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Volumn 14, Issue 3, 2009, Pages 1182-1196

PML nuclear bodies and their spatial relationships in the mammalian cell nucleus

Author keywords

Centromeres; Chromatin; Co localization; DNA damage; DNA replication; Immunofluorescence; Interferon; Mammalian nucleus; MHC; Nuclear architecture; Nuclear compartments; Nuclear organization; Nucleoli; PML; PML nuclear bodies; PML nuclear body function; Proteolysis; Review; Spatial associations; Spatial organization; Spatial relationships; Stress; Telomeres; Transcription; Viral response

Indexed keywords

MAMMALIA;

EID: 63849135038     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3302     Document Type: Article
Times cited : (17)

References (105)
  • 1
    • 33645731002 scopus 로고    scopus 로고
    • The number of PML nuclear bodies increases in early S phase by a fission mechanism
    • Dellaire, G., R. W. Ching, H. Dehghani, Y. Ren & D. P. Bazett-Jones: The number of PML nuclear bodies increases in early S phase by a fission mechanism. J Cell Sci, 119, 1026-33 (2006).
    • (2006) J Cell Sci , vol.119 , pp. 1026-1033
    • Dellaire, G.1    Ching, R.W.2    Dehghani, H.3    Ren, Y.4    Bazett-Jones, D.P.5
  • 4
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • DOI 10.1038/sj.onc.1204765
    • Jensen, K., C. Shiels & P. S. Freemont: PML protein isoforms and the RBCC/TRIM motif. Oncogene, 20, 7223- 33 (2001). (Pubitemid 33105011)
    • (2001) Oncogene , vol.20 , Issue.49 REV. IIS. 6 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 6
    • 34447116912 scopus 로고    scopus 로고
    • New insights into the cytoplasmic function of PML
    • Salomoni, P. & C. Bellodi: New insights into the cytoplasmic function of PML. Histol Histopathol, 22, 937- 46 (2007). (Pubitemid 47034159)
    • (2007) Histology and Histopathology , vol.22 , Issue.7-9 , pp. 937-946
    • Salomoni, P.1    Bellodi, C.2
  • 9
    • 33750447586 scopus 로고    scopus 로고
    • The Mechanisms of PML-Nuclear Body Formation
    • DOI 10.1016/j.molcel.2006.09.013, PII S1097276506006617
    • Shen, T. H., H. K. Lin, P. P. Scaglioni, T. M. Yung & P. P. Pandolfi: The mechanisms of PML-nuclear body formation. Mol Cell, 24, 331-9 (2006). (Pubitemid 44647906)
    • (2006) Molecular Cell , vol.24 , Issue.3 , pp. 331-339
    • Shen, T.H.1    Lin, H.-K.2    Scaglioni, P.P.3    Yung, T.M.4    Pandolfi, P.P.5
  • 10
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • DOI 10.1038/nrm2277, PII NRM2277
    • Bernardi, R. & P. P. Pandolfi: Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol, 8, 1006-16 (2007). (Pubitemid 350174636)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.12 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 11
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • DOI 10.1093/emboj/17.1.61
    • Muller, S., M. J. Matunis & A. Dejean: Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. Embo J, 17, 61-70 (1998). (Pubitemid 28041048)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 61-70
    • Muller, S.1    Matunis, M.J.2    Dejean, A.3
  • 13
    • 0032574737 scopus 로고    scopus 로고
    • Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body
    • LaMorte, V. J., J. A. Dyck, R. L. Ochs & R. M. Evans: Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body. Proc Natl Acad Sci U S A, 95, 4991-6 (1998).
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4991-4996
    • LaMorte, V.J.1    Dyck, J.A.2    Ochs, R.L.3    Evans, R.M.4
  • 15
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1
    • DOI 10.1083/jcb.139.7.1621
    • Sternsdorf, T., K. Jensen & H. Will: Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1. J Cell Biol, 139, 1621-34 (1997). (Pubitemid 28079228)
    • (1997) Journal of Cell Biology , vol.139 , Issue.7 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 16
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • DOI 10.1016/0092-8674(94)90340-9
    • Dyck, J. A., G. G. Maul, W. H. Miller Jr., J. D. Chen, A. Kakizuka & R. M. Evans: A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell, 76, 333-43 (1994). (Pubitemid 24046695)
    • (1994) Cell , vol.76 , Issue.2 , 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
  • 18
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells
    • DOI 10.1016/0092-8674(94)90341-7
    • Weis, K., S. Rambaud, C. Lavau, J. Jansen, T. Carvalho, M. Carmo-Fonseca, A. Lamond & A. Dejean: Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell, 76, 345-56 (1994). (Pubitemid 24046696)
    • (1994) Cell , vol.76 , Issue.2 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejeant, A.8
  • 19
    • 0025875679 scopus 로고
    • The PML-RARα fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The, H., C. Lavau, A. Marchio, C. Chomienne, L. Degos & A. Dejean: The PML-RAR alpha fusion mRNA generated by the t (15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell, 66, 675-84 (1991). (Pubitemid 121001703)
    • (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
  • 20
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML
    • Kakizuka, A., W. H. Miller Jr., K. Umesono, R. P. Warrell Jr., S. R. Frankel, V. V. Murty, E. Dmitrovsky & R. M. Evans: Chromosomal translocation t (15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML. Cell, 66, 663-74 (1991). (Pubitemid 121001702)
    • (1991) Cell , vol.66 , Issue.4 , 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.V.S.6    Dmitrovsky, E.7    Evans, R.M.8
  • 21
    • 0025917413 scopus 로고
    • Structure and origin of the acute promyelocytic leukemia myl/RARα cDNA and characterization of its retinoid-binding and transactivation properties
    • Pandolfi, P. P., F. Grignani, M. Alcalay, A. Mencarelli, A. Biondi, F. LoCoco, F. Grignani & P. G. Pelicci: Structure and origin of the acute promyelocytic leukemia myl/RAR alpha cDNA and characterization of its retinoid-binding and transactivation properties. Oncogene, 6, 1285-92 (1991). (Pubitemid 21924220)
    • (1991) Oncogene , vol.6 , Issue.7 , pp. 1285-1292
    • Pandolfi, P.P.1    Grignani, F.2    Alcalay, M.3    Mencarelli, A.4    Biondi, A.5    LoCoco, F.6    Grignani, F.7    Pelicci, P.G.8
  • 22
    • 0026326963 scopus 로고
    • Characterization of a zinc finger gene disrupted by the t(15;17) in acute promyelocytic leukemia
    • Goddard, A. D., J. Borrow, P. S. Freemont & E. Solomon: Characterization of a zinc finger gene disrupted by the t (15;17) in acute promyelocytic leukemia. Science, 254, 1371-4 (1991). (Pubitemid 21917471)
    • (1991) Science , vol.254 , Issue.5036 , pp. 1371-1374
    • Goddard, A.D.1    Borrow, J.2    Freemont, P.S.3    Solomon, E.4
  • 23
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: Possible functions for PML nuclear bodies
    • DOI 10.1128/MCB.22.15.5259-5269.2002
    • Borden, K. L.: Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies. Mol Cell Biol, 22, 5259-69 (2002). (Pubitemid 34755740)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.15 , pp. 5259-5269
    • Borden, K.L.B.1
  • 24
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • DOI 10.1016/S0092-8674(02)00626-8
    • Salomoni, P. & P. P. Pandolfi: The role of PML in tumor suppression. Cell, 108, 165-70 (2002). (Pubitemid 34161137)
    • (2002) Cell , vol.108 , Issue.2 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 25
    • 2442711599 scopus 로고    scopus 로고
    • PML nuclear bodies and apoptosis
    • DOI 10.1038/sj.onc.1207533
    • Takahashi, Y., V. Lallemand-Breitenbach, J. Zhu & H. de The: PML nuclear bodies and apoptosis. Oncogene, 23, 2819- 24 (2004). (Pubitemid 38659528)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2819-2824
    • Takahashi, Y.1    Lallemand-Breitenbach, V.2    Zhu, J.3    De The, H.4
  • 26
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • DOI 10.1002/bies.20089
    • Dellaire, G. & D. P. Bazett-Jones: PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays, 26, 963-77 (2004). (Pubitemid 39273070)
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 27
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong, S., P. Salomoni & P. P. Pandolfi: The transcriptional role of PML and the nuclear body. Nat Cell Biol, 2, E85-90 (2000).
    • (2000) Nat Cell Biol , vol.2
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3
  • 28
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: Implications in antiviral defence
    • DOI 10.1016/j.biochi.2007.01.004, PII S0300908407000132
    • Everett, R. D. & M. K. Chelbi-Alix: PML and PML nuclear bodies: implications in antiviral defence. Biochimie, 89, 819-30 (2007). (Pubitemid 47008945)
    • (2007) Biochimie , vol.89 , Issue.6-7 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 29
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • DOI 10.1038/sj.onc.1204764
    • Negorev, D. & G. G. Maul: Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene, 20, 7234- 42 (2001). (Pubitemid 33105012)
    • (2001) Oncogene , vol.20 , Issue.49 REV. IIS. 6 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 30
    • 2142718452 scopus 로고    scopus 로고
    • Spatial genome organization
    • DOI 10.1016/j.yexcr.2004.03.013, PII S0014482704001296
    • Parada, L. A., S. Sotiriou & T. Misteli: Spatial genome organization. Exp Cell Res, 296, 64-70 (2004). (Pubitemid 38543214)
    • (2004) Experimental Cell Research , vol.296 , Issue.1 , pp. 64-70
    • Parada, L.A.1    Sotiriou, S.2    Misteli, T.3
  • 31
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • DOI 10.1083/jcb.200108110
    • Misteli, T.: The concept of self-organization in cellular architecture. J Cell Biol, 155, 181-5 (2001). (Pubitemid 34289292)
    • (2001) Journal of Cell Biology , vol.155 , Issue.2 , pp. 181-185
    • Misteli, T.1
  • 32
    • 0035365808 scopus 로고    scopus 로고
    • Functional architecture in the cell nucleus
    • DOI 10.1042/0264-6021:3560297
    • Dundr, M. & T. Misteli: Functional architecture in the cell nucleus. Biochem J, 356, 297-310 (2001). (Pubitemid 32532339)
    • (2001) Biochemical Journal , vol.356 , Issue.2 , pp. 297-310
    • Dundr, M.1    Misteli, T.2
  • 33
    • 9444257007 scopus 로고    scopus 로고
    • Internal organisation of the nucleus: Assembly of compartments by macromolecular crowding and the nuclear matrix model
    • DOI 10.1016/j.biolcel.2004.05.003, PII S0248490004001236, Functional Architecture of the Cell Nucleus
    • Hancock, R.: Internal organisation of the nucleus: assembly of compartments by macromolecular crowding and the nuclear matrix model. Biol Cell, 96, 595-601 (2004). (Pubitemid 39562234)
    • (2004) Biology of the Cell , vol.96 , Issue.8 , pp. 595-601
    • Hancock, R.1
  • 34
    • 0034888077 scopus 로고    scopus 로고
    • CBP, a transcriptional coactivator and acetyltransferase
    • DOI 10.1139/bcb-79-3-253
    • McManus, K. J. & M. J. Hendzel: CBP, a transcriptional coactivator and acetyltransferase. Biochem Cell Biol, 79, 253-66 (2001). (Pubitemid 32751918)
    • (2001) Biochemistry and Cell Biology , vol.79 , Issue.3 , pp. 253-266
    • McManus, K.J.1    Hendzel, M.J.2
  • 35
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis
    • Szostecki, C., H. H. Guldner, H. J. Netter & H. Will: Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis. J Immunol, 145, 4338-47 (1990).
    • (1990) J Immunol , vol.145 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3    Will, H.4
  • 36
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy, M. N., K. Howe, L. D. Etkin, E. Solomon & P. S. Freemont: PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene, 13, 971-82 (1996). (Pubitemid 26329084)
    • (1996) Oncogene , vol.13 , Issue.5 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 37
    • 0035809924 scopus 로고    scopus 로고
    • The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body
    • DOI 10.1083/jcb.152.5.1099
    • Boisvert, F. M., M. J. Kruhlak, A. K. Box, M. J. Hendzel & D. P. Bazett-Jones: The transcription coactivator CBP is a dynamic component of the promyelocytic leukemia nuclear body. J Cell Biol, 152, 1099-106 (2001). (Pubitemid 34286084)
    • (2001) Journal of Cell Biology , 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
  • 38
    • 0033952527 scopus 로고    scopus 로고
    • Sequestration and inhibition of Daxx-mediated transcriptional repression by PML
    • DOI 10.1128/MCB.20.5.1784-1796.2000
    • Li,H., C. Leo, J. Zhu, X. Wu, J. O'Neil, E. J. Park & J. D. Chen: Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol Cell Biol, 20, 1784- 96 (2000). (Pubitemid 30100196)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.5 , pp. 1784-1796
    • Li, H.1    Leo, C.2    Zhu, J.3    Wu, X.4    O'Neil, J.5    Park, E.-J.6    Chen, J.D.7
  • 43
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf, T., K. Jensen, B. Reich & H. Will: The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J Biol Chem, 274, 12555-66 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 46
    • 33845871732 scopus 로고    scopus 로고
    • Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus
    • DOI 10.1038/ncb1516, PII NCB1516
    • Kumar, P. P., O. Bischof, P. K. Purbey, D. Notani, H. Urlaub, A. Dejean & S. Galande: Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus. Nat Cell Biol, 9, 45-56 (2007). (Pubitemid 46024196)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 45-56
    • Pavan Kumar, P.1    Bischof, O.2    Purbey, P.K.3    Notani, D.4    Urlaub, H.5    Dejean, A.6    Galande, S.7
  • 47
    • 0036516869 scopus 로고    scopus 로고
    • The emerging roles of translation factor eIF4E in the nucleus
    • DOI 10.1046/j.1432-0436.2002.700102.x
    • Strudwick, S. & K. L. Borden: The emerging roles of translation factor eIF4E in the nucleus. Differentiation, 70, 10-22 (2002). (Pubitemid 38232695)
    • (2002) Differentiation , vol.70 , Issue.1 , pp. 10-22
    • Strudwick, S.1    Borden, K.L.B.2
  • 48
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap
    • Lazaris-Karatzas, A., K. S. Montine & N. Sonenberg: Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap. Nature, 345, 544-7 (1990).
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 49
    • 0035881526 scopus 로고    scopus 로고
    • PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA
    • DOI 10.1093/emboj/20.16.4547
    • Cohen, N., M. Sharma, A. Kentsis, J. M. Perez, S. Strudwick & K. L. Borden: PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA. Embo J, 20, 4547-59 (2001). (Pubitemid 32772048)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4547-4559
    • Cohen, N.1    Sharma, M.2    Kentsis, A.3    Perez, J.M.4    Strudwick, S.5    Borden, K.L.B.6
  • 54
    • 34248561147 scopus 로고    scopus 로고
    • Cajal body number and nucleolar size correlate with the cell body mass in human sensory ganglia neurons
    • DOI 10.1016/j.jsb.2006.12.008, PII S1047847706003959
    • Berciano, M. T., M. Novell, N. T. Villagra, I. Casafont, R. Bengoechea, J. F. Val-Bernal & M. Lafarga: Cajal body number and nucleolar size correlate with the cell body mass in human sensory ganglia neurons. J Struct Biol, 158, 410- 20 (2007). (Pubitemid 46764568)
    • (2007) Journal of Structural Biology , vol.158 , Issue.3 , pp. 410-420
    • Berciano, M.T.1    Novell, M.2    Villagra, N.T.3    Casafont, I.4    Bengoechea, R.5    Val-Bernal, J.F.6    Lafarga, M.7
  • 55
    • 27944450063 scopus 로고    scopus 로고
    • Interactions between coilin and PIASy partially link Cajal bodies to PML bodies
    • DOI 10.1242/jcs.02613
    • Sun, J., H. Xu, S. H. Subramony & M. D. Hebert: Interactions between coilin and PIASy partially link Cajal bodies to PML bodies. J Cell Sci, 118, 4995-5003 (2005). (Pubitemid 41672431)
    • (2005) Journal of Cell Science , vol.118 , Issue.21 , pp. 4995-5003
    • Sun, J.1    Xu, H.2    Subramony, S.H.3    Hebert, M.D.4
  • 57
    • 2442704958 scopus 로고    scopus 로고
    • Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammalian cells
    • DOI 10.1016/S1047-8477(02)00571-3, PII S1047847702005713
    • Kiesslich, A., A. von Mikecz & P. Hemmerich: Cell cycle-dependent association of PML bodies with sites of active transcription in nuclei of mammalian cells. J Struct Biol, 140, 167-79 (2002). (Pubitemid 36139858)
    • (2002) Journal of Structural Biology , vol.140 , Issue.1-3 , pp. 167-179
    • Kiesslich, A.1    Von Mikecz, A.2    Hemmerich, P.3
  • 58
    • 0034631852 scopus 로고    scopus 로고
    • CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus
    • DOI 10.1083/jcb.150.1.265
    • von Mikecz, A., S. Zhang, M. Montminy, E. M. Tan & P. Hemmerich: CREB-binding protein (CBP)/p300 and RNA polymerase II colocalize in transcriptionally active domains in the nucleus. J Cell Biol, 150, 265-73 (2000). (Pubitemid 30480242)
    • (2000) Journal of Cell Biology , vol.150 , Issue.1 , pp. 265-273
    • Von Mikecz, A.1    Zhang, S.2    Montminy, M.3    Tan, E.M.4    Hemmerich, P.5
  • 59
    • 30044435209 scopus 로고    scopus 로고
    • Distribution of different phosphorylated forms of RNA polymerase II in relation to Cajal and PML bodies in human cells: An ultrastructural study
    • DOI 10.1007/s00418-005-0064-2
    • Xie, S. Q. & A. Pombo: Distribution of different phosphorylated forms of RNA polymerase II in relation to Cajal and PML bodies in human cells: an ultrastructural study. Histochem Cell Biol, 125, 21-31 (2006). (Pubitemid 43049969)
    • (2006) Histochemistry and Cell Biology , vol.125 , Issue.1-2 , pp. 21-31
    • Xie, S.Q.1    Pombo, A.2
  • 60
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • DOI 10.1083/jcb.148.2.283
    • Boisvert, F. M., M. J. Hendzel & D. P. Bazett-Jones: Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA. J Cell Biol, 148, 283-92 (2000). (Pubitemid 30078240)
    • (2000) Journal of Cell Biology , vol.148 , Issue.2 , pp. 283-292
    • Boisvert, F.-M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 61
    • 1242329998 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions
    • DOI 10.1083/jcb.200305142
    • Wang, J., C. Shiels, P. Sasieni, P. J. Wu, S. A. Islam, P. S. Freemont & D. Sheer: Promyelocytic leukemia nuclear bodies associate with transcriptionally active genomic regions. J Cell Biol, 164, 515-26 (2004). (Pubitemid 38233313)
    • (2004) Journal of Cell Biology , 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    Sheer, D.7
  • 62
    • 29244480602 scopus 로고    scopus 로고
    • Proteasomes degrade proteins in focal subdomains of the human cell nucleus
    • DOI 10.1242/jcs.02642
    • Rockel, T. D., D. Stuhlmann & A. von Mikecz: Proteasomes degrade proteins in focal subdomains of the human cell nucleus. J Cell Sci, 118, 5231-42 (2005). (Pubitemid 41819586)
    • (2005) Journal of Cell Science , vol.118 , Issue.22 , pp. 5231-5242
    • Rockel, T.D.1    Stuhlmann, D.2    Von Mikecz, A.3
  • 63
    • 33745192054 scopus 로고    scopus 로고
    • The nuclear ubiquitin-proteasome system
    • von Mikecz, A.: The nuclear ubiquitin-proteasome system. J Cell Sci, 119, 1977-84 (2006).
    • (2006) J Cell Sci , vol.119 , pp. 1977-1984
    • Von Mikecz, A.1
  • 64
    • 34648843213 scopus 로고    scopus 로고
    • How telomeres are replicated
    • DOI 10.1038/nrm2259, PII NRM2259
    • Gilson, E. & V. Geli: How telomeres are replicated. Nat Rev Mol Cell Biol, 8, 825-38 (2007). (Pubitemid 47462137)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 825-838
    • Gilson, E.1    Geli, V.2
  • 65
    • 34548667973 scopus 로고    scopus 로고
    • Telomere length, stem cells and aging
    • DOI 10.1038/nchembio.2007.38, PII NCHEMBIO200738
    • Blasco, M. A.: Telomere length, stem cells and aging. Nat Chem Biol, 3, 640-9 (2007). (Pubitemid 47417712)
    • (2007) Nature Chemical Biology , vol.3 , Issue.10 , pp. 640-649
    • Blasco, M.A.1
  • 66
    • 0030697342 scopus 로고    scopus 로고
    • Evidence for an alternative mechanism for maintaining telomere length in human tumors and tumor-derived cell lines
    • Bryan, T. M., A. Englezou, L. Dalla-Pozza, M. A. Dunham & R. R. Reddel: Evidence for an alternative mechanism for maintaining telomere length in human tumors and tumor-derived cell lines. Nat Med, 3, 1271-4 (1997). (Pubitemid 27508830)
    • (1997) Nature Medicine , vol.3 , Issue.11 , pp. 1271-1274
    • Bryan, T.M.1    Englezou, A.2    Dalla-Pozza, L.3    Dunham, M.A.4    Reddel, R.R.5
  • 67
    • 0033672470 scopus 로고    scopus 로고
    • Telomere maintenance by recombination in human cells
    • Dunham, M. A., A. A. Neumann, C. L. Fasching & R. R. Reddel: Telomere maintenance by recombination in human cells. Nat Genet, 26, 447-50 (2000).
    • (2000) Nat Genet , vol.26 , pp. 447-450
    • Dunham, M.A.1    Neumann, A.A.2    Fasching, C.L.3    Reddel, R.R.4
  • 68
    • 0033199695 scopus 로고    scopus 로고
    • Telomerase-negative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body
    • Yeager, T. R., A. A. Neumann, A. Englezou, L. I. Huschtscha, J. R. Noble & R. R. Reddel: Telomerasenegative immortalized human cells contain a novel type of promyelocytic leukemia (PML) body. Cancer Res, 59, 4175-9 (1999). (Pubitemid 29418720)
    • (1999) Cancer Research , 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
  • 69
    • 0037148281 scopus 로고    scopus 로고
    • Alternative lengthening of telomeres in mammalian cells
    • DOI 10.1038/sj/onc/1205058
    • Henson, J. D., A. A. Neumann, T. R. Yeager & R. R. Reddel: Alternative lengthening of telomeres in mammalian cells. Oncogene, 21, 598-610 (2002). (Pubitemid 34146260)
    • (2002) Oncogene , vol.21 , Issue.4 REV. ISS. 1 , pp. 598-610
    • Henson, J.D.1    Neumann, A.A.2    Yeager, T.R.3    Reddel, R.R.4
  • 70
    • 34447129654 scopus 로고    scopus 로고
    • The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins
    • DOI 10.1038/nsmb1259, PII NSMB1259
    • Potts, P. R. & H. Yu: The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nat Struct Mol Biol, 14, 581-90 (2007). (Pubitemid 47037066)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.7 , pp. 581-590
    • Potts, P.R.1    Yu, H.2
  • 71
    • 34249305793 scopus 로고    scopus 로고
    • Nuclear phospholipase C gamma: Punctate distribution and association with the promyelocyte leukemia protein
    • DOI 10.1021/pr060684v
    • Ferguson, B. J., C. L. Dovey, K. Lilley, A. H. Wyllie & T. Rich: Nuclear phospholipase C gamma: punctate distribution and association with the promyelocytic leukemia protein. J Proteome Res, 6, 2027-32 (2007). (Pubitemid 46814524)
    • (2007) Journal of Proteome Research , vol.6 , Issue.5 , pp. 2027-2032
    • Ferguson, B.J.1    Dovey, C.L.2    Lilley, K.3    Wyllie, A.H.4    Rich, T.5
  • 72
    • 0031802612 scopus 로고    scopus 로고
    • Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin
    • Bridger, J. M., H. Herrmann, C. Munkel & P. Lichter: Identification of an interchromosomal compartment by polymerization of nuclear-targeted vimentin. J Cell Sci, 111 ( Pt 9), 1241-53 (1998). (Pubitemid 28266479)
    • (1998) Journal of Cell Science , vol.111 , Issue.9 , pp. 1241-1253
    • Bridger, J.M.1    Herrmann, H.2    Munkel, C.3    Lichter, P.4
  • 73
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: A model for nuclear organelles
    • DOI 10.1038/nrm1172
    • Lamond, A. I. & D. L. Spector: Nuclear speckles: a model for nuclear organelles. Nat Rev Mol Cell Biol, 4, 605-12 (2003). (Pubitemid 36934962)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.8 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 74
    • 0030840687 scopus 로고    scopus 로고
    • Human cytomegalovirus immediate early interaction with host nuclear structures: Definition of an immediate transcript environment
    • DOI 10.1083/jcb.138.1.5
    • Ishov, A. M., R. M. Stenberg & G. G. Maul: Human cytomegalovirus immediate early interaction with host nuclear structures: definition of an immediate transcript environment. J Cell Biol, 138, 5-16 (1997). (Pubitemid 27337448)
    • (1997) Journal of Cell Biology , vol.138 , Issue.1 , pp. 5-16
    • Ishov, A.M.1    Stenberg, R.M.2    Maul, G.G.3
  • 75
    • 0037034829 scopus 로고    scopus 로고
    • PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage
    • DOI 10.1038/sj/onc/1205227
    • Carbone, R., M. Pearson, S. Minucci & P. G. Pelicci: PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage. Oncogene, 21, 1633-40 (2002). (Pubitemid 34259026)
    • (2002) Oncogene , vol.21 , Issue.11 , pp. 1633-1640
    • Carbone, R.1    Pearson, M.2    Minucci, S.3    Pelicci, P.G.4
  • 76
    • 33748794780 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA
    • DOI 10.1242/jcs.03068
    • Boe, S. O., M. Haave, A. Jul-Larsen, A. Grudic, R. Bjerkvig & P. E. Lonning: Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA. J Cell Sci, 119, 3284-95 (2006). (Pubitemid 44405214)
    • (2006) Journal of Cell Science , vol.119 , Issue.16 , pp. 3284-3295
    • Boe, S.O.1    Haave, M.2    Jul-Larsen, A.3    Grudic, A.4    Bjerkvig, R.5    Lonning, P.E.6
  • 78
    • 33749547681 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR
    • DOI 10.1083/jcb.200604009
    • Dellaire, G., R. W. Ching, K. Ahmed, F. Jalali, K. C. Tse, R. G. Bristow & D. P. Bazett-Jones: Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR. J Cell Biol, 175, 55-66 (2006). (Pubitemid 44537198)
    • (2006) Journal of Cell Biology , vol.175 , Issue.1 , pp. 55-66
    • Dellaire, G.1    Ching, R.W.2    Ahmed, K.3    Jalali, F.4    Tse, K.C.K.5    Bristow, R.G.6    Bazett-Jones, D.P.7
  • 79
    • 33644821166 scopus 로고    scopus 로고
    • Interactions between DNA viruses, ND10 and the DNA damage response
    • DOI 10.1111/j.1462-5822.2005.00677.x
    • Everett, R. D.: Interactions between DNA viruses, ND10 and the DNA damage response. Cell Microbiol, 8, 365-74 (2006). (Pubitemid 43356028)
    • (2006) Cellular Microbiology , vol.8 , Issue.3 , pp. 365-374
    • Everett, R.D.1
  • 80
    • 0029838230 scopus 로고    scopus 로고
    • The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition
    • Ishov, A. M. & G. G. Maul: The periphery of nuclear domain 10 (ND10) as site of DNA virus deposition. J Cell Biol, 134, 815-26 (1996). (Pubitemid 26278209)
    • (1996) Journal of Cell Biology , vol.134 , Issue.4 , pp. 815-826
    • Ishov, A.M.1    Maul, G.G.2
  • 81
    • 0029862620 scopus 로고    scopus 로고
    • Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1
    • DOI 10.1006/viro.1996.0094
    • Maul, G. G., A. M. Ishov & R. D. Everett: Nuclear domain 10 as preexisting potential replication start sites of herpes simplex virus type-1. Virology, 217, 67-75 (1996). (Pubitemid 26103599)
    • (1996) Virology , vol.217 , Issue.1 , pp. 67-75
    • Maul, G.G.1    Ishov, A.M.2    Everett, R.D.3
  • 84
    • 33645218381 scopus 로고    scopus 로고
    • Role for centromeric heterochromatin and PML nuclear bodies in the cellular response to foreign DNA
    • Bishop, C. L., M. Ramalho, N. Nadkarni, W. May Kong, C. F. Higgins & N. Krauzewicz: Role for centromeric heterochromatin and PML nuclear bodies in the cellular response to foreign DNA. Mol Cell Biol, 26, 2583-94 (2006).
    • (2006) Mol Cell Biol , vol.26 , pp. 2583-2594
    • Bishop, C.L.1    Ramalho, M.2    Nadkarni, N.3    Kong, W.M.4    Higgins, C.F.5    Krauzewicz, N.6
  • 86
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • DOI 10.1038/sj.onc.1204854
    • Regad, T. & M. K. Chelbi-Alix: Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene, 20, 7274-86 (2001). (Pubitemid 33105016)
    • (2001) Oncogene , vol.20 , Issue.49 REV. IIS. 6 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 88
    • 0036327097 scopus 로고    scopus 로고
    • Nuclear DNA helicase II is recruited to IFN-α-activated transcription sites at PML nuclear bodies
    • DOI 10.1083/jcb.200202035
    • Fuchsova, B., P. Novak, J. Kafkova & P. Hozak: Nuclear DNA helicase II is recruited to IFN-alpha activated transcription sites at PML nuclear bodies. J Cell Biol, 158, 463-73 (2002). (Pubitemid 34851705)
    • (2002) Journal of Cell Biology , vol.158 , Issue.3 , pp. 463-473
    • Fuchsova, B.1    Novak, P.2    Kafkova, J.3    Hozak, P.4
  • 89
    • 0035147230 scopus 로고    scopus 로고
    • Interferon γ regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies
    • Fabunmi, R. P., W. C. Wigley, P. J. Thomas & G. N. DeMartino: Interferon gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies. J Cell Sci, 114, 29-36 (2001). (Pubitemid 32118054)
    • (2001) Journal of Cell Science , vol.114 , Issue.1 , pp. 29-36
    • Fabunmi, R.P.1    Christian Wigley, W.2    Thomas, P.J.3    DeMartino, G.N.4
  • 91
    • 35548950835 scopus 로고    scopus 로고
    • A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells
    • DOI 10.1242/jcs.007492
    • Condemine, W., Y. Takahashi, M. Le Bras & H. de The: A nucleolar targeting signal in PML-I addresses PML to nucleolar caps in stressed or senescent cells. J Cell Sci, 120, 3219-27 (2007). (Pubitemid 350018413)
    • (2007) Journal of Cell Science , vol.120 , Issue.18 , pp. 3219-3227
    • Condemine, W.1    Takahashi, Y.2    Le Bras, M.3    De The, H.4
  • 93
    • 34249938802 scopus 로고    scopus 로고
    • PML protein association with specific nucleolar structures differs in normal, tumor and senescent human cells
    • DOI 10.1016/j.jsb.2007.02.008, PII S104784770700055X
    • Janderova-Rossmeislova, L., Z. Novakova, J. Vlasakova, V. Philimonenko, P. Hozak & Z. Hodny: PML protein association with specific nucleolar structures differs in normal, tumor and senescent human cells. J Struct Biol, 159, 56-70 (2007). (Pubitemid 46880553)
    • (2007) Journal of Structural Biology , vol.159 , Issue.1 , pp. 56-70
    • Janderova-Rossmeislova, L.1    Novakova, Z.2    Vlasakova, J.3    Philimonenko, V.4    Hozak, P.5    Hodny, Z.6
  • 96
    • 0023752982 scopus 로고
    • Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia
    • Huang, M. E., Y. C. Ye, S. R. Chen, J. R. Chai, J. X. Lu, L. Zhoa, L. J. Gu & Z. Y. Wang: Use of all-trans retinoic acid in the treatment of acute promyelocytic leukemia. Blood, 72, 567-72 (1988).
    • (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    Gu, L.J.7    Wang, Z.Y.8
  • 100
    • 33645749156 scopus 로고    scopus 로고
    • Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1
    • Dellaire, G., C. H. Eskiw, H. Dehghani, R. W. Ching & D. P. Bazett-Jones: Mitotic accumulations of PML protein contribute to the re-establishment of PML nuclear bodies in G1. J Cell Sci, 119, 1034-42 (2006).
    • (2006) J Cell Sci , vol.119 , pp. 1034-1042
    • Dellaire, G.1    Eskiw, C.H.2    Dehghani, H.3    Ching, R.W.4    Bazett-Jones, D.P.5
  • 102
    • 0036170782 scopus 로고    scopus 로고
    • Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleas
    • DOI 10.1038/ncb740
    • Muratani, M., D. Gerlich, S. M. Janicki, M. Gebhard, R. Eils & D. L. Spector: Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus. Nat Cell Biol, 4, 106-10 (2002). (Pubitemid 34141475)
    • (2002) Nature Cell Biology , vol.4 , Issue.2 , pp. 106-110
    • Muratani, M.1    Gerlich, D.2    Janicki, S.M.3    Gebhard, M.4    Eils, R.5    Spector, D.L.6
  • 103
    • 0242550970 scopus 로고    scopus 로고
    • Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly
    • DOI 10.1242/jcs.00758
    • Eskiw, C. H., G. Dellaire, J. S. Mymryk & D. P. Bazett-Jones: Size, position and dynamic behavior of PML nuclear bodies following cell stress as a paradigm for supramolecular trafficking and assembly. J Cell Sci, 116, 4455-66 (2003). (Pubitemid 37369600)
    • (2003) Journal of Cell Science , vol.116 , Issue.21 , pp. 4455-4466
    • Eskiw, C.H.1    Dellaire, G.2    Mymryk, J.S.3    Bazett-Jones, D.P.4
  • 104
    • 1842861733 scopus 로고    scopus 로고
    • Fixation-induced redistribution of hyperphosphorylated RNA polymerase II in the nucleus of human cells
    • DOI 10.1016/j.yexcr.2004.01.020, PII S0014482704000485
    • Guillot, P. V., S. Q. Xie, M. Hollinshead & A. Pombo: Fixation-induced redistribution of hyperphosphorylated RNA polymerase II in the nucleus of human cells. Exp Cell Res, 295, 460-8 (2004). (Pubitemid 38490499)
    • (2004) Experimental Cell Research , vol.295 , Issue.2 , pp. 460-468
    • Guillot, P.V.1    Xie, S.Q.2    Hollinshead, M.3    Pombo, A.4


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