메뉴 건너뛰기




Volumn , Issue , 2011, Pages 393-413

Nuclear Domains

Author keywords

Gene expression regulating domains, nucleus warehouse for cellular DNA in eukaryotes; PML nuclear bodies, and PML protein tumor suppressor, punctate nuclear structures or bodies; SAM68 SAM68 like mammalian (SLM) nuclear bodies Sam68 SLM nuclear bodies (SNBs), nuclear structures visualized in HeLa cells

Indexed keywords


EID: 84886144456     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118015759.ch23     Document Type: Chapter
Times cited : (2)

References (195)
  • 1
    • 0031050261 scopus 로고    scopus 로고
    • Identification of Bim1-interacting proteins as constituents of a multimeric mammalian polycomb complex
    • Alkema MJ, Bronk M , Verhoeven E , Otte A , van't Veer LJ , Berns A , va Lohuizen M 1997 Identification of Bim1-interacting proteins as constituents of a multimeric mammalian polycomb complex Genes Dev 11 : 226-40.
    • (1997) Genes Dev , vol.11 , pp. 226-240
    • Alkema, M.J.1    Bronk, M.2    Verhoeven, E.3    Otte, A.4    van't Veer, L.J.5    Berns, A.6    va Lohuizen, M.7
  • 4
    • 0030750614 scopus 로고    scopus 로고
    • Coiled bodies without coilin
    • Bauer DW , Gall JG 1997 Coiled bodies without coilin Mol Biol Cell 8 : 73-82.
    • (1997) Mol Biol Cell , vol.8 , pp. 73-82
    • Bauer, D.W.1    Gall, J.G.2
  • 5
    • 50549173206 scopus 로고
    • Variations in the morphological patterns of " autoimmune " nuclear fluorescence
    • Beck JS 1961 Variations in the morphological patterns of " autoimmune " nuclear fluorescence Lancet 1 : 1203-5.
    • (1961) Lancet , vol.1 , pp. 1203-1205
    • Beck, J.S.1
  • 6
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and function of promyelocytic leukemia nuclear bodies
    • Bernardi R, Pandolfi PP 2007 Structure, dynamics and function of promyelocytic leukemia nuclear bodies Nat Rev Mol Cell Biol 8 : 1006-16.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 7
    • 33748794780 scopus 로고    scopus 로고
    • Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA
    • Boe SO, Haave M , Jul-Larsen A , Grudic A , Bjerkvig R , Lonning PE 2006 Promyelocytic leukemia nuclear bodies are predetermined processing sites for damaged DNA J Cell Sci 119 : 3284-95.
    • (2006) J Cell Sci , vol.119 , pp. 3284-3295
    • Boe, S.O.1    Haave, M.2    Jul-Larsen, A.3    Grudic, A.4    Bjerkvig, R.5    Lonning, P.E.6
  • 8
    • 0034707690 scopus 로고    scopus 로고
    • Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA
    • Boisvert FM, Hendzel MJ , Bazett-Jones DP 2000 Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA J Cell Biol 148 : 283-92.
    • (2000) J Cell Biol , vol.148 , pp. 283-292
    • Boisvert, F.M.1    Hendzel, M.J.2    Bazett-Jones, D.P.3
  • 10
    • 0036318221 scopus 로고    scopus 로고
    • Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies
    • Borden KL 2002 Pondering the promyelocytic leukemia protein (PML) puzzle: possible functions for PML nuclear bodies Mol Cell Biol 22 : 5259-69.
    • (2002) Mol Cell Biol , vol.22 , pp. 5259-5269
    • Borden, K.L.1
  • 11
    • 0036641071 scopus 로고    scopus 로고
    • X-chromosome inactivation: closing in on proteins that bind Xist RNA
    • Brockdorff N 2002 X-chromosome inactivation: closing in on proteins that bind Xist RNA Trends Genet 18 : 352-8
    • (2002) Trends Genet , vol.18 , pp. 352-358
    • Brockdorff, N.1
  • 12
    • 0032550226 scopus 로고    scopus 로고
    • The distribution of polycomb-group proteins during cell division and development in Drosophila embryos: impact on models for silencing
    • Buchenau P, Hodgson J , Strutt H , Arndt-Jovin DJ 1998 The distribution of polycomb-group proteins during cell division and development in Drosophila embryos: impact on models for silencing J Cell Biol 141 : 469-81.
    • (1998) J Cell Biol , vol.141 , pp. 469-481
    • Buchenau, P.1    Hodgson, J.2    Strutt, H.3    Arndt-Jovin, D.J.4
  • 14
    • 0038401969 scopus 로고    scopus 로고
    • Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity
    • Caceres JF, Misteli T , Screaton GR , Spector DL , Krainer AR 1997 Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity J Cell Biol 138 : 225-38.
    • (1997) J Cell Biol , vol.138 , pp. 225-238
    • Caceres, J.F.1    Misteli, T.2    Screaton, G.R.3    Spector, D.L.4    Krainer, A.R.5
  • 15
    • 0031929940 scopus 로고    scopus 로고
    • A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm
    • Caceres JF, Screaton GR , Krainer AR 1998 A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm Genes Dev 12 : 55-66.
    • (1998) Genes Dev , vol.12 , pp. 55-66
    • Caceres, J.F.1    Screaton, G.R.2    Krainer, A.R.3
  • 16
    • 0037034829 scopus 로고    scopus 로고
    • PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage
    • Carbone R, Pearson M , Minucci S , Pelicci PG 2002 PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage Oncogene 21 : 1633-40.
    • (2002) Oncogene , vol.21 , pp. 1633-1640
    • Carbone, R.1    Pearson, M.2    Minucci, S.3    Pelicci, P.G.4
  • 18
    • 0033571601 scopus 로고    scopus 로고
    • The spinal muscular atrophy disease gene product, SMN: a link between snRNP biogenesis and the Cajal (coiled) body
    • Carvalho T, Almeida F , Calapez A , Lafarga M , Berciano MT , Carmo-Fonseca M 1999 The spinal muscular atrophy disease gene product, SMN: a link between snRNP biogenesis and the Cajal (coiled) body J Cell Biol 147 : 715-28
    • (1999) J Cell Biol , vol.147 , pp. 715-728
    • Carvalho, T.1    Almeida, F.2    Calapez, A.3    Lafarga, M.4    Berciano, M.T.5    Carmo-Fonseca, M.6
  • 20
    • 2442695407 scopus 로고    scopus 로고
    • Chromatin decondensation and nuclear reorganization of the HoxB locus upon induction of transcription
    • Chambeyron S , Bickmore WA 2004 Chromatin decondensation and nuclear reorganization of the HoxB locus upon induction of transcription Genes Dev 18 : 1119-30
    • (2004) Genes Dev , vol.18 , pp. 1119-1130
    • Chambeyron, S.1    Bickmore, W.A.2
  • 21
    • 19744379789 scopus 로고    scopus 로고
    • Nuclear reorganization of the HoxB complex during mouse embryonic development
    • Chambeyron S, Da Silva NR , Lawson KA , Bickmore WA 2005 Nuclear reorganization of the HoxB complex during mouse embryonic development Development 132 : 2215-23
    • (2005) Development , vol.132 , pp. 2215-2223
    • Chambeyron, S.1    Da Silva, N.R.2    Lawson, K.A.3    Bickmore, W.A.4
  • 22
    • 0032844207 scopus 로고    scopus 로고
    • A role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cell lines
    • Chen T, Boisvert FM , Bazett-Jones DP , Richard S 1999 A role for the GSG domain in localizing Sam68 to novel nuclear structures in cancer cell lines Mol Biol Cell 10 : 3015-33
    • (1999) Mol Biol Cell , vol.10 , pp. 3015-3033
    • Chen, T.1    Boisvert, F.M.2    Bazett-Jones, D.P.3    Richard, S.4
  • 23
    • 33846318219 scopus 로고    scopus 로고
    • Myotonic dystrophy: emerging mechanisms for DM1 and DM2
    • Cho DH, Tapscott SJ 2007 Myotonic dystrophy: emerging mechanisms for DM1 and DM2 Biochim Biophys Acta 1772 : 195-204
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 195-204
    • Cho, D.H.1    Tapscott, S.J.2
  • 24
    • 28444456713 scopus 로고    scopus 로고
    • Cajal bodies: a long history of discovery
    • Cioce M, Lamond AI 2005 Cajal bodies: a long history of discovery Ann Rev Cell Dev Biol 21 : 105-31
    • (2005) Ann Rev Cell Dev Biol , vol.21 , pp. 105-131
    • Cioce, M.1    Lamond, A.I.2
  • 26
    • 0030028882 scopus 로고    scopus 로고
    • The clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill K, Pawson T , Andrews B , Prasad J , Manley JL , Bell JC , Duncan PI 1996 The clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution EMBO J 15 : 265-75
    • (1996) EMBO J , vol.15 , pp. 265-275
    • Colwill, K.1    Pawson, T.2    Andrews, B.3    Prasad, J.4    Manley, J.L.5    Bell, J.C.6    Duncan, P.I.7
  • 30
    • 0033553877 scopus 로고    scopus 로고
    • Differences in the localization and morphology of chromosomes in the human nucleus
    • Croft JA, Bridger JM , Boyle S , Perry P , Teague P , Bickmore WA 1999 Differences in the localization and morphology of chromosomes in the human nucleus J Cell Biol 145 : 1119-31
    • (1999) J Cell Biol , vol.145 , pp. 1119-1131
    • Croft, J.A.1    Bridger, J.M.2    Boyle, S.3    Perry, P.4    Teague, P.5    Bickmore, W.A.6
  • 31
    • 14044252328 scopus 로고    scopus 로고
    • MBNL1 is the primary determinant of focus formation and aberrant insulin receptor splicing in DM1
    • Dansithong W, Paul S , Comai L , Reddy S 2005 MBNL1 is the primary determinant of focus formation and aberrant insulin receptor splicing in DM1 J Biol Chem 280 : 5773-80
    • (2005) J Biol Chem , vol.280 , pp. 5773-5780
    • Dansithong, W.1    Paul, S.2    Comai, L.3    Reddy, S.4
  • 32
    • 0037013831 scopus 로고    scopus 로고
    • Cajal body-specific small nuclear RNAs: a novel class of 2'-O-methylation and pseudouridylation guide RNAs
    • Darzacq X, Jády BE , Verheggen C , Kiss AM , Bertrand E , Kiss T 2002 Cajal body-specific small nuclear RNAs: a novel class of 2'-O-methylation and pseudouridylation guide RNAs EMBO J 21 : 2746-56
    • (2002) EMBO J , vol.21 , pp. 2746-2756
    • Darzacq, X.1    Jády, J.2    Verheggen, B.E.3    Kiss, C.4    Bertrand, A.M.5    Kiss, E.T.6
  • 33
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: dynamic sensors of DNA damage and cellular stress
    • Dellaire G, Bazett-Jones DP 2004 PML nuclear bodies: dynamic sensors of DNA damage and cellular stress Bioessays 26 : 963-77
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 34
    • 34548288605 scopus 로고    scopus 로고
    • Beyond repair foci: subnuclear domains and the cellular response to DNA damage
    • Dellaire G, Bazett-Jones DP 2007 Beyond repair foci: subnuclear domains and the cellular response to DNA damage Cell Cycle 6 : 1864-72
    • (2007) Cell Cycle , vol.6 , pp. 1864-1872
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 35
    • 0037255042 scopus 로고    scopus 로고
    • The Nuclear Protein Database (NPD): sub-nuclear localisation and functional annotation of the nuclear proteome
    • Dellaire G, Farrall R , Bickmore WA 2003 The Nuclear Protein Database (NPD): sub-nuclear localisation and functional annotation of the nuclear proteome Nucleic Acids Res 31 : 328-30
    • (2003) Nucleic Acids Res , vol.31 , pp. 328-333
    • Dellaire, G.1    Farrall, R.2    Bickmore, W.A.3
  • 36
    • 1642453549 scopus 로고    scopus 로고
    • Correlative light and electron spectroscopic imaging of chromatin in situ
    • Dellaire G, Nisman R , Bazett-Jones DP 2004 Correlative light and electron spectroscopic imaging of chromatin in situ Methods Enzymol 375 : 456-78
    • (2004) Methods Enzymol , vol.375 , pp. 456-478
    • Dellaire, G.1    Nisman, R.2    Bazett-Jones, D.P.3
  • 37
    • 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
    • Dellaire G, Ching RW , Ahmed K , Jalali F , Tse KC , Bristow RG , Bazett-Jones DP 2006a 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) J Cell Biol , vol.175 , pp. 55-66
    • Dellaire, G.1    Ching, R.W.2    Ahmed, K.3    Jalali, F.4    Tse, K.C.5    Bristow, R.G.6    Bazett-Jones, D.P.7
  • 38
    • 33645731002 scopus 로고    scopus 로고
    • The number of PML nuclear bodies increases in early S phase by a fission mechanism
    • Dellaire G, Ching RW , Dehghani H , Ren Y , Bazett-Jones DP 2006b The number of PML nuclear bodies increases in early S phase by a fission mechanism J Cell Sci 119 : 1026-33
    • (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
  • 39
    • 0035192625 scopus 로고    scopus 로고
    • Stress-induced nuclear bodies are sites of accumulation of pre-mRNA processing factors
    • Denegri M, Chiodi I , Corioni M , Cobianchi F , Riva S , Biamonti G 2001 Stress-induced nuclear bodies are sites of accumulation of pre-mRNA processing factors Mol Biol Cell 12 : 3502-14
    • (2001) Mol Biol Cell , vol.12 , pp. 3502-3514
    • Denegri, M.1    Chiodi, I.2    Corioni, M.3    Cobianchi, F.4    Riva, S.5    Biamonti, G.6
  • 40
    • 65349143672 scopus 로고    scopus 로고
    • What the nucleolus says to a tumour pathologist
    • Derenzini M, Montanaro L , Trere D 2009 What the nucleolus says to a tumour pathologist Histopathology 54 : 753-62
    • (2009) Histopathology , vol.54 , pp. 753-762
    • Derenzini, M.1    Montanaro, L.2    Trere, D.3
  • 42
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The H , Lavau C , Marchio A , Chomienne C , Degos L , Dejean A 1991 The PML-RAR alpha fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR Cell 66 : 675-84
    • (1991) Cell , vol.66 , pp. 675-684
    • de The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5    Dejean, A.6
  • 43
    • 33750478380 scopus 로고    scopus 로고
    • c-Abl phosphorylates Hdm2 at tyrosine 276 in response to DNA damage and regulates interaction with ARF
    • Dias SS , Milne DM , Meek DW 2006 c-Abl phosphorylates Hdm2 at tyrosine 276 in response to DNA damage and regulates interaction with ARF Oncogene 25 : 6666-71
    • (2006) Oncogene , vol.25 , pp. 6666-6671
    • Dias, S.S.1    Milne, D.M.2    Meek, D.W.3
  • 45
    • 0035365808 scopus 로고    scopus 로고
    • Functional architecture in the cell nucleus
    • Dundr M, Misteli T 2001 Functional architecture in the cell nucleus Biochem J 356 : 297-310
    • (2001) Biochem J , vol.356 , pp. 297-310
    • Dundr, M.1    Misteli, T.2
  • 47
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck JA, Maul GG , Miller WH , Jr. , Chen JD , Kakizuka A , Evans RM 1994 A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein Cell 76 : 333-43
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller Jr, W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 48
    • 0029097216 scopus 로고
    • Rapid diagnosis of acute promyelocytic leukemia by immunohistochemical localization of PML/RAR-alpha protein
    • Dyck JA, Warrell RP , Jr. , Evans RM , Miller WH , Jr. 1995 Rapid diagnosis of acute promyelocytic leukemia by immunohistochemical localization of PML/RAR-alpha protein Blood 86 : 862-7
    • (1995) Blood , vol.86 , pp. 862-867
    • Dyck, J.A.1    Warrell Jr, R.P.2    Evans, R.M.3    Miller Jr, W.H.4
  • 49
    • 1542304599 scopus 로고    scopus 로고
    • Chromatin contributes to structural integrity of promyelocytic leukemia bodies through a SUMO-1-independent mechanism
    • Eskiw CH, Dellaire G , Bazett-Jones DP 2004 Chromatin contributes to structural integrity of promyelocytic leukemia bodies through a SUMO-1-independent mechanism J Biol Chem 279 : 9577-85
    • (2004) J Biol Chem , vol.279 , pp. 9577-9585
    • Eskiw, C.H.1    Dellaire, G.2    Bazett-Jones, D.P.3
  • 50
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett RD 2001 DNA viruses and viral proteins that interact with PML nuclear bodies Oncogene 20 : 7266-73
    • (2001) Oncogene , vol.20 , pp. 7266-7273
    • Everett, R.D.1
  • 51
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • Everett RD, Meredith M , Orr A , Cross A , Kathoria M , Parkinson J 1997 A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein EMBO J 16 : 1519-30
    • (1997) EMBO J , vol.16 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 52
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett RD, Chelbi-Alix MK 2007 PML and PML nuclear bodies: implications in antiviral defence Biochimie 89 : 819-30
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 53
    • 0015091214 scopus 로고
    • Localization of rapidly and slowly labelled nuclear RNA as visualized by high resolution autoradiography
    • Fakan S, Bernhard W 1971 Localization of rapidly and slowly labelled nuclear RNA as visualized by high resolution autoradiography Exp Cell Res 67 : 129-41
    • (1971) Exp Cell Res , vol.67 , pp. 129-141
    • Fakan, S.1    Bernhard, W.2
  • 54
    • 0028910338 scopus 로고
    • The eed mutation disrupts anterior mesoderm production in mice
    • Faust C, Schumacher A , Holdener B , Magnuson T 1995 The eed mutation disrupts anterior mesoderm production in mice Development 121 : 273-85
    • (1995) Development , vol.121 , pp. 273-285
    • Faust, C.1    Schumacher, A.2    Holdener, B.3    Magnuson, T.4
  • 55
    • 53449097673 scopus 로고    scopus 로고
    • Nuclear architecture and gene regulation
    • Fedorova E, Zink D 2008 Nuclear architecture and gene regulation Biochim Biophys Acta 1783 : 2174-84
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 2174-2184
    • Fedorova, E.1    Zink, D.2
  • 57
    • 0030928716 scopus 로고    scopus 로고
    • The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis
    • Fischer U, Liu Q , Dreyfuss G 1997 The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis Cell 90 : 1023-9
    • (1997) Cell , vol.90 , pp. 1023-1029
    • Fischer, U.1    Liu, Q.2    Dreyfuss, G.3
  • 58
    • 0029372979 scopus 로고
    • The superfamily of argentine/serine-rich splicing factors
    • Fu XD 1995 The superfamily of argentine/serine-rich splicing factors RNA 1 : 663-80
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 59
    • 0034524515 scopus 로고    scopus 로고
    • Cajal bodies: the first 1000 years
    • Gall JG 2000 Cajal bodies: the first 1000 years Annu Rev Cell Dev Biol 16 : 273-300
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 273-300
    • Gall, J.G.1
  • 60
    • 0032740248 scopus 로고    scopus 로고
    • Assembly of the nuclear transcription and processing machinery: cajal bodies (coiled bodies) and transcriptosomes
    • Gall JG , Bellini M , Wu Z , Murphy C 1999 Assembly of the nuclear transcription and processing machinery: cajal bodies (coiled bodies) and transcriptosomes Mol Biol Cell 10 : 4385-402
    • (1999) Mol Biol Cell , vol.10 , pp. 4385-4402
    • Gall, J.G.1    Bellini, M.2    Wu, Z.3    Murphy, C.4
  • 61
    • 0026660025 scopus 로고
    • hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs
    • Ghetti A, Pinol-Roma S , Michael WM , Morandi C , Dreyfuss G 1992 hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs Nucleic Acids Res 20 : 3671-8
    • (1992) Nucleic Acids Res , vol.20 , pp. 3671-3678
    • Ghetti, A.1    Pinol-Roma, S.2    Michael, W.M.3    Morandi, C.4    Dreyfuss, G.5
  • 62
    • 33751279248 scopus 로고    scopus 로고
    • DNA damage, p14ARF, nucleophosmin (NPM/B23), and cancer
    • Gjerset RA 2006. DNA damage, p14ARF, nucleophosmin (NPM/B23), and cancer J Mol Histol 37 : 239-51
    • (2006) J Mol Histol , vol.37 , pp. 239-251
    • Gjerset, R.A.1
  • 63
    • 0030772115 scopus 로고    scopus 로고
    • Functions of mammalian Polycomb group and trithorax group related genes
    • Gould A 1997 Functions of mammalian Polycomb group and trithorax group related genes Curr Opin Genet Dev 7 : 488-94
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 488-494
    • Gould, A.1
  • 64
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley BR 2000 Sorting out the complexity of SR protein functions RNA 6 : 1197-211
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 65
    • 33845755946 scopus 로고    scopus 로고
    • Heterochromatin revisited
    • Grewal SI , Jia S 2007 Heterochromatin revisited Nat Rev Genet 8 : 35-46
    • (2007) Nat Rev Genet , vol.8 , pp. 35-46
    • Grewal, S.I.1    Jia, S.2
  • 66
    • 37549060645 scopus 로고    scopus 로고
    • Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres
    • Grudic A, Jul-Larsen A , Haring SJ , Wold MS , Lonning PE , Bjerkvig R , Boe SO 2007 Replication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeres Nucleic Acids Res 35 : 7267-78
    • (2007) Nucleic Acids Res , vol.35 , pp. 7267-7278
    • Grudic, A.1    Jul-Larsen, A.2    Haring, S.J.3    Wold, M.S.4    Lonning, P.E.5    Bjerkvig, R.6    Boe, S.O.7
  • 67
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui JF, Lane WS , Fu XD 1994 A serine kinase regulates intracellular localization of splicing factors in the cell cycle Nature 369 : 678-82
    • (1994) Nature , vol.369 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 70
    • 30444437477 scopus 로고    scopus 로고
    • Subnuclear organelles: new insights into form and function
    • Handwerger KE, Gall JG 2006 Subnuclear organelles: new insights into form and function Trends Cell Biol 16 : 19-26
    • (2006) Trends Cell Biol , vol.16 , pp. 19-26
    • Handwerger, K.E.1    Gall, J.G.2
  • 71
    • 0014555462 scopus 로고
    • The para-nucleolar structure, accessory body of Cajal, sex chromatin, and related structures in nuclei of rat trigeminal neurons: a cytochemical and ultrastructural study
    • Hardin JH, Spicer SS , Greene WB 1969 The para-nucleolar structure, accessory body of Cajal, sex chromatin, and related structures in nuclei of rat trigeminal neurons: a cytochemical and ultrastructural study Anat Rec 164 : 403-32
    • (1969) Anat Rec , vol.164 , pp. 403-432
    • Hardin, J.H.1    Spicer, S.S.2    Greene, W.B.3
  • 72
    • 0032739144 scopus 로고    scopus 로고
    • The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn)
    • Hartmann AM, Nayler O , Schwaiger FW , Obermeier A , Stamm S 1999 The interaction and colocalization of Sam68 with the splicing-associated factor YT521-B in nuclear dots is regulated by the Src family kinase p59(fyn) Mol Cell Biol 10 : 3909-26
    • (1999) Mol Cell Biol , vol.10 , pp. 3909-3926
    • Hartmann, A.M.1    Nayler, O.2    Schwaiger, F.W.3    Obermeier, A.4    Stamm, S.5
  • 73
    • 33845400134 scopus 로고    scopus 로고
    • The nucleolus: a model for the organization of nuclear functions
    • Hernandez-Verdun D 2006a The nucleolus: a model for the organization of nuclear functions Histochem Cell Biol 126 : 135-48
    • (2006) Histochem Cell Biol , vol.126 , pp. 135-148
    • Hernandez-Verdun, D.1
  • 74
    • 30044434446 scopus 로고    scopus 로고
    • Nucleolus: from structure to dynamics
    • Hernandez-Verdun D 2006b Nucleolus: from structure to dynamics Histochem Cell Biol 125 : 127-37
    • (2006) Histochem Cell Biol , vol.125 , pp. 127-137
    • Hernandez-Verdun, D.1
  • 75
    • 34548441225 scopus 로고    scopus 로고
    • Defective mRNA in myotonic dystrophy accumulates at the periphery of nuclear splicing speckles
    • Holt I, Mittal S , Furling D , Butler-Brown GS , Brook JD , Morris GE 2007 Defective mRNA in myotonic dystrophy accumulates at the periphery of nuclear splicing speckles Genes Cell 12 : 1035-48
    • (2007) Genes Cell , vol.12 , pp. 1035-1048
    • Holt, I.1    Mittal, S.2    Furling, D.3    Butler-Brown, G.S.4    Brook, J.D.5    Morris, G.E.6
  • 76
    • 0033925532 scopus 로고    scopus 로고
    • Review: perinucleolar structures
    • Huang S 2000 Review: perinucleolar structures J Struct Biol 129 : 233-40
    • (2000) J Struct Biol , vol.129 , pp. 233-240
    • Huang, S.1
  • 77
    • 0031005765 scopus 로고    scopus 로고
    • The dynamic organization of the perinucleolar compartment in the cell nucleus
    • Huang S , Deerinck TJ , Ellisman MH , Spector DL 1997 The dynamic organization of the perinucleolar compartment in the cell nucleus J Cell Biol 137 : 965-74
    • (1997) J Cell Biol , vol.137 , pp. 965-974
    • Huang, S.1    Deerinck, T.J.2    Ellisman, M.H.3    Spector, D.L.4
  • 79
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang Y, Steitz JA 2001 Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA Mol Cell 7 : 899-905
    • (2001) Mol Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 80
  • 81
    • 0026579621 scopus 로고
    • Nucleolar antigens and autoantibodies in hepatocellular carcinoma and other malignancies
    • Imai H, Ochs RL , Kiyosawa K , Furuta S , Nakamura RM , Tan EM 1992 Nucleolar antigens and autoantibodies in hepatocellular carcinoma and other malignancies Am J Pathol 140 : 859-70
    • (1992) Am J Pathol , vol.140 , pp. 859-870
    • Imai, H.1    Ochs, R.L.2    Kiyosawa, K.3    Furuta, S.4    Nakamura, R.M.5    Tan, E.M.6
  • 85
    • 0034618038 scopus 로고    scopus 로고
    • Tracking COL1A1 RNA in osteogenesis imperfecta. Splice defective transcripts initiate transport from the gene but are retained within the SC35 domain
    • Johnson C, Primorac D , McKinstry M , McNeil J , Rowe D , Lawrence JB 2000 Tracking COL1A1 RNA in osteogenesis imperfecta. Splice defective transcripts initiate transport from the gene but are retained within the SC35 domain J Cell Biol 150 : 417-32
    • (2000) J Cell Biol , vol.150 , pp. 417-432
    • Johnson, C.1    Primorac, D.2    McKinstry, M.3    McNeil, J.4    Rowe, D.5    Lawrence, J.B.6
  • 87
    • 0025780876 scopus 로고
    • Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RAR alpha with a novel putative transcription factor, PML
    • Kakizuka A, Miller WH , Jr. , Umesono K , Warrell RP , Jr. , Frankel SR , Murty VV , Dmitrovsky E , Evans RM 1991 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) Cell , vol.66 , pp. 663-674
    • Kakizuka, A.1    Miller Jr, W.H.2    Umesono, K.3    Warrell Jr, R.P.4    Frankel, S.R.5    Murty, V.V.6    Dmitrovsky, E.7    Evans, R.M.8
  • 90
    • 4444278440 scopus 로고    scopus 로고
    • p14ARF is a component of the p53 response following ionizing irradiation of normal human fibroblasts
    • Khan S, Guevara C , Fujii G , Parry D 2004 p14ARF is a component of the p53 response following ionizing irradiation of normal human fibroblasts Oncogene 23 : 6040-6
    • (2004) Oncogene , vol.23 , pp. 6040-6046
    • Khan, S.1    Guevara, C.2    Fujii, G.3    Parry, D.4
  • 91
    • 0030932869 scopus 로고    scopus 로고
    • Cancer-susceptibility genes. Gatekeepers and caretakers
    • Kinzler KW, Vogelstein B 1997 Cancer-susceptibility genes. Gatekeepers and caretakers Nature 386 : 761 , 763
    • (1997) Nature , vol.386 , Issue.761 , pp. 763
    • Kinzler, K.W.1    Vogelstein, B.2
  • 94
    • 26444615468 scopus 로고    scopus 로고
    • Perinucleolar compartment and transformation
    • Kopp K, Huang S 2005 Perinucleolar compartment and transformation J Cell Biochem 95 : 217-25
    • (2005) J Cell Biochem , vol.95 , pp. 217-225
    • Kopp, K.1    Huang, S.2
  • 95
    • 0016221697 scopus 로고
    • Chromatin structure: a repeating unit of histones and DNA
    • Kornberg RD 1974 Chromatin structure: a repeating unit of histones and DNA Science 184 : 868-71
    • (1974) Science , vol.184 , pp. 868-871
    • Kornberg, R.D.1
  • 96
    • 0142106346 scopus 로고    scopus 로고
    • Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization
    • Kurki S, Latonen L , Laiho M 2003 Cellular stress and DNA damage invoke temporally distinct Mdm2, p53 and PML complexes and damage-specific nuclear relocalization J Cell Sci 116 : 3917-25
    • (2003) J Cell Sci , vol.116 , pp. 3917-3925
    • Kurki, S.1    Latonen, L.2    Laiho, M.3
  • 97
    • 0029862498 scopus 로고    scopus 로고
    • Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleus: a possible coordinate role in ribosome biogenesis
    • Lee B, Matera AG , Ward DC , Craft J 1996 Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleus: a possible coordinate role in ribosome biogenesis Proc Natl Acad Sci U S A 93 : 11471-6
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 11471-11476
    • Lee, B.1    Matera, A.G.2    Ward, D.C.3    Craft, J.4
  • 99
    • 0019570066 scopus 로고
    • Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease
    • Lerner EA, Lerner MR , Janeway CA , Steitz JA 1981 Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease Proc Natl Acad Sci U S A 78 : 2737-41
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 2737-2741
    • Lerner, E.A.1    Lerner, M.R.2    Janeway, C.A.3    Steitz, J.A.4
  • 100
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine AJ 1997 p53, the cellular gatekeeper for growth and division Cell 88 : 323-31
    • (1997) , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 101
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M, Chen D , Shiloh A , Luo J , Nikolaev AY , Qin J , Gu W 2002 Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization Nature 416 : 648-53
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 102
    • 0023692635 scopus 로고
    • Delineation of individual human chromosomes in metaphase and interphase cells by in situ suppression hybridization using recombinant DNA libraries
    • Lichter P, Cremer T , Borden J , Manuelidis L , Ward DC 1988 Delineation of individual human chromosomes in metaphase and interphase cells by in situ suppression hybridization using recombinant DNA libraries Hum Genet 80 : 224-34
    • (1988) Hum Genet , vol.80 , pp. 224-234
    • Lichter, P.1    Cremer, T.2    Borden, J.3    Manuelidis, L.4    Ward, D.C.5
  • 104
    • 0041856232 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation
    • Louria;Hayon I , Grossman T , Sionov RV , Alsheich O , Pandolfi PP , Haupt Y 2003 The promyelocytic leukemia protein protects p53 from Mdm2-mediated inhibition and degradation J Biol Chem 278 : 33134-41
    • (2003) J Biol Chem , vol.278 , pp. 33134-33141
    • Louria Hayon, I.1    Grossman, T.2    Sionov, R.V.3    Alsheich, O.4    Pandolfi, P.P.5    Haupt, Y.6
  • 105
    • 0242526150 scopus 로고    scopus 로고
    • An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene
    • Lu F, Gladden AB , Diehl JA 2003 An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene Cancer Res 63 : 7056-61
    • (2003) Cancer Res , vol.63 , pp. 7056-7061
    • Lu, F.1    Gladden, A.B.2    Diehl, J.A.3
  • 106
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8A resolution
    • Luger K, Mader AW , Richmond RK , Sargent DF , Richmond TJ 1997. Crystal structure of the nucleosome core particle at 2.8A resolution Nature 389 : 251-60
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 107
    • 33344469184 scopus 로고    scopus 로고
    • Nucleolar adaptation in human cancer
    • Maggi LB, Jr. , Weber JD 2005 Nucleolar adaptation in human cancer Cancer Invest 23 : 599-608
    • (2005) Cancer Invest , vol.23 , pp. 599-608
    • Maggi Jr, L.B.1    Weber, J.D.2
  • 108
    • 0037049548 scopus 로고    scopus 로고
    • Gene density and transcription influence the localization of chromatin outside of chromosome territories detectable by FISH
    • Mahy NL, Perry PE , Bickmore WA 2002a Gene density and transcription influence the localization of chromatin outside of chromosome territories detectable by FISH J Cell Biol 159 : 753-63
    • (2002) J Cell Biol , vol.159 , pp. 753-763
    • Mahy, N.L.1    Perry, P.E.2    Bickmore, W.A.3
  • 109
    • 0037071535 scopus 로고    scopus 로고
    • Spatial organization of active and inactive genes and noncoding DNA within chromosome territories
    • Mahy NL, Perry PE , Gilchrist S , Baldock RA , Bickmore WA 2002b Spatial organization of active and inactive genes and noncoding DNA within chromosome territories J Cell Biol 157 : 579-89
    • (2002) J Cell Biol , vol.157 , pp. 579-589
    • Mahy, N.L.1    Perry, P.E.2    Gilchrist, S.3    Baldock, R.A.4    Bickmore, W.A.5
  • 111
    • 0037062982 scopus 로고    scopus 로고
    • Alternative pre- mRNA splicing and proteome expansion in metazoans
    • Maniatis T, Tasic B 2002. Alternative pre- mRNA splicing and proteome expansion in metazoans Nature 418 : 236-43 .
    • (2002) Nature , vol.418 , pp. 236-243
    • Maniatis, T.1    Tasic, B.2
  • 112
    • 0031686476 scopus 로고    scopus 로고
    • Mutations in the Treacher Collins syndrome gene lead to mislocalization of the nucleolar protein treacle
    • Marsh KL, Dixon J , Dixon MJ 1998 Mutations in the Treacher Collins syndrome gene lead to mislocalization of the nucleolar protein treacle Hum Mol Genet 11 : 1795-800
    • (1998) Hum Mol Genet , vol.11 , pp. 1795-1800
    • Marsh, K.L.1    Dixon, J.2    Dixon, M.J.3
  • 113
    • 0033179146 scopus 로고    scopus 로고
    • Nuclear bodies: multifaceted subdomains of the interchromatin space
    • Matera AG 1999 Nuclear bodies: multifaceted subdomains of the interchromatin space Trends Cell Biol 9 : 302-9
    • (1999) Trends Cell Biol , vol.9 , pp. 302-309
    • Matera, A.G.1
  • 114
    • 0029055036 scopus 로고
    • A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I
    • Matera AG, Frey MR , Margelot K , Wolin SL 1995 A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I J Cell Biol 129 : 1181-93
    • (1995) J Cell Biol , vol.129 , pp. 1181-1193
    • Matera, A.G.1    Frey, M.R.2    Margelot, K.3    Wolin, S.L.4
  • 115
    • 0033925534 scopus 로고    scopus 로고
    • Review: properties and assembly mechanisms of ND10, PML bodies, or PODs
    • Maul GG, Negorev D , Bell P , Ishov AM 2000 Review: properties and assembly mechanisms of ND10, PML bodies, or PODs J Struct Biol 129 : 278-87
    • (2000) J Struct Biol , vol.129 , pp. 278-287
    • Maul, G.G.1    Negorev, D.2    Bell, P.3    Ishov, A.M.4
  • 116
    • 25444473870 scopus 로고    scopus 로고
    • Cellular stress and nucleolar function
    • Mayer C, Grummt I 2005 Cellular stress and nucleolar function Cell Cycle 4 : 1036-8
    • (2005) Cell Cycle , vol.4 , pp. 1036-1038
    • Mayer, C.1    Grummt, I.2
  • 117
    • 42949109848 scopus 로고    scopus 로고
    • The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4 E-BP1
    • Michlewski G, Sanford JR , Caceres JF 2008. The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4 E-BP1 Mol Cell 30 : 179-89
    • (2008) Mol Cell , vol.30 , pp. 179-189
    • Michlewski, G.1    Sanford, J.R.2    Caceres, J.F.3
  • 118
    • 0033926038 scopus 로고    scopus 로고
    • Compartmentalization of RNA processing factors within nuclear speckles
    • Mintz PJ, Spector DL 2000 Compartmentalization of RNA processing factors within nuclear speckles J Struct Biol 129 : 241-51
    • (2000) J Struct Biol , vol.129 , pp. 241-251
    • Mintz, P.J.1    Spector, D.L.2
  • 119
    • 0033517103 scopus 로고    scopus 로고
    • Purification and biochemical characterization of interchromatin granule clusters
    • Mintz PJ, Patterson SD , Neuwald AF , Spahr CS , Spector DL 1999 Purification and biochemical characterization of interchromatin granule clusters EMBO J 18 : 4308-20
    • (1999) EMBO J , vol.18 , pp. 4308-4320
    • Mintz, P.J.1    Patterson, S.D.2    Neuwald, A.F.3    Spahr, C.S.4    Spector, D.L.5
  • 120
    • 0033602473 scopus 로고    scopus 로고
    • RNA splicing: what has phosphorylation got to do with it?
    • Misteli T 1999 RNA splicing: what has phosphorylation got to do with it? Curr Biol 9 : 198-200
    • (1999) Curr Biol , vol.9 , pp. 198-200
    • Misteli, T.1
  • 121
    • 0033153543 scopus 로고    scopus 로고
    • RNA polymerase II targets pre-mRNA splicing factors to transcription sites in vivo
    • Misteli T, Spector DL 1999 RNA polymerase II targets pre-mRNA splicing factors to transcription sites in vivo Mol Cell 3 : 697-705
    • (1999) Mol Cell , vol.3 , pp. 697-705
    • Misteli, T.1    Spector, D.L.2
  • 122
    • 1842376906 scopus 로고    scopus 로고
    • The dynamics of a pre-mRNA splicing factor in living cells
    • Misteli T, Caceres JF , Spector DL 1997 The dynamics of a pre-mRNA splicing factor in living cells Nature 387 : 523-7
    • (1997) Nature , vol.387 , pp. 523-527
    • Misteli, T.1    Caceres, J.F.2    Spector, D.L.3
  • 123
    • 0032547829 scopus 로고    scopus 로고
    • Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo
    • Misteli T, Caceres JF , Clement JQ , Krainer AR , Wilkinson MF , Spector DL 1998. Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo J Cell Biol 143 : 297-307
    • (1998) J Cell Biol , vol.143 , pp. 297-307
    • Misteli, T.1    Caceres, J.F.2    Clement, J.Q.3    Krainer, A.R.4    Wilkinson, M.F.5    Spector, D.L.6
  • 124
  • 125
    • 0014510121 scopus 로고
    • Fine structural organization of the interphase nucleus in some interphase cells
    • Monneron A, Bernhard W 1969 Fine structural organization of the interphase nucleus in some interphase cells J Ultrastruct Res 27 : 266-88
    • (1969) J Ultrastruct Res , vol.27 , pp. 266-288
    • Monneron, A.1    Bernhard, W.2
  • 127
    • 34248593510 scopus 로고    scopus 로고
    • Nuclear reorganisation and chromatin decondensation are conserved, but distinct, mechanisms linked to Hox gene activation
    • Morey C, Da Silva NR , Perry P , Bickmore WA 2007 Nuclear reorganisation and chromatin decondensation are conserved, but distinct, mechanisms linked to Hox gene activation Development 134 : 909-19
    • (2007) Development , vol.134 , pp. 909-919
    • Morey, C.1    Da Silva, N.R.2    Perry, P.3    Bickmore, W.A.4
  • 128
    • 67650064596 scopus 로고    scopus 로고
    • Lack of bystander activation shows that localization exterior to chromosome territories is not sufficient to up-regulate gene expression
    • Morey C, Kress C , Bickmore WA 2009 Lack of bystander activation shows that localization exterior to chromosome territories is not sufficient to up-regulate gene expression Genome Res 19 : 1184-94
    • (2009) Genome Res , vol.19 , pp. 1184-1194
    • Morey, C.1    Kress, C.2    Bickmore, W.A.3
  • 129
    • 0029145512 scopus 로고
    • Function of the polycomb protein is conserved in mice and flies
    • Muller J, Gaunt S , Lawrence PA 1995 Function of the polycomb protein is conserved in mice and flies Development 121 : 2847-52
    • (1995) Development , vol.121 , pp. 2847-2852
    • Muller, J.1    Gaunt, S.2    Lawrence, P.A.3
  • 130
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/ PODs suggest functions of a nuclear depot
    • Negorev D, Maul GG 2001 Cellular proteins localized at and interacting within ND10/PML nuclear bodies/ PODs suggest functions of a nuclear depot Oncogene 20 : 7234-42
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 131
    • 27244444559 scopus 로고    scopus 로고
    • TRIM family proteins: retroviral restriction and antiviral defence
    • Nisole S, Stoye JP , Saib A 2005 TRIM family proteins: retroviral restriction and antiviral defence Nat Rev Microbiol 3 : 799-808
    • (2005) Nat Rev Microbiol , vol.3 , pp. 799-808
    • Nisole, S.1    Stoye, J.P.2    Saib, A.3
  • 133
    • 50249088917 scopus 로고    scopus 로고
    • Perinucleolar compartment prevalence is a phenotypic pancancer marker of malignancy
    • Norton JT Pollock CB , Wang C , Schink JC , Kim JJ , Huang S 2008 Perinucleolar compartment prevalence is a phenotypic pancancer marker of malignancy Cancer 113 : 861-9
    • (2008) Cancer , vol.113 , pp. 861-869
    • Norton, J.T.1    Pollock, C.B.2    Wang, C.3    Schink, J.C.4    Kim, J.J.5    Huang, S.6
  • 134
    • 12144288857 scopus 로고    scopus 로고
    • Sensing cellular stress: another new function for the nucleolus?
    • 2004
    • Olson MO 2004 Sensing cellular stress: another new function for the nucleolus? Sci STKE 2004 : pe10
    • (2004) Sci STKE
    • Olson, M.O.1
  • 135
    • 18744364184 scopus 로고    scopus 로고
    • The moving parts of the nucleolus
    • Olson MO , Dundr M 2005 The moving parts of the nucleolus Histochem Cell Biol 123 : 203-16
    • (2005) Histochem Cell Biol , vol.123 , pp. 203-216
    • Olson, M.O.1    Dundr, M.2
  • 136
    • 0034193778 scopus 로고    scopus 로고
    • The nucleolus: an old factory with unexpected capabilities
    • Olson MO, Dundr M , Szebeni A 2000 The nucleolus: an old factory with unexpected capabilities Trends Cell Biol 10 : 189-96
    • (2000) Trends Cell Biol , vol.10 , pp. 189-196
    • Olson, M.O.1    Dundr, M.2    Szebeni, A.3
  • 138
    • 0018604613 scopus 로고
    • Intranuclear structures of monkey kidney cells recognised by immunofluorescence and immuno-electron microscopy using anti-ribonucleoprotein antibodies
    • .Perraud M, Gioud M , Monier JC 1979 Intranuclear structures of monkey kidney cells recognised by immunofluorescence and immuno-electron microscopy using anti-ribonucleoprotein antibodies Ann Immunol 130 : 635-47
    • (1979) Ann Immunol , vol.130 , pp. 635-647
    • Perraud, M.1    Gioud, M.2    Monier, J.C.3
  • 139
    • 0000362243 scopus 로고
    • The cellular sites of ribosomal and 4S RNA
    • Perry RP 1962 The cellular sites of ribosomal and 4S RNA Proc Natl Acad Sci USA 48 : 2179-86
    • (1962) Proc Natl Acad Sci USA , vol.48 , pp. 2179-2186
    • Perry, R.P.1
  • 140
    • 0030223057 scopus 로고    scopus 로고
    • Selection of highly metastatic variants of different human prostatic carcinomas using orthotopic implantation in nude mice
    • Pettaway CA, Pathak S , Greene G , Ramirez E , Wilson MR , Killion JJ , Fidler IJ 1996 Selection of highly metastatic variants of different human prostatic carcinomas using orthotopic implantation in nude mice Clin Cancer Res 2 : 1627-36
    • (1996) Clin Cancer Res , vol.2 , pp. 1627-1636
    • Pettaway, C.A.1    Pathak, S.2    Greene, G.3    Ramirez, E.4    Wilson, M.R.5    Killion, J.J.6    Fidler, I.J.7
  • 141
    • 0034174682 scopus 로고    scopus 로고
    • Prognostic relevance of AgNORs in tumor pathology
    • Pich A , Chiusa L , Margaria E 2000 Prognostic relevance of AgNORs in tumor pathology Micron 31 : 133-41
    • (2000) Micron , vol.31 , pp. 133-141
    • Pich, A.1    Chiusa, L.2    Margaria, E.3
  • 142
    • 0037064572 scopus 로고    scopus 로고
    • Signal recognition particle RNA localization within the nucleolus differs from the classical sites of ribosome synthesis
    • Politz JC , Lewandowski LB , Pederson T 2002 Signal recognition particle RNA localization within the nucleolus differs from the classical sites of ribosome synthesis J Cell Biol 159 : 411-18
    • (2002) J Cell Biol , vol.159 , pp. 411-418
    • Politz, J.C.1    Lewandowski, L.B.2    Pederson, T.3
  • 143
    • 33646859205 scopus 로고    scopus 로고
    • The promyelocytic leukemia protein stimulates SUMO conjugation in yeast
    • Quimby BB, Yong-Gonzalez V , Anan T , Strunnikov AV , Dasso M 2006 The promyelocytic leukemia protein stimulates SUMO conjugation in yeast Oncogene 25 : 2999-3005
    • (2006) Oncogene , vol.25 , pp. 2999-3005
    • Quimby, B.B.1    Yong-Gonzalez, V.2    Anan, T.3    Strunnikov, A.V.4    Dasso, M.5
  • 144
    • 0001227249 scopus 로고
    • Un sencillo metodo de coloracion selective del reticulo protoplasmico y sus efectos en los diversos organos nerviosos de vertabrados e invertebrados
    • Ramon y Cajal S 1903 Un sencillo metodo de coloracion selective del reticulo protoplasmico y sus efectos en los diversos organos nerviosos de vertabrados e invertebrados Trab Lab Invest Biol 2 : 129-221
    • (1903) Trab Lab Invest Biol , vol.2 , pp. 129-221
    • Ramon y Cajal, S.1
  • 145
    • 33845525592 scopus 로고    scopus 로고
    • New insights into nucleolar architecture and activity
    • Raska I, Shaw PJ , Cmarko D 2006 New insights into nucleolar architecture and activity Int Rev Cytol 255 : 177-235 .
    • (2006) Int Rev Cytol , vol.255 , pp. 177-235
    • Raska, I.1    Shaw, P.J.2    Cmarko, D.3
  • 146
    • 35548948498 scopus 로고    scopus 로고
    • Dynamic organization of the cell nucleus
    • Rippe K 2007 Dynamic organization of the cell nucleus Curr Opin Genet Dev 17 : 373-80
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 373-380
    • Rippe, K.1
  • 147
    • 0001603021 scopus 로고
    • Localization of DNA complementary to rRNA in the nucleolus organizer region of Drosophila melanogaster
    • Ritossa F, Spiegelman S 1965 Localization of DNA complementary to rRNA in the nucleolus organizer region of Drosophila melanogaster Proc Natl Acad Sci USA 53 : 737-45
    • (1965) Proc Natl Acad Sci USA , vol.53 , pp. 737-745
    • Ritossa, F.1    Spiegelman, S.2
  • 148
    • 38048999665 scopus 로고    scopus 로고
    • Two faces of p53: aging and tumor suppression
    • Rodier F, Campisi J , Bhaumik D 2007 Two faces of p53: aging and tumor suppression Nucleic Acids Res 35 : 7475-84
    • (2007) Nucleic Acids Res , vol.35 , pp. 7475-7484
    • Rodier, F.1    Campisi, J.2    Bhaumik, D.3
  • 149
    • 3242683387 scopus 로고    scopus 로고
    • Osteogenesis imperfecta-clinical and molecular diversity
    • Roughly PJ, Rauch F , Glorieux FH 2003 Osteogenesis imperfecta-clinical and molecular diversity Eur Cell Mater 5 : 41-7 .
    • (2003) Eur Cell Mater , vol.5 , pp. 41-47
    • Roughly, P.J.1    Rauch, F.2    Glorieux, F.H.3
  • 150
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • Rubbi CP, Milner J 2003 Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses EMBO J 22 : 6068-77
    • (2003) EMBO J , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 152
    • 1842632326 scopus 로고    scopus 로고
    • A novel role for shuttling SR proteins in mRNA translation
    • Sanford JR, Gray NK , Beckmann K , Caceres JF 2004 A novel role for shuttling SR proteins in mRNA translation Genes Dev 18 : 755-68
    • (2004) Genes Dev , vol.18 , pp. 755-768
    • Sanford, J.R.1    Gray, N.K.2    Beckmann, K.3    Caceres, J.F.4
  • 154
    • 0032563598 scopus 로고    scopus 로고
    • The human polycomb group complex associates with pericentromeric heterochromatin to form a novel domain
    • Saurin AJ, Shiels C , Williamson J , Satijn DP , Otte AP , Sheer D , Freemont PS 1998 The human polycomb group complex associates with pericentromeric heterochromatin to form a novel domain J Cell Biol 142 : 887-98
    • (1998) J Cell Biol , vol.142 , pp. 887-898
    • Saurin, A.J.1    Shiels, C.2    Williamson, J.3    Satijn, D.P.4    Otte, A.P.5    Sheer, D.6    Freemont, P.S.7
  • 155
    • 33751313020 scopus 로고    scopus 로고
    • Nucleolin inhibits Hdm2 by multiple pathways leading to p53 stabilization
    • Saxena A, Rorie CJ , Dimitrova D , Daniely Y , Borowiec JA 2006 Nucleolin inhibits Hdm2 by multiple pathways leading to p53 stabilization Oncogene 25 : 7274-88
    • (2006) Oncogene , vol.25 , pp. 7274-7288
    • Saxena, A.1    Rorie, C.J.2    Dimitrova, D.3    Daniely, Y.4    Borowiec, J.A.5
  • 156
    • 0022349296 scopus 로고
    • Specific staining of human chromosome position in Chinese hamster Xman hybrid cell lines demonstrates interphase chromosome territories
    • Schardin M, Cremer T , Hager HD , Lang M 1985 Specific staining of human chromosome position in Chinese hamster Xman hybrid cell lines demonstrates interphase chromosome territories Hum Genet 71 : 281-7
    • (1985) Hum Genet , vol.71 , pp. 281-287
    • Schardin, M.1    Cremer, T.2    Hager, H.D.3    Lang, M.4
  • 161
    • 0033533730 scopus 로고    scopus 로고
    • Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway
    • Sleeman JE, Lamond AI 1999 Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway Curr Biol 9 : 1065-74
    • (1999) Curr Biol , vol.9 , pp. 1065-1074
    • Sleeman, J.E.1    Lamond, A.I.2
  • 162
    • 0035691790 scopus 로고    scopus 로고
    • sRNP expression enhances the formation of Cajal bodies containing p80-coilin and SMN
    • Sleeman JE, Ajuh P , Lamond AI 2001 sRNP expression enhances the formation of Cajal bodies containing p80-coilin and SMN J Cell Sci 114 : 4407-19
    • (2001) J Cell Sci , vol.114 , pp. 4407-4419
    • Sleeman, J.E.1    Ajuh, P.2    Lamond, A.I.3
  • 163
    • 34548842522 scopus 로고    scopus 로고
    • Defining early steps in mRNA transport: mutant mRNA in myotonic dystrophy type 1 is blocked at entry into SC-35 domains
    • Smith KP, Byron M , Johnson C , Xing Y , Lawrence JB 2007 Defining early steps in mRNA transport: mutant mRNA in myotonic dystrophy type 1 is blocked at entry into SC-35 domains J Cell Biol 178 : 951-64
    • (2007) J Cell Biol , vol.178 , pp. 951-964
    • Smith, K.P.1    Byron, M.2    Johnson, C.3    Xing, Y.4    Lawrence, J.B.5
  • 165
    • 0034851781 scopus 로고    scopus 로고
    • Nuclear domains
    • Spector DL. 2001 Nuclear domains J Cell Sci 114 : 2891-3
    • (2001) J Cell Sci , vol.114 , pp. 2891-2893
    • Spector, D.L.1
  • 166
    • 0021082681 scopus 로고
    • Immunoelectron microscopic localization of snRNPs
    • Spector DL, Schrier WH , Busch H 1983 Immunoelectron microscopic localization of snRNPs Biol Cell 49 : 1-10
    • (1983) Biol Cell , vol.49 , pp. 1-10
    • Spector, D.L.1    Schrier, W.H.2    Busch, H.3
  • 167
    • 0027360277 scopus 로고
    • Defective splicing of mRNA from one COL1A1 allele of type 1 collagen in nondeforming (type 1) osteogenesis imperfecta
    • Stover ML, Primorac D , Liu SC , McKinstry MB , Rowe DW 1993 Defective splicing of mRNA from one COL1A1 allele of type 1 collagen in nondeforming (type 1) osteogenesis imperfecta J Clin Invest 92 : 1994-2002
    • (1993) J Clin Invest , vol.92 , pp. 1994-2002
    • Stover, M.L.1    Primorac, D.2    Liu, S.C.3    McKinstry, M.B.4    Rowe, D.W.5
  • 169
    • 0012044768 scopus 로고
    • Studies on nuclear fine structure
    • Swift H. 1959 Studies on nuclear fine structure Brookhaven Symp Biol 12 : 134-52
    • (1959) Brookhaven Symp Biol , vol.12 , pp. 134-152
    • Swift, H.1
  • 170
    • 0033536063 scopus 로고    scopus 로고
    • P19 ARF stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • Tao W, Levine AJ 1999 P19 ARF stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2 Proc Natl Acad Sci 96 : 6937-41
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 171
    • 26244459242 scopus 로고    scopus 로고
    • Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin
    • Takagi M, Absalon MJ , McLure KG , Kastan MB 2005 Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin Cell 123 : 49-63
    • (2005) Cell , vol.123 , pp. 49-63
    • Takagi, M.1    Absalon, M.J.2    McLure, K.G.3    Kastan, M.B.4
  • 173
    • 2342547025 scopus 로고    scopus 로고
    • Sam68 exerts separable effects on cell cycle progression and apoptosis
    • Taylor SJ, Resnick RJ , Shalloway D .2004 Sam68 exerts separable effects on cell cycle progression and apoptosis BMC Cell Biol 5 : 5
    • (2004) BMC Cell Biol , vol.5 , pp. 5
    • Taylor, S.J.1    Resnick, R.J.2    Shalloway, D.3
  • 175
    • 36749100886 scopus 로고    scopus 로고
    • Toward a high-resolution view of nuclear dynamics
    • Trinkle, Mulcahy L , Lamond AI 2007 Toward a high-resolution view of nuclear dynamics Science 318 : 1402-7
    • (2007) Science , vol.318 , pp. 1402-1407
    • Trinkle, M.L.1    Lamond, A.I.2
  • 178
    • 0033678851 scopus 로고    scopus 로고
    • The nucleolus: a magicians hat for cell cycle tricks
    • Visintin R, Amon A 2000 The nucleolus: a magicians hat for cell cycle tricks Curr Opin Cell Biol 12 : 752 .
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 752
    • Visintin, R.1    Amon, A.2
  • 179
    • 0033614303 scopus 로고    scopus 로고
    • Cfi1 prevents premature exit from mitosis by anchoring Cdc14 phosphatase in the nucleolus
    • Visintin R, Hwang ES , Amon A 1999 Cfi1 prevents premature exit from mitosis by anchoring Cdc14 phosphatase in the nucleolus Nature 398 : 818-23
    • (1999) Nature , vol.398 , pp. 818-823
    • Visintin, R.1    Hwang, E.S.2    Amon, A.3
  • 180
    • 1842334436 scopus 로고    scopus 로고
    • Mechanism of repression of RNA polymerase I transcription by the retinoblastoma protein
    • Voit R, Schafer K , Grummt I 1997 Mechanism of repression of RNA polymerase I transcription by the retinoblastoma protein Mol Cell Biol 17 : 4230-7
    • (1997) Mol Cell Biol , vol.17 , pp. 4230-4237
    • Voit, R.1    Schafer, K.2    Grummt, I.3
  • 182
    • 0033398254 scopus 로고    scopus 로고
    • Chromatin-association of the Polycomb group protein BMI1 is cell cycle-regulated and correlates with its phosphorylation status
    • Voncken JW Schweizer D , Aagaard L , Sattler L , Jantsch MF , van Lohuizen M 1999 Chromatin-association of the Polycomb group protein BMI1 is cell cycle-regulated and correlates with its phosphorylation status J Cell Sci 112 : 4627-39
    • (1999) J Cell Sci , vol.112 , pp. 4627-4639
    • Voncken, J.W.1    Schweizer, D.2    Aagaard, L.3    Sattler, L.4    Jantsch, M.F.5    van Lohuizen, M.6
  • 183
    • 41949111045 scopus 로고    scopus 로고
    • Acute promyelocytic leukemia: from highly fatal to highly curable
    • Wang ZY, Chen Z 2008 Acute promyelocytic leukemia: from highly fatal to highly curable Blood 111 : 2505-15
    • (2008) Blood , vol.111 , pp. 2505-2515
    • Wang, Z.Y.1    Chen, Z.2
  • 184
    • 0038647454 scopus 로고    scopus 로고
    • RNA polymerase III transcripts and the PTB domain are essential for the integrity of the perinucleolar compartment
    • Wang C, Politz JC , Pederson T , Huang S 2003 RNA polymerase III transcripts and the PTB domain are essential for the integrity of the perinucleolar compartment Mol Biol Cell 14 : 2425-35
    • (2003) Mol Biol Cell , vol.14 , pp. 2425-2435
    • Wang, C.1    Politz, J.C.2    Pederson, T.3    Huang, S.4
  • 185
    • 0027305616 scopus 로고
    • Fluorescent labelling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus
    • Wansink DG, Schul W , van der Kraan I , van Steensel B , van Driel R , de Jong L 1993 Fluorescent labelling of nascent RNA reveals transcription by RNA polymerase II in domains scattered throughout the nucleus J Cell Biol 122 : 283-93
    • (1993) J Cell Biol , vol.122 , pp. 283-293
    • Wansink, D.G.1    Schul, W.2    van der Kraan, I.3    van Steensel, B.4    van Driel, R.5    de Jong, L.6
  • 187
    • 0036061468 scopus 로고    scopus 로고
    • Subchromosomal positioning of the epidermal differentiation complex (EDC) in keratinocyte and lymphoblast interphase nuclei
    • Williams RRE, Broad S , Sheer D , Ragoussis J 2002 Subchromosomal positioning of the epidermal differentiation complex (EDC) in keratinocyte and lymphoblast interphase nuclei Exp Cell Res 272 : 163-75
    • (2002) Exp Cell Res , vol.272 , pp. 163-175
    • Williams, R.R.E.1    Broad, S.2    Sheer, D.3    Ragoussis, J.4
  • 189
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/ SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao SH, Manley JL 1997 Phosphorylation of the ASF/ SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing Genes Dev 11 : 334-44
    • (1997) Genes Dev , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 190
    • 0032476604 scopus 로고    scopus 로고
    • Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2
    • Xiao SH, Manley JL 1998 Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2 EMBO J 17 : 6359-67
    • (1998) EMBO J , vol.17 , pp. 6359-6367
    • Xiao, S.H.1    Manley, J.L.2
  • 191
    • 0034194444 scopus 로고    scopus 로고
    • The relationship between SMN, the spinal muscular atrophy protein, and nuclear coiled bodies in differentiated tissues and cultured cells
    • Young PJ, Le TT , thi Man N , Burghes AH , Morris GE 2000 The relationship between SMN, the spinal muscular atrophy protein, and nuclear coiled bodies in differentiated tissues and cultured cells Exp Cell Res 256 : 365-74
    • (2000) Exp Cell Res , vol.256 , pp. 365-374
    • Young, P.J.1    Le, T.T.2    thi Man, N.3    Burghes, A.H.4    Morris, G.E.5
  • 192
    • 0033867975 scopus 로고    scopus 로고
    • Repression of RNA polymerase I transcription by the tumor suppressor p53
    • Zhai W, Comai L 2000 Repression of RNA polymerase I transcription by the tumor suppressor p53 Mol Cell Biol 20 : 5930-8
    • (2000) Mol Cell Biol , vol.20 , pp. 5930-5938
    • Zhai, W.1    Comai, L.2
  • 193
    • 70350497397 scopus 로고    scopus 로고
    • Signaling to p53: ribosomal proteins find their way
    • Zhang Y , Lu H 2009 Signaling to p53: ribosomal proteins find their way Cancer Cell 16 : 369-77
    • (2009) Cancer Cell , vol.16 , pp. 369-377
    • Zhang, Y.1    Lu, H.2
  • 195
    • 0034186133 scopus 로고    scopus 로고
    • The transcriptional role of PML and the nuclear body
    • Zhong S, Salomoni P , Pandolfi PP 2000b The transcriptional role of PML and the nuclear body Nat Cell Biol 2 : E85-90
    • (2000) Nat Cell Biol , vol.2 , pp. 85-90
    • Zhong, S.1    Salomoni, P.2    Pandolfi, P.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.