메뉴 건너뛰기




Volumn 16, Issue 1, 2006, Pages 19-26

Subnuclear organelles: New insights into form and function

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA;

EID: 30444437477     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2005.11.005     Document Type: Review
Times cited : (208)

References (78)
  • 1
    • 0035150726 scopus 로고    scopus 로고
    • Origin of eukaryotic cell nuclei by symbiosis of Archaea in Bacteria is revealed by homology-hit analysis
    • T. Horiike Origin of eukaryotic cell nuclei by symbiosis of Archaea in Bacteria is revealed by homology-hit analysis Nat. Cell Biol. 3 2001 210 214
    • (2001) Nat. Cell Biol. , vol.3 , pp. 210-214
    • Horiike, T.1
  • 2
    • 0034851781 scopus 로고    scopus 로고
    • Nuclear domains
    • D.L. Spector Nuclear domains J. Cell Sci. 114 2001 2891 2893
    • (2001) J. Cell Sci. , vol.114 , pp. 2891-2893
    • Spector, D.L.1
  • 3
    • 0035365808 scopus 로고    scopus 로고
    • Functional architecture in the cell nucleus
    • M. Dundr, and T. Misteli Functional architecture in the cell nucleus Biochem. J. 356 2001 297 310
    • (2001) Biochem. J. , vol.356 , pp. 297-310
    • Dundr, M.1    Misteli, T.2
  • 4
    • 3142654673 scopus 로고    scopus 로고
    • Nuclear bodies and compartments: Functional roles and cellular signalling in health and disease
    • A. Zimber Nuclear bodies and compartments: functional roles and cellular signalling in health and disease Cell. Signal. 16 2004 1085 1104
    • (2004) Cell. Signal. , vol.16 , pp. 1085-1104
    • Zimber, A.1
  • 5
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • T. Misteli Protein dynamics: implications for nuclear architecture and gene expression Science 291 2001 843 847
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 6
    • 0036903022 scopus 로고    scopus 로고
    • Dynamics and genome-centricity of interchromatin domains in the nucleus
    • T. Pederson Dynamics and genome-centricity of interchromatin domains in the nucleus Nat. Cell Biol. 4 2002 E287 E291
    • (2002) Nat. Cell Biol. , vol.4
    • Pederson, T.1
  • 7
    • 0038022717 scopus 로고    scopus 로고
    • Dynamics of chromatin, proteins, and bodies within the cell nucleus
    • A. Belmont Dynamics of chromatin, proteins, and bodies within the cell nucleus Curr. Opin. Cell Biol. 15 2003 304 310
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 304-310
    • Belmont, A.1
  • 8
    • 0036323673 scopus 로고    scopus 로고
    • Large-scale isolation of Cajal bodies from HeLa cells
    • Y.W. Lam Large-scale isolation of Cajal bodies from HeLa cells Mol. Biol. Cell 13 2002 2461 2473
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2461-2473
    • Lam, Y.W.1
  • 9
    • 0036856312 scopus 로고    scopus 로고
    • Functional proteomic analysis of human nucleolus
    • A. Scherl Functional proteomic analysis of human nucleolus Mol. Biol. Cell 13 2002 4100 4109
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4100-4109
    • Scherl, A.1
  • 10
    • 0346095273 scopus 로고    scopus 로고
    • Bioinformatic analysis of the nucleolus
    • A.K. Leung Bioinformatic analysis of the nucleolus Biochem. J. 376 2003 553 569
    • (2003) Biochem. J. , vol.376 , pp. 553-569
    • Leung, A.K.1
  • 11
    • 19944400417 scopus 로고    scopus 로고
    • Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar functions
    • A.F. Pendle Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar functions Mol. Biol. Cell 16 2005 260 269
    • (2005) Mol. Biol. Cell , vol.16 , pp. 260-269
    • Pendle, A.F.1
  • 12
    • 11944274520 scopus 로고    scopus 로고
    • Nucleolar proteome dynamics
    • J.S. Andersen Nucleolar proteome dynamics Nature 433 2005 77 83
    • (2005) Nature , vol.433 , pp. 77-83
    • Andersen, J.S.1
  • 13
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • T. Misteli The concept of self-organization in cellular architecture J. Cell Biol. 155 2001 181 185
    • (2001) J. Cell Biol. , vol.155 , pp. 181-185
    • Misteli, T.1
  • 14
    • 0014510121 scopus 로고
    • Fine structural organization of the interphase nucleus in some mammalian cells
    • A. Monneron, and W. Bernhard Fine structural organization of the interphase nucleus in some mammalian cells J. Ultrastruct. Res. 27 1969 266 288
    • (1969) J. Ultrastruct. Res. , vol.27 , pp. 266-288
    • Monneron, A.1    Bernhard, W.2
  • 15
    • 0034524515 scopus 로고    scopus 로고
    • Cajal bodies: The first 100 years
    • J.G. Gall Cajal bodies: the first 100 years Annu. Rev. Cell Dev. Biol. 16 2000 273 300
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 273-300
    • Gall, J.G.1
  • 17
    • 11144328968 scopus 로고    scopus 로고
    • Cajal bodies, nucleoli, and speckles in the Xenopus oocyte nucleus have a low-density, sponge-like structure
    • K.E. Handwerger Cajal bodies, nucleoli, and speckles in the Xenopus oocyte nucleus have a low-density, sponge-like structure Mol. Biol. Cell 16 2005 202 211
    • (2005) Mol. Biol. Cell , vol.16 , pp. 202-211
    • Handwerger, K.E.1
  • 18
    • 0032837037 scopus 로고    scopus 로고
    • The movement of coiled bodies visualized in living plant cells by the green fluorescent protein
    • K. Boudonck The movement of coiled bodies visualized in living plant cells by the green fluorescent protein Mol. Biol. Cell 10 1999 2297 2307
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2297-2307
    • Boudonck, K.1
  • 19
    • 0034739848 scopus 로고    scopus 로고
    • In vivo analysis of Cajal body movement, separation, and joining in live human cells
    • M. Platani In vivo analysis of Cajal body movement, separation, and joining in live human cells J. Cell Biol. 151 2000 1561 1574
    • (2000) J. Cell Biol. , vol.151 , pp. 1561-1574
    • Platani, M.1
  • 20
    • 0036302047 scopus 로고    scopus 로고
    • Cajal body dynamics and association with chromatin are ATP-dependent
    • M. Platani Cajal body dynamics and association with chromatin are ATP-dependent Nat. Cell Biol. 4 2002 502 508
    • (2002) Nat. Cell Biol. , vol.4 , pp. 502-508
    • Platani, M.1
  • 21
    • 10144235484 scopus 로고    scopus 로고
    • 4-D single particle tracking of synthetic and proteinaceous microspheres reveals preferential movement of nuclear particles along chromatin-poor tracks
    • C.P. Bacher 4-D single particle tracking of synthetic and proteinaceous microspheres reveals preferential movement of nuclear particles along chromatin-poor tracks BMC Cell Biol. 5 2004 45
    • (2004) BMC Cell Biol. , vol.5 , pp. 45
    • Bacher, C.P.1
  • 22
    • 0038526320 scopus 로고    scopus 로고
    • Cajal body proteins SMN and Coilin show differential dynamic behaviour in vivo
    • J.E. Sleeman Cajal body proteins SMN and Coilin show differential dynamic behaviour in vivo J. Cell Sci. 116 2003 2039 2050
    • (2003) J. Cell Sci. , vol.116 , pp. 2039-2050
    • Sleeman, J.E.1
  • 23
    • 17844384835 scopus 로고    scopus 로고
    • The nucleolus
    • Y.W. Lam The nucleolus J. Cell Sci. 118 2005 1335 1337
    • (2005) J. Cell Sci. , vol.118 , pp. 1335-1337
    • Lam, Y.W.1
  • 24
    • 0036703330 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases generates RNA and protein diversity
    • M. Schaub, and W. Keller RNA editing by adenosine deaminases generates RNA and protein diversity Biochimie 84 2002 791 803
    • (2002) Biochimie , vol.84 , pp. 791-803
    • Schaub, M.1    Keller, W.2
  • 25
    • 0035997389 scopus 로고    scopus 로고
    • RNA editing by adenosine deaminases that act on RNA
    • B.L. Bass RNA editing by adenosine deaminases that act on RNA Annu. Rev. Biochem. 71 2002 817 846
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 817-846
    • Bass, B.L.1
  • 26
    • 4544284817 scopus 로고    scopus 로고
    • Seven novel mutations of the ADAR gene in Chinese families and sporadic patients with dyschromatosis symmetrica hereditaria (DSH)
    • X.J. Zhang Seven novel mutations of the ADAR gene in Chinese families and sporadic patients with dyschromatosis symmetrica hereditaria (DSH) Hum. Mutat. 23 2004 629 630
    • (2004) Hum. Mutat. , vol.23 , pp. 629-630
    • Zhang, X.J.1
  • 27
    • 0345133268 scopus 로고    scopus 로고
    • Modulation of RNA editing by functional nucleolar sequestration of ADAR2
    • C.L. Sansam Modulation of RNA editing by functional nucleolar sequestration of ADAR2 Proc. Natl. Acad. Sci. U. S. A. 100 2003 14018 14023
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14018-14023
    • Sansam, C.L.1
  • 28
    • 13844294281 scopus 로고    scopus 로고
    • A multistep, GTP-driven mechanism controlling the dynamic cycling of nucleostemin
    • R.Y. Tsai, and R.D. McKay A multistep, GTP-driven mechanism controlling the dynamic cycling of nucleostemin J. Cell Biol. 168 2005 179 184
    • (2005) J. Cell Biol. , vol.168 , pp. 179-184
    • Tsai, R.Y.1    McKay, R.D.2
  • 29
    • 13844252078 scopus 로고    scopus 로고
    • Going in GTP cycles in the nucleolus
    • T. Misteli Going in GTP cycles in the nucleolus J. Cell Biol. 168 2005 177 178
    • (2005) J. Cell Biol. , vol.168 , pp. 177-178
    • Misteli, T.1
  • 30
    • 0037064572 scopus 로고    scopus 로고
    • Signal recognition particle RNA localization within the nucleolus differs from the classical sites of ribosome synthesis
    • J.C. Politz Signal recognition particle RNA localization within the nucleolus differs from the classical sites of ribosome synthesis J. Cell Biol. 159 2002 411 418
    • (2002) J. Cell Biol. , vol.159 , pp. 411-418
    • Politz, J.C.1
  • 31
    • 18044396522 scopus 로고    scopus 로고
    • Telomeres, telomerase and malignant transformation
    • O.G. Opitz Telomeres, telomerase and malignant transformation Curr. Mol. Med. 5 2005 219 226
    • (2005) Curr. Mol. Med. , vol.5 , pp. 219-226
    • Opitz, O.G.1
  • 32
    • 10944266466 scopus 로고    scopus 로고
    • Nucleolin interacts with telomerase
    • S. Khurts Nucleolin interacts with telomerase J. Biol. Chem. 279 2004 51508 51515
    • (2004) J. Biol. Chem. , vol.279 , pp. 51508-51515
    • Khurts, S.1
  • 33
    • 0036732390 scopus 로고    scopus 로고
    • Keeping telomerase in its place
    • R.S. Maser, and R.A. DePinho Keeping telomerase in its place Nat. Med. 8 2002 934 936
    • (2002) Nat. Med. , vol.8 , pp. 934-936
    • Maser, R.S.1    Depinho, R.A.2
  • 34
    • 0036711651 scopus 로고    scopus 로고
    • Subnuclear shuttling of human telomerase induced by transformation and DNA damage
    • J.M. Wong Subnuclear shuttling of human telomerase induced by transformation and DNA damage Nat. Cell Biol. 4 2002 731 736
    • (2002) Nat. Cell Biol. , vol.4 , pp. 731-736
    • Wong, J.M.1
  • 35
    • 8844239874 scopus 로고    scopus 로고
    • SRP-mediated protein targeting: Structure and function revisited
    • J. Luirink, and I. Sinning SRP-mediated protein targeting: structure and function revisited Biochim. Biophys. Acta 1694 2004 17 35
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 17-35
    • Luirink, J.1    Sinning, I.2
  • 36
    • 0032493374 scopus 로고    scopus 로고
    • Localization of signal recognition particle RNA in the nucleolus of mammalian cells
    • M.R. Jacobson, and T. Pederson Localization of signal recognition particle RNA in the nucleolus of mammalian cells Proc. Natl. Acad. Sci. U. S. A. 95 1998 7981 7986
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7981-7986
    • Jacobson, M.R.1    Pederson, T.2
  • 37
    • 0034602645 scopus 로고    scopus 로고
    • Signal recognition particle components in the nucleolus
    • J.C. Politz Signal recognition particle components in the nucleolus Proc. Natl. Acad. Sci. U. S. A. 97 2000 55 60
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 55-60
    • Politz, J.C.1
  • 38
    • 17244366460 scopus 로고    scopus 로고
    • Signal recognition particle assembly in relation to the function of amplified nucleoli of Xenopus oocytes
    • J. Sommerville Signal recognition particle assembly in relation to the function of amplified nucleoli of Xenopus oocytes J. Cell Sci. 118 2005 1299 1307
    • (2005) J. Cell Sci. , vol.118 , pp. 1299-1307
    • Sommerville, J.1
  • 39
    • 0035858874 scopus 로고    scopus 로고
    • Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export
    • H. Grosshans Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export J. Cell Biol. 153 2001 745 762
    • (2001) J. Cell Biol. , vol.153 , pp. 745-762
    • Grosshans, H.1
  • 41
    • 0035827267 scopus 로고    scopus 로고
    • A role for Cajal bodies in assembly of the nuclear transcription machinery
    • J.G. Gall A role for Cajal bodies in assembly of the nuclear transcription machinery FEBS Lett. 498 2001 164 167
    • (2001) FEBS Lett. , vol.498 , pp. 164-167
    • Gall, J.G.1
  • 42
    • 0037078322 scopus 로고    scopus 로고
    • Cajal bodies and coilin - Moving towards function
    • S.C. Ogg, and A.I. Lamond Cajal bodies and coilin - moving towards function J. Cell Biol. 159 2002 17 21
    • (2002) J. Cell Biol. , vol.159 , pp. 17-21
    • Ogg, S.C.1    Lamond, A.I.2
  • 43
    • 0030656387 scopus 로고    scopus 로고
    • Sno storm in the nucleolus: New roles for myriad small RNPs
    • C.M. Smith, and J.A. Steitz Sno storm in the nucleolus: new roles for myriad small RNPs Cell 89 1997 669 672
    • (1997) Cell , vol.89 , pp. 669-672
    • Smith, C.M.1    Steitz, J.A.2
  • 44
    • 0036703184 scopus 로고    scopus 로고
    • The expanding snoRNA world
    • J.P. Bachellerie The expanding snoRNA world Biochimie 84 2002 775 790
    • (2002) Biochimie , vol.84 , pp. 775-790
    • Bachellerie, J.P.1
  • 45
    • 0032189145 scopus 로고    scopus 로고
    • Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing
    • Y.T. Yu Modifications of U2 snRNA are required for snRNP assembly and pre-mRNA splicing EMBO J. 17 1998 5783 5795
    • (1998) EMBO J. , vol.17 , pp. 5783-5795
    • Yu, Y.T.1
  • 46
    • 0037013831 scopus 로고    scopus 로고
    • Cajal body-specific small nuclear RNAs: A novel class of 2′-O-methylation and pseudouridylation guide RNAs
    • X. Darzacq Cajal body-specific small nuclear RNAs: a novel class of 2′-O-methylation and pseudouridylation guide RNAs EMBO J. 21 2002 2746 2756
    • (2002) EMBO J. , vol.21 , pp. 2746-2756
    • Darzacq, X.1
  • 47
    • 0344080588 scopus 로고    scopus 로고
    • Modification of Sm small nuclear RNAs occurs in the nucleoplasmic Cajal body following import from the cytoplasm
    • B.E. Jady Modification of Sm small nuclear RNAs occurs in the nucleoplasmic Cajal body following import from the cytoplasm EMBO J. 22 2003 1878 1888
    • (2003) EMBO J. , vol.22 , pp. 1878-1888
    • Jady, B.E.1
  • 48
    • 0037450726 scopus 로고    scopus 로고
    • Steady-state dynamics of Cajal body components in the Xenopus germinal vesicle
    • K.E. Handwerger Steady-state dynamics of Cajal body components in the Xenopus germinal vesicle J. Cell Biol. 160 2003 495 504
    • (2003) J. Cell Biol. , vol.160 , pp. 495-504
    • Handwerger, K.E.1
  • 49
    • 1842687498 scopus 로고    scopus 로고
    • Dynamics of coilin in Cajal bodies of the Xenopus germinal vesicle
    • S. Deryusheva, and J.G. Gall Dynamics of coilin in Cajal bodies of the Xenopus germinal vesicle Proc. Natl. Acad. Sci. U. S. A. 101 2004 4810 4814
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4810-4814
    • Deryusheva, S.1    Gall, J.G.2
  • 50
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • C.L. Will, and R. Luhrmann Spliceosomal UsnRNP biogenesis, structure and function Curr. Opin. Cell Biol. 13 2001 290 301
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 51
    • 4143124637 scopus 로고    scopus 로고
    • RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 di-snRNPs in Cajal bodies
    • N. Schaffert RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 di-snRNPs in Cajal bodies EMBO J. 23 2004 3000 3009
    • (2004) EMBO J. , vol.23 , pp. 3000-3009
    • Schaffert, N.1
  • 52
    • 4644309827 scopus 로고    scopus 로고
    • Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer
    • D. Stanek, and K.M. Neugebauer Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer J. Cell Biol. 166 2004 1015 1025
    • (2004) J. Cell Biol. , vol.166 , pp. 1015-1025
    • Stanek, D.1    Neugebauer, K.M.2
  • 53
    • 5444231229 scopus 로고    scopus 로고
    • A role for Cajal bodies in the final steps of U2 snRNP biogenesis
    • D. Nesic A role for Cajal bodies in the final steps of U2 snRNP biogenesis J. Cell Sci. 117 2004 4423 4433
    • (2004) J. Cell Sci. , vol.117 , pp. 4423-4433
    • Nesic, D.1
  • 54
    • 1842813934 scopus 로고    scopus 로고
    • Telomerase RNA structure and function: Implications for dyskeratosis congenita
    • J.L. Chen, and C.W. Greider Telomerase RNA structure and function: implications for dyskeratosis congenita Trends Biochem. Sci. 29 2004 183 192
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 183-192
    • Chen, J.L.1    Greider, C.W.2
  • 55
    • 0035887042 scopus 로고    scopus 로고
    • Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein
    • M.D. Hebert Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein Genes Dev. 15 2001 2720 2729
    • (2001) Genes Dev. , vol.15 , pp. 2720-2729
    • Hebert, M.D.1
  • 56
    • 0037164866 scopus 로고    scopus 로고
    • Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing
    • F.M. Boisvert Symmetrical dimethylarginine methylation is required for the localization of SMN in Cajal bodies and pre-mRNA splicing J. Cell Biol. 159 2002 957 969
    • (2002) J. Cell Biol. , vol.159 , pp. 957-969
    • Boisvert, F.M.1
  • 57
    • 0036746771 scopus 로고    scopus 로고
    • Coilin methylation regulates nuclear body formation
    • M.D. Hebert Coilin methylation regulates nuclear body formation Dev. Cell 3 2002 329 337
    • (2002) Dev. Cell , vol.3 , pp. 329-337
    • Hebert, M.D.1
  • 58
    • 0037439633 scopus 로고    scopus 로고
    • Control of Cajal body number is mediated by the coilin C-terminus
    • K.B. Shpargel Control of Cajal body number is mediated by the coilin C-terminus J. Cell Sci. 116 2003 303 312
    • (2003) J. Cell Sci. , vol.116 , pp. 303-312
    • Shpargel, K.B.1
  • 59
    • 0041669439 scopus 로고    scopus 로고
    • Nuclear speckles: A model for nuclear organelles
    • A.I. Lamond, and D.L. Spector Nuclear speckles: a model for nuclear organelles Nat. Rev. Mol. Cell Biol. 4 2003 605 612
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 605-612
    • Lamond, A.I.1    Spector, D.L.2
  • 60
    • 0032547829 scopus 로고    scopus 로고
    • Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo
    • T. Misteli Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo J. Cell Biol. 143 1998 297 307
    • (1998) J. Cell Biol. , vol.143 , pp. 297-307
    • Misteli, T.1
  • 61
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • J.E. Mermoud Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism EMBO J. 13 1994 5679 5688
    • (1994) EMBO J. , vol.13 , pp. 5679-5688
    • Mermoud, J.E.1
  • 62
    • 0037017406 scopus 로고    scopus 로고
    • Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing
    • P. Sacco-Bubulya, and D.L. Spector Disassembly of interchromatin granule clusters alters the coordination of transcription and pre-mRNA splicing J. Cell Biol. 156 2002 425 436
    • (2002) J. Cell Biol. , vol.156 , pp. 425-436
    • Sacco-Bubulya, P.1    Spector, D.L.2
  • 63
    • 4344559662 scopus 로고    scopus 로고
    • Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles
    • C.L. Lin Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR family splicing factors from nuclear speckles Biochem. Biophys. Res. Commun. 321 2004 638 647
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 638-647
    • Lin, C.L.1
  • 64
    • 0037013939 scopus 로고    scopus 로고
    • Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments
    • C. Verheggen Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments EMBO J. 21 2002 2736 2745
    • (2002) EMBO J. , vol.21 , pp. 2736-2745
    • Verheggen, C.1
  • 65
    • 0028256467 scopus 로고
    • Coiled bodies in the nucleolus of breast cancer cells
    • R.L. Ochs Coiled bodies in the nucleolus of breast cancer cells J. Cell Sci. 107 1994 385 399
    • (1994) J. Cell Sci. , vol.107 , pp. 385-399
    • Ochs, R.L.1
  • 66
    • 0037092504 scopus 로고    scopus 로고
    • Heat shock induces mini-Cajal bodies in the Xenopus germinal vesicle
    • K.E. Handwerger Heat shock induces mini-Cajal bodies in the Xenopus germinal vesicle J. Cell Sci. 115 2002 2011 2020
    • (2002) J. Cell Sci. , vol.115 , pp. 2011-2020
    • Handwerger, K.E.1
  • 67
    • 0034193778 scopus 로고    scopus 로고
    • The nucleolus: An old factory with unexpected capabilities
    • M.O. Olson The nucleolus: an old factory with unexpected capabilities Trends Cell Biol. 10 2000 189 196
    • (2000) Trends Cell Biol. , vol.10 , pp. 189-196
    • Olson, M.O.1
  • 68
    • 0038699142 scopus 로고    scopus 로고
    • The nucleolus: A site of ribonucleoprotein maturation
    • S.A. Gerbi The nucleolus: a site of ribonucleoprotein maturation Curr. Opin. Cell Biol. 15 2003 318 325
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 318-325
    • Gerbi, S.A.1
  • 69
    • 1542569574 scopus 로고    scopus 로고
    • Cajal bodies
    • A.G. Matera Cajal bodies Curr. Biol. 13 2003 R503
    • (2003) Curr. Biol. , vol.13 , pp. 503
    • Matera, A.G.1
  • 70
    • 0036591880 scopus 로고    scopus 로고
    • The SMN complex, an assemblyosome of ribonucleoproteins
    • S. Paushkin The SMN complex, an assemblyosome of ribonucleoproteins Curr. Opin. Cell Biol. 14 2002 305 312
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 305-312
    • Paushkin, S.1
  • 71
    • 0034081740 scopus 로고    scopus 로고
    • The role of SMN in spinal muscular atrophy
    • S. Jablonka The role of SMN in spinal muscular atrophy J. Neurol. 247 Suppl 1 2000 I37 I42
    • (2000) J. Neurol. , vol.247 , Issue.1 SUPPL.
    • Jablonka, S.1
  • 72
    • 0035654399 scopus 로고    scopus 로고
    • Kinetic modelling approaches to in vivo imaging
    • R.D. Phair, and T. Misteli Kinetic modelling approaches to in vivo imaging Nat. Rev. Mol. Cell Biol. 2 2001 898 907
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 898-907
    • Phair, R.D.1    Misteli, T.2
  • 73
    • 0036849935 scopus 로고    scopus 로고
    • Macromolecular mobility inside the cell nucleus
    • M. Carmo-Fonseca Macromolecular mobility inside the cell nucleus Trends Cell Biol. 12 2002 491 495
    • (2002) Trends Cell Biol. , vol.12 , pp. 491-495
    • Carmo-Fonseca, M.1
  • 74
    • 0037598647 scopus 로고    scopus 로고
    • Computational imaging in cell biology
    • R. Eils, and C. Athale Computational imaging in cell biology J. Cell Biol. 161 2003 477 481
    • (2003) J. Cell Biol. , vol.161 , pp. 477-481
    • Eils, R.1    Athale, C.2
  • 75
    • 12144290254 scopus 로고    scopus 로고
    • In vivo kinetics of Cajal body components
    • M. Dundr In vivo kinetics of Cajal body components J. Cell Biol. 164 2004 831 842
    • (2004) J. Cell Biol. , vol.164 , pp. 831-842
    • Dundr, M.1
  • 76
    • 2142823918 scopus 로고    scopus 로고
    • On the movements of nuclear components in living cells
    • P.A. Bubulya, and D.L. Spector On the movements of nuclear components in living cells Exp. Cell Res. 296 2004 4 11
    • (2004) Exp. Cell Res. , vol.296 , pp. 4-11
    • Bubulya, P.A.1    Spector, D.L.2
  • 77
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • G.H. Patterson, and J. Lippincott-Schwartz A photoactivatable GFP for selective photolabeling of proteins and cells Science 297 2002 1873 1877
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 78
    • 0346099349 scopus 로고    scopus 로고
    • Telomerase RNA accumulates in Cajal bodies in human cancer cells
    • Y. Zhu Telomerase RNA accumulates in Cajal bodies in human cancer cells Mol. Biol. Cell 15 2004 81 90
    • (2004) Mol. Biol. Cell , vol.15 , pp. 81-90
    • Zhu, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.