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Volumn 109, Issue 7, 1996, Pages 1775-1785

Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: Increase of lamin L(I) protein synthesis during meiotic maturation

Author keywords

Lamin synthesis; Lamin associated egg vesicle; Quantitation of oocyte lamin; Xenopus egg extract

Indexed keywords

LAMIN B; NUCLEAR PROTEIN;

EID: 0030004283     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (53)

References (68)
  • 1
    • 0027932670 scopus 로고
    • Study of the cell cycle-dependent assembly of the DNA pre-replication centers in Xenopus egg extracts
    • Adachi, Y. and Laemmli, U. (1994). Study of the cell cycle-dependent assembly of the DNA pre-replication centers in Xenopus egg extracts. EMBO J. 13, 4153-4164.
    • (1994) EMBO J. , vol.13 , pp. 4153-4164
    • Adachi, Y.1    Laemmli, U.2
  • 2
    • 0017581482 scopus 로고
    • Changes in the rate of historine synthesis during oocyte maturation and very early development of Xenopus laevis
    • Adamson, E. and Woodland, H. (1977). Changes in the rate of historine synthesis during oocyte maturation and very early development of Xenopus laevis. Dev. Biol. 57, 136-149.
    • (1977) Dev. Biol. , vol.57 , pp. 136-149
    • Adamson, E.1    Woodland, H.2
  • 3
    • 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
  • 4
    • 0027258499 scopus 로고
    • Nuclear assembly, structure, and function: The use of Xenopus in vitro systems
    • Almouzni, G. and Wolffe, A. (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.2
  • 5
    • 0028171402 scopus 로고
    • Regulated expression of the β-globin gene locus in synthetic nuclei
    • Barton, M. and Emerson, B. (1994). Regulated expression of the β-globin gene locus in synthetic nuclei. Genes Dev. 8, 2453-2465.
    • (1994) Genes Dev. , vol.8 , pp. 2453-2465
    • Barton, M.1    Emerson, B.2
  • 6
    • 0011216168 scopus 로고
    • IV, a nuclear lamina protein specific for the male germ line
    • IV, a nuclear lamina protein specific for the male germ line. Proc. Nat. Acad. Sci. USA 82, 6176-6180.
    • (1985) Proc. Nat. Acad. Sci. USA , vol.82 , pp. 6176-6180
    • Benavente, R.1    Krohne, G.2
  • 7
    • 0021842623 scopus 로고
    • Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis
    • Benavente, R., Krohne, G. and Franke, 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
    • Benavente, R.1    Krohne, G.2    Franke, W.3
  • 8
    • 0022977187 scopus 로고
    • Involvement of nuclear lamins in postmitotic reorganization of chromatin as demonstrated by microinjection of lamin antibodies
    • Benavente, R. and Krohne, G. (1986). Involvement of nuclear lamins in postmitotic reorganization of chromatin as demonstrated by microinjection of lamin antibodies. J. Cell Biol. 103, 1847-1854.
    • (1986) J. Cell Biol. , vol.103 , pp. 1847-1854
    • Benavente, R.1    Krohne, G.2
  • 9
    • 0026556684 scopus 로고
    • GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro
    • Boman, A., Delannoy, M. and Wilson, K. (1992). GTP hydrolysis is required for vesicle fusion during nuclear envelope assembly in vitro. J. Cell Biol. 116, 281-294.
    • (1992) J. Cell Biol. , vol.116 , pp. 281-294
    • Boman, A.1    Delannoy, M.2    Wilson, K.3
  • 11
    • 0022517260 scopus 로고
    • A cell free system to study reassembly of the nuclear envelope at the end of mitosis
    • Burke, B. and Gerace, L. (1986). A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 44, 639-652.
    • (1986) Cell , vol.44 , pp. 639-652
    • Burke, B.1    Gerace, L.2
  • 12
    • 0025771404 scopus 로고
    • Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylation region
    • Cordes, V., Waizenegger, I. and Krohne, G. (1991). Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylation region. Eur. J. Cell Biol. 55, 31-47.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 31-47
    • Cordes, V.1    Waizenegger, I.2    Krohne, G.3
  • 13
    • 0029015931 scopus 로고
    • Immunocytochemistry of annulate lamellae: Potential cell biological markers for studies of cell differentiation and pathology
    • Cordes, V., Gajewski, A., Stumpp, S. and Krohne, G. (1995). Immunocytochemistry of annulate lamellae: potential cell biological markers for studies of cell differentiation and pathology. Differentiation 58, 307-312.
    • (1995) Differentiation , vol.58 , pp. 307-312
    • Cordes, V.1    Gajewski, A.2    Stumpp, S.3    Krohne, G.4
  • 14
    • 0026099941 scopus 로고
    • Spontaneous assembly of pore complex-containing membranes ('annulate lamellae') in Xenopus egg extracts in the absence of chromatin
    • Dabauvalle, M.-C., Loos, K., Merkert, H. and Scheer, U. (1991). Spontaneous assembly of pore complex-containing membranes ('annulate lamellae') in Xenopus egg extracts in the absence of chromatin. J. Cell Biol. 112, 1073-1082.
    • (1991) J. Cell Biol. , vol.112 , pp. 1073-1082
    • Dabauvalle, M.-C.1    Loos, K.2    Merkert, H.3    Scheer, U.4
  • 15
    • 0028587368 scopus 로고
    • Nuclear assembly is independent of linker histones
    • Dasso, M., Dimitrov, S. and Wolffe, A. (1994). Nuclear assembly is independent of linker histones. Proc. Nat. Acad. Sci. USA 91, 12477-12481.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 12477-12481
    • Dasso, M.1    Dimitrov, S.2    Wolffe, A.3
  • 16
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals
    • Dumont, J. (1972). Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals. J. Morphol. 136, 153-180.
    • (1972) J. Morphol. , vol.136 , pp. 153-180
    • Dumont, J.1
  • 17
    • 0027763283 scopus 로고
    • The role of CaaX-dependent modifications in membrane association of Xenopus nuclear lamin B3 during meiosis and the fate of B3 in transfected cells
    • Firmbach-Kraft, I. and Stick, R. (1993). The role of CaaX-dependent modifications in membrane association of Xenopus nuclear lamin B3 during meiosis and the fate of B3 in transfected cells. J. Cell Biol. 123, 1661-1670.
    • (1993) J. Cell Biol. , vol.123 , pp. 1661-1670
    • Firmbach-Kraft, I.1    Stick, R.2
  • 18
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner, R. and Gerace, L. (1993). Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73, 1267-1279.
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 19
    • 0027509502 scopus 로고
    • cDNA cloning of a germ cell-specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells
    • Furukawa, K. and Hotta, Y. (1993). cDNA cloning of a germ cell-specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells. EMBO J. 12, 97-106.
    • (1993) EMBO J. , vol.12 , pp. 97-106
    • Furukawa, K.1    Hotta, Y.2
  • 20
    • 0028294522 scopus 로고
    • Integral membrane proteins and dynamic organization of the nuclear envelope
    • Gerace, L. and Foisner, R. (1994). Integral membrane proteins and dynamic organization of the nuclear envelope. Trends Cell Biol. 4, 127-131.
    • (1994) Trends Cell Biol. , vol.4 , pp. 127-131
    • Gerace, L.1    Foisner, R.2
  • 21
    • 0025745453 scopus 로고
    • In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail
    • Gieffers, C. and Krohne, G. (1991). In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail. Eur. J. Cell Biol. 55, 191-199.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 191-199
    • Gieffers, C.1    Krohne, G.2
  • 23
    • 0027442899 scopus 로고
    • The α-helical rod domain of human lamins A and C contains a chromatin binding site
    • Glass, C., Glass, J., Taniura, H., Hasel, K., Blevitt, J. and Gerace, L. (1993). The α-helical rod domain of human lamins A and C contains a chromatin binding site. EMBO J. 12, 4413-4424.
    • (1993) EMBO J. , vol.12 , pp. 4413-4424
    • Glass, C.1    Glass, J.2    Taniura, H.3    Hasel, K.4    Blevitt, J.5    Gerace, L.6
  • 24
    • 0025005766 scopus 로고
    • Lamins A and C bind and assemble at the surface of mitotic chromosomes
    • Glass, J. and Gerace, L. (1990). Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111, 1047-1057.
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1057
    • Glass, J.1    Gerace, L.2
  • 25
    • 0028972870 scopus 로고
    • Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus:evidence from cell-free extracts
    • Goldberg, M., Jenkins, H., Allen, T., Whitfield, W. and Hutchison, C. (1995). Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus:evidence from cell-free extracts. J. Cell Sci. 108, 3451-3461.
    • (1995) J. Cell Sci. , vol.108 , pp. 3451-3461
    • Goldberg, M.1    Jenkins, H.2    Allen, T.3    Whitfield, W.4    Hutchison, C.5
  • 26
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins
    • Hennekes, H. and Nigg, E. (1994). The role of isoprenylation in membrane attachment of nuclear lamins. J. Cell Sci. 107, 1019-1029.
    • (1994) J. Cell Sci. , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.2
  • 27
    • 0025165401 scopus 로고
    • Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin
    • Höger, T., Zatloukal, K., Waizenegger, I. and Krohne, G. (1990). Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Chromosoma 99, 379-390.
    • (1990) Chromosoma , vol.99 , pp. 379-390
    • Höger, T.1    Zatloukal, K.2    Waizenegger, I.3    Krohne, G.4
  • 28
    • 0026343513 scopus 로고
    • Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain
    • Höger, T., Krohne, G. and Kleinschmidt, J. (1991a). Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain. Exp. Cell Res. 197, 280-289.
    • (1991) Exp. Cell Res. , vol.197 , pp. 280-289
    • Höger, T.1    Krohne, G.2    Kleinschmidt, J.3
  • 29
    • 0025922755 scopus 로고
    • Immunolocalization of lamins in the thick nuclear lamina of human synovial cells
    • Höger, T., Grund, C., Franke, W. and Krohne, G. (1991b). Immunolocalization of lamins in the thick nuclear lamina of human synovial cells. Eur. J. Cell Biol. 54, 150-156.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 150-156
    • Höger, T.1    Grund, C.2    Franke, W.3    Krohne, G.4
  • 30
    • 0028587430 scopus 로고
    • Weaving a pattern from disparate threads: Lamin function in nuclear assembly and DNA replication
    • Hutchison, C., Bridger, J., Cox, L. and Kill, I. (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.1    Bridger, J.2    Cox, L.3    Kill, I.4
  • 31
    • 0021274367 scopus 로고
    • Interconversion of metaphase and interphase microtubule arrays, as studied by the injection of centrosomes and nuclei into Xenopus eggs
    • Karsenti, E., Newport, J., Hubble, R. and Kirschner, M. (1984). Interconversion of metaphase and interphase microtubule arrays, as studied by the injection of centrosomes and nuclei into Xenopus eggs. J. Cell Biol. 98, 1730-1745.
    • (1984) J. Cell Biol. , vol.98 , pp. 1730-1745
    • Karsenti, E.1    Newport, J.2    Hubble, R.3    Kirschner, M.4
  • 32
    • 0025845750 scopus 로고
    • The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2
    • Kitten, G. and Nigg, E. (1991). The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2. J. Cell Biol. 113, 13-23.
    • (1991) J. Cell Biol. , vol.113 , pp. 13-23
    • Kitten, G.1    Nigg, E.2
  • 33
    • 0022569822 scopus 로고
    • The nuclear lamins: A multigene family of proteins in evolution and differentiation
    • Krohne, G. and Benavente, R. (1986). The nuclear lamins: a multigene family of proteins in evolution and differentiation. Exp. Cell Res. 162, 1-10.
    • (1986) Exp. Cell Res. , vol.162 , pp. 1-10
    • Krohne, G.1    Benavente, R.2
  • 34
    • 0023505969 scopus 로고
    • 1 of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily
    • 1 of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. EMBO J. 6, 3801-3808.
    • (1987) EMBO J. , vol.6 , pp. 3801-3808
    • Krohne, G.1    Wolin, S.2    McKeon, F.3    Franke, W.4    Kirschner, M.5
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of the bacteriophage T4
    • Laemmli, U. (1970). Cleavage of structural proteins during assembly of the head of the bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 36
    • 0023180365 scopus 로고
    • Differential expression of nuclear lamin proteins during chicken development
    • Lehner, C., Stick, R., Eppenberger, H. and Nigg, E. (1987). Differential expression of nuclear lamin proteins during chicken development. J. Cell Biol. 105, 577-587.
    • (1987) J. Cell Biol. , vol.105 , pp. 577-587
    • Lehner, C.1    Stick, R.2    Eppenberger, H.3    Nigg, E.4
  • 37
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka, M. and Masui, Y. (1983). Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220, 719-721.
    • (1983) Science , vol.220 , pp. 719-721
    • Lohka, M.1    Masui, Y.2
  • 38
    • 0027437569 scopus 로고
    • Membrane-associated lamins in Xenopus egg extracts: Identification of two vesicle populations
    • Lourim, D. and Krohne, G. (1993). Membrane-associated lamins in Xenopus egg extracts: Identification of two vesicle populations. J. Cell Biol. 123, 501-512.
    • (1993) J. Cell Biol. , vol.123 , pp. 501-512
    • Lourim, D.1    Krohne, G.2
  • 39
    • 0028067708 scopus 로고
    • Lamin-dependent nuclear envelope reassembly following mitosis: An argument
    • Lourim, D. and Krohne, G. (1994). Lamin-dependent nuclear envelope reassembly following mitosis: an argument. Trends Cell Biol. 4, 314-318.
    • (1994) Trends Cell Biol. , vol.4 , pp. 314-318
    • Lourim, D.1    Krohne, G.2
  • 40
    • 0024389951 scopus 로고
    • Expression of nuclear lamin A and muscle-specific proteins in differentiating muscle cells in ovo and in vitro
    • Lourim, D. and Lin, J. J.-C. (1989). Expression of nuclear lamin A and muscle-specific proteins in differentiating muscle cells in ovo and in vitro. J. Cell Biol. 109, 495-504.
    • (1989) J. Cell Biol. , vol.109 , pp. 495-504
    • Lourim, D.1    Lin, J.J.-C.2
  • 41
    • 0027097084 scopus 로고
    • Expression of wild-type and nuclear localization-deficient human lamin A in chick myogenic cells
    • Lourim, D. and Lin, J. J.-C. (1992). Expression of wild-type and nuclear localization-deficient human lamin A in chick myogenic cells. J. Cell Sci. 103, 863-874.
    • (1992) J. Cell Sci. , vol.103 , pp. 863-874
    • Lourim, D.1    Lin, J.J.-C.2
  • 43
    • 0028168825 scopus 로고
    • Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove
    • Ludérus, M., den Blaauwen, J., de Smit, O., Compton, D. and van Driel, R. (1994). Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove. Mol. Cell. Biol. 14, 6297-6305.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6297-6305
    • Ludérus, M.1    Den Blaauwen, J.2    De Smit, O.3    Compton, D.4    Van Driel, R.5
  • 44
    • 0025754857 scopus 로고
    • Nuclear lamin proteins: Domains required for nuclear targeting, assembly and cell-cycle-regulated dynamics
    • McKeon, F. (1991). Nuclear lamin proteins: domains required for nuclear targeting, assembly and cell-cycle-regulated dynamics. Curr. Opin. Cell Biol. 3, 82-86.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 82-86
    • McKeon, F.1
  • 45
    • 0029011832 scopus 로고
    • Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation
    • Meier, E., Miller, B. and Forbes, D. (1995). Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation. J. Cell Biol. 129, 1459-1472.
    • (1995) J. Cell Biol. , vol.129 , pp. 1459-1472
    • Meier, E.1    Miller, B.2    Forbes, D.3
  • 46
    • 0028204109 scopus 로고
    • Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: Implications for nuclear reassembly
    • Meier, J. and Georgatos, S. (1994). Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: implications for nuclear reassembly. EMBO J. 13, 1888-1898.
    • (1994) EMBO J. , vol.13 , pp. 1888-1898
    • Meier, J.1    Georgatos, S.2
  • 48
    • 0026020578 scopus 로고
    • Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos
    • Murray, M., Krohne, G., Franke, W. (1991). Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos. J. Cell Biol. 112, 1-11.
    • (1991) J. Cell Biol. , vol.112 , pp. 1-11
    • Murray, M.1    Krohne, G.2    Franke, W.3
  • 49
    • 0024377368 scopus 로고
    • A somatic cell-derived system for studying both early and late mitotic events in vitro
    • Nakagawa, J., Kitten, G. and Nigg, E. (1989). A somatic cell-derived system for studying both early and late mitotic events in vitro. J. Cell Sci. 94, 449-462.
    • (1989) J. Cell Sci. , vol.94 , pp. 449-462
    • Nakagawa, J.1    Kitten, G.2    Nigg, E.3
  • 50
    • 0026271470 scopus 로고
    • Egg extracts for nuclear import and nuclear assembly reactions
    • Newmeyer, D. and Wilson, K. (1991). Egg extracts for nuclear import and nuclear assembly reactions. Meth. Cell Biol. 36, 607-635.
    • (1991) Meth. Cell Biol. , vol.36 , pp. 607-635
    • Newmeyer, D.1    Wilson, K.2
  • 51
    • 0026501103 scopus 로고
    • Characterization of the membrane binding and fusion events during nuclear envelope assembly using purified components
    • Newport, J. and 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
  • 52
    • 0025612124 scopus 로고
    • A lamin-independent pathway for nuclear envelope assembly
    • Newport, J., Wilson, K. and Dunphy, W. (1990). A lamin-independent pathway for nuclear envelope assembly. J. Cell Biol. 111, 2247-2259.
    • (1990) J. Cell Biol. , vol.111 , pp. 2247-2259
    • Newport, J.1    Wilson, K.2    Dunphy, W.3
  • 53
    • 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, 205-217.
    • (1987) Cell , vol.48 , pp. 205-217
    • Newport, J.1
  • 54
    • 0026813618 scopus 로고
    • Assembly-disassembly of the nuclear envelope
    • Nigg, E. (1992). Assembly-disassembly of the nuclear envelope. Curr. Opin. Cell Biol. 4, 105-109.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 105-109
    • Nigg, E.1
  • 55
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. (1975). High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.1
  • 56
    • 0024561417 scopus 로고
    • Differential timing of nuclear lamin A/C expression in various organs of the mouse embryo and the young animal; a developmental study
    • Röber, R., Weber, K. and Osborn, M. (1989). Differential timing of nuclear lamin A/C expression in various organs of the mouse embryo and the young animal; a developmental study. Development 105, 365-378.
    • (1989) Development , vol.105 , pp. 365-378
    • Röber, R.1    Weber, K.2    Osborn, M.3
  • 57
    • 0020980522 scopus 로고
    • Easy identification of cDNA clones
    • Rüther, U. and Müller-Hill, B. (1983). Easy identification of cDNA clones. EMBO J. 2, 1791-1794.
    • (1983) EMBO J. , vol.2 , pp. 1791-1794
    • Rüther, U.1    Müller-Hill, B.2
  • 59
    • 0027499094 scopus 로고
    • Identification of a short nuclear lamin protein selectively expressed during meiotic stages of rat spermatogenesis
    • Smith, A. and Benavente, R. (1992). Identification of a short nuclear lamin protein selectively expressed during meiotic stages of rat spermatogenesis. Differentiation 52, 55-60.
    • (1992) Differentiation , vol.52 , pp. 55-60
    • Smith, A.1    Benavente, R.2
  • 60
    • 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
  • 61
    • 0024095062 scopus 로고
    • III of Xenopus laevis
    • III of Xenopus laevis. EMBO J. 7, 3189-3197.
    • (1988) EMBO J. , vol.7 , pp. 3189-3197
    • Stick, R.1
  • 62
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura, H., Glass, C. and 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
  • 63
    • 0024828115 scopus 로고
    • Nuclear envelope assembly around sperm chromatin in cell-free preparations from Drosophila embryos
    • Ulitzur, N. and Gruenbaum, Y. (1989). Nuclear envelope assembly around sperm chromatin in cell-free preparations from Drosophila embryos. FEBS Lett. 259, 113-116.
    • (1989) FEBS Lett. , vol.259 , pp. 113-116
    • Ulitzur, N.1    Gruenbaum, Y.2
  • 64
    • 0026657886 scopus 로고
    • Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract
    • Ulitzur, N., Harel, A., Feinstein, N. and Gruenbaum, Y. (1992). Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract. J. Cell Biol. 119, 17-25.
    • (1992) J. Cell Biol. , vol.119 , pp. 17-25
    • Ulitzur, N.1    Harel, A.2    Feinstein, N.3    Gruenbaum, Y.4
  • 65
    • 0026071202 scopus 로고
    • A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs
    • Vigers, G. and Lohka, M. (1991). A distinct vesicle population targets membranes and pore complexes to the nuclear envelope in Xenopus eggs. J. Cell Biol. 112, 545-556.
    • (1991) J. Cell Biol. , vol.112 , pp. 545-556
    • Vigers, G.1    Lohka, M.2
  • 66
    • 0023765935 scopus 로고
    • A trypsin-sensitive receptor on membrane vesicles is required for nuclear envelope formation in vitro
    • Wilson, K. and 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.1    Newport, J.2
  • 67
    • 0025149541 scopus 로고
    • The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains
    • Worman, H., Evans, C. and 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, 1535-1542.
    • (1990) J. Cell Biol. , vol.111 , pp. 1535-1542
    • Worman, H.1    Evans, C.2    Blobel, G.3
  • 68
    • 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. and Worman, H. (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, 11306-11311.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.2


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