메뉴 건너뛰기




Volumn 109, Issue 9, 1996, Pages 2275-2286

Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract

Author keywords

Nuclear lamina; Nuclear matrix; Xenopus egg extract

Indexed keywords

LAMIN; LAMIN B;

EID: 0029814578     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (41)

References (73)
  • 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
    • 0025362748 scopus 로고
    • Isoprenylation is required for the processing of the lamin A precursor
    • Beck, L. A., Hosick, T. J. and Sinensky, M. (1990). Isoprenylation is required for the processing of the lamin A precursor. J. Cell Biol. 110, 1489-1499.
    • (1990) J. Cell Biol. , vol.110 , pp. 1489-1499
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 3
    • 0021842623 scopus 로고
    • Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis
    • Benevente, R., Krohne, G. and Franke, W. W. (1985). Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis. Cell 41, 177-190.
    • (1985) Cell , vol.41 , pp. 177-190
    • Benevente, R.1    Krohne, G.2    Franke, W.W.3
  • 5
    • 0017687532 scopus 로고
    • Nuclear matrix: Isolation and characterization of a framework structure from rat liver nuclei
    • Berezney, R. and Coffey, D. S. (1977). Nuclear matrix: isolation and characterization of a framework structure from rat liver nuclei. J. Cell Biol. 73, 616-637.
    • (1977) J. Cell Biol. , vol.73 , pp. 616-637
    • Berezney, R.1    Coffey, D.S.2
  • 6
    • 0019883926 scopus 로고
    • Isolation and characterization of rat liver nuclear matrices containing high molecular weight deoxyribonucleic acid
    • Berezney, R. and Buchold, L. A. (1981). Isolation and characterization of rat liver nuclear matrices containing high molecular weight deoxyribonucleic acid. Biochemistry 20, 4495-5002.
    • (1981) Biochemistry , vol.20 , pp. 4495-5002
    • Berezney, R.1    Buchold, L.A.2
  • 7
    • 0022981734 scopus 로고
    • Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs
    • Blow, J. J. and Laskey, R. A. (1986). Initiation of DNA replication in nuclei and purified DNA by a cell-free extract of Xenopus eggs. Cell 47, 577-587.
    • (1986) Cell , vol.47 , pp. 577-587
    • Blow, J.J.1    Laskey, R.A.2
  • 8
    • 1842322089 scopus 로고
    • Nuclei act as independent and integrated units of DNA replication in within the cell cycle
    • Blow, J. J. and Watson, J. V. (1987). Nuclei act as independent and integrated units of DNA replication in within the cell cycle. EMBO J. 6, 1997-2002.
    • (1987) EMBO J. , vol.6 , pp. 1997-2002
    • Blow, J.J.1    Watson, J.V.2
  • 9
    • 0023904730 scopus 로고
    • A role for the nuclear envelope in controlling DNA replication within the cell cycle
    • Blow, J. J. and Laskey, R. A. (1988). A role for the nuclear envelope in controlling DNA replication within the cell cycle. Nature 332, 546-548.
    • (1988) Nature , vol.332 , pp. 546-548
    • Blow, J.J.1    Laskey, R.A.2
  • 10
    • 0343699488 scopus 로고
    • Lamin B methylation and assembly into nuclear envelope
    • Chelsky, D., Olson, J. F. and Koskland, D. E. (1987). Lamin B methylation and assembly into nuclear envelope. J. Biol. Chem. 262, 4304-4309.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4304-4309
    • Chelsky, D.1    Olson, J.F.2    Koskland, D.E.3
  • 11
    • 0026600132 scopus 로고
    • Primary structure of NuMa, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis
    • Compton, D. A., Szilak, I. and Cleveland, D. W. (1992). Primary structure of NuMa, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis. J. Cell Biol. 116, 1395-1408.
    • (1992) J. Cell Biol. , vol.116 , pp. 1395-1408
    • Compton, D.A.1    Szilak, I.2    Cleveland, D.W.3
  • 12
    • 0028247393 scopus 로고
    • Nuclear envelope assembly and disassembly
    • (ed. A. H. Maddy and J. R. Harris), Plenum Press, NY
    • Cox, L. S. and Hutchison, C. J. (1994). Nuclear envelope assembly and disassembly. In Subcellular Biochemistry, vol. 22, Membrane Biogenesis (ed. A. H. Maddy and J. R. Harris), pp. 263-325. Plenum Press, NY.
    • (1994) Subcellular Biochemistry, Vol. 22, Membrane Biogenesis , vol.22 , pp. 263-325
    • Cox, L.S.1    Hutchison, C.J.2
  • 13
    • 0025053673 scopus 로고
    • Gene structure for nuclear lamin Liii of Xenopus laevis: A model for the evolution of if proteins from a lamin-like ancestor
    • Doring, V. and Stick, R. (1990). Gene structure for nuclear lamin Liii of Xenopus laevis: A model for the evolution of IF proteins from a lamin-like ancestor. EMBO J. 9, 4073-4081.
    • (1990) EMBO J. , vol.9 , pp. 4073-4081
    • Doring, V.1    Stick, R.2
  • 14
    • 0017134119 scopus 로고
    • A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei
    • Dwyer, N. and Blobel, G. (1976). A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei, J. Cell Biol. 70, 581-591.
    • (1976) J. Cell Biol. , vol.70 , pp. 581-591
    • Dwyer, N.1    Blobel, G.2
  • 15
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three dimensional organisation and protein composition
    • Fey, E. G., Wan, K. M. and Penman, S. (1984). Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: Three dimensional organisation and protein composition, J. Cell Biol. 98, 1973-1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 16
    • 0022521416 scopus 로고
    • The nonchromatin substructures of the nucleus: The ribonucleoprotein(RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy
    • Fey, E. G., Kronchmalic, G. and Penman, S. (1986). The nonchromatin substructures of the nucleus: the ribonucleoprotein(RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy. J. Cell Biol. 102, 1654-1665.
    • (1986) J. Cell Biol. , vol.102 , pp. 1654-1665
    • Fey, E.G.1    Kronchmalic, G.2    Penman, S.3
  • 17
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamina A and C reveals primary and secondary structural homology to intermediate filaments
    • Fisher, D. Z., Chaudhary, N. and Blobel, G. (1986). cDNA sequencing of nuclear lamina A and C reveals primary and secondary structural homology to intermediate filaments. Proc. Nat. Acad. Sci. USA 83, 6450-6454.
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 19
    • 0018093261 scopus 로고
    • Immunocytochemical localization of the major polypeptides of the pore complex-lamina fraction: Interphase and mitotic distribution
    • Gerace, L., Blum, A. and Blobel, G. (1978). Immunocytochemical localization of the major polypeptides of the pore complex-lamina fraction: Interphase and mitotic distribution. J. Cell Biol. 79, 546-566.
    • (1978) J. Cell Biol. , vol.79 , pp. 546-566
    • Gerace, L.1    Blum, A.2    Blobel, G.3
  • 20
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L. and Blobel, G. (1980). The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277-287.
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 21
    • 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, M. W. and Allen, T. D. (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, 1429-1440.
    • (1992) J. Cell Biol. , vol.119 , pp. 1429-1440
    • Goldberg, M.W.1    Allen, T.D.2
  • 22
    • 0028972870 scopus 로고
    • Xenopus lamin 83 has a direct role in the assembly of a replication competent nucleus: Evidence from cell-free egg extracts
    • Goldberg, W. W., Jenkins, H. E., Allen, T. D., Whitfield, W. G. F. and Hutchison, C. J. (1995). Xenopus lamin 83 has a direct role in the assembly of a replication competent nucleus: evidence from cell-free egg extracts. J. Cell Sci. 108, 3451-3461.
    • (1995) J. Cell Sci. , vol.108 , pp. 3451-3461
    • Goldberg, W.W.1    Jenkins, H.E.2    Allen, T.D.3    Whitfield, W.G.F.4    Hutchison, C.J.5
  • 23
    • 0026478894 scopus 로고
    • Pathway of incorporation of microinjected lamin A into the nuclear envelope
    • Goldman, A. E., Moir, R. D., Montag-Lowy, M., Stewart, M. and Goldman, R. D. (1992). Pathway of incorporation of microinjected lamin A into the nuclear envelope, J. Cell Biol. 119, 725-735.
    • (1992) J. Cell Biol. , vol.119 , pp. 725-735
    • Goldman, A.E.1    Moir, R.D.2    Montag-Lowy, M.3    Stewart, M.4    Goldman, R.D.5
  • 24
    • 0017032838 scopus 로고
    • Injected nuclei in frog oocytes, rate enlargement and chromatin dispersal
    • Gurdon, J. B. (1976). Injected nuclei in frog oocytes, rate enlargement and chromatin dispersal. J. Embryol. Exp. Morphol. 36, 523-540.
    • (1976) J. Embryol. Exp. Morphol. , vol.36 , pp. 523-540
    • Gurdon, J.B.1
  • 25
    • 0029042452 scopus 로고
    • Epitope mapping and direct visualisation of the parallel in-register arrangement of the double-stranded coiled coil in the NuMa protein
    • Harborth, J., Weber, K. and Osborn, M. (1995). Epitope mapping and direct visualisation of the parallel in-register arrangement of the double-stranded coiled coil in the NuMa protein. EMBO J. 14, 2447-2460.
    • (1995) EMBO J. , vol.14 , pp. 2447-2460
    • Harborth, J.1    Weber, K.2    Osborn, M.3
  • 26
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald, R. and McKeon, F. (1990). Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61, 579-589.
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 27
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • He, D., Nickerson, J. A. and Penman, S. (1990). Core filaments of the nuclear matrix. J. Cell Biol. 110, 569-580.
    • (1990) J. Cell Biol. , vol.110 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penman, S.3
  • 28
    • 0024241247 scopus 로고
    • Amino acid sequence and molecular characterisation of a murine lamin B as deduced from cDNA clones
    • Höger, T. H., Krohne, G. and Franke, W. W. (1988). Amino acid sequence and molecular characterisation of a murine lamin B as deduced from cDNA clones. Eur. J. Cell Biol. 47, 283-290.
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 283-290
    • Höger, T.H.1    Krohne, G.2    Franke, W.W.3
  • 29
    • 0027311843 scopus 로고
    • Visualisation of replication factories attached to the nucleoskeleton
    • Hozak, P., Hassen, A. B., Jackson, D. A. and Cook, P. R. (1993). Visualisation of replication factories attached to the nucleoskeleton. Cell 73, 361-373.
    • (1993) Cell , vol.73 , pp. 361-373
    • Hozak, P.1    Hassen, A.B.2    Jackson, D.A.3    Cook, P.R.4
  • 30
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak, P., Sasseville, A. M.-J., Raymond, Y. and Cook, P. R. (1995). Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci. 108, 635-644.
    • (1995) J. Cell Sci. , vol.108 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.-J.2    Raymond, Y.3    Cook, P.R.4
  • 31
    • 0023801390 scopus 로고
    • The control of DNA replication in a cell-free extract that recapitulates a basic cell cycle in vitro
    • Hutchison, C. J., Cox, R. and Ford, C. C. (1988). The control of DNA replication in a cell-free extract that recapitulates a basic cell cycle in vitro. Development 103, 553-566.
    • (1988) Development , vol.103 , pp. 553-566
    • Hutchison, C.J.1    Cox, R.2    Ford, C.C.3
  • 32
    • 0028587430 scopus 로고
    • Weaving a pattern from disparate threads: Lamin function in nuclear assembly and DNA replication
    • Hutchison, C. J., Bridger, J. M., Cox, L. S. and Kill, I. R. (1994). Weaving a pattern from disparate threads: lamin function in nuclear assembly and DNA replication. J. Cell Sci. 107, 3259-3269.
    • (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
  • 33
    • 0001816058 scopus 로고
    • The use of cell-free extracts of Xenopus eggs for studying DNA replication in vitro
    • (ed. P. Fantes and R. Brooks), IRL Press
    • Hutchison, C. J. (1994). The use of cell-free extracts of Xenopus eggs for studying DNA replication in vitro. In The Cell Cycle: A Practical Approach (ed. P. Fantes and R. Brooks), pp. 177-196. IRL Press.
    • (1994) The Cell Cycle: A Practical Approach , pp. 177-196
    • Hutchison, C.J.1
  • 34
    • 0028943219 scopus 로고
    • Local and global changes in the distribution of replication centres in rapidly expanding nuclei
    • Hutchison, C. J. (1995). Local and global changes in the distribution of replication centres in rapidly expanding nuclei. Chromosome Res. 3, 16-26.
    • (1995) Chromosome Res. , vol.3 , pp. 16-26
    • Hutchison, C.J.1
  • 35
    • 0023339956 scopus 로고
    • Extracellular matrix regulates endothelial growth factor action through modulation of cell and nuclear expansion
    • Ingber, D. E., Madri, J. A. and Folkman, J. (1987). Extracellular matrix regulates endothelial growth factor action through modulation of cell and nuclear expansion. In Vitro Cell Dev. Biol. 23, 387-394.
    • (1987) In Vitro Cell Dev. Biol. , vol.23 , pp. 387-394
    • Ingber, D.E.1    Madri, J.A.2    Folkman, J.3
  • 36
    • 0025372477 scopus 로고
    • Fibronectin controls capillary endothelial cell growth by modulating cell shape
    • Ingber, D. E. (1990). Fibronectin controls capillary endothelial cell growth by modulating cell shape. Proc. Nat. Acad. Sci. USA 87, 3579-3583.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 3579-3583
    • Ingber, D.E.1
  • 37
    • 0027221483 scopus 로고
    • Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton
    • Ingber, D. E. (1993). Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 104, 613-627.
    • (1993) J. Cell Sci. , vol.104 , pp. 613-627
    • Ingber, D.E.1
  • 38
    • 0022729888 scopus 로고
    • Replication occurs at a nucleoskeleton
    • Jackson, D. A. and Cook, P. R. (1986a). Replication occurs at a nucleoskeleton. EMBO J. 5, 1403-1410.
    • (1986) EMBO J. , vol.5 , pp. 1403-1410
    • Jackson, D.A.1    Cook, P.R.2
  • 39
    • 0023032977 scopus 로고
    • A cell-cycle dependent DNA polymerase activity that replicates intact DNA in chromatin
    • Jackson, D. A. and Cook, P. R. (1986b). A cell-cycle dependent DNA polymerase activity that replicates intact DNA in chromatin. J. Mol. Biol. 192, 65-76.
    • (1986) J. Mol. Biol. , vol.192 , pp. 65-76
    • Jackson, D.A.1    Cook, P.R.2
  • 40
    • 0024221204 scopus 로고
    • Visualization of a filamentous nucleoskeleton with a 23nm axial repeat
    • Jackson, P. R. and Cook, P. R. (1988). Visualization of a filamentous nucleoskeleton with a 23nm axial repeat. EMBO J. 7, 3667-3677.
    • (1988) EMBO J. , vol.7 , pp. 3667-3677
    • Jackson, P.R.1    Cook, P.R.2
  • 41
    • 0027489289 scopus 로고
    • Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix
    • Jenkins, H. E., Holleman, T., Lyon, C., Lane, E. B., Stick, R. and Hutchison, C. J. (1993). Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix. J. Cell Sci. 106, 275-285.
    • (1993) J. Cell Sci. , vol.106 , pp. 275-285
    • Jenkins, H.E.1    Holleman, T.2    Lyon, C.3    Lane, E.B.4    Stick, R.5    Hutchison, C.J.6
  • 43
    • 0343699479 scopus 로고
    • Differential expression of nuclear lamin proteins during chick development
    • Lehner, C. F., Stick, R., Eppenberger, H. M. and Nigg, E. A. (1987). Differential expression of nuclear lamin proteins during chick development. J. Cell Biol. 112, 557-566.
    • (1987) J. Cell Biol. , vol.112 , pp. 557-566
    • Lehner, C.F.1    Stick, R.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 44
    • 0019132556 scopus 로고
    • Human specific nuclear protein that associates with the polar region of the mitotic spindle apparatus: Distribution in a human/hamster hybrid cell
    • Lydersen, B. K. and Pettijohn, D. E. (1980). Human specific nuclear protein that associates with the polar region of the mitotic spindle apparatus: distribution in a human/hamster hybrid cell. Cell 22, 489-499.
    • (1980) Cell , vol.22 , pp. 489-499
    • Lydersen, B.K.1    Pettijohn, D.E.2
  • 45
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • McKeon, F. D., Kirschner, M. W. and Caput, D. (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319, 463-468.
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 46
    • 0026016285 scopus 로고
    • The role of lamin Liii in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs
    • Meier, J., Campbell, K. H. S., Ford, C. C., Stick, R. and Hutchison, C. J. (1991). The role of lamin Liii in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs. J. Cell Sci. 98, 271-279.
    • (1991) J. Cell Sci. , vol.98 , pp. 271-279
    • Meier, J.1    Campbell, K.H.S.2    Ford, C.C.3    Stick, R.4    Hutchison, C.J.5
  • 47
    • 0028204109 scopus 로고
    • Type B lamins remain associated with integral nuclear envelope protein p58 during mitosis; implications for nuclear assembly
    • Meier, J. and Georgatos, S. (1994). Type B lamins remain associated with integral nuclear envelope protein p58 during mitosis; implications for nuclear assembly. EMBO J. 13, 1888-1897.
    • (1994) EMBO J. , vol.13 , pp. 1888-1897
    • Meier, J.1    Georgatos, S.2
  • 48
    • 0021819913 scopus 로고
    • Induction of early mitotic events in a cell-free system
    • Miake-Lye, R. and Kirschner, M. W. (1985). Induction of early mitotic events in a cell-free system. Cell 41, 165-175.
    • (1985) Cell , vol.41 , pp. 165-175
    • Miake-Lye, R.1    Kirschner, M.W.2
  • 49
    • 0024388420 scopus 로고
    • Replication occurs at discrete centres spaced throughout nuclei replicating in vitro
    • Mills, A., Blow, J. J., White, J. G., Amos, W. B., Wilcock, D. and Laskey, R. A. (1989). Replication occurs at discrete centres spaced throughout nuclei replicating in vitro. J. Cell Sci. 94, 471-477.
    • (1989) J. Cell Sci. , vol.94 , pp. 471-477
    • Mills, A.1    Blow, J.J.2    White, J.G.3    Amos, W.B.4    Wilcock, D.5    Laskey, R.A.6
  • 50
    • 0028247078 scopus 로고
    • Dynamic properties of nuclear lamins: Lamin B is associated with sites of DNA replication
    • Moir, R. D., Montag-Lowy, M. and Goldman, R. D. (1994). Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J. Cell Biol. 125, 1201-1212.
    • (1994) J. Cell Biol. , vol.125 , pp. 1201-1212
    • Moir, R.D.1    Montag-Lowy, M.2    Goldman, R.D.3
  • 51
    • 0028836621 scopus 로고
    • The role of protein phosphorylation in the assembly of a replication competent nucleus: Investigations in Xenopus egg extracts using the cyanobacterial toxin microcystin-LR
    • Murphy, J., Crompton, C. M., Hainey, S., Codd, G. A. and Hutchison, C. J. (1995). The role of protein phosphorylation in the assembly of a replication competent nucleus: investigations in Xenopus egg extracts using the cyanobacterial toxin microcystin-LR. J. Cell Sci. 108, 235-244.
    • (1995) J. Cell Sci. , vol.108 , pp. 235-244
    • Murphy, J.1    Crompton, C.M.2    Hainey, S.3    Codd, G.A.4    Hutchison, C.J.5
  • 52
    • 0024526184 scopus 로고
    • Mapping replicational sites in the eucaryotic cell nucleus
    • Nakayasu, H. and Berezney, R. (1989). Mapping replicational sites in the eucaryotic cell nucleus. J. Cell Biol. 108, 1-11.
    • (1989) J. Cell Biol. , vol.108 , pp. 1-11
    • Nakayasu, H.1    Berezney, R.2
  • 53
    • 0025612124 scopus 로고
    • A lamin-dependent pathway for nuclear envelope assembly
    • Newport, J. W., Wilson, K. L. and Dunphy, W. G. (1990). A lamin-dependent pathway for nuclear envelope assembly. J. Cell Biol. 111, 2247-2259.
    • (1990) J. Cell Biol. , vol.111 , pp. 2247-2259
    • Newport, J.W.1    Wilson, K.L.2    Dunphy, W.G.3
  • 55
    • 0022703487 scopus 로고
    • Critical nuclear DNA size and distribution associated with S-phase initiation
    • Nicolini, C., Belmont, A. S. and Martelli, A. (1986). Critical nuclear DNA size and distribution associated with S-phase initiation. Cell Biophys. 8, 103-117.
    • (1986) Cell Biophys. , vol.8 , pp. 103-117
    • Nicolini, C.1    Belmont, A.S.2    Martelli, A.3
  • 56
    • 0342394250 scopus 로고
    • Phosphorylation of the nuclear lamins during interphase and mitosis
    • Ottaviano, Y. and Gerace, L. (1985). Phosphorylation of the nuclear lamins during interphase and mitosis, J. Cell Biol. 101, 518-523.
    • (1985) J. Cell Biol. , vol.101 , pp. 518-523
    • Ottaviano, Y.1    Gerace, L.2
  • 57
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M-phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M., Nakagawa, J., Doree, M., Labbe, J. C. and Nigg, E. A. (1990). In vitro disassembly of the nuclear lamina and M-phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61, 591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 58
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by cdc2 kinase
    • Peter, M., Heitlinger, E., Haner, M., Aebi, U. and Nigg, E. A. (1991). Disassembly of in vitro formed lamin head-to-tail polymers by cdc2 kinase. EMBO J. 10, 1535-1544.
    • (1991) EMBO J. , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Haner, M.3    Aebi, U.4    Nigg, E.A.5
  • 59
    • 0026730766 scopus 로고
    • Nucleo-cytoskeletal interactions: Evidence for physical connections between the nucleus and cell periphery and their alteration by transformation
    • Pienta, K. J. and Coffey, D. S. (1992). Nucleo-cytoskeletal interactions: evidence for physical connections between the nucleus and cell periphery and their alteration by transformation. J. Cell. Biochem. 49, 357-365.
    • (1992) J. Cell. Biochem. , vol.49 , pp. 357-365
    • Pienta, K.J.1    Coffey, D.S.2
  • 60
    • 0024561417 scopus 로고
    • Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study
    • Rober, R.-A., Weber, K. and Osborn, M. (1989). Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: a developmental study. Development 105, 365-378.
    • (1989) Development , vol.105 , pp. 365-378
    • Rober, R.-A.1    Weber, K.2    Osborn, M.3
  • 61
    • 0027090097 scopus 로고
    • Altering the cellular mechanical force balances results in integrated changes in cell, cytoskeletal and nuclear shape
    • Sims, J. R., Karp, S. and Ingber, D. E. (1992). Altering the cellular mechanical force balances results in integrated changes in cell, cytoskeletal and nuclear shape. J. Cell Sci. 103, 1215-1222.
    • (1992) J. Cell Sci. , vol.103 , pp. 1215-1222
    • Sims, J.R.1    Karp, S.2    Ingber, D.E.3
  • 62
    • 0021109437 scopus 로고
    • Dynamic domains of DNA polymerase α in regenerating rat liver
    • Smith, H. C. and Berezney, R. (1983). Dynamic domains of DNA polymerase α in regenerating rat liver. Biochemistry 22, 3042-3046.
    • (1983) Biochemistry , vol.22 , pp. 3042-3046
    • Smith, H.C.1    Berezney, R.2
  • 63
    • 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, 3189-3197.
    • (1988) EMBO J. , vol.7 , pp. 3189-3197
    • Stick, R.1
  • 64
    • 0021859643 scopus 로고
    • Changes in the nuclear lamina composition during early development of Xenopus laevis
    • Stick, R. and Hausen, P. (1985). Changes in the nuclear lamina composition during early development of Xenopus laevis. Cell 41, 191-200.
    • (1985) Cell , vol.41 , pp. 191-200
    • Stick, R.1    Hausen, P.2
  • 65
    • 0023690364 scopus 로고
    • 2 between inner nuclear membrane and elements of the endoplasmic reticulum
    • 2 between inner nuclear membrane and elements of the endoplasmic reticulum. 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
  • 67
    • 0024839672 scopus 로고
    • Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif
    • Vorburger, K., Kitten, G. T. and Nigg, E. A. (1989b). Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif. EMBO J. 8, 4007-4013.
    • (1989) EMBO J. , vol.8 , pp. 4007-4013
    • Vorburger, K.1    Kitten, G.T.2    Nigg, E.A.3
  • 68
    • 0024828257 scopus 로고
    • Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor, implications for the structure of the nuclear lamina
    • Weber, K., Plessman, U. and Traub, P. (1989). Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor, implications for the structure of the nuclear lamina. FEBS Lett. 257, 411-414.
    • (1989) FEBS Lett. , vol.257 , pp. 411-414
    • Weber, K.1    Plessman, U.2    Traub, P.3
  • 69
    • 0023917971 scopus 로고
    • Evidence for modification of lamin B by a product of mevalonic acid
    • Wolda, S. L. and Glomset, J. A. (1988). Evidence for modification of lamin B by a product of mevalonic acid. J. Biol. Chem. 263, 5997-6000.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5997-6000
    • Wolda, S.L.1    Glomset, J.A.2
  • 70
    • 0023517709 scopus 로고
    • A new lamin in Xenopus somatic tissues displays strong homology to a human lamin A
    • Wolin, S. L., Krohne, G. and Kirschner, M. W. (1987). A new lamin in Xenopus somatic tissues displays strong homology to a human lamin A. EMBO J. 6, 3809-3818.
    • (1987) EMBO J. , vol.6 , pp. 3809-3818
    • Wolin, S.L.1    Krohne, G.2    Kirschner, M.W.3
  • 71
    • 0026508382 scopus 로고
    • NuMa: An unusually long coiled-coil related protein in the mammalian nucleus
    • Yang, C. H., Lambie, E. J. and Snyder, M. (1992). NuMa: an unusually long coiled-coil related protein in the mammalian nucleus. J. Cell Biol. 116, 1303-1317.
    • (1992) J. Cell Biol. , vol.116 , pp. 1303-1317
    • Yang, C.H.1    Lambie, E.J.2    Snyder, M.3
  • 72
    • 0018773038 scopus 로고
    • Role of nuclear size in cell growth initiation
    • Yen, A. and Pardee, A. B. (1979). Role of nuclear size in cell growth initiation. Science 204, 1315-1317.
    • (1979) Science , vol.204 , pp. 1315-1317
    • Yen, A.1    Pardee, A.B.2
  • 73
    • 0343488062 scopus 로고
    • Nuclear reassembly in a cell-free system from metaphase HeLa cells
    • Zhang, C., Luo, W. and Zhai, Z. (1993). Nuclear reassembly in a cell-free system from metaphase HeLa cells. Acta Anat. Sinica 24, 158-162.
    • (1993) Acta Anat. Sinica , vol.24 , pp. 158-162
    • Zhang, C.1    Luo, W.2    Zhai, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.