메뉴 건너뛰기




Volumn 13, Issue , 1997, Pages 669-695

Nuclear assembly

Author keywords

Cell cycle; Emerin; LAP1; LAP2; LBR; Nuclear envelope; Nuclear lamina; Nuclear pore complexes; Nucleoskeleton

Indexed keywords

ACTIN; HYBRID PROTEIN; LAMIN; LAMIN B;

EID: 0031439877     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.13.1.669     Document Type: Review
Times cited : (202)

References (166)
  • 1
    • 0029021928 scopus 로고
    • Structural plasticity of the nuclear pore complex
    • Akey CW. 1995. Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248:273-93
    • (1995) J. Mol. Biol. , vol.248 , pp. 273-293
    • Akey, C.W.1
  • 2
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey CW, Radermacher M. 1993. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122:1-19
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 4
    • 0027258499 scopus 로고
    • Nuclear assembly, structure and function - The use of Xenopus in vitro systems
    • Almouzni G, Wolffe AP. 1993. Nuclear assembly, structure and function - the use of Xenopus in vitro systems. Exp. Cell. Res. 205:1-15
    • (1993) Exp. Cell. Res. , vol.205 , pp. 1-15
    • Almouzni, G.1    Wolffe, A.P.2
  • 5
    • 0025264189 scopus 로고
    • In vivo phosphorylation of the lamin B receptor. Binding of lamin B to its nuclear membrane receptor is affected by phosphorylation
    • Appelbaum J, Blobel G, Georgatos SD. 1990. In vivo phosphorylation of the lamin B receptor. Binding of lamin B to its nuclear membrane receptor is affected by phosphorylation. J. Biol. Chem. 265:4181-84
    • (1990) J. Biol. Chem. , vol.265 , pp. 4181-4184
    • Appelbaum, J.1    Blobel, G.2    Georgatos, S.D.3
  • 6
    • 0031029561 scopus 로고    scopus 로고
    • Distinct regions specify the targeting of otefin to the nucleoplasmic side of the nuclear envelope
    • Ashery-Padan R, Weiss AM, Feinstein N, Gruenbaum Y. 1997. Distinct regions specify the targeting of otefin to the nucleoplasmic side of the nuclear envelope. J. Biol. Chem. 272:2493-99
    • (1997) J. Biol. Chem. , vol.272 , pp. 2493-2499
    • Ashery-Padan, R.1    Weiss, A.M.2    Feinstein, N.3    Gruenbaum, Y.4
  • 7
    • 0025861822 scopus 로고
    • Characterization of a 54-kD protein of the inner nuclear membrane: Evidence for cell cycle-dependent interaction with the nuclear lamina
    • Bailer SM, Eppenberger HM, Griffiths G, Nigg EA. 1991. Characterization of a 54-kD protein of the inner nuclear membrane: evidence for cell cycle-dependent interaction with the nuclear lamina. J. Cell Biol. 114:389-400
    • (1991) J. Cell Biol. , vol.114 , pp. 389-400
    • Bailer, S.M.1    Eppenberger, H.M.2    Griffiths, G.3    Nigg, E.A.4
  • 8
    • 0031019245 scopus 로고    scopus 로고
    • Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells
    • Belgareh N, Doye V. 1997. Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. J. Cell Biol. 136:747-59
    • (1997) J. Cell Biol. , vol.136 , pp. 747-759
    • Belgareh, N.1    Doye, V.2
  • 9
    • 0024429614 scopus 로고
    • Functional role of newly formed pore complexes in postmitotic nuclear reorganization
    • Benavente R, Dabauvalle MC, Scheer U, Chaly N. 1989. Functional role of newly formed pore complexes in postmitotic nuclear reorganization. Chromosoma 98:233-41
    • (1989) Chromosoma , vol.98 , pp. 233-241
    • Benavente, R.1    Dabauvalle, M.C.2    Scheer, U.3    Chaly, N.4
  • 10
    • 0027985787 scopus 로고
    • Identification of a novel X-Iinked gene responsible for Emery-Dreifuss muscular dystrophy
    • Bione S, Maestrini E, Rivella A, Mancini M, Regis S, et al. 1994. Identification of a novel X-Iinked gene responsible for Emery-Dreifuss muscular dystrophy. Nat. Genet. 8: 323-27
    • (1994) Nat. Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, A.3    Mancini, M.4    Regis, S.5
  • 11
    • 0022981734 scopus 로고
    • Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs
    • Blow JJ, Laskey RA. 1986. Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs. Cell 47: 577-87
    • (1986) Cell , vol.47 , pp. 577-587
    • Blow, J.J.1    Laskey, R.A.2
  • 12
    • 1842322089 scopus 로고
    • Nuclei act as independent and integrated units of replication in a Xenopus cell-free DNA replication system
    • Blow JJ, Watson JV. 1987. Nuclei act as independent and integrated units of replication in a Xenopus cell-free DNA replication system. EMBO J. 6:1997-2002
    • (1987) EMBO J. , vol.6 , pp. 1997-2002
    • Blow, J.J.1    Watson, J.V.2
  • 13
    • 0026556684 scopus 로고
    • GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro
    • Boman AL, Delannoy MR, Wilson KL. 1992a. GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro. J. Cell Biol. 116:281-94
    • (1992) J. Cell Biol. , vol.116 , pp. 281-294
    • Boman, A.L.1    Delannoy, M.R.2    Wilson, K.L.3
  • 14
    • 0026682791 scopus 로고
    • A role for ADP-ribosybtion factor in nuclear vesicle dynamics
    • Boman AL, Taylor TC, Melançon P, Wilson KL. 1992b. A role for ADP-ribosybtion factor in nuclear vesicle dynamics. Nature 358:512-14
    • (1992) Nature , vol.358 , pp. 512-514
    • Boman, A.L.1    Taylor, T.C.2    Melançon, P.3    Wilson, K.L.4
  • 15
    • 0027416334 scopus 로고
    • Internal lamin structures within GI nuclei of human dermal fibroblasts
    • Bridger JM, Kill IR, O'Fanell M, Hutchison CJ. 1993. Internal lamin structures within GI nuclei of human dermal fibroblasts. J. Cell Sci. 104:297-306
    • (1993) J. Cell Sci. , vol.104 , pp. 297-306
    • Bridger, J.M.1    Kill, I.R.2    O'Fanell, M.3    Hutchison, C.J.4
  • 16
    • 0030793799 scopus 로고    scopus 로고
    • In vivo dynamics of nuclear pore complexes in yeast
    • Bucci M, Wente SR. 1997. In vivo dynamics of nuclear pore complexes in yeast. J. Cell Biol. 136:1185-99
    • (1997) J. Cell Biol. , vol.136 , pp. 1185-1199
    • Bucci, M.1    Wente, S.R.2
  • 17
    • 0031561731 scopus 로고    scopus 로고
    • Domain-specific disassembly and reassembly of nuclear membranes during mitosis
    • Buendia B, Courvalin J-C. 1997. Domain-specific disassembly and reassembly of nuclear membranes during mitosis. Exp. Cell Res. 230:133-14
    • (1997) Exp. Cell Res. , vol.230 , pp. 133-214
    • Buendia, B.1    Courvalin, J.-C.2
  • 18
    • 0025056506 scopus 로고
    • On the cell-free association of lamins A and C with metaphase chromosomes
    • Burke B. 1990. On the cell-free association of lamins A and C with metaphase chromosomes. Exp. Cell Res. 186:169-76
    • (1990) Exp. Cell Res. , vol.186 , pp. 169-176
    • Burke, B.1
  • 19
    • 0022517260 scopus 로고
    • A cell free system to study reassembly of the nuclear envelope at the end of mitosis
    • Burke B, Gerace L. 1986. A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 44:639-52
    • (1986) Cell , vol.44 , pp. 639-652
    • Burke, B.1    Gerace, L.2
  • 20
    • 0028299148 scopus 로고
    • In vitro devel-opment of the sea urchin male pronucleus
    • Cameron LA, Poccia DL. 1994. In vitro devel-opment of the sea urchin male pronucleus. Dev. Biol. 162:568-78
    • (1994) Dev. Biol. , vol.162 , pp. 568-578
    • Cameron, L.A.1    Poccia, D.L.2
  • 21
    • 0027275334 scopus 로고
    • Stepwise reassembly of the nuclear envelope at the end of mitosis
    • Chaudhary N, Courvalin JC. 1993. Stepwise reassembly of the nuclear envelope at the end of mitosis. J. Cell Biol. 122:295-306
    • (1993) J. Cell Biol. , vol.122 , pp. 295-306
    • Chaudhary, N.1    Courvalin, J.C.2
  • 22
    • 0030461544 scopus 로고    scopus 로고
    • Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein
    • Collas P, Courvalin J-C, Poccia D. 1996. Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein. J. Cell Biol. 135:1715-25
    • (1996) J. Cell Biol. , vol.135 , pp. 1715-1725
    • Collas, P.1    Courvalin, J.-C.2    Poccia, D.3
  • 23
    • 0029055578 scopus 로고
    • Lipophilic organizing structures of sperm nuclei target membrane vesicle binding and are incorporated into the nuclear envelope
    • Collas P, Poccia D. 1995. Lipophilic organizing structures of sperm nuclei target membrane vesicle binding and are incorporated into the nuclear envelope. Dev. Biol. 169:123-35
    • (1995) Dev. Biol. , vol.169 , pp. 123-135
    • Collas, P.1    Poccia, D.2
  • 24
    • 0029982203 scopus 로고    scopus 로고
    • Distinct egg membrane vesicles differing in binding and fusion properties contribute to sea urchin male pronuclear envelope formed in vitro
    • Collas P, Poccia D. 1996. Distinct egg membrane vesicles differing in binding and fusion properties contribute to sea urchin male pronuclear envelope formed in vitro. J. Cell Sci. 109:1275-83
    • (1996) J. Cell Sci. , vol.109 , pp. 1275-1283
    • Collas, P.1    Poccia, D.2
  • 25
    • 0028239617 scopus 로고
    • NuMA, a nuclear protein involved in mitosis and nuclear reformation
    • Compton DA, Cleveland DW. 1994. NuMA, a nuclear protein involved in mitosis and nuclear reformation. Curr. Opin. Cell Biol. 6:343-46
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 343-346
    • Compton, D.A.1    Cleveland, D.W.2
  • 27
    • 0031043895 scopus 로고    scopus 로고
    • Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments
    • Cordes VC, Reidenbach S, Rackwitz H-R, Franke WW. 1996. Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol. 136:515-29
    • (1996) J. Cell Biol. , vol.136 , pp. 515-529
    • Cordes, V.C.1    Reidenbach, S.2    Rackwitz, H.-R.3    Franke, W.W.4
  • 28
    • 0026783801 scopus 로고
    • The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase
    • Courvalin JC, Segil N, Blobel G, Worman HJ. 1992. The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase. J. Biol. Chem. 267:19035-38
    • (1992) J. Biol. Chem. , vol.267 , pp. 19035-19038
    • Courvalin, J.C.1    Segil, N.2    Blobel, G.3    Worman, H.J.4
  • 29
    • 0026542841 scopus 로고
    • DNA replication in cell-free extracts from Xenopus eggs is prevented by disrupting nuclear envelope function
    • Cox LS. 1992. DNA replication in cell-free extracts from Xenopus eggs is prevented by disrupting nuclear envelope function. J. Cell Sci. 101:43-53
    • (1992) J. Cell Sci. , vol.101 , pp. 43-53
    • Cox, L.S.1
  • 30
    • 0026099941 scopus 로고
    • Spontaneous assembly of pore complex-containing membranes ("annulate lamellae") in Xenopus egg extract in the absence of chromatin
    • Dabauvalle M-C, Loos K, Merken H, Scheer U. 1991. Spontaneous assembly of pore complex-containing membranes ("annulate lamellae") in Xenopus egg extract in the absence of chromatin. J. Cell Biol. 112:1073-82
    • (1991) J. Cell Biol. , vol.112 , pp. 1073-1082
    • Dabauvalle, M.-C.1    Loos, K.2    Merken, H.3    Scheer, U.4
  • 31
    • 0025223824 scopus 로고
    • Identification of a soluble precursor complex essential for nuclear pore assembly in vitro
    • Dabauvalle M-C, Loos K, Scheer U. 1990. Identification of a soluble precursor complex essential for nuclear pore assembly in vitro. Chromosoma 100:56-66
    • (1990) Chromosoma , vol.100 , pp. 56-66
    • Dabauvalle, M.-C.1    Loos, K.2    Scheer, U.3
  • 32
    • 0026048152 scopus 로고
    • Assembly of nuclear pore complexes in Xenopus egg extract
    • Dabauvalle M-C, Scheer U. 1991. Assembly of nuclear pore complexes in Xenopus egg extract. Biol. Cell 72:25-29
    • (1991) Biol. Cell , vol.72 , pp. 25-29
    • Dabauvalle, M.-C.1    Scheer, U.2
  • 34
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis LI. 1995. The nuclear pore complex. Annu. Rev. Biochem. 64:865-96
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 865-896
    • Davis, L.I.1
  • 35
    • 0024615999 scopus 로고
    • Disassembly of the nuclear envelope of Spisula oocytes in a cell-free system
    • Dessev G, Palazzo R, Rebhun L, Goldman R. 1989. Disassembly of the nuclear envelope of Spisula oocytes in a cell-free system. Dev. Biol. 131:496-504
    • (1989) Dev. Biol. , vol.131 , pp. 496-504
    • Dessev, G.1    Palazzo, R.2    Rebhun, L.3    Goldman, R.4
  • 36
    • 0017134119 scopus 로고
    • A modified procedure for the isolation of a pore complexlamina fraction from rat liver nuclei
    • Dwyer N, Blobel G. 1976. A modified procedure for the isolation of a pore complexlamina fraction from rat liver nuclei. J. Cell Biol. 70:581-91
    • (1976) J. Cell Biol. , vol.70 , pp. 581-591
    • Dwyer, N.1    Blobel, G.2
  • 37
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear envelope dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • In press
    • Ellenberg J, Siggia ED, Moreira J, Smith CL, Presley JF, et al. 1997. Nuclear envelope dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis J. Cell Biol. In press
    • (1997) J. Cell Biol.
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.3    Smith, C.L.4    Presley, J.F.5
  • 38
    • 0030731381 scopus 로고    scopus 로고
    • GST-lamin fusion proteins act as dominant negative mutants in Xenopus egg extract and reveal the function of the lamina in DNA replication
    • In press
    • Ellis DJ, Jenkins H, Whitfield WGF, Hutchison CJ. 1997. GST-lamin fusion proteins act as dominant negative mutants in Xenopus egg extract and reveal the function of the lamina in DNA replication. J. Cell Sci. In press
    • (1997) J. Cell Sci.
    • Ellis, D.J.1    Jenkins, H.2    Whitfield, W.G.F.3    Hutchison, C.J.4
  • 39
    • 0029888702 scopus 로고    scopus 로고
    • A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes
    • Ewald A, Kossner U, Scheer U, Dabauvalle M-C. 1996. A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes. J. Cell Sci. 109:1813-24
    • (1996) J. Cell Sci. , vol.109 , pp. 1813-1824
    • Ewald, A.1    Kossner, U.2    Scheer, U.3    Dabauvalle, M.-C.4
  • 40
    • 0029945130 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210
    • Favreau C, Worman HJ, Wozniak RW, Frappier T, Courvalin J. 1996. Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210. Biochemistry 35:8035-44
    • (1996) Biochemistry , vol.35 , pp. 8035-8044
    • Favreau, C.1    Worman, H.J.2    Wozniak, R.W.3    Frappier, T.4    Courvalin, J.5
  • 41
    • 0021987228 scopus 로고
    • Monoclonal antibodies prepared against the major Drosophila nuclear matrix-pore complex-lamina glycoprotein bind specifically to the nuclear envelope in situ
    • Filson AJ, Lewis A, Blobel G, Fisher PA. 1985. Monoclonal antibodies prepared against the major Drosophila nuclear matrix-pore complex-lamina glycoprotein bind specifically to the nuclear envelope in situ. J. Biol. Chem. 260:3164-72
    • (1985) J. Biol. Chem. , vol.260 , pp. 3164-3172
    • Filson, A.J.1    Lewis, A.2    Blobel, G.3    Fisher, P.A.4
  • 42
    • 0025162266 scopus 로고
    • Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored
    • Finlay DR, Forbes DJ. 1990. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 60:17-29
    • (1990) Cell , vol.60 , pp. 17-29
    • Finlay, D.R.1    Forbes, D.J.2
  • 44
    • 0028913164 scopus 로고
    • Analysis of nuclear lamin isoprenylation in Xenopus oocytes: Isoprenylation of lamin B3 precedes its uptake into the nucleus
    • Firmbach-Kraft I, Stick R. 1995. Analysis of nuclear lamin isoprenylation in Xenopus oocytes: isoprenylation of lamin B3 precedes its uptake into the nucleus. J. Cell Biol. 129: 17-24
    • (1995) J. Cell Biol. , vol.129 , pp. 17-24
    • Firmbach-Kraft, I.1    Stick, R.2
  • 45
    • 58149355665 scopus 로고    scopus 로고
    • Methods for studying nuclear assembly and disassembly using Drosophila cell-free systems
    • ed. M Berrios, New York: Academic In press
    • Fisher PA, Berrios M. 1997. Methods for studying nuclear assembly and disassembly using Drosophila cell-free systems. In Methods in Cell Biology, ed. M Berrios, New York: Academic. Vol. 53. In press
    • (1997) Methods in Cell Biology , vol.53
    • Fisher, P.A.1    Berrios, M.2
  • 46
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R, Gerace L. 1993. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73:1267-79
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 47
    • 0019842267 scopus 로고
    • The nuclear envelope and the architecture of the nuclear periphery
    • Franke WW, Scheer U, Krohne G, Jarasch E-D. 1981. The nuclear envelope and the architecture of the nuclear periphery. J. Cell Biol. 91:39s-50
    • (1981) J. Cell Biol. , vol.91
    • Franke, W.W.1    Scheer, U.2    Krohne, G.3    Jarasch, E.-D.4
  • 48
    • 0031051629 scopus 로고    scopus 로고
    • Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope
    • Flicker M, Hollinshead M, White N, Vaux D. 1997. Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope. J. Cell Biol. 136:531-44
    • (1997) J. Cell Biol. , vol.136 , pp. 531-544
    • Flicker, M.1    Hollinshead, M.2    White, N.3    Vaux, D.4
  • 49
    • 0028989340 scopus 로고
    • Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope
    • Furukawa K, Panté N, Aebi U, Gerace L. 1995. Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J. 14:1626-36
    • (1995) EMBO J. , vol.14 , pp. 1626-1636
    • Furukawa, K.1    Panté, N.2    Aebi, U.3    Gerace, L.4
  • 50
    • 0030882002 scopus 로고    scopus 로고
    • ARF is not required for nuclear vesicle fusion or mitotic membrane disassembly in vitro: Evidence for a non-ARF GRPase in fusion
    • In press
    • Cant TM, Wilson KL. 1997. ARF is not required for nuclear vesicle fusion or mitotic membrane disassembly in vitro: evidence for a non-ARF GRPase in fusion. Eur. J. Cell Biol. 74: In press
    • (1997) Eur. J. Cell Biol. , vol.74
    • Cant, T.M.1    Wilson, K.L.2
  • 51
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace L, Blobel G. 1980. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19:277-87
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 52
    • 0018093261 scopus 로고
    • Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction: Interphase and mitotic distribution
    • Gerace L, Blum A, Blobel G. 1978. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction: interphase and mitotic distribution. J. Cell Biol. 79:546-66
    • (1978) J. Cell Biol. , vol.79 , pp. 546-566
    • Gerace, L.1    Blum, A.2    Blobel, G.3
  • 53
    • 0021702708 scopus 로고
    • Organization and modulation of nuclear lamina structure
    • Gerace L, Comeau C, Benson M. 1984. Organization and modulation of nuclear lamina structure. J. Cell Sci. Suppl. 1:137-60
    • (1984) J. Cell Sci. Suppl. , vol.1 , pp. 137-160
    • Gerace, L.1    Comeau, C.2    Benson, M.3
  • 54
    • 0028294522 scopus 로고
    • Integral membrane proteins and dynamic organization of the nuclear envelope
    • Gerace L, Foisner R. 1994. Integral membrane proteins and dynamic organization of the nuclear envelope. Trends Cell Biol. 4:127-31
    • (1994) Trends Cell Biol. , vol.4 , pp. 127-131
    • Gerace, L.1    Foisner, R.2
  • 55
    • 0020399177 scopus 로고
    • Identification of a major polypeptide of the nuclear pore complex
    • Gerace L, Ottaviano Y, Kondor-Koch C. 1982. Identification of a major polypeptide of the nuclear pore complex. J. Cell Biol. 95:826-37
    • (1982) J. Cell Biol. , vol.95 , pp. 826-837
    • Gerace, L.1    Ottaviano, Y.2    Kondor-Koch, C.3
  • 56
    • 0025005766 scopus 로고
    • Lamins A and C bind and assemble at the surface of mitotic chromosomes
    • Glass JR, Gerace L. 1990. Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111:1047-57
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1057
    • Glass, J.R.1    Gerace, L.2
  • 57
    • 0027442899 scopus 로고
    • The alpha-helical rod domain of human lamins A and C contains a chromatin binding site
    • Glass CA, Glass JR. Taniura H, Hasel KW, Blevitt JM, Gerace L. 1993. The alpha-helical rod domain of human lamins A and C contains a chromatin binding site. EMBO J. 12:4413-24
    • (1993) EMBO J. , vol.12 , pp. 4413-4424
    • Glass, C.A.1    Glass, J.R.2    Taniura, H.3    Hasel, K.W.4    Blevitt, J.M.5    Gerace, L.6
  • 58
    • 0027104231 scopus 로고
    • High resolution scanning electron microscopy of the nuclear envelope: Demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores
    • Goldberg MW, Allen TD. 1992. High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J. Cell Biol. 119:1429-40
    • (1992) J. Cell Biol. , vol.119 , pp. 1429-1440
    • Goldberg, M.W.1    Allen, T.D.2
  • 59
    • 0029869424 scopus 로고    scopus 로고
    • The nuclear pore complex and lamina: Three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy
    • Goldberg MW, Allen TD. 1996. The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J. Mol. Biol. 257:848-65
    • (1996) J. Mol. Biol. , vol.257 , pp. 848-865
    • Goldberg, M.W.1    Allen, T.D.2
  • 60
    • 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 MW, Wiese C, Allen TD, Wilson KL. 1997. Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly. J. Cell Sci. 110:409-20
    • (1997) J. Cell Sci. , vol.110 , pp. 409-420
    • Goldberg, M.W.1    Wiese, C.2    Allen, T.D.3    Wilson, K.L.4
  • 62
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich D, Mattaj IW. 1996. Nucleocytoplasmic transport. Science 271:1513-18
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 63
    • 0025253486 scopus 로고
    • A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail
    • Greber UF, Senior A, Gerace L. 1990. A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. EMBO J. 9:1495-502
    • (1990) EMBO J. , vol.9 , pp. 1495-1502
    • Greber, U.F.1    Senior, A.2    Gerace, L.3
  • 64
    • 0028786983 scopus 로고
    • Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
    • Guan T, Müller S, Klier G, Panté N, Blevitt JM, et al. 1995. Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol. Biol. Cell 6:1591-603
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1591-1603
    • Guan, T.1    Müller, S.2    Klier, G.3    Panté, N.4    Blevitt, J.M.5
  • 65
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg E, Wozniak RW, Blobel G. 1993. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J. Cell Biol. 122:513-21
    • (1993) J. Cell Biol. , vol.122 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 66
    • 0029042452 scopus 로고
    • Epitope mapping and direct visualization of the parallel, in-register arrangement of the double-stranded coiled-coil in the NuMA protein
    • Harborth J, Weber K, Osbom M. 1995. Epitope mapping and direct visualization of the parallel, in-register arrangement of the double-stranded coiled-coil in the NuMA protein. EMBO J. 14:2447-60
    • (1995) EMBO J. , vol.14 , pp. 2447-2460
    • Harborth, J.1    Weber, K.2    Osbom, M.3
  • 67
    • 0029155876 scopus 로고
    • Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO β to rat lamin-associated polypeptide 2
    • Harris CA, Andryuk PJ, Cline SW, Mathew S, Siekierka JJ, Goldstein G. 1995. Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO β to rat lamin-associated polypeptide 2. Genomics 28:198-205
    • (1995) Genomics , vol.28 , pp. 198-205
    • Harris, C.A.1    Andryuk, P.J.2    Cline, S.W.3    Mathew, S.4    Siekierka, J.J.5    Goldstein, G.6
  • 68
    • 0027954910 scopus 로고
    • Nuclear assembly with λ DNA in fractionated Xenopus egg extracts: An unexpected role for glycogen in formation of a higher order chromatin intermediate
    • Hartl P, Olson E, Dang T, Forbes DJ. 1994. Nuclear assembly with λ DNA in fractionated Xenopus egg extracts: an unexpected role for glycogen in formation of a higher order chromatin intermediate. J. Cell Biol. 124:235-48
    • (1994) J. Cell Biol. , vol.124 , pp. 235-248
    • Hartl, P.1    Olson, E.2    Dang, T.3    Forbes, D.J.4
  • 69
    • 0029836330 scopus 로고    scopus 로고
    • Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts
    • Heald R, Tournebize R, Blank T, Sandaltzopoulos R, Becker P, et al. 1996. Self-organization of microtubules into bipolar spindles around artificial chromosomes in Xenopus egg extracts. Nature 382:420-25
    • (1996) Nature , vol.382 , pp. 420-425
    • Heald, R.1    Tournebize, R.2    Blank, T.3    Sandaltzopoulos, R.4    Becker, P.5
  • 70
    • 0026343513 scopus 로고
    • Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain
    • Hoger TH, Krohne G, Kleinschmidt JA. 1991. Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain. Exp. Cell Res. 197:280-89
    • (1991) Exp. Cell Res. , vol.197 , pp. 280-289
    • Hoger, T.H.1    Krohne, G.2    Kleinschmidt, J.A.3
  • 71
    • 0028038215 scopus 로고
    • Replication factories and nuclear bodies: The ultra-structural characterization of replication sites during the cell cycle
    • Hozák P, Jackson DA, Cook PR. 1994. Replication factories and nuclear bodies: the ultra-structural characterization of replication sites during the cell cycle. J. Cell Sci. 107:2191-202
    • (1994) J. Cell Sci. , vol.107 , pp. 2191-2202
    • Hozák, P.1    Jackson, D.A.2    Cook, P.R.3
  • 72
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozák P, Sasseville AM, Raymond Y, Cook PR. 1995. Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci. 108:635-44
    • (1995) J. Cell Sci. , vol.108 , pp. 635-644
    • Hozák, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 73
    • 0028587430 scopus 로고
    • Weaving a pattern from disparate threads: Lamin function in nuclear assembly and DNA replication
    • Hutchison CJ, Bridger JM, Cox LS, Kill IR. 1994. Weaving a pattern from disparate threads: lamin function in nuclear assembly and DNA replication. J. Cell Sci. 107:3259-69
    • (1994) J. Cell Sci. , vol.107 , pp. 3259-3269
    • Hutchison, C.J.1    Bridger, J.M.2    Cox, L.S.3    Kill, I.R.4
  • 74
    • 0024221204 scopus 로고
    • Visualization of a filamentous nucleoskeleton with a 23 nm axial repeat
    • Jackson DA, Cook PR. 1988. Visualization of a filamentous nucleoskeleton with a 23 nm axial repeat. EMBO J. 7:3667-77
    • (1988) EMBO J. , vol.7 , pp. 3667-3677
    • Jackson, D.A.1    Cook, P.R.2
  • 75
    • 0027489289 scopus 로고
    • Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix
    • Jenkins H, Holman T, Lyon C, Lane B, Stick R, Hutchison C. 1993. Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix. J. Cell Sci. 106:275-85
    • (1993) J. Cell Sci. , vol.106 , pp. 275-285
    • Jenkins, H.1    Holman, T.2    Lyon, C.3    Lane, B.4    Stick, R.5    Hutchison, C.6
  • 76
    • 0029930929 scopus 로고    scopus 로고
    • Single nuclear pores visualized by confocal microscopy and image processing
    • Kubitscheck U, Wedekind P, Zeidler O, Grote M, Peters R. 1996. Single nuclear pores visualized by confocal microscopy and image processing. Biophys. J. 70:2067-77
    • (1996) Biophys. J. , vol.70 , pp. 2067-2077
    • Kubitscheck, U.1    Wedekind, P.2    Zeidler, O.3    Grote, M.4    Peters, R.5
  • 77
    • 0027964421 scopus 로고
    • Nuclear congression and membrane fusion: Two distinct events in the yeast karyogamy pathway
    • Kurihara LJ, Beh CT, Latterich M, Schekman R, Rose MD. 1994. Nuclear congression and membrane fusion: two distinct events in the yeast karyogamy pathway. J. Cell Biol. 126:911-23
    • (1994) J. Cell Biol. , vol.126 , pp. 911-923
    • Kurihara, L.J.1    Beh, C.T.2    Latterich, M.3    Schekman, R.4    Rose, M.D.5
  • 78
    • 0028365624 scopus 로고
    • The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion
    • Latterich M, Schekman R. 1994. The karyogamy gene KAR2 and novel proteins are required for ER-membrane fusion. Cell 78:87-98
    • (1994) Cell , vol.78 , pp. 87-98
    • Latterich, M.1    Schekman, R.2
  • 79
    • 0026910403 scopus 로고
    • Regulation of DNA replication by the nuclear envelope
    • Leno GH. 1992. Regulation of DNA replication by the nuclear envelope. Sem. Cell Biol. 3:237-43
    • (1992) Sem. Cell Biol. , vol.3 , pp. 237-243
    • Leno, G.H.1
  • 80
    • 0026271760 scopus 로고
    • DNA replication in cell-free extracts from Xenopus laevis
    • ed. M Berrios, New York: Academic
    • Leno GH, Laskey RA. 1991. DNA replication in cell-free extracts from Xenopus laevis. In Methods in Cell Biology, ed. M Berrios, 36:561-79. New York: Academic
    • (1991) Methods in Cell Biology , vol.36 , pp. 561-579
    • Leno, G.H.1    Laskey, R.A.2
  • 81
    • 0024085929 scopus 로고
    • The reconstitution of nuclear envelopes in cell-free extracts
    • Lohka MJ. 1988. The reconstitution of nuclear envelopes in cell-free extracts. Cell Biol. Int. Rep. 12:833-48
    • (1988) Cell Biol. Int. Rep. , vol.12 , pp. 833-848
    • Lohka, M.J.1
  • 82
    • 0022415960 scopus 로고
    • Induction of nuclear envelope breakdown, chromosome condensation, and spindle formation in cell-free extracts
    • Lohka MJ, Maller JL. 1985. Induction of nuclear envelope breakdown, chromosome condensation, and spindle formation in cell-free extracts. J. Cell Biol. 101:518-23
    • (1985) J. Cell Biol. , vol.101 , pp. 518-523
    • Lohka, M.J.1    Maller, J.L.2
  • 83
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka MJ, Masui Y. 1983. Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220:719-21
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 84
    • 0021176610 scopus 로고
    • Roles of cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs
    • Lohka MJ, Masui Y. 1984. Roles of cytosol and cytoplasmic particles in nuclear envelope assembly and sperm pronuclear formation in cell-free preparations from amphibian eggs. J. Cell Biol. 98:1222-30
    • (1984) J. Cell Biol. , vol.98 , pp. 1222-1230
    • Lohka, M.J.1    Masui, Y.2
  • 85
    • 0028355167 scopus 로고
    • Sperm nuclear transformations in cytoplasmic extracts from surf clam (Spisula solidissima) oocytes
    • Longo FJ, Mathews L, Palazzo RE. 1994. Sperm nuclear transformations in cytoplasmic extracts from surf clam (Spisula solidissima) oocytes. Dev. Biol. 162:245-58
    • (1994) Dev. Biol. , vol.162 , pp. 245-258
    • Longo, F.J.1    Mathews, L.2    Palazzo, R.E.3
  • 86
    • 0030004283 scopus 로고    scopus 로고
    • Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: Increase of lamin LI protein synthesis during meiotic maturation
    • Lourim D, Kempf A, Krohne G. 1996. Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: increase of lamin LI protein synthesis during meiotic maturation. J. Cell Sci. 109:1775-85
    • (1996) J. Cell Sci. , vol.109 , pp. 1775-1785
    • Lourim, D.1    Kempf, A.2    Krohne, G.3
  • 87
    • 0027437569 scopus 로고
    • Membrane-associated lamins in Xenopus egg extracts: Identification of two vesicle populations
    • Lourim D, Krohne G. 1993. Membrane-associated lamins in Xenopus egg extracts: identification of two vesicle populations. J. Cell Biol. 123(3):501-12
    • (1993) J. Cell Biol. , vol.123 , Issue.3 , pp. 501-512
    • Lourim, D.1    Krohne, G.2
  • 88
    • 0028067708 scopus 로고
    • Lamin-dependent nuclear envelope reassembly following mitosis: An argument
    • Lourim D, Krohne G. 1994. Lamin-dependent nuclear envelope reassembly following mitosis: an argument. Trends Cell Biol. 4:314-18
    • (1994) Trends Cell Biol. , vol.4 , pp. 314-318
    • Lourim, D.1    Krohne, G.2
  • 89
    • 0026559677 scopus 로고
    • Nucleoplasmic localization of prelamin A: Implications for prenylation-dependent lamin A assembly into the nuclear lamina
    • Lutz RJ, Trujillo MA, Denham KS, Wenger L, Sinensky M. 1992. Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc. Natl. Acad. Sci. USA 89:3000-4
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3000-3004
    • Lutz, R.J.1    Trujillo, M.A.2    Denham, K.S.3    Wenger, L.4    Sinensky, M.5
  • 90
    • 0000450002 scopus 로고    scopus 로고
    • Reconstitution of nuclear pore assembly and function
    • Macaulay C, Forbes DJ. 1996a. Reconstitution of nuclear pore assembly and function. Semin. Cell Dev. Biol. 7:475-86
    • (1996) Semin. Cell Dev. Biol. , vol.7 , pp. 475-486
    • Macaulay, C.1    Forbes, D.J.2
  • 91
    • 0030047960 scopus 로고    scopus 로고
    • Assembly of the nuclear pore-biochemically distinct steps revealed with NEM, GTPγS, and BAPTA
    • Macaulay C, Forbes DJ. 1996b. Assembly of the nuclear pore-biochemically distinct steps revealed with NEM, GTPγS, and BAPTA. J. Cell Biol. 132:5-20
    • (1996) J. Cell Biol. , vol.132 , pp. 5-20
    • Macaulay, C.1    Forbes, D.J.2
  • 92
    • 0028853451 scopus 로고
    • Differential mitotic phosphorylation of proteins of the nuclear pore complex
    • Macaulay C, Meier E, Forbes DJ. 1995. Differential mitotic phosphorylation of proteins of the nuclear pore complex. J. Biol. Chem. 270:254-62
    • (1995) J. Biol. Chem. , vol.270 , pp. 254-262
    • Macaulay, C.1    Meier, E.2    Forbes, D.J.3
  • 93
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • Manilal S, Man NT, Sewry CA, Morris GE. 1996. The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet. 5:801-8
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 801-808
    • Manilal, S.1    Man, N.T.2    Sewry, C.A.3    Morris, G.E.4
  • 94
    • 0031044199 scopus 로고    scopus 로고
    • 2+ stores are not required for nuclear envelope assembly or nuclear protein import in Xenopus egg extract
    • 2+ stores are not required for nuclear envelope assembly or nuclear protein import in Xenopus egg extract. Cell Calcium 21:151-61
    • (1997) Cell Calcium , vol.21 , pp. 151-161
    • Marshall, I.C.B.1    Gant, T.M.2    Wilson, K.W.3
  • 96
    • 0028949732 scopus 로고
    • CDNA cloning and characterization of laminaassociated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane
    • Martin L, Crimaudo C, Gerace L. 1995. cDNA cloning and characterization of laminaassociated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane. J. Biol. Chem. 270:8822-28
    • (1995) J. Biol. Chem. , vol.270 , pp. 8822-8828
    • Martin, L.1    Crimaudo, C.2    Gerace, L.3
  • 97
    • 0017744795 scopus 로고
    • Nuclear pore complexes. Elimination and reconstruction during mitosis
    • Maul GG. 1977. Nuclear pore complexes. Elimination and reconstruction during mitosis. J. Cell Biol. 74:492-500
    • (1977) J. Cell Biol. , vol.74 , pp. 492-500
    • Maul, G.G.1
  • 98
    • 0029011832 scopus 로고
    • Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation
    • Meier E, Miller BR, Forbes DJ. 1995. Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation. J. Cell Biol. 129:1459-72
    • (1995) J. Cell Biol. , vol.129 , pp. 1459-1472
    • Meier, E.1    Miller, B.R.2    Forbes, D.J.3
  • 99
    • 0026016285 scopus 로고
    • The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs
    • Meier J, Campbell KH, Ford CC, Stick R, Hutchison CJ. 1991. The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs. J. Cell Sci. 98:271-79
    • (1991) J. Cell Sci. , vol.98 , pp. 271-279
    • Meier, J.1    Campbell, K.H.2    Ford, C.C.3    Stick, R.4    Hutchison, C.J.5
  • 100
    • 0028204109 scopus 로고
    • Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: Implications for nuclear reassembly
    • Meier J, Georgatos SD. 1994. Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: implications for nuclear reassembly. EMBO J. 13:1888-98
    • (1994) EMBO J. , vol.13 , pp. 1888-1898
    • Meier, J.1    Georgatos, S.D.2
  • 101
    • 0028365865 scopus 로고
    • Functional nuclear pores reconstituted with beta 1-4 galactose-modified O-linked N-acetylglucosamine glycoproteins
    • Miller MW, Hanover JA. 1994. Functional nuclear pores reconstituted with beta 1-4 galactose-modified O-linked N-acetylglucosamine glycoproteins. J. Biol. Chem. 269: 9289-97
    • (1994) J. Biol. Chem. , vol.269 , pp. 9289-9297
    • Miller, M.W.1    Hanover, J.A.2
  • 103
    • 0028130694 scopus 로고
    • Dinoflagellates have a eukaiyotic nuclear matrix with lamin-like proteins and topoisomerase II
    • Mínguez A, Franca S, de la Espina SMD. 1994. Dinoflagellates have a eukaiyotic nuclear matrix with lamin-like proteins and topoisomerase II. J. Cell Sci. 107:2861-73
    • (1994) J. Cell Sci. , vol.107 , pp. 2861-2873
    • Mínguez, A.1    Franca, S.2    De La Espina, S.M.D.3
  • 105
    • 0028247078 scopus 로고
    • Dynamic properties of nuclear lamins: Lamin B is associated with sites of DNA replication
    • Moir RD, Montag-Lowy M, Goldman RD. 1994. Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J. Cell Biol. 125:1201-12
    • (1994) J. Cell Biol. , vol.125 , pp. 1201-1212
    • Moir, R.D.1    Montag-Lowy, M.2    Goldman, R.D.3
  • 106
    • 0029874852 scopus 로고    scopus 로고
    • Ernenn deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy
    • Nagano A, Koga R, Ogawa M, Kurano Y, Kawada J, et al. 1996. Ernenn deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy. Nat. Genet. 12:254-59
    • (1996) Nat. Genet. , vol.12 , pp. 254-259
    • Nagano, A.1    Koga, R.2    Ogawa, M.3    Kurano, Y.4    Kawada, J.5
  • 107
    • 0023667788 scopus 로고
    • Nuclear reconstitution in vitro: Stages of assembly around protein-free DNA
    • Newport J. 1987. Nuclear reconstitution in vitro: stages of assembly around protein-free DNA. Cell 48:205-17
    • (1987) Cell , vol.48 , pp. 205-217
    • Newport, J.1
  • 108
    • 0026501103 scopus 로고
    • Characterization of the membrane binding and fusion events during nuclear envelope assembly using purified components
    • Newport J, Dunphy W. 1992. Characterization of the membrane binding and fusion events during nuclear envelope assembly using purified components. J. Cell Biol. 116:295-306
    • (1992) J. Cell Biol. , vol.116 , pp. 295-306
    • Newport, J.1    Dunphy, W.2
  • 109
    • 0023085878 scopus 로고
    • The nucleus: Structure, function, and dynamics
    • Newport JW, Forbes DJ. 1987. The nucleus: structure, function, and dynamics. Annu. Rev. Biochem. 56:535-65
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 535-565
    • Newport, J.W.1    Forbes, D.J.2
  • 110
    • 0025612124 scopus 로고
    • A lamin-independent pathway for nuclear envelope assembly
    • Newport JW, Wilson KL, Dunphy WG. 1990. A lamin-independent pathway for nuclear envelope assembly. J. Cell Biol. 111:2247-59
    • (1990) J. Cell Biol. , vol.111 , pp. 2247-2259
    • Newport, J.W.1    Wilson, K.L.2    Dunphy, W.G.3
  • 111
    • 0030051440 scopus 로고    scopus 로고
    • ER membrane protein complex required for nuclear fusion
    • Ng DT, Walter P. 1996. ER membrane protein complex required for nuclear fusion. J. Cell Biol. 132:499-509
    • (1996) J. Cell Biol. , vol.132 , pp. 499-509
    • Ng, D.T.1    Walter, P.2
  • 112
    • 0029558856 scopus 로고
    • The architectural organization of nuclear metabolism
    • Nickerson JA, Blencowe BJ, Penman S. 1995. The architectural organization of nuclear metabolism. Int. Rev. Cytol. 162A:67-123
    • (1995) Int. Rev. Cytol. , vol.162 A , pp. 67-123
    • Nickerson, J.A.1    Blencowe, B.J.2    Penman, S.3
  • 113
    • 0029942782 scopus 로고    scopus 로고
    • A nuclear envelope-associated kinase phosphorylates arginine-serine motifs and modulates interactions between the lamin B receptor and other nuclear proteins
    • Nikolakaki E, Simos G, Spyros D, Georgatos SD, Giannakouros T. 1996. A nuclear envelope-associated kinase phosphorylates arginine-serine motifs and modulates interactions between the lamin B receptor and other nuclear proteins. J. Biol. Chem. 271:8365-72
    • (1996) J. Biol. Chem. , vol.271 , pp. 8365-8372
    • Nikolakaki, E.1    Simos, G.2    Spyros, D.3    Georgatos, S.D.4    Giannakouros, T.5
  • 115
    • 0021688788 scopus 로고
    • GTP stimulates fusion between homologous and heterologous nuclear membranes
    • Paiement J. 1984. GTP stimulates fusion between homologous and heterologous nuclear membranes. Biochim. Biophys. Acta 777:274-82
    • (1984) Biochim. Biophys. Acta , vol.777 , pp. 274-282
    • Paiement, J.1
  • 116
    • 0029922169 scopus 로고    scopus 로고
    • Molecular dissection of the nuclear pore complex
    • Panté N, Aebi U. 1996. Molecular dissection of the nuclear pore complex. Crit. Rev. Biochem. Mol. Biol. 31:153-99
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 153-199
    • Panté, N.1    Aebi, U.2
  • 117
    • 0023409127 scopus 로고
    • A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant
    • Park MK, D'Onofrio M, Willingham MC, Hanover JA. 1987. A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant. Proc. Natl. Acad. Sci. USA 84:6462-66
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6462-6466
    • Park, M.K.1    D'Onofrio, M.2    Willingham, M.C.3    Hanover, J.A.4
  • 118
    • 0030029383 scopus 로고    scopus 로고
    • The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
    • Paulin-Levasseur M, Blake DL, Julien M, Rouleau L. 1996. The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells. Chromosoma 104:367-79
    • (1996) Chromosoma , vol.104 , pp. 367-379
    • Paulin-Levasseur, M.1    Blake, D.L.2    Julien, M.3    Rouleau, L.4
  • 119
    • 0029078045 scopus 로고
    • Rethinking cell structure
    • Penman S. 1995. Rethinking cell structure. Proc. Natl. Acad. Sci. USA 92:5251-57
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5251-5257
    • Penman, S.1
  • 120
    • 0025666495 scopus 로고
    • Intemuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: In vivo evidence for the interaction of p55 with the nuclear lamina
    • Powell L, Burke B. 1990. Intemuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina. J. Cell Biol. 111:2225-34
    • (1990) J. Cell Biol. , vol.111 , pp. 2225-2234
    • Powell, L.1    Burke, B.2
  • 121
    • 0031046477 scopus 로고    scopus 로고
    • The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways
    • Powers MA, Forbes DJ, Dahlberg JE, Lund E. 1997. The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J. Cell Biol. 136:241-50
    • (1997) J. Cell Biol. , vol.136 , pp. 241-250
    • Powers, M.A.1    Forbes, D.J.2    Dahlberg, J.E.3    Lund, E.4
  • 122
    • 0028906840 scopus 로고
    • Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication
    • Powers MA, Macaulay C, Masiarz FR, Forbes DJ. 1995. Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication. J. Cell Biol. 128:721-36
    • (1995) J. Cell Biol. , vol.128 , pp. 721-736
    • Powers, M.A.1    Macaulay, C.2    Masiarz, F.R.3    Forbes, D.J.4
  • 123
    • 0030480104 scopus 로고    scopus 로고
    • The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope
    • Pyrpasopoulou A, Meier J, Maison C, Simos G, Georgatos SD. 1996. The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope. EMBO J. 15:7108-19
    • (1996) EMBO J. , vol.15 , pp. 7108-7119
    • Pyrpasopoulou, A.1    Meier, J.2    Maison, C.3    Simos, G.4    Georgatos, S.D.5
  • 124
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R, Holzenburg A, Buhle E Jr, Jarnik M, Engel A, Aebi U. 1990. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110:883-94
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle Jr., E.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 125
    • 0027989786 scopus 로고
    • Pores for thought: Nuclear pore complex proteins
    • Rout MP, Wente SR. 1994. Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4:357-65
    • (1994) Trends Cell Biol. , vol.4 , pp. 357-365
    • Rout, M.P.1    Wente, S.R.2
  • 126
    • 0029775680 scopus 로고    scopus 로고
    • Nuclear fusion in the yeast Saccharomyces cerevisiae
    • Rose MD. 1996. Nuclear fusion in the yeast Saccharomyces cerevisiae. Annu. Rev. Cell Dev. Biol. 12:663-95
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 663-695
    • Rose, M.D.1
  • 127
    • 0029930331 scopus 로고    scopus 로고
    • NuMA assembles into an extensive filamentous structure when expressed in the cell cytoplasm
    • Saredi A, Howard L, Compton DA. 1996. NuMA assembles into an extensive filamentous structure when expressed in the cell cytoplasm. J. Cell Sci. 109:619-30
    • (1996) J. Cell Sci. , vol.109 , pp. 619-630
    • Saredi, A.1    Howard, L.2    Compton, D.A.3
  • 128
    • 0029585540 scopus 로고
    • In vivo assembly kinetics of fluorescently labeled Xenopus lamin A mutants
    • Schmidt M, Krohne G. 1995. In vivo assembly kinetics of fluorescently labeled Xenopus lamin A mutants. Eur. J. Cell Biol. 68:345-54
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 345-354
    • Schmidt, M.1    Krohne, G.2
  • 130
    • 0029973561 scopus 로고    scopus 로고
    • A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex
    • Schneller R, Hitomi M, Ivessa AS, Fasch E-V, Kohlwein SD, Tartakoff AM. 1996. A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex. Mol. Cell. Biol. 16:7161-72
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7161-7172
    • Schneller, R.1    Hitomi, M.2    Ivessa, A.S.3    Fasch, E.-V.4    Kohlwein, S.D.5    Tartakoff, A.M.6
  • 131
    • 0028237891 scopus 로고
    • Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane
    • Schuler E, Lin F, Worman HJ. 1994. Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane. J. Biol. Chem. 269:11312-17
    • (1994) J. Biol. Chem. , vol.269 , pp. 11312-11317
    • Schuler, E.1    Lin, F.2    Worman, H.J.3
  • 132
    • 0024263203 scopus 로고
    • Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina
    • Senior A, Gerace L. 1988. Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol. 107:2029-36
    • (1988) J. Cell Biol. , vol.107 , pp. 2029-2036
    • Senior, A.1    Gerace, L.2
  • 133
    • 0026671560 scopus 로고
    • The inner nuclear membrane protein p58 associates in vivo with ap58 kinase and the nuclear lamins
    • Simos G, Georgatos SD. 1992. The inner nuclear membrane protein p58 associates in vivo with ap58 kinase and the nuclear lamins. EMBO J. 11:4027-36
    • (1992) EMBO J. , vol.11 , pp. 4027-4036
    • Simos, G.1    Georgatos, S.D.2
  • 134
    • 0027940369 scopus 로고
    • Colocalization of vertebrate lamin B and lamin B receptor (LBR) in nuclear envelopes and in LBR-induced membrane stacks of the yeast Saccharomyces cerevisiae
    • Smith S, Blobel G. 1994. Colocalization of vertebrate lamin B and lamin B receptor (LBR) in nuclear envelopes and in LBR-induced membrane stacks of the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 91:10124-28
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10124-10128
    • Smith, S.1    Blobel, G.2
  • 135
    • 0027500249 scopus 로고
    • The aminoterminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B, Worman H. 1993. The aminoterminal domain of the lamin B receptor is a nuclear envelope targeting signal. J. Cell Biol. 120:1093-100
    • (1993) J. Cell Biol. , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.2
  • 136
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • Soullam B, Worman H. 1995. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J. Cell Biol. 130:15-27
    • (1995) J. Cell Biol. , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.2
  • 137
    • 0029981666 scopus 로고    scopus 로고
    • Nuclear pores and macromolecular assemblies involved in nucleocytoplasmic transport
    • Stewart M, Clarkson WD. 1996. Nuclear pores and macromolecular assemblies involved in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 6:162-65
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 162-165
    • Stewart, M.1    Clarkson, W.D.2
  • 138
    • 0024095062 scopus 로고
    • CDNA cloning of the. developmentally regulated lamin Liii of Xenopus laevis
    • Stick R. 1988. cDNA cloning of the. developmentally regulated lamin Liii of Xenopus laevis. EMBO J. 7:3189-97
    • (1988) EMBO J. , vol.7 , pp. 3189-3197
    • Stick, R.1
  • 139
    • 0023690364 scopus 로고
    • 2 between inner nuclear membrane and elements of the endoplasmicrettculum
    • 2 between inner nuclear membrane and elements of the endoplasmicrettculum. J. Cell Biol. 107:397-406
    • (1988) J. Cell Biol. , vol.107 , pp. 397-406
    • Stick, R.1    Angres, B.2    Lehner, C.F.3    Nigg, E.A.4
  • 140
    • 0029791261 scopus 로고    scopus 로고
    • Functional compartmentalization of the nucleus
    • Strouboulis J, Wolffe AR 1996. Functional compartmentalization of the nucleus. J. Cell Sci. 109:1991-2000
    • (1996) J. Cell Sci. , vol.109 , pp. 1991-2000
    • Strouboulis, J.1    Wolffe, A.R.2
  • 142
    • 0029027826 scopus 로고
    • Inhibition of nuclear vesicle fusion by antibodies that block activation of inositol 1,4,5-trisphosphate receptors
    • Sullivan KMC, Lin DD, Agnew W, Wilson KL. 1995. Inhibition of nuclear vesicle fusion by antibodies that block activation of inositol 1,4,5-trisphosphate receptors, Proc. Natl. Acad. Sci. USA 92:8611-15
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8611-8615
    • Sullivan, K.M.C.1    Lin, D.D.2    Agnew, W.3    Wilson, K.L.4
  • 143
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura H, Glass C, Gerace L. 1995. A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J. Cell Biol. 131:33-44
    • (1995) J. Cell Biol. , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 144
    • 0024828115 scopus 로고
    • Nuclear envelope assembly around sperm chromatin in cell-free preparations from Drosophila embryos
    • Ulitzur N, Gruenbaum Y. 1989. Nuclear envelope assembly around sperm chromatin in cell-free preparations from Drosophila embryos. FEBS Lett. 259:113-16
    • (1989) FEBS Lett. , vol.259 , pp. 113-116
    • Ulitzur, N.1    Gruenbaum, Y.2
  • 145
    • 0026071202 scopus 로고
    • A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs
    • Vigers GP, Lohka MJ. 1991. A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs. J. Cell Biol. 112:545-56
    • (1991) J. Cell Biol. , vol.112 , pp. 545-556
    • Vigers, G.P.1    Lohka, M.J.2
  • 146
    • 0026650511 scopus 로고
    • Regulation of nuclear envelope precursor functions during cell division
    • Vigers GP, Lohka MJ. 1992. Regulation of nuclear envelope precursor functions during cell division. J. Cell Sci. 102:273-84
    • (1992) J. Cell Sci. , vol.102 , pp. 273-284
    • Vigers, G.P.1    Lohka, M.J.2
  • 147
    • 0022395805 scopus 로고
    • Membrane traffic and organelle division
    • Warren G. 1985. Membrane traffic and organelle division. Trends Bioch. Sci. 11:439-43
    • (1985) Trends Bioch. Sci. , vol.11 , pp. 439-443
    • Warren, G.1
  • 148
    • 0030040690 scopus 로고    scopus 로고
    • Organelle inheritance
    • Warren G, Wickner W. 1996. Organelle inheritance. Cell 84:395-400
    • (1996) Cell , vol.84 , pp. 395-400
    • Warren, G.1    Wickner, W.2
  • 149
    • 0027290725 scopus 로고
    • Dynamics of organelles in the mitotic spindles of living cells: Membrane and microtubule interactions
    • Waterman-Storer CM, Sanger JW, Sanger JM. 1993. Dynamics of organelles in the mitotic spindles of living cells: membrane and microtubule interactions. Cell Motil. Cytoskelet. 26:19-39
    • (1993) Cell Motil. Cytoskelet. , vol.26 , pp. 19-39
    • Waterman-Storer, C.M.1    Sanger, J.W.2    Sanger, J.M.3
  • 150
    • 0028863843 scopus 로고
    • The actin-related protein Act3 of Saccharomyces cerevisiae is located in the nucleus
    • Weber V, Harata M, Hauser H, Wintersberger U. 1995. The actin-related protein Act3 of Saccharomyces cerevisiae is located in the nucleus. Mol. Biol. Cell 6:1263-70
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1263-1270
    • Weber, V.1    Harata, M.2    Hauser, H.3    Wintersberger, U.4
  • 151
    • 0023765935 scopus 로고
    • A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro
    • Wilson KL, Newport J. 1988. A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro. J. Cell Biol. 107:57-68
    • (1988) J. Cell Biol. , vol.107 , pp. 57-68
    • Wilson, K.L.1    Newport, J.2
  • 152
    • 0000305005 scopus 로고    scopus 로고
    • Reconstituting the nuclear envelope and endoplasmic reticulum in vitro
    • Wilson KL, Wiese C. 1996. Reconstituting the nuclear envelope and endoplasmic reticulum in vitro. Semin. Cell Dev. Biol. 7:487-96
    • (1996) Semin. Cell Dev. Biol. , vol.7 , pp. 487-496
    • Wilson, K.L.1    Wiese, C.2
  • 153
    • 0030794456 scopus 로고    scopus 로고
    • Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent 'envelope smoothing' event
    • Wiese C, Goldberg MW, Allen TD, Wilson KL. 1997. Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent 'envelope smoothing' event. J. Cell Sci. 110:1489-502
    • (1997) J. Cell Sci. , vol.110 , pp. 1489-1502
    • Wiese, C.1    Goldberg, M.W.2    Allen, T.D.3    Wilson, K.L.4
  • 154
    • 0025149541 scopus 로고
    • The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains
    • Worman HJ, Evans CD, Blobel G. 1990. The lamin B receptor of the nuclear envelope inner membrane: a polytopic protein with eight potential transmembrane domains. J. Cell Biol. 111:1535-42
    • (1990) J. Cell Biol. , vol.111 , pp. 1535-1542
    • Worman, H.J.1    Evans, C.D.2    Blobel, G.3
  • 156
    • 0024360678 scopus 로고
    • Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
    • Wozniak RW, Bartnik E, Blobel G. 1989. Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J. Cell Biol. 108:2083-92
    • (1989) J. Cell Biol. , vol.108 , pp. 2083-2092
    • Wozniak, R.W.1    Bartnik, E.2    Blobel, G.3
  • 157
    • 0027043255 scopus 로고
    • The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope
    • Wozniak RW. Blobel G. 1992. The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. J. Cell Biol. 119:1441-49
    • (1992) J. Cell Biol. , vol.119 , pp. 1441-1449
    • Wozniak, R.W.1    Blobel, G.2
  • 158
    • 0029917273 scopus 로고    scopus 로고
    • Chromosome assignment of human nuclear envelope protein genes LMNB1, LMNB2, and LBR by fluorescent in situ hybridzation
    • Wydner KL, McNeil JA, Lin F, Worman JH, Lawrence JB. 1996. Chromosome assignment of human nuclear envelope protein genes LMNB1, LMNB2, and LBR by fluorescent in situ hybridzation. Genomics 32:474-78
    • (1996) Genomics , vol.32 , pp. 474-478
    • Wydner, K.L.1    McNeil, J.A.2    Lin, F.3    Worman, J.H.4    Lawrence, J.B.5
  • 159
    • 0029615378 scopus 로고
    • Nonrandom gene organization: Structural arrangements of specific pre-mRNA transcription and splicing with SC-35 domains
    • Xing Y, Johnson CV, Moen PT Jr, McNeil MA, Lawrence JB. 1995. Nonrandom gene organization: structural arrangements of specific pre-mRNA transcription and splicing with SC-35 domains. J. Cell Biol. 131:1635-47
    • (1995) J. Cell Biol. , vol.131 , pp. 1635-1647
    • Xing, Y.1    Johnson, C.V.2    Moen Jr., P.T.3    McNeil, M.A.4    Lawrence, J.B.5
  • 160
    • 0030979570 scopus 로고    scopus 로고
    • A role for the divergent actin gene, ACT2, in nuclear pore structure and function
    • Yan C, Leibovitz N, Mélèse T. 1997. A role for the divergent actin gene, ACT2, in nuclear pore structure and function. EMBO J. 16:3572-86
    • (1997) EMBO J. , vol.16 , pp. 3572-3586
    • Yan, C.1    Leibovitz, N.2    Mélèse, T.3
  • 161
    • 0030987777 scopus 로고    scopus 로고
    • Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR
    • Ye Q, Callebaut I, Pezhman A, Courvalin J-C, Worman HJ. 1997. Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. J. Biol Chem. 272:14983-89
    • (1997) J. Biol Chem. , vol.272 , pp. 14983-14989
    • Ye, Q.1    Callebaut, I.2    Pezhman, A.3    Courvalin, J.-C.4    Worman, H.J.5
  • 162
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane
    • Ye Q, Worman HJ. 1994. Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane. J. Biol. Chem. 269:11306-11
    • (1994) J. Biol. Chem. , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 163
    • 17544383469 scopus 로고    scopus 로고
    • Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1
    • Ye Q, Worman HJ. 1996. Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J. Biol. Chem. 271:14653-56
    • (1996) J. Biol. Chem. , vol.271 , pp. 14653-14656
    • Ye, Q.1    Worman, H.J.2
  • 165
    • 0018772482 scopus 로고
    • Mitosis in rat thyroid epithelial cells in vivo: Ultrastructural changes in cytoplasmic organelles during the mitotic cycle
    • Zeugs JD, Wollman SH. 1979. Mitosis in rat thyroid epithelial cells in vivo: ultrastructural changes in cytoplasmic organelles during the mitotic cycle. J. Ultrastruc. Res. 66:53-77
    • (1979) J. Ultrastruc. Res. , vol.66 , pp. 53-77
    • Zeugs, J.D.1    Wollman, S.H.2
  • 166
    • 0029814578 scopus 로고    scopus 로고
    • Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract
    • Zhang C, Jenkins H, Goldberg MW, Allen TD, Hutchison CJ. 1996. Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract. J. Cell Sci. 109:2275-86
    • (1996) J. Cell Sci. , vol.109 , pp. 2275-2286
    • Zhang, C.1    Jenkins, H.2    Goldberg, M.W.3    Allen, T.D.4    Hutchison, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.