    • Ferbeyre G. PML a target of translocations in APL is a regulator of cellular senescence. Leukemia 2002 Oct;16(10):1918-26.
    • (2002) Leukemia , vol.16 , Issue.10 , pp. 1918-1926
    • Ferbeyre, G.1
  • 51
    • 0942301175 scopus 로고    scopus 로고
    • Human fibroblasts require the Rb family of tumor suppressors, but not p53, for PML-induced senescence
    • Jan 8
    • Mallette FA, Goumard S, Gaumont-Leclerc MF, Moiseeva O, Ferbeyre G. Human fibroblasts require the Rb family of tumor suppressors, but not p53, for PML-induced senescence. Oncogene 2004 Jan 8;23(1):91-9.
    • (2004) Oncogene , vol.23 , Issue.1 , pp. 91-99
    • Mallette, F.A.1    Goumard, S.2    Gaumont-Leclerc, M.F.3    Moiseeva, O.4    Ferbeyre, G.5
  • 52
    • 0034704782 scopus 로고    scopus 로고
    • The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA
    • Mar 23
    • Lai HK, Borden KL. The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA. Oncogene 2000 Mar 23;19(13):1623-34.
    • (2000) Oncogene , vol.19 , Issue.13 , pp. 1623-1634
    • Lai, H.K.1    Borden, K.L.2
  • 53
    • 57349101560 scopus 로고    scopus 로고
    • PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation
    • Dec
    • Shima Y, Shima T, Chiba T, Irimura T, Pandolfi PP, Kitabayashi I. PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation. Mol Cell Biol 2008 Dec;28(23):7126-38.
    • (2008) Mol Cell Biol , vol.28 , Issue.23 , pp. 7126-7138
    • Shima, Y.1    Shima, T.2    Chiba, T.3    Irimura, T.4    Pandolfi, P.P.5    Kitabayashi, I.6
  • 54
    • 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
    • Aug 23
    • de The H., Lavau C, Marchio A, Chomienne C, Degos L, Dejean A. The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 1991 Aug 23;66(4):675-84.
    • (1991) Cell , vol.66 , Issue.4 , pp. 675-684
    • de The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 55
    • 0031907092 scopus 로고    scopus 로고
    • Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein
    • Feb
    • Chelbi-Alix MK, Quignon F, Pelicano L, Koken MH, de TH. Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein. J Virol 1998 Feb;72(2):1043-51.
    • (1998) J Virol , vol.72 , Issue.2 , pp. 1043-1051
    • Chelbi-Alix, M.K.1    Quignon, F.2    Pelicano, L.3    Koken, M.H.4    de, T.H.5
  • 56
    • 0038521287 scopus 로고    scopus 로고
    • ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses
    • May 2
    • Espert L, Degols G, Gongora C, Blondel D, Williams BR, Silverman RH, et al. ISG20, a new interferon-induced RNase specific for single-stranded RNA, defines an alternative antiviral pathway against RNA genomic viruses. J Biol Chem 2003 May 2;278(18):16151-8.
    • (2003) J Biol Chem , vol.278 , Issue.18 , pp. 16151-16158
    • Espert, L.1    Degols, G.2    Gongora, C.3    Blondel, D.4    Williams, B.R.5    Silverman, R.H.6
  • 57
    • 0000237552 scopus 로고    scopus 로고
    • Role of PML in cell growth and the retinoic acid pathway
    • Mar 6
    • Wang ZG, Delva L, Gaboli M, Rivi R, Giorgio M, Cordon-Cardo C, et al. Role of PML in cell growth and the retinoic acid pathway. Science 1998 Mar 6;279(5356):1547-51.
    • (1998) Science , vol.279 , Issue.5356 , pp. 1547-1551
    • Wang, Z.G.1    Delva, L.2    Gaboli, M.3    Rivi, R.4    Giorgio, M.5    Cordon-Cardo, C.6
  • 58
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • Oct 29
    • Negorev D, Maul GG. Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 2001 Oct 29;20(49):7234-42.
    • (2001) Oncogene , vol.20 , Issue.49 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 59
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Jan 24
    • Boisvert FM, Hendzel MJ, Bazett-Jones DP. Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J Cell Biol 2000 Jan 24;148(2):283-92.
    • (2000) J Cell Biol , vol.148 , Issue.2 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 60
    • 1242329998 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions
    • Feb 16
    • Wang J, Shiels C, Sasieni P, Wu PJ, Islam SA, Freemont PS, et al. Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions. J Cell Biol 2004 Feb 16;164(4):515-26.
    • (2004) J Cell Biol , vol.164 , Issue.4 , pp. 515-526
    • Wang, J.1    Shiels, C.2    Sasieni, P.3    Wu, P.J.4    Islam, S.A.5    Freemont, P.S.6
  • 61
    • 2442704958 scopus 로고    scopus 로고
    • Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammalian cells
    • Oct
    • Kiesslich A, von MA, Hemmerich P. Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammalian cells. J Struct Biol 2002 Oct;140(1-3):167-79.
    • (2002) J Struct Biol , vol.140 , Issue.1-3 , pp. 167-179
    • Kiesslich, A.1    von, M.A.2    Hemmerich, P.3
  • 63
    • 0034669124 scopus 로고    scopus 로고
    • Regulation of p53 activity in nuclear bodies by a specific PML isoform
    • Nov 15
    • Fogal V, Gostissa M, Sandy P, Zacchi P, Sternsdorf T, Jensen K, et al. Regulation of p53 activity in nuclear bodies by a specific PML isoform. EMBO J 2000 Nov 15;19(22):6185-95.
    • (2000) Embo J , vol.19 , Issue.22 , pp. 6185-6195
    • Fogal, V.1    Gostissa, M.2    Sandy, P.3    Zacchi, P.4    Sternsdorf, T.5    Jensen, K.6
  • 64
    • 0142106346 scopus 로고    scopus 로고
    • Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization
    • Oct 1
    • Kurki S, Latonen L, Laiho M. Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization. J Cell Sci 2003 Oct 1;116(Pt 19):3917-25.
    • (2003) J Cell Sci , vol.116 , Issue.Pt 19 , pp. 3917-3925
    • Kurki, S.1    Latonen, L.2    Laiho, M.3
  • 65
    • 0034644274 scopus 로고    scopus 로고
    • PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
    • Jul 13
    • Pearson M, Carbone R, Sebastiani C, Cioce M, Fagioli M, Saito S, et al. PML regulates p53 acetylation and premature senescence induced by oncogenic Ras. Nature 2000 Jul 13;406(6792):207-10.
    • (2000) Nature , vol.406 , Issue.6792 , pp. 207-210
    • Pearson, M.1    Carbone, R.2    Sebastiani, C.3    Cioce, M.4    Fagioli, M.5    Saito, S.6
  • 66
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis
    • Dec 15
    • Szostecki C, Guldner HH, Netter HJ, Will H. Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J Immunol 1990 Dec 15;145(12):4338-47.
    • (1990) J Immunol , vol.145 , Issue.12 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3    Will, H.4
  • 67
    • 63849135037 scopus 로고    scopus 로고
    • PML nuclear bodies as sites of epigenetic regulation
    • Torok D, Ching RW, Bazett-Jones DP. PML nuclear bodies as sites of epigenetic regulation. Front Biosci 2009;14:1325-36.
    • (2009) Front Biosci , vol.14 , pp. 1325-1336
    • Torok, D.1    Ching, R.W.2    Bazett-Jones, D.P.3
  • 68
    • 2442678753 scopus 로고    scopus 로고
    • PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains
    • Aug 1
    • Moller A, Sirma H, Hofmann TG, Rueffer S, Klimczak E, Droge W, et al. PML is required for homeodomain-interacting protein kinase 2 (HIPK2)-mediated p53 phosphorylation and cell cycle arrest but is dispensable for the formation of HIPK domains. Cancer Res 2003 Aug 1;63(15):4310-4.
    • (2003) Cancer Res , vol.63 , Issue.15 , pp. 4310-4314
    • Moller, A.1    Sirma, H.2    Hofmann, T.G.3    Rueffer, S.4    Klimczak, E.5    Droge, W.6
  • 69
    • 33748747143 scopus 로고    scopus 로고
    • Promyelocytic leukemia activates Chk2 by mediating Chk2 autophosphorylation
    • Sep 8
    • Yang S, Jeong JH, Brown AL, Lee CH, Pandolfi PP, Chung JH, et al. Promyelocytic leukemia activates Chk2 by mediating Chk2 autophosphorylation. J Biol Chem 2006 Sep 8;281(36):26645-54.
    • (2006) J Biol Chem , vol.281 , Issue.36 , pp. 26645-26654
    • Yang, S.1    Jeong, J.H.2    Brown, A.L.3    Lee, C.H.4    Pandolfi, P.P.5    Chung, J.H.6
  • 70
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • May 15
    • Langley E, Pearson M, Faretta M, Bauer UM, Frye RA, Minucci S, et al. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J 2002 May 15;21(10):2383-96.
    • (2002) Embo J , vol.21 , Issue.10 , pp. 2383-2396
    • Langley, E.1    Pearson, M.2    Faretta, M.3    Bauer, U.M.4    Frye, R.A.5    Minucci, S.6
  • 75
    • 10744224197 scopus 로고    scopus 로고
    • Development of human protein reference database as an initial platform for approaching systems biology in humans
    • Oct
    • Peri S, Navarro JD, Amanchy R, Kristiansen TZ, Jonnalagadda CK, Surendranath V, et al. Development of human protein reference database as an initial platform for approaching systems biology in humans. Genome Res 2003 Oct;13(10):2363-71.
    • (2003) Genome Res , vol.13 , Issue.10 , pp. 2363-2371
    • Peri, S.1    Navarro, J.D.2    Amanchy, R.3    Kristiansen, T.Z.4    Jonnalagadda, C.K.5    Surendranath, V.6
  • 76
    • 0037255042 scopus 로고    scopus 로고
    • The Nuclear Protein Database (NPD): Sub-nuclear localisation and functional annotation of the nuclear proteome
    • Jan 1
    • Dellaire G, Farrall R, Bickmore WA. The Nuclear Protein Database (NPD): sub-nuclear localisation and functional annotation of the nuclear proteome. Nucleic Acids Res 2003 Jan 1;31(1):328-30.
    • (2003) Nucleic Acids Res , vol.31 , Issue.1 , pp. 328-330
    • Dellaire, G.1    Farrall, R.2    Bickmore, W.A.3
  • 77
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software environment for integrated models of biomolecular interaction networks
    • Nov
    • Shannon P, Markiel A, Ozier O, Baliga NS, Wang JT, Ramage D, et al. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res 2003 Nov;13(11):2498-504.
    • (2003) Genome Res , vol.13 , Issue.11 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4    Wang, J.T.5    Ramage, D.6
  • 78
    • 33751435209 scopus 로고    scopus 로고
    • Sander C. cPath: Open source software for collecting, storing, and querying biological pathways
    • Cerami EG, Bader GD, Gross BE, Sander C. cPath: open source software for collecting, storing, and querying biological pathways. BMC Bioinformatics 2006;7:497.
    • (2006) Bmc Bioinformatics , vol.7 , pp. 497
    • Cerami, E.G.1    Bader, G.D.2    Gross, B.E.3
  • 79
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • Sep 1
    • Yeager TR, Neumann AA, Englezou A, Huschtscha LI, Noble JR, Reddel RR. Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res 1999 Sep 1;59(17):4175-9.
    • (1999) Cancer Res , vol.59 , Issue.17 , pp. 4175-4179
    • Yeager, T.R.1    Neumann, A.A.2    Englezou, A.3    Huschtscha, L.I.4    Noble, J.R.5    Reddel, R.R.6
  • 80
    • 0034503110 scopus 로고    scopus 로고
    • ALT-associated PML bodies are present in viable cells and are enriched in cells in the G(2)/M phase of the cell cycle
    • Grobelny JV, Godwin AK, Broccoli D. ALT-associated PML bodies are present in viable cells and are enriched in cells in the G(2)/M phase of the cell cycle. J Cell Sci 2000;113 (Pt 24):4577-85.
    • (2000) J Cell Sci , vol.113 , Issue.Pt 24 , pp. 4577-4585
    • Grobelny, J.V.1    Godwin, A.K.2    Broccoli, D.3
  • 81
    • 0034730633 scopus 로고    scopus 로고
    • NBS1 and TRF1 colocalize at promyelocytic leukemia bodies during late S/G2 phases in immortalized telomerase-negative cells. Implication of NBS1 in alternative lengthening of telomeres
    • Sep 29
    • Wu G, Lee WH, Chen PL. NBS1 and TRF1 colocalize at promyelocytic leukemia bodies during late S/G2 phases in immortalized telomerase-negative cells. Implication of NBS1 in alternative lengthening of telomeres. J Biol Chem 2000 Sep 29;275(39):30618-22.
    • (2000) J Biol Chem , vol.275 , Issue.39 , pp. 30618-30622
    • Wu, G.1    Lee, W.H.2    Chen, P.L.3
  • 82
    • 0037843426 scopus 로고    scopus 로고
    • Assembly of functional ALT-associated promyelocytic leukemia bodies requires Nijmegen Breakage Syndrome 1
    • May 15
    • Wu G, Jiang X, Lee WH, Chen PL. Assembly of functional ALT-associated promyelocytic leukemia bodies requires Nijmegen Breakage Syndrome 1. Cancer Res 2003 May 15;63(10):2589-95.
    • (2003) Cancer Res , vol.63 , Issue.10 , pp. 2589-2595
    • Wu, G.1    Jiang, X.2    Lee, W.H.3    Chen, P.L.4
  • 83
    • 2942623564 scopus 로고    scopus 로고
    • Localization of hRad9, hHus1, hRad1, and hRad17 and caffeine-sensitive DNA replication at the alternative lengthening of telomeres-associated promyelocytic leukemia body
    • Jun 11
    • Nabetani A, Yokoyama O, Ishikawa F. Localization of hRad9, hHus1, hRad1, and hRad17 and caffeine-sensitive DNA replication at the alternative lengthening of telomeres-associated promyelocytic leukemia body. J Biol Chem 2004 Jun 11;279(24):25849-57.
    • (2004) J Biol Chem , vol.279 , Issue.24 , pp. 25849-25857
    • Nabetani, A.1    Yokoyama, O.2    Ishikawa, F.3
  • 84
    • 0034192363 scopus 로고    scopus 로고
    • Nijmegen breakage syndrome disease protein and MRE11 at PML nuclear bodies and meiotic telomeres
    • May 1
    • Lombard DB, Guarente L. Nijmegen breakage syndrome disease protein and MRE11 at PML nuclear bodies and meiotic telomeres. Cancer Res 2000 May 1;60(9):2331-4.
    • (2000) Cancer Res , vol.60 , Issue.9 , pp. 2331-2334
    • Lombard, D.B.1    Guarente, L.2
  • 85
    • 34447559500 scopus 로고    scopus 로고
    • Identification of candidate alternative lengthening of telomeres genes by methionine restriction and RNA interference
    • Jul 12
    • Jiang WQ, Zhong ZH, Henson JD, Reddel RR. Identification of candidate alternative lengthening of telomeres genes by methionine restriction and RNA interference. Oncogene 2007 Jul 12;26(32):4635-47.
    • (2007) Oncogene , vol.26 , Issue.32 , pp. 4635-4647
    • Jiang, W.Q.1    Zhong, Z.H.2    Henson, J.D.3    Reddel, R.R.4
  • 86
    • 36849003494 scopus 로고    scopus 로고
    • Lack of TRF2 in ALT cells causes PML-dependent p53 activation and loss of telomeric DNA
    • Dec 3
    • Stagno DM, Mendez-Bermudez A, Foxon JL, Royle NJ, Salomoni P. Lack of TRF2 in ALT cells causes PML-dependent p53 activation and loss of telomeric DNA. J Cell Biol 2007 Dec 3;179(5):855-67.
    • (2007) J Cell Biol , vol.179 , Issue.5 , pp. 855-867
    • Stagno, D.M.1    Mendez-Bermudez, A.2    Foxon, J.L.3    Royle, N.J.4    Salomoni, P.5
  • 89
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • Aug 15
    • Maere S, Heymans K, Kuiper M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 2005 Aug 15;21(16):3448-9.
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 90
    • 0037249501 scopus 로고    scopus 로고
    • PANTHER: A browsable database of gene products organized by biological function, using curated protein family and subfamily classification
    • Jan 1
    • Thomas PD, Kejariwal A, Campbell MJ, Mi H, Diemer K, Guo N, et al. PANTHER: a browsable database of gene products organized by biological function, using curated protein family and subfamily classification. Nucleic Acids Res 2003 Jan 1;31(1):334-41.
    • (2003) Nucleic Acids Res , vol.31 , Issue.1 , pp. 334-341
    • Thomas, P.D.1    Kejariwal, A.2    Campbell, M.J.3    Mi, H.4    Diemer, K.5    Guo, N.6
  • 91
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • Nov 1
    • Yang SH, Galanis A, Witty J, Sharrocks AD. An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J 2006 Nov 1;25(21):5083-93.
    • (2006) Embo J , vol.25 , Issue.21 , pp. 5083-5093
    • Yang, S.H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 93
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Nov
    • Tavalai N, Stamminger T. New insights into the role of the subnuclear structure ND10 for viral infection. Biochim Biophys Acta 2008 Nov;1783(11):2207-21.
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.11 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 94
    • 34250214907 scopus 로고    scopus 로고
    • SUMOrganization of the nucleus
    • Jun
    • Heun P. SUMOrganization of the nucleus. Curr Opin Cell Biol 2007 Jun;19(3):350-5.
    • (2007) Curr Opin Cell Biol , vol.19 , Issue.3 , pp. 350-355
    • Heun, P.1
  • 95
    • 0033925534 scopus 로고    scopus 로고
    • Review: Properties and assembly mechanisms of ND10, PML bodies, or PODs
    • Apr
    • Maul GG, Negorev D, Bell P, Ishov AM. Review: properties and assembly mechanisms of ND10, PML bodies, or PODs. J Struct Biol 2000 Apr;129(2-3):278-87.
    • (2000) J Struct Biol , vol.129 , Issue.2-3 , pp. 278-287
    • Maul, G.G.1    Negorev, D.2    Bell, P.3    Ishov, A.M.4
  • 96
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • Mar 5
    • Boisvert FM, Kruhlak MJ, Box AK, Hendzel MJ, Bazett-Jones DP. The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J Cell Biol 2001 Mar 5;152(5):1099-106.
    • (2001) J Cell Biol , vol.152 , Issue.5 , pp. 1099-1106
    • Boisvert, F.M.1    Kruhlak, M.J.2    Box, A.K.3    Hendzel, M.J.4    Bazett-Jones, D.P.5
  • 97
    • 31744447890 scopus 로고    scopus 로고
    • CGI-55 interacts with nuclear proteins and co-localizes to p80-coilin positive-coiled bodies in the nucleus
    • Lemos TA, Kobarg J. CGI-55 interacts with nuclear proteins and co-localizes to p80-coilin positive-coiled bodies in the nucleus. Cell Biochem Biophys 2006;44(3):463-74.
    • (2006) Cell Biochem Biophys , vol.44 , Issue.3 , pp. 463-474
    • Lemos, T.A.1    Kobarg, J.2
  • 98
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation
    • Feb
    • Duprez E, Saurin AJ, Desterro JM, Lallemand-Breitenbach V, Howe K, Boddy MN, et al. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J Cell Sci 1999 Feb;112 (Pt 3):381-93.
    • (1999) J Cell Sci , vol.112 , Issue.Pt 3 , pp. 381-393
    • Duprez, E.1    Saurin, A.J.2    Desterro, J.M.3    Lallemand-Breitenbach, V.4    Howe, K.5    Boddy, M.N.6
  • 100
    • 11444271001 scopus 로고    scopus 로고
    • Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection
    • Jan
    • Tatham MH, Kim S, Jaffray E, Song J, Chen Y, Hay RT. Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat Struct Mol Biol 2005 Jan;12(1):67-74.
    • (2005) Nat Struct Mol Biol , vol.12 , Issue.1 , pp. 67-74
    • Tatham, M.H.1    Kim, S.2    Jaffray, E.3    Song, J.4    Chen, Y.5    Hay, R.T.6
  • 101
    • 0036314919 scopus 로고    scopus 로고
    • The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies
    • Jul 15
    • Rasheed ZA, Saleem A, Ravee Y, Pandolfi PP, Rubin EH. The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies. Exp Cell Res 2002 Jul 15;277(2):152-60.
    • (2002) Exp Cell Res , vol.277 , Issue.2 , pp. 152-160
    • Rasheed, Z.A.1    Saleem, A.2    Ravee, Y.3    Pandolfi, P.P.4    Rubin, E.H.5
  • 102
    • 0038558190 scopus 로고    scopus 로고
    • Sumoylation is involved in beta-catenin-dependent activation of Tcf-4
    • May 1
    • Yamamoto H, Ihara M, Matsuura Y, Kikuchi A. Sumoylation is involved in beta-catenin-dependent activation of Tcf-4. EMBO J 2003 May 1;22(9):2047-59.
    • (2003) Embo J , vol.22 , Issue.9 , pp. 2047-2059
    • Yamamoto, H.1    Ihara, M.2    Matsuura, Y.3    Kikuchi, A.4
  • 103
    • 17644365783 scopus 로고    scopus 로고
    • SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4
    • May
    • Ihara M, Yamamoto H, Kikuchi A. SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4. Mol Cell Biol 2005 May;25(9):3506-18.
    • (2005) Mol Cell Biol , vol.25 , Issue.9 , pp. 3506-3518
    • Ihara, M.1    Yamamoto, H.2    Kikuchi, A.3
  • 104
    • 33646031179 scopus 로고    scopus 로고
    • In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies
    • May 1
    • Saitoh N, Uchimura Y, Tachibana T, Sugahara S, Saitoh H, Nakao M. In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp Cell Res 2006 May 1;312(8):1418-30.
    • (2006) Exp Cell Res , vol.312 , Issue.8 , pp. 1418-1430
    • Saitoh, N.1    Uchimura, Y.2    Tachibana, T.3    Sugahara, S.4    Saitoh, H.5    Nakao, M.6
  • 105
    • 51349091041 scopus 로고    scopus 로고
    • Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body formation
    • Sep
    • Gao C, Ho CC, Reineke E, Lam M, Cheng X, Stanya KJ, et al. Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body formation. Mol Cell Biol 2008 Sep;28(18):5658-67.
    • (2008) Mol Cell Biol , vol.28 , Issue.18 , pp. 5658-5667
    • Gao, C.1    Ho, C.C.2    Reineke, E.3    Lam, M.4    Cheng, X.5    Stanya, K.J.6
  • 106
    • 33646859205 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein stimulates SUMO conjugation in yeast
    • May 18
    • Quimby BB, Yong-Gonzalez V, Anan T, Strunnikov AV, Dasso M. The promyelocytic leukemia protein stimulates SUMO conjugation in yeast. Oncogene 2006 May 18;25(21):2999-3005.
    • (2006) Oncogene , vol.25 , Issue.21 , pp. 2999-3005
    • Quimby, B.B.1    Yong-Gonzalez, V.2    Anan, T.3    Strunnikov, A.V.4    Dasso, M.5
  • 108
    • 57749084642 scopus 로고    scopus 로고
    • PML, YAP, and p73 are components of a proapoptotic autoregulatory feedback loop
    • Dec 26
    • Lapi E, Di AS, Donzelli S, Gal H, Domany E, Rechavi G, et al. PML, YAP, and p73 are components of a proapoptotic autoregulatory feedback loop. Mol Cell 2008 Dec 26;32(6):803-14.
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 803-814
    • Lapi, E.1    Di, A.S.2    Donzelli, S.3    Gal, H.4    Domany, E.5    Rechavi, G.6
  • 109
    • 44149097785 scopus 로고    scopus 로고
    • The IL-6 family of cytokines modulates STAT3 activation by desumoylation of PML through SENP1 induction
    • Jul 11
    • Ohbayashi N, Kawakami S, Muromoto R, Togi S, Ikeda O, Kamitani S, et al. The IL-6 family of cytokines modulates STAT3 activation by desumoylation of PML through SENP1 induction. Biochem Biophys Res Commun 2008 Jul 11;371(4):823-8.
    • (2008) Biochem Biophys Res Commun , vol.371 , Issue.4 , pp. 823-828
    • Ohbayashi, N.1    Kawakami, S.2    Muromoto, R.3    Togi, S.4    Ikeda, O.5    Kamitani, S.6
  • 110
    • 52449102121 scopus 로고    scopus 로고
    • Repression of the SUMO-specific protease Senp1 induces p53-dependent premature senescence in normal human fibroblasts
    • Oct
    • Yates KE, Korbel GA, Shtutman M, Roninson IB, DiMaio D. Repression of the SUMO-specific protease Senp1 induces p53-dependent premature senescence in normal human fibroblasts. Aging Cell 2008 Oct;7(5):609-21.
    • (2008) Aging Cell , vol.7 , Issue.5 , pp. 609-621
    • Yates, K.E.1    Korbel, G.A.2    Shtutman, M.3    Roninson, I.B.4    Dimaio, D.5
  • 112
    • 57249105125 scopus 로고    scopus 로고
    • Prediction of kinase-specific phosphorylation sites using conditional random fields
    • Dec 15
    • Dang TH, Van LK, Verschoren A, Laukens K. Prediction of kinase-specific phosphorylation sites using conditional random fields. Bioinformatics 2008 Dec 15;24(24):2857-64.
    • (2008) Bioinformatics , vol.24 , Issue.24 , pp. 2857-2864
    • Dang, T.H.1    van, L.K.2    Verschoren, A.3    Laukens, K.4
  • 113
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • Sep 1
    • Gill G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev 2004 Sep 1;18(17):2046-59.
    • (2004) Genes Dev , vol.18 , Issue.17 , pp. 2046-2059
    • Gill, G.1
  • 114
    • 37749021009 scopus 로고    scopus 로고
    • A role for SUMO modification in transcriptional repression and activation
    • Dec
    • Lyst MJ, Stancheva I. A role for SUMO modification in transcriptional repression and activation. Biochem Soc Trans 2007 Dec;35(Pt 6):1389-92.
    • (2007) Biochem Soc Trans , vol.35 , Issue.Pt 6 , pp. 1389-1392
    • Lyst, M.J.1    Stancheva, I.2
  • 115
    • 33751212744 scopus 로고    scopus 로고
    • SUMO-specific proteases and the cell cycle. An essential role for SENP5 in cell proliferation
    • Oct
    • Di BA, Gill G. SUMO-specific proteases and the cell cycle. An essential role for SENP5 in cell proliferation. Cell Cycle 2006 Oct;5(20):2310-3.
    • (2006) Cell Cycle , vol.5 , Issue.20 , pp. 2310-2313
    • Di, B.A.1    Gill, G.2
  • 116
    • 63049131295 scopus 로고    scopus 로고
    • Regulation of p53 family members by the ubiquitin-like SUMO system
    • Apr 5
    • Stehmeier P, Muller S. Regulation of p53 family members by the ubiquitin-like SUMO system. DNA Repair (Amst) 2009 Apr 5;8(4):491-8.
    • (2009) Dna Repair (amst) , vol.8 , Issue.4 , pp. 491-498
    • Stehmeier, P.1    Muller, S.2
  • 117
    • 34047205692 scopus 로고    scopus 로고
    • SUMO is growing senescent
    • Mar 15
    • Bischof O, Dejean A. SUMO is growing senescent. Cell Cycle 2007 Mar 15;6(6):677-81.
    • (2007) Cell Cycle , vol.6 , Issue.6 , pp. 677-681
    • Bischof, O.1    Dejean, A.2
  • 118
    • 33746305530 scopus 로고    scopus 로고
    • Viruses and sumoylation: Recent highlights
    • Aug
    • Boggio R, Chiocca S. Viruses and sumoylation: recent highlights. Curr Opin Microbiol 2006 Aug;9(4):430-6.
    • (2006) Curr Opin Microbiol , vol.9 , Issue.4 , pp. 430-436
    • Boggio, R.1    Chiocca, S.2
  • 119
    • 0344299239 scopus 로고    scopus 로고
    • Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption
    • Jun
    • Muller S, Dejean A. Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. J Virol 1999 Jun;73(6):5137-43.
    • (1999) J Virol , vol.73 , Issue.6 , pp. 5137-5143
    • Muller, S.1    Dejean, A.2
  • 120
    • 0033779805 scopus 로고    scopus 로고
    • Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins
    • Nov
    • Parkinson J, Everett RD. Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins. J Virol 2000 Nov;74(21):10006-17.
    • (2000) J Virol , vol.74 , Issue.21 , pp. 10006-10017
    • Parkinson, J.1    Everett, R.D.2
  • 121
    • 44649135155 scopus 로고    scopus 로고
    • Regulation of the sumoylation system in gene expression
    • Jun
    • Liu B, Shuai K. Regulation of the sumoylation system in gene expression. Curr Opin Cell Biol 2008 Jun;20(3):288-93.
    • (2008) Curr Opin Cell Biol , vol.20 , Issue.3 , pp. 288-293
    • Liu, B.1    Shuai, K.2
  • 122
    • 37749031273 scopus 로고    scopus 로고
    • SUMO: Getting it on
    • Dec
    • Anckar J, Sistonen L. SUMO: getting it on. Biochem Soc Trans 2007 Dec;35(Pt 6):1409-13.
    • (2007) Biochem Soc Trans , vol.35 , Issue.Pt 6 , pp. 1409-1413
    • Anckar, J.1    Sistonen, L.2
  • 123
    • 66449131733 scopus 로고    scopus 로고
    • SUMO modification regulates the transcriptional repressor function of aryl hydrocarbon receptor repressor
    • Apr 24
    • Oshima M, Mimura J, Sekine H, Okawa H, Fujii-Kuriyama Y. SUMO modification regulates the transcriptional repressor function of aryl hydrocarbon receptor repressor. J Biol Chem 2009 Apr 24;284(17):11017-26.
    • (2009) J Biol Chem , vol.284 , Issue.17 , pp. 11017-11026
    • Oshima, M.1    Mimura, J.2    Sekine, H.3    Okawa, H.4    Fujii-Kuriyama, Y.5
  • 124
    • 38949088638 scopus 로고    scopus 로고
    • The mobility of Bach2 nuclear foci is regulated by SUMO-1 modification
    • Feb 15
    • Kono K, Harano Y, Hoshino H, Kobayashi M, Bazett-Jones DP, Muto A, et al. The mobility of Bach2 nuclear foci is regulated by SUMO-1 modification. Exp Cell Res 2008 Feb 15;314(4):903-13.
    • (2008) Exp Cell Res , vol.314 , Issue.4 , pp. 903-913
    • Kono, K.1    Harano, Y.2    Hoshino, H.3    Kobayashi, M.4    Bazett-Jones, D.P.5    Muto, A.6
  • 125
    • 28044437730 scopus 로고    scopus 로고
    • SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx
    • Nov 22
    • Kuo HY, Chang CC, Jeng JC, Hu HM, Lin DY, Maul GG, et al. SUMO modification negatively modulates the transcriptional activity of CREB-binding protein via the recruitment of Daxx. Proc Natl Acad Sci U S A 2005 Nov 22;102(47):16973-8.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.47 , pp. 16973-16978
    • Kuo, H.Y.1    Chang, C.C.2    Jeng, J.C.3    Hu, H.M.4    Lin, D.Y.5    Maul, G.G.6
  • 127
    • 0037088588 scopus 로고    scopus 로고
    • Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity
    • Mar 15;
    • Bies J, Markus J, Wolff L. Covalent attachment of the SUMO-1 protein to the negative regulatory domain of the c-Myb transcription factor modifies its stability and transactivation capacity. J Biol Chem 2002 Mar 15;277(11):8999-9009.
    • (2002) J Biol Chem , vol.277 , Issue.11 , pp. 8999-9009
    • Bies, J.1    Markus, J.2    Wolff, L.3
  • 128
    • 33750491062 scopus 로고    scopus 로고
    • Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors
    • Nov 3
    • Lin DY, Huang YS, Jeng JC, Kuo HY, Chang CC, Chao TT, et al. Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol Cell 2006 Nov 3;24(3):341-54.
    • (2006) Mol Cell , vol.24 , Issue.3 , pp. 341-354
    • Lin, D.Y.1    Huang, Y.S.2    Jeng, J.C.3    Kuo, H.Y.4    Chang, C.C.5    Chao, T.T.6
  • 129
    • 50549091334 scopus 로고    scopus 로고
    • The polycomb repressive complex 2 is a potential target of SUMO modifications
    • Riising EM, Boggio R, Chiocca S, Helin K, Pasini D. The polycomb repressive complex 2 is a potential target of SUMO modifications. PLoS ONE 2008;3(7):e2704.
    • (2008) Plos One , vol.3 , Issue.7
    • Riising, E.M.1    Boggio, R.2    Chiocca, S.3    Helin, K.4    Pasini, D.5
  • 130
    • 0038380273 scopus 로고    scopus 로고
    • Modification of GATA-2 transcriptional activity in endothelial cells by the SUMO E3 ligase PIASy
    • Jun 13
    • Chun TH, Itoh H, Subramanian L, Iniguez-Lluhi JA, Nakao K. Modification of GATA-2 transcriptional activity in endothelial cells by the SUMO E3 ligase PIASy. Circ Res 2003 Jun 13;92(11):1201-8.
    • (2003) Circ Res , vol.92 , Issue.11 , pp. 1201-1208
    • Chun, T.H.1    Itoh, H.2    Subramanian, L.3    Iniguez-Lluhi, J.A.4    Nakao, K.5
  • 131
    • 0037189568 scopus 로고    scopus 로고
    • SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
    • Jun 28
    • David G, Neptune MA, DePinho RA. SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities. J Biol Chem 2002 Jun 28;277(26):23658-63.
    • (2002) J Biol Chem , vol.277 , Issue.26 , pp. 23658-23663
    • David, G.1    Neptune, M.A.2    Depinho, R.A.3
  • 132
    • 40949111340 scopus 로고    scopus 로고
    • SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis
    • Apr
    • Li X, Luo Y, Yu L, Lin Y, Luo D, Zhang H, et al. SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis. Cell Death Differ 2008 Apr;15(4):739-50.
    • (2008) Cell Death Differ , vol.15 , Issue.4 , pp. 739-750
    • Li, X.1    Luo, Y.2    Yu, L.3    Lin, Y.4    Luo, D.5    Zhang, H.6
  • 133
    • 23844433285 scopus 로고    scopus 로고
    • Regulation of homeodomain-interacting protein kinase 2 (HIPK2) effector function through dynamic small ubiquitin-related modifier-1 (SUMO-1) modification
    • Aug 12
    • Hofmann TG, Jaffray E, Stollberg N, Hay RT, Will H. Regulation of homeodomain-interacting protein kinase 2 (HIPK2) effector function through dynamic small ubiquitin-related modifier-1 (SUMO-1) modification. J Biol Chem 2005 Aug 12;280(32):29224-32.
    • (2005) J Biol Chem , vol.280 , Issue.32 , pp. 29224-29232
    • Hofmann, T.G.1    Jaffray, E.2    Stollberg, N.3    Hay, R.T.4    Will, H.5
  • 134
    • 0035947677 scopus 로고    scopus 로고
    • Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor
    • May 25
    • Goodson ML, Hong Y, Rogers R, Matunis MJ, Park-Sarge OK, Sarge KD. Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factor. J Biol Chem 2001 May 25;276(21):18513-8.
    • (2001) J Biol Chem , vol.276 , Issue.21 , pp. 18513-18518
    • Goodson, M.L.1    Hong, Y.2    Rogers, R.3    Matunis, M.J.4    Park-Sarge, O.K.5    Sarge, K.D.6
  • 135
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • Dec 1
    • Sachdev S, Bruhn L, Sieber H, Pichler A, Melchior F, Grosschedl R. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev 2001 Dec 1;15(23):3088-103.
    • (2001) Genes Dev , vol.15 , Issue.23 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 137
    • 0037119457 scopus 로고    scopus 로고
    • The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1
    • Aug 16
    • Kotaja N, Karvonen U, Janne OA, Palvimo JJ. The nuclear receptor interaction domain of GRIP1 is modulated by covalent attachment of SUMO-1. J Biol Chem 2002 Aug 16;277(33):30283-8.
    • (2002) J Biol Chem , vol.277 , Issue.33 , pp. 30283-30288
    • Kotaja, N.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 138
    • 3142544806 scopus 로고    scopus 로고
    • Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1
    • Jul 2
    • Terui Y, Saad N, Jia S, McKeon F, Yuan J. Dual role of sumoylation in the nuclear localization and transcriptional activation of NFAT1. J Biol Chem 2004 Jul 2;279(27):28257-65.
    • (2004) J Biol Chem , vol.279 , Issue.27 , pp. 28257-28265
    • Terui, Y.1    Saad, N.2    Jia, S.3    McKeon, F.4    Yuan, J.5
  • 139
    • 58149149885 scopus 로고    scopus 로고
    • Liver receptor homolog-1 localization in the nuclear body is regulated by sumoylation and cAMP signaling in rat granulosa cells
    • Jan
    • Yang FM, Pan CT, Tsai HM, Chiu TW, Wu ML, Hu MC. Liver receptor homolog-1 localization in the nuclear body is regulated by sumoylation and cAMP signaling in rat granulosa cells. FEBS J 2009 Jan;276(2):425-36.
    • (2009) Febs J , vol.276 , Issue.2 , pp. 425-436
    • Yang, F.M.1    Pan, C.T.2    Tsai, H.M.3    Chiu, T.W.4    Wu, M.L.5    Hu, M.C.6
  • 140
    • 17644407601 scopus 로고    scopus 로고
    • The protein stability and transcriptional activity of p63alpha are regulated by SUMO-1 conjugation
    • Jan
    • Ghioni P, D'Alessandra Y, Mansueto G, Jaffray E, Hay RT, La MG, et al. The protein stability and transcriptional activity of p63alpha are regulated by SUMO-1 conjugation. Cell Cycle 2005 Jan;4(1):183-90.
    • (2005) Cell Cycle , vol.4 , Issue.1 , pp. 183-190
    • Ghioni, P.1    D'alessandra, Y.2    Mansueto, G.3    Jaffray, E.4    Hay, R.T.5    la, M.G.6
  • 141
    • 34248595692 scopus 로고    scopus 로고
    • SUMO modification modulates the transrepression activity of PLZF
    • Jun 29
    • Chao TT, Chang CC, Shih HM. SUMO modification modulates the transrepression activity of PLZF. Biochem Biophys Res Commun 2007 Jun 29;358(2):475-82.
    • (2007) Biochem Biophys Res Commun , vol.358 , Issue.2 , pp. 475-482
    • Chao, T.T.1    Chang, C.C.2    Shih, H.M.3
  • 142
    • 33644557129 scopus 로고    scopus 로고
    • RBP1 family proteins exhibit SUMOylation-dependent transcriptional repression and induce cell growth inhibition reminiscent of senescence
    • Mar
    • Binda O, Roy JS, Branton PE. RBP1 family proteins exhibit SUMOylation-dependent transcriptional repression and induce cell growth inhibition reminiscent of senescence. Mol Cell Biol 2006 Mar;26(5):1917-31.
    • (2006) Mol Cell Biol , vol.26 , Issue.5 , pp. 1917-1931
    • Binda, O.1    Roy, J.S.2    Branton, P.E.3
  • 143
    • 22144482659 scopus 로고    scopus 로고
    • PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein
    • Aug 1
    • Matsuura T, Shimono Y, Kawai K, Murakami H, Urano T, Niwa Y, et al. PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein. Exp Cell Res 2005 Aug 1;308(1):65-77.
    • (2005) Exp Cell Res , vol.308 , Issue.1 , pp. 65-77
    • Matsuura, T.1    Shimono, Y.2    Kawai, K.3    Murakami, H.4    Urano, T.5    Niwa, Y.6
  • 144
    • 49649100923 scopus 로고    scopus 로고
    • SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage
    • Jun 27
    • Tan JA, Sun Y, Song J, Chen Y, Krontiris TG, Durrin LK. SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage. J Biol Chem 2008 Jun 27;283(26):18124-34.
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 18124-18134
    • Tan, J.A.1    Sun, Y.2    Song, J.3    Chen, Y.4    Krontiris, T.G.5    Durrin, L.K.6
  • 145
    • 67749145683 scopus 로고    scopus 로고
    • SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation
    • Jul 17
    • Cho G, Lim Y, Golden JA. SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation. J Biol Chem 2009 Jul 17;284(29):19592-600.
    • (2009) J Biol Chem , vol.284 , Issue.29 , pp. 19592-19600
    • Cho, G.1    Lim, Y.2    Golden, J.A.3
  • 146
    • 42249101377 scopus 로고    scopus 로고
    • Sumoylation of Smad3 stimulates its nuclear export during PIASy-mediated suppression of TGF-beta signaling
    • May 30
    • Imoto S, Ohbayashi N, Ikeda O, Kamitani S, Muromoto R, Sekine Y, et al. Sumoylation of Smad3 stimulates its nuclear export during PIASy-mediated suppression of TGF-beta signaling. Biochem Biophys Res Commun 2008 May 30;370(2):359-65.
    • (2008) Biochem Biophys Res Commun , vol.370 , Issue.2 , pp. 359-365
    • Imoto, S.1    Ohbayashi, N.2    Ikeda, O.3    Kamitani, S.4    Muromoto, R.5    Sekine, Y.6
  • 147
    • 33646838989 scopus 로고    scopus 로고
    • Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription
    • Mar 3
    • Spengler ML, Brattain MG. Sumoylation inhibits cleavage of Sp1 N-terminal negative regulatory domain and inhibits Sp1-dependent transcription. J Biol Chem 2006 Mar 3;281(9):5567-74.
    • (2006) J Biol Chem , vol.281 , Issue.9 , pp. 5567-5574
    • Spengler, M.L.1    Brattain, M.G.2
  • 149
    • 38949206260 scopus 로고    scopus 로고
    • Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response
    • Feb 7
    • Cheng Z, Ke Y, Ding X, Wang F, Wang H, Wang W, et al. Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response. Oncogene 2008 Feb 7;27(7):931-41.
    • (2008) Oncogene , vol.27 , Issue.7 , pp. 931-941
    • Cheng, Z.1    Ke, Y.2    Ding, X.3    Wang, F.4    Wang, H.5    Wang, W.6
  • 150
    • 49649090416 scopus 로고    scopus 로고
    • Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression
    • Aug 12
    • Gupta P, Ho PC, Huq MM, Ha SG, Park SW, Khan AA, et al. Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression. Proc Natl Acad Sci U S A 2008 Aug 12;105(32):11424-9.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.32 , pp. 11424-11429
    • Gupta, P.1    Ho, P.C.2    Huq, M.M.3    Ha, S.G.4    Park, S.W.5    Khan, A.A.6
  • 151
    • 33750414820 scopus 로고    scopus 로고
    • ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML
    • Nov 15
    • Kunapuli P, Kasyapa CS, Chin SF, Caldas C, Cowell JK. ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML. Exp Cell Res 2006 Nov 15;312(19):3739-51.
    • (2006) Exp Cell Res , vol.312 , Issue.19 , pp. 3739-3751
    • Kunapuli, P.1    Kasyapa, C.S.2    Chin, S.F.3    Caldas, C.4    Cowell, J.K.5
  • 152
    • 50149112651 scopus 로고    scopus 로고
    • ZNF451 is a novel PML body- and SUMO-associated transcriptional coregulator
    • Oct 10
    • Karvonen U, Jaaskelainen T, Rytinki M, Kaikkonen S, Palvimo JJ. ZNF451 is a novel PML body- and SUMO-associated transcriptional coregulator. J Mol Biol 2008 Oct 10;382(3):585-600.
    • (2008) J Mol Biol , vol.382 , Issue.3 , pp. 585-600
    • Karvonen, U.1    Jaaskelainen, T.2    Rytinki, M.3    Kaikkonen, S.4    Palvimo, J.J.5


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