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Volumn 117, Issue 12, 2004, Pages 2481-2490

Actin-and protien-4.1-containing filaments link nuclear pore complexes to subnuclear organelles in Xenopus oocyte nuclei

Author keywords

Actin; Cajal bodies; Nuclear matrix; Nuclear pore complex; Nucleocytoplasmic transport; Nucleous; Protien 4.1

Indexed keywords

ACTIN; ERYTHROCYTE BAND 4.1 PROTEIN; JASPAMIDE; LATRUNCULIN A; CYTOSKELETON PROTEIN; DEPSIPEPTIDE; FUSED HETEROCYCLIC RINGS; MEMBRANE PROTEIN; THIAZOLE DERIVATIVE; THIAZOLIDINE DERIVATIVE;

EID: 3042777656     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01098     Document Type: Article
Times cited : (122)

References (82)
  • 1
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., Cohn, J., Buhle, L. and Gerace, L. (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323, 560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 2
    • 0032419950 scopus 로고    scopus 로고
    • The nuclear basket of the nuclear pore complex is part of a higher-order filamentous network that is related to chromatin
    • Arlucea, J., Andrade, R., Alonso, R. and Arechaga, J. (1998). The nuclear basket of the nuclear pore complex is part of a higher-order filamentous network that is related to chromatin. J. Struct. Biol. 124, 51-58.
    • (1998) J. Struct. Biol. , vol.124 , pp. 51-58
    • Arlucea, J.1    Andrade, R.2    Alonso, R.3    Arechaga, J.4
  • 4
    • 0026040680 scopus 로고
    • Association of RNA with the B and C snurposomes of Xenopus oocyte nuclei
    • Callan, H. G. and Gall, J. G. (1991). Association of RNA with the B and C snurposomes of Xenopus oocyte nuclei. Chromosoma 101, 69-82.
    • (1991) Chromosoma , vol.101 , pp. 69-82
    • Callan, H.G.1    Gall, J.G.2
  • 6
    • 0017716157 scopus 로고
    • Diffusible and bound actin in nuclei of Xenopus laevis oocytes
    • Clark, T. G. and Merriam, R. W. (1977). Diffusible and bound actin in nuclei of Xenopus laevis oocytes. Cell 12, 883-891.
    • (1977) Cell , vol.12 , pp. 883-891
    • Clark, T.G.1    Merriam, R.W.2
  • 7
    • 0018601589 scopus 로고
    • An actin filament matrix in hand-isolated nuclei of X. laevis oocytes
    • Clark, T. G. and Rosenbaum, J. L. (1979). An actin filament matrix in hand-isolated nuclei of X. laevis oocytes. Cell 18, 1101-1108.
    • (1979) Cell , vol.18 , pp. 1101-1108
    • Clark, T.G.1    Rosenbaum, J.L.2
  • 8
    • 0141764733 scopus 로고    scopus 로고
    • Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans
    • Cohen, M., Feinstein, N., Wilson, K. L. and Gruenbaum, Y. (2003). Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans. Mol. Biol. Cell 14, 4230-4237.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4230-4237
    • Cohen, M.1    Feinstein, N.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 10
    • 0031043895 scopus 로고    scopus 로고
    • Identification of protein 270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments
    • Cordes, V., Reidenbach, S., Rackwitz, H. R. and Franke, W. W. (1997). Identification of protein 270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol. 136, 515-529.
    • (1997) J. Cell Biol. , vol.136 , pp. 515-529
    • Cordes, V.1    Reidenbach, S.2    Rackwitz, H.R.3    Franke, W.W.4
  • 11
    • 0025952352 scopus 로고
    • Characterization of isoforms of protein 4.1 present in the nucleus
    • Correas, I. (1991). Characterization of isoforms of protein 4.1 present in the nucleus. Biochem. J. 279, 581-585.
    • (1991) Biochem. J. , vol.279 , pp. 581-585
    • Correas, I.1
  • 14
    • 0029616406 scopus 로고
    • Protein 4.1 is a component of the nuclear matrix of mammalian cells
    • De Carcer, G., Lallena, M. J. and Correas, I. (1995). Protein 4.1 is a component of the nuclear matrix of mammalian cells. Biochem. J. 312, 871-877.
    • (1995) Biochem. J. , vol.312 , pp. 871-877
    • De Carcer, G.1    Lallena, M.J.2    Correas, I.3
  • 16
    • 0037043334 scopus 로고    scopus 로고
    • Interference with the cytoplasmic tail of gp210 disrupts 'close apposition' of nuclear membranes and blocks nuclear pore dilation
    • Drummond, S. P. and Wilson, K. L. (2002). Interference with the cytoplasmic tail of gp210 disrupts 'close apposition' of nuclear membranes and blocks nuclear pore dilation. J. Cell Biol. 158, 53-62.
    • (2002) J. Cell Biol. , vol.158 , pp. 53-62
    • Drummond, S.P.1    Wilson, K.L.2
  • 17
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg, J., Siggia, E. D., Moreira, J. E., Smith, C. L., Presley, J. F., Worman, H. J. and Lippencott-Schwartz, J. (1997). Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138, 1193-1206.
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippencott-Schwartz, J.7
  • 18
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: Nucleocytoplasmic transport and beyond
    • Fahrenkrog, B. and Aebi, U. (2003). The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat. Rev. Mol. Cell Biol. 4, 757-766.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 19
    • 0031454975 scopus 로고    scopus 로고
    • The location of the transport gate in the nuclear pore complex
    • Feldherr, C. M. and Akin, D. (1997). The location of the transport gate in the nuclear pore complex. J. Cell Sci. 110, 3065-3070.
    • (1997) J. Cell Sci. , vol.110 , pp. 3065-3070
    • Feldherr, C.M.1    Akin, D.2
  • 20
    • 0035853099 scopus 로고    scopus 로고
    • The nucleoporin Nup98 associates with the intranuclear filamentous protein network of TPR
    • Fontoura, B. M. A., Dales, S., Blobel, G. and Zhong, H. (2001). The nucleoporin Nup98 associates with the intranuclear filamentous protein network of TPR. Proc. Natl. Acad. Sci. USA 98, 3208-3213.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3208-3213
    • Fontoura, B.M.A.1    Dales, S.2    Blobel, G.3    Zhong, H.4
  • 21
    • 0037128215 scopus 로고    scopus 로고
    • Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export
    • Frosst, P., Guan, T., Subauste, C., Hahn, K. and Gerace, L. (2002). Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J. Cell Biol. 156, 617-630.
    • (2002) J. Cell Biol. , vol.156 , pp. 617-630
    • Frosst, P.1    Guan, T.2    Subauste, C.3    Hahn, K.4    Gerace, L.5
  • 22
    • 0029617666 scopus 로고
    • Immunocytochemical localization of actin in the nucleolus of rat oocytes
    • Funaki, K., Katsumoto, T. and Iino, A. (1995). Immunocytochemical localization of actin in the nucleolus of rat oocytes. Biol. Cell 84, 139-146.
    • (1995) Biol. Cell , vol.84 , pp. 139-146
    • Funaki, K.1    Katsumoto, T.2    Iino, A.3
  • 23
    • 0032740248 scopus 로고    scopus 로고
    • Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes
    • Gall, J. G., Bellini, M., Wu, Z. and Murphy, C. (1999). Assembly of the nuclear transcription and processing machinery: Cajal bodies (coiled bodies) and transcriptosomes. Mol. Biol. Cell 10, 4385-4402.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4385-4402
    • Gall, J.G.1    Bellini, M.2    Wu, Z.3    Murphy, C.4
  • 25
    • 0031056904 scopus 로고    scopus 로고
    • Dimples, pores, star-rings and thin rings on growing nuclear envelopes: Evidence for structural intermediates in nuclear pore complex assembly
    • Goldberg, M. W., Wiese, C., Allen, T. D. and Wilson, K. L. (1997). Dimples, pores, star-rings and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly. J. Cell Sci. 110, 409-420.
    • (1997) J. Cell Sci. , vol.110 , pp. 409-420
    • Goldberg, M.W.1    Wiese, C.2    Allen, T.D.3    Wilson, K.L.4
  • 26
    • 0036629334 scopus 로고    scopus 로고
    • Molecular evolution of the actin family
    • Goodson, H. V. and Hawse, W. F. (2002). Molecular evolution of the actin family. J. Cell Sci. 115, 2619-2622.
    • (2002) J. Cell Sci. , vol.115 , pp. 2619-2622
    • Goodson, H.V.1    Hawse, W.F.2
  • 27
    • 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
    • Grosshans, H., Deinert, K., Hurt, E. and Simos, G. (2001). 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, 745-761.
    • (2001) J. Cell Biol. , vol.153 , pp. 745-761
    • Grosshans, H.1    Deinert, K.2    Hurt, E.3    Simos, G.4
  • 28
    • 0034108049 scopus 로고    scopus 로고
    • Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup 153 to reforming functional nuclear envelopes
    • Haraguchi, T., Koujin, T., Kayakawa, T., Tsutsumi, C., Imamoto, N., Akazawa, C., Sukegawa, J., Yoneda, Y. and Hiraoka, Y. (2000). Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup 153 to reforming functional nuclear envelopes. J. Cell Sci. 113, 779-94.
    • (2000) J. Cell Sci. , vol.113 , pp. 779-794
    • Haraguchi, T.1    Koujin, T.2    Kayakawa, T.3    Tsutsumi, C.4    Imamoto, N.5    Akazawa, C.6    Sukegawa, J.7    Yoneda, Y.8    Hiraoka, Y.9
  • 30
    • 0038586471 scopus 로고    scopus 로고
    • Direct interaction with nup153 mediates binding of tpr to the periphery of the nuclear pore complex
    • Hase, M. E. and Cordes, V. C. (2003). Direct interaction with nup153 mediates binding of tpr to the periphery of the nuclear pore complex. Mol. Biol. Cell 14, 1923-1940.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1923-1940
    • Hase, M.E.1    Cordes, V.C.2
  • 31
    • 0035809913 scopus 로고    scopus 로고
    • Cofactor requirements for nuclear export of Rev response element (RRE)- And constitutive transport element (CTE)-containing retroviral RNAs: An unexpected role for actin
    • Hofmann, W., Reichart, B., Ewald, A., Muller, E., Schmitt, I., Stauber, H., Lottspeich, F., Jockusch, J. M., Scheer, U., Hauber, J. and Dabauvalle, M. C. (2001). Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs: An unexpected role for actin. J. Cell Biol. 152, 895-910.
    • (2001) J. Cell Biol. , vol.152 , pp. 895-910
    • Hofmann, W.1    Reichart, B.2    Ewald, A.3    Muller, E.4    Schmitt, I.5    Stauber, H.6    Lottspeich, F.7    Jockusch, J.M.8    Scheer, U.9    Hauber, J.10    Dabauvalle, M.C.11
  • 32
    • 0037205232 scopus 로고    scopus 로고
    • Chromatin boundaries in budding yeast: The nuclear pore connection
    • Ishii, K., Arib, G., Lin, C., van Housve, G. and Laemmli, U. K. (2002). Chromatin boundaries in budding yeast: the nuclear pore connection. Cell 31, 551-562.
    • (2002) Cell , vol.31 , pp. 551-562
    • Ishii, K.1    Arib, G.2    Lin, C.3    van Housve, G.4    Laemmli, U.K.5
  • 33
    • 0034110276 scopus 로고    scopus 로고
    • Rev-dependent association of the intron-containing HIV-1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin-B
    • Kimura, T., Hashimoto, I., Yamamoto, A., Nishikawa, M., Fujisawa, J.-I. (2000). Rev-dependent association of the intron-containing HIV-1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin-B. Genes Cells 5, 289-307.
    • (2000) Genes Cells , vol.5 , pp. 289-307
    • Kimura, T.1    Hashimoto, I.2    Yamamoto, A.3    Nishikawa, M.4    Fujisawa, J.-I.5
  • 34
    • 0034759412 scopus 로고    scopus 로고
    • Steps of nuclear pore complex disassembly and reassembly during mitosis in early Drosophila embryos
    • Kiseleva, E., Rutherford, S., Cotter, L. M., Allen, T. D. and Goldberg, M. W. (2001). Steps of nuclear pore complex disassembly and reassembly during mitosis in early Drosophila embryos. J. Cell Sci. 114, 3607-3618.
    • (2001) J. Cell Sci. , vol.114 , pp. 3607-3618
    • Kiseleva, E.1    Rutherford, S.2    Cotter, L.M.3    Allen, T.D.4    Goldberg, M.W.5
  • 36
    • 0030992443 scopus 로고    scopus 로고
    • Structural protein 4.1 in the nucleus of human cells: Dynamic rearrangements during cell division
    • Krauss, S. W., Larabell, C. A., Lockett, S., Gascard, P., Penman, S., Mohandas, N. and Chasis, J. A. (1997). Structural protein 4.1 in the nucleus of human cells: dynamic rearrangements during cell division. J. Cell Biol. 137, 275-289.
    • (1997) J. Cell Biol. , vol.137 , pp. 275-289
    • Krauss, S.W.1    Larabell, C.A.2    Lockett, S.3    Gascard, P.4    Penman, S.5    Mohandas, N.6    Chasis, J.A.7
  • 37
    • 0346106162 scopus 로고    scopus 로고
    • Two distinct domains of protein 4.1 critical for assembly of functional nuclei in vitro
    • Krauss, S. W., Heald, R., Lee, G., Nunomura, W., Gimm, J. A., Mohandas, N. and Chasis, J. A. (2002). Two distinct domains of protein 4.1 critical for assembly of functional nuclei in vitro. J. Biol. Chem. 277, 44339-44346.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44339-44346
    • Krauss, S.W.1    Heald, R.2    Lee, G.3    Nunomura, W.4    Gimm, J.A.5    Mohandas, N.6    Chasis, J.A.7
  • 38
    • 0141703273 scopus 로고    scopus 로고
    • Nuclear actin and protein 4.1: Essential interactions during nuclear assembly in vitro
    • Krauss, S. W., Chen, C., Penman, S. and Heald, R. (2003). Nuclear actin and protein 4.1: essential interactions during nuclear assembly in vitro. Proc. Natl. Acad. Sci. USA 100, 10752-10757.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10752-10757
    • Krauss, S.W.1    Chen, C.2    Penman, S.3    Heald, R.4
  • 39
    • 0031914182 scopus 로고    scopus 로고
    • Formation of F-actin aggregates in cells treated with actin stabilizing drugs
    • Lee, E., Shelden, E. A. and Knecht, D. A. (1998). Formation of F-actin aggregates in cells treated with actin stabilizing drugs. Cell Motil. Cytoskeleton 39, 122-133.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 122-133
    • Lee, E.1    Shelden, E.A.2    Knecht, D.A.3
  • 40
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka, M. J. and Masui, Y. (1983). Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220, 719-721.
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 41
    • 0033852114 scopus 로고    scopus 로고
    • A constitutive region is responsible for nuclear targeting of 4.1R: Modulation by alternative sequences results in differential intracellular localization
    • Luque, C. M. and Correas, I. (2000). A constitutive region is responsible for nuclear targeting of 4.1R: modulation by alternative sequences results in differential intracellular localization. J. Cell Sci. 113, 2485-2495.
    • (2000) J. Cell Sci. , vol.113 , pp. 2485-2495
    • Luque, C.M.1    Correas, I.2
  • 42
    • 0030047960 scopus 로고    scopus 로고
    • Assembly of the nuclear pore: Biochemically distinct steps revealed with NEM, GTPγS and BAPTA
    • Macaulay, C. and Forbes, D. J. (1996). Assembly of the nuclear pore: biochemically distinct steps revealed with NEM, GTPγ S and BAPTA. J. Cell Biol. 132, 5-20.
    • (1996) J. Cell Biol. , vol.132 , pp. 5-20
    • Macaulay, C.1    Forbes, D.J.2
  • 45
    • 0035085612 scopus 로고    scopus 로고
    • Molecular architecture of the amplified nucleoli of Xenopus oocytes
    • Mais, C. and Scheer, U. (2001). Molecular architecture of the amplified nucleoli of Xenopus oocytes. J. Cell Sci. 114, 709-718.
    • (2001) J. Cell Sci. , vol.114 , pp. 709-718
    • Mais, C.1    Scheer, U.2
  • 46
    • 0015160139 scopus 로고
    • Formation and distribution of nuclear pore complexes in interphase
    • Maul, G. G., Price, J. W. and Lieberman, M. W. (1971). Formation and distribution of nuclear pore complexes in interphase. J. Cell Biol. 51, 405-418.
    • (1971) J. Cell Biol. , vol.51 , pp. 405-418
    • Maul, G.G.1    Price, J.W.2    Lieberman, M.W.3
  • 47
    • 0026773097 scopus 로고
    • Nopp140 shuttles on tracks between nucleolus and cytoplasm
    • Meier, U. T. and Blobel, G. (1992). Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 70, 127-138.
    • (1992) Cell , vol.70 , pp. 127-138
    • Meier, U.T.1    Blobel, G.2
  • 48
    • 0033925931 scopus 로고    scopus 로고
    • RNA polymerase II in Cajal bodies of amphibian oocytes
    • Morgan, G. T., Doyle, O., Murphy, C. and Gall, J. G. (2000). RNA polymerase II in Cajal bodies of amphibian oocytes. J. Struct. Biol. 129, 258-268.
    • (2000) J. Struct. Biol. , vol.129 , pp. 258-268
    • Morgan, G.T.1    Doyle, O.2    Murphy, C.3    Gall, J.G.4
  • 49
    • 0036170782 scopus 로고    scopus 로고
    • Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus
    • Muratani, M., Gerlich, D., Janicki, S. M., Gebhard, M., Eils, R. and Spector, D. L. (2002). Metabolic-energy-dependent movement of PML bodies within the mammalian cell nucleus. Nat. Cell Biol. 4, 106-110.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 106-110
    • Muratani, M.1    Gerlich, D.2    Janicki, S.M.3    Gebhard, M.4    Eils, R.5    Spector, D.L.6
  • 50
    • 0035110880 scopus 로고    scopus 로고
    • Experimental observations of a nuclear matrix
    • Nickerson, J. A. (2001). Experimental observations of a nuclear matrix. J. Cell Sci. 114, 463-474.
    • (2001) J. Cell Sci. , vol.114 , pp. 463-474
    • Nickerson, J.A.1
  • 51
    • 0032231378 scopus 로고    scopus 로고
    • The Tpr protein: Linking structure and function in the nuclear interior?
    • Paddy, M. R. (1998). The Tpr protein: linking structure and function in the nuclear interior? Am. J. Hunt. Genet. 63, 305-310.
    • (1998) Am. J. Hunt. Genet. , vol.63 , pp. 305-310
    • Paddy, M.R.1
  • 52
    • 0027931054 scopus 로고
    • Interactions and three-dimensional localization of a group of nuclear pore complex proteins
    • Panté, N., Bastos, R., McMorrow, I., Burke, B. and Aebi, U. (1994). Interactions and three-dimensional localization of a group of nuclear pore complex proteins. J. Cell Biol. 126, 603-617.
    • (1994) J. Cell Biol. , vol.126 , pp. 603-617
    • Panté, N.1    Bastos, R.2    McMorrow, I.3    Burke, B.4    Aebi, U.5
  • 54
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • Pederson, T. and Aebi, U. (2002). Actin in the nucleus: what form and what for? J. Struct. Biol. 140, 3-9.
    • (2002) J. Struct. Biol. , vol.140 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 56
    • 0035795419 scopus 로고    scopus 로고
    • Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes
    • Percipalle, P., Zhao, J., Pope, B., Weeds, A., Lindberg, U. and Daneholt, B. (2001). Actin bound to the heterogeneous nuclear ribonucleoprotein hrp36 is associated with Balbiani ring mRNA from the gene to polysomes. J. Cell Biol. 153, 229-235.
    • (2001) J. Cell Biol. , vol.153 , pp. 229-235
    • Percipalle, P.1    Zhao, J.2    Pope, B.3    Weeds, A.4    Lindberg, U.5    Daneholt, B.6
  • 58
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D. and Misteli, T. (2000). High mobility of proteins in the mammalian cell nucleus. Nature 404, 604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 59
    • 0033909431 scopus 로고    scopus 로고
    • Movement of mRNA from transcription site to nuclear pores
    • Politz, J. C. and Pederson, T. (2000). Movement of mRNA from transcription site to nuclear pores. J. Struct. Biol. 129, 252-257.
    • (2000) J. Struct. Biol. , vol.129 , pp. 252-257
    • Politz, J.C.1    Pederson, T.2
  • 61
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple export pathways
    • Powers, M. A., Forbes, D. J., Dahlberg, J. E. and Lund, E. (1997). The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple export pathways. J. Cell Biol. 136, 241-250.
    • (1997) J. Cell Biol. , vol.136 , pp. 241-250
    • Powers, M.A.1    Forbes, D.J.2    Dahlberg, J.E.3    Lund, E.4
  • 62
    • 0034160165 scopus 로고    scopus 로고
    • Searching for a function for nuclear actin
    • Rando, O. J., Zhao, K. and Crabtree, G. R. (2000). Searching for a function for nuclear actin. Trends Cell Biol. 10, 92-97.
    • (2000) Trends Cell Biol. , vol.10 , pp. 92-97
    • Rando, O.J.1    Zhao, K.2    Crabtree, G.R.3
  • 63
    • 0033909368 scopus 로고    scopus 로고
    • In vivo observation of a nuclear channel-like system: Evidence for a distinct interchromatin domain compartment in interphase cells
    • Reichenzeller, M., Burzlaff, A., Lichter, P. and Herrmann, H. (2000). In vivo observation of a nuclear channel-like system: evidence for a distinct interchromatin domain compartment in interphase cells. J. Struct. Biol. 129, 175-185.
    • (2000) J. Struct. Biol. , vol.129 , pp. 175-185
    • Reichenzeller, M.1    Burzlaff, A.2    Lichter, P.3    Herrmann, H.4
  • 64
    • 0031200855 scopus 로고    scopus 로고
    • High-resolution field emission scanning electron microscopy of nuclear pore complex
    • Ris, H. (1997). High-resolution field emission scanning electron microscopy of nuclear pore complex. Scanning 19, 368-375.
    • (1997) Scanning , vol.19 , pp. 368-375
    • Ris, H.1
  • 65
    • 0032478672 scopus 로고    scopus 로고
    • In vitro interaction of the carboxy-terminal domain of lamin A with actin
    • Sasseville, A. M-J. and Langelier, Y. (1998). In vitro interaction of the carboxy-terminal domain of lamin A with actin. FEBS Lett. 425, 485-489.
    • (1998) FEBS Lett. , vol.425 , pp. 485-489
    • Sasseville, A.M-J.1    Langelier, Y.2
  • 66
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes
    • Scheer, U., Hinssen, H., Franke, W. W. and Jockusch, B. M. (1984). Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 39, 111-122.
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 68
    • 0034851781 scopus 로고    scopus 로고
    • Nuclear domains
    • Spector, D. L. (2001). Nuclear domains. J. Cell Sci. 114, 2891-2893.
    • (2001) J. Cell Sci. , vol.114 , pp. 2891-2893
    • Spector, D.L.1
  • 69
    • 0032829103 scopus 로고    scopus 로고
    • New antiactin drugs in the study of the organization and function of the actin cytoskeleton
    • Spector, I., Braet, F., Shochet, N. R. and Bubb, M. R. (1999). New antiactin drugs in the study of the organization and function of the actin cytoskeleton. Microsc. Res. Tech. 47, 18-37.
    • (1999) Microsc. Res. Tech. , vol.47 , pp. 18-37
    • Spector, I.1    Braet, F.2    Shochet, N.R.3    Bubb, M.R.4
  • 70
    • 0033535342 scopus 로고    scopus 로고
    • Proteins connecting the nuclear pore complex with the nuclear interior
    • Strambio-de-Castillia, C., Blobel, G. and Rout, M. P. (1999). Proteins connecting the nuclear pore complex with the nuclear interior. J. Cell Biol. 144, 839-855.
    • (1999) J. Cell Biol. , vol.144 , pp. 839-855
    • Strambio-de-Castillia, C.1    Blobel, G.2    Rout, M.P.3
  • 71
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profilin-actin complexes
    • Stuven, T., Hartmann, E. and Gorlich, D. (2003). Exportin 6: a novel nuclear export receptor that is specific for profilin-actin complexes. EMBO J. 22, 5928-5940.
    • (2003) EMBO J. , vol.22 , pp. 5928-5940
    • Stuven, T.1    Hartmann, E.2    Gorlich, D.3
  • 72
    • 0035370938 scopus 로고    scopus 로고
    • Nuclear pores and nuclear assembly
    • Vasu, S. K. and Forbes, D. J. (2001). Nuclear pores and nuclear assembly. Curr. Opin. Cell Biol. 13, 363-375.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 363-375
    • Vasu, S.K.1    Forbes, D.J.2
  • 73
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • Wada, A., Fukuda, M., Mishima, M. and Nishida, E. (1998). Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17, 1635-1641.
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 75
    • 0033625535 scopus 로고    scopus 로고
    • The EAST protein of Drosophila controls an expandable nuclear endoskeleton
    • Wasser, M. and Chia, W. (2000). The EAST protein of Drosophila controls an expandable nuclear endoskeleton. Nat. Cell Biol. 2, 268-275.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 268-275
    • Wasser, M.1    Chia, W.2
  • 76
    • 0030794456 scopus 로고    scopus 로고
    • Nuclear assembly in Xenopus extracts visualized by scanning EM reveals a transport dependent 'envelope smoothing' event
    • Wiese, C., Goldberg, M. W., Allen, T. D. and Wilson, K. L. (1997). Nuclear assembly in Xenopus extracts visualized by scanning EM reveals a transport dependent 'envelope smoothing' event. J. Cell Sci. 110, 1489-1502.
    • (1997) J. Cell Sci. , vol.110 , pp. 1489-1502
    • Wiese, C.1    Goldberg, M.W.2    Allen, T.D.3    Wilson, K.L.4
  • 77
    • 0025818887 scopus 로고
    • Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: Loops, spheres, and snurposomes
    • Wu, Z. A., Murphy, C., Callan, H. G. and Gall, J. G. (1991). Small nuclear ribonucleoproteins and heterogeneous nuclear ribonucleoproteins in the amphibian germinal vesicle: loops, spheres, and snurposomes. J. Cell Biol. 113, 465-483.
    • (1991) J. Cell Biol. , vol.113 , pp. 465-483
    • Wu, Z.A.1    Murphy, C.2    Callan, H.G.3    Gall, J.G.4
  • 78
    • 0030739959 scopus 로고    scopus 로고
    • Micronucleoli in Xenopus germinal vesicles
    • Wu, Z. and Gall, J. G. (1997). Micronucleoli in Xenopus germinal vesicles. Chromosoma 105, 438-443.
    • (1997) Chromosoma , vol.105 , pp. 438-443
    • Wu, Z.1    Gall, J.G.2
  • 80
    • 0036429266 scopus 로고    scopus 로고
    • The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300
    • Zhang, Q., Ragnauth, C., Greener, M. J., Shanahan, C. M. and Roberts, R. G. (2002b). The nesprins are giant actin-binding proteins, orthologous to Drosophila melanogaster muscle protein MSP-300. Genomics 80, 473-481.
    • (2002) Genomics , vol.80 , pp. 473-481
    • Zhang, Q.1    Ragnauth, C.2    Greener, M.J.3    Shanahan, C.M.4    Roberts, R.G.5
  • 81
    • 0036674866 scopus 로고    scopus 로고
    • NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
    • Zhen, Y. Y., Libotte, Y., Munck, M., Noegel, A. A. and Korenbaum, E. (2002). NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J. Cell Sci. 115, 3207-3222.
    • (2002) J. Cell Sci. , vol.115 , pp. 3207-3222
    • Zhen, Y.Y.1    Libotte, Y.2    Munck, M.3    Noegel, A.A.4    Korenbaum, E.5
  • 82
    • 0036351037 scopus 로고    scopus 로고
    • Structures and dynamics of Drosophila Tpr inconsistent with a static, filamentous structure
    • Zimowska, G. and Paddy, M. R. (2002). Structures and dynamics of Drosophila Tpr inconsistent with a static, filamentous structure. Exp. Cell Res. 276, 223-232.
    • (2002) Exp. Cell Res. , vol.276 , pp. 223-232
    • Zimowska, G.1    Paddy, M.R.2


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