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Volumn 112, Issue 5, 1999, Pages 749-759

Molecular characterization and developmentally regulated expression of Xenopus lamina-associated polypeptide 2 (XLAP2)

Author keywords

Oocyte egg LAP2 protein; Somatic LAP2 protein; Xenopus LAP2

Indexed keywords

COMPLEMENTARY DNA; MEMBRANE PROTEIN; MESSENGER RNA; MONOCLONAL ANTIBODY; POLYPEPTIDE;

EID: 0033000856     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (41)

References (55)
  • 1
    • 0031686272 scopus 로고    scopus 로고
    • Nuclear envelope remodelling during rat spermiogenesis: Distribution and expression pattern of LAP2/thymopoietins
    • Alsheimer, M., Fecher, E. and Benavente, R. (1998). Nuclear envelope remodelling during rat spermiogenesis: distribution and expression pattern of LAP2/thymopoietins. J. Cell Sci. 111, 2227-2234.
    • (1998) J. Cell Sci. , vol.111 , pp. 2227-2234
    • Alsheimer, M.1    Fecher, E.2    Benavente, R.3
  • 2
    • 0030959642 scopus 로고    scopus 로고
    • Localization and posttranslational modifications of otefin, a protein required for vesicle attachment to chromatin, during Drosophila melanogaster development
    • Ashery-Padan, R., Ulitzur, N., Arbel, A., Goldberg, M., Weiss, A., Maus, N., Fisher, P. A. and Gruenbaum, Y. (1997). Localization and posttranslational modifications of otefin, a protein required for vesicle attachment to chromatin, during Drosophila melanogaster development. Mol. Cell. Biol. 17, 4114-4123.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4114-4123
    • Ashery-Padan, R.1    Ulitzur, N.2    Arbel, A.3    Goldberg, M.4    Weiss, A.5    Maus, N.6    Fisher, P.A.7    Gruenbaum, Y.8
  • 3
    • 0021842623 scopus 로고
    • Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis
    • Benavente, 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
    • Benavente, R.1    Krohne, G.2    Franke, W.W.3
  • 4
    • 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
  • 5
    • 0025727487 scopus 로고
    • Postmitotic nuclear reorganization events analyzed in living cells
    • Benavente, R. (1991). Postmitotic nuclear reorganization events analyzed in living cells. Chromosoma 100, 215-220.
    • (1991) Chromosoma , vol.100 , pp. 215-220
    • Benavente, R.1
  • 6
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene reponsible for Emery-Dreifuss muscular dystrophy
    • Bione, S., Maestrini, E., Rivella, S., Mancini, M., Regis, S., Romeo, G. and Toniolo, D. (1994). Identification of a novel X-linked gene reponsible for Emery-Dreifuss muscular dystrophy. Nature Genet. 8, 323-327.
    • (1994) Nature Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 7
    • 0031561731 scopus 로고    scopus 로고
    • Domain specific disassembly and reassembly of nuclear membranes during mitosis
    • Buendia, B. and Courvalin, J. C. (1997). Domain specific disassembly and reassembly of nuclear membranes during mitosis. Exp. Cell Res. 230, 133-144.
    • (1997) Exp. Cell Res. , vol.230 , pp. 133-144
    • Buendia, B.1    Courvalin, J.C.2
  • 8
    • 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. and 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, 1715-1725.
    • (1996) J. Cell Biol. , vol.135 , pp. 1715-1725
    • Collas, P.1    Courvalin, J.C.2    Poccia, D.3
  • 9
    • 0025771404 scopus 로고
    • Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse. cDNA cloning and identification of its glycosylated regions
    • Cordes, V., Waizenegger, I. and Krohne, G. (1991). Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse. cDNA cloning and identification of its glycosylated regions. 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
  • 10
    • 0028858573 scopus 로고
    • High content of nuclear pore complex protein in cytoplasm annulate lamellae of Xenopus oocytes
    • Cordes, V. C., Reidenbach, S. and Franke, W. W. (1995). High content of nuclear pore complex protein in cytoplasm annulate lamellae of Xenopus oocytes. Eur. J. Cell Biol. 68, 240-255.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 240-255
    • Cordes, V.C.1    Reidenbach, S.2    Franke, W.W.3
  • 11
    • 0032541346 scopus 로고    scopus 로고
    • Detergent-salt resistance of LAP2β in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics
    • Dechat, T., Gotzmann, J., Stockinger, A., Harris, C. A., Talle, M. A., Siekierka, J. J. and Foisner, R. (1998). Detergent-salt resistance of LAP2β in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics. EMBO J. 17, 4887-4902.
    • (1998) EMBO J. , vol.17 , pp. 4887-4902
    • Dechat, T.1    Gotzmann, J.2    Stockinger, A.3    Harris, C.A.4    Talle, M.A.5    Siekierka, J.J.6    Foisner, R.7
  • 12
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus laevis (Daudin). I. Stages of oocyte development in laboratory maintained animals
    • Dumont, J. N. (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.N.1
  • 13
    • 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
  • 14
    • 0028989340 scopus 로고
    • Cloning and cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to nuclear envelope
    • Furukawa, K., Panté, N., Aebi, U. and Gerace, L. (1995). Cloning and cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to nuclear envelope. EMBO J. 14, 1626-1636.
    • (1995) EMBO J. , vol.14 , pp. 1626-1636
    • Furukawa, K.1    Panté, N.2    Aebi, U.3    Gerace, L.4
  • 15
    • 0031559831 scopus 로고    scopus 로고
    • Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2
    • Furukawa, K., Glass, C. and Kondo, T. (1997). Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2. Biochem. Biophys. Res. Commun. 238, 240-246.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 240-246
    • Furukawa, K.1    Glass, C.2    Kondo, T.3
  • 16
    • 0032005232 scopus 로고    scopus 로고
    • Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin
    • Furukawa, K. and Kondo, T. (1998). Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin. Eur. J. Biochem. 251, 729-733.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 729-733
    • Furukawa, K.1    Kondo, T.2
  • 17
    • 0032512832 scopus 로고    scopus 로고
    • The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain
    • Furukawa, K., Fritze, C. E. and Gerace, L. (1998). The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain. J. Biol. Chem. 273, 4213-4219.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4213-4219
    • Furukawa, K.1    Fritze, C.E.2    Gerace, L.3
  • 20
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace, L. and Burke, B. (1988). Functional organization of the nuclear envelope. Annu. Rev. Cell Biol 4, 335-374.
    • (1988) Annu. Rev. Cell Biol , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 21
    • 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, 127-130.
    • (1994) Trends Cell Biol. , vol.4 , pp. 127-130
    • Gerace, L.1    Foisner, R.2
  • 22
    • 0028972870 scopus 로고
    • Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: Evidence from cell-free egg extracts
    • Goldberg, W., 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 egg extracts. J. Cell Sci. 108, 3451-3461.
    • (1995) J. Cell Sci. , vol.108 , pp. 3451-3461
    • Goldberg, W.1    Jenkins, H.2    Allen, T.3    Whitfield, W.4    Hutchison, C.5
  • 23
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Harlowe, E. and Lane, D. (1988). Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1988) Antibodies: A Laboratory Manual
    • Harlowe, E.1    Lane, D.2
  • 25
    • 0029155876 scopus 로고
    • Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO to rat lamin-associated polypeptide 2
    • Harris, C. A., Andryuk, P. J., Cline, S. C., Mathew, S., Siekierka, J. J. and Goldstein, G. (1995). Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO 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.C.3    Mathew, S.4    Siekierka, J.J.5    Goldstein, G.6
  • 26
    • 0026343513 scopus 로고
    • II with chromatin in vitro mediated by a sequence element in the carboxyterminal domain
    • II 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
  • 27
    • 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
  • 28
    • 0021005632 scopus 로고
    • Proteins of pore complex-lamina structures from nuclei and membranes
    • Krohne, G. and Franke, W. W. (1983). Proteins of pore complex-lamina structures from nuclei and membranes. Meth. Enzymol. 96J, 597-608.
    • (1983) Meth. Enzymol. , vol.96 J , pp. 597-608
    • Krohne, G.1    Franke, W.W.2
  • 29
    • 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
  • 30
    • 0032242490 scopus 로고    scopus 로고
    • Lamin assembly in vivo
    • ed. H. Herrmann and J. Robin Harris. Plenum Publishing/London, UK
    • Krohne, G. (1998). Lamin assembly in vivo. In Subcellular Biochemistry: Intermediate filaments (ed. H. Herrmann and J. Robin Harris), pp. 563-586. Plenum Publishing/London, UK.
    • (1998) Subcellular Biochemistry: Intermediate Filaments , pp. 563-586
    • Krohne, G.1
  • 31
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without tank for rapid transfer of proteins form polyacrylamide to nitrocellulose
    • Kyhse-Andersen, J. (1984). Electroblotting of multiple gels: a simple apparatus without tank for rapid transfer of proteins form polyacrylamide to nitrocellulose. J. Biochem. Biophys. Meth. 10, 203-210.
    • (1984) J. Biochem. Biophys. Meth. , vol.10 , pp. 203-210
    • Kyhse-Andersen, J.1
  • 32
    • 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
  • 33
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective NEs, clustering of nuclear pore complexes, and accumulation of annulate lamellae
    • Lenz-Böhme, B., Wismar, J., Fuchs, S., Reifegerste, R., Buchner, E., Betz, H. and Schmitt, B. (1997). Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective NEs, clustering of nuclear pore complexes, and accumulation of annulate lamellae. J. Cell Biol. 137, 1001-1016.
    • (1997) J. Cell Biol. , vol.137 , pp. 1001-1016
    • Lenz-Böhme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6    Schmitt, B.7
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0030004283 scopus 로고    scopus 로고
    • i protein synthesis during meoitic maturation
    • I protein synthesis during meoitic maturation. J. Cell Sci. 109, 1775-1785.
    • (1996) J. Cell Sci. , vol.109 , pp. 1775-1785
    • Lourim, D.1    Kempf, A.2    Krohne, G.3
  • 37
    • 0030745846 scopus 로고    scopus 로고
    • The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles
    • Maison, C., Pyrpasopoulou, A., Theodoropoulos, P. A. and Georgatos, S. D. (1997). The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles. EMBO J. 16, 4839-4850.
    • (1997) EMBO J. , vol.16 , pp. 4839-4850
    • Maison, C.1    Pyrpasopoulou, A.2    Theodoropoulos, P.A.3    Georgatos, S.D.4
  • 38
    • 0028949732 scopus 로고
    • cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane
    • Martin, L., Crimaudo, C. and Gerace, L. (1995). cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane. J. Biol. Chem. 270, 8822-8828.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8822-8828
    • Martin, L.1    Crimaudo, C.2    Gerace, L.3
  • 39
    • 0029198668 scopus 로고
    • The dynamic properties and possible functions of nuclear lamins
    • Moir, R. D., Spann, T. P. and Goldmann, R. D. (1995). The dynamic properties and possible functions of nuclear lamins. Int. Rev. Cytol. 162B, 141-182.
    • (1995) Int. Rev. Cytol. , vol.162 B , pp. 141-182
    • Moir, R.D.1    Spann, T.P.2    Goldmann, R.D.3
  • 41
    • 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
  • 43
    • 0030029383 scopus 로고    scopus 로고
    • The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
    • Paulin-Levasseur, M., Blake, D. L., Julien, M. and Rouleau, L. (1996). The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells. Chromosoma 104, 367-379.
    • (1996) Chromosoma , vol.104 , pp. 367-379
    • Paulin-Levasseur, M.1    Blake, D.L.2    Julien, M.3    Rouleau, L.4
  • 44
    • 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. and Georgatos, S. D. (1996). The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope. EMBO J. 24, 7108-7119.
    • (1996) EMBO J. , vol.24 , pp. 7108-7119
    • Pyrpasopoulou, A.1    Meier, J.2    Maison, C.3    Simos, G.4    Georgatos, S.D.5
  • 47
    • 0024263203 scopus 로고
    • Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina
    • Senior, A. and Gerace, L. (1988). Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol. 107, 2029-2036.
    • (1988) J. Cell Biol. , vol.107 , pp. 2029-2036
    • Senior, A.1    Gerace, L.2
  • 48
    • 0030863126 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis
    • Spann, T. P., Moir, R. D., Goldman, A. E., Stick, R. and Goldman, R. D. (1997). Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. J. Cell Biol. 136, 1201-1212.
    • (1997) J. Cell Biol. , vol.136 , pp. 1201-1212
    • Spann, T.P.1    Moir, R.D.2    Goldman, A.E.3    Stick, R.4    Goldman, R.D.5
  • 49
    • 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
  • 50
    • 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
  • 51
    • 0015093280 scopus 로고
    • A molecular approach to fertilization. II. Viability and artificial fertilization of Xenopus gametes
    • Wolf, D. P. and Hedrick, J. L. (1971). A molecular approach to fertilization. II. Viability and artificial fertilization of Xenopus gametes. Dev. Biol. 25, 348-359.
    • (1971) Dev. Biol. , vol.25 , pp. 348-359
    • Wolf, D.P.1    Hedrick, J.L.2
  • 52
    • 0023517709 scopus 로고
    • A new lamin in Xenopus somatic tissues displays strong homology to human lamin A
    • Wolin, S., Krohne, G. and Kirschner, M. (1987). A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. EMBO J. 6, 3809-3818.
    • (1987) EMBO J. , vol.6 , pp. 3809-3818
    • Wolin, S.1    Krohne, G.2    Kirschner, M.3
  • 53
    • 0009573453 scopus 로고
    • The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains
    • Worman, H. J., Evans, C. D. 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. 117, 245-258.
    • (1990) J. Cell Biol. , vol.117 , pp. 245-258
    • Worman, H.J.1    Evans, C.D.2    Blobel, G.3
  • 54
    • 0030774272 scopus 로고    scopus 로고
    • Lamin-binding fragment of LAP2 inhibits increase in nuclear volume during the cell cycle and progression into S phase
    • Yang, L., Guan, T. and Gerace, L. (1997). Lamin-binding fragment of LAP2 inhibits increase in nuclear volume during the cell cycle and progression into S phase. J. Cell Biol. 139, 1077-1087.
    • (1997) J. Cell Biol. , vol.139 , pp. 1077-1087
    • Yang, L.1    Guan, T.2    Gerace, L.3
  • 55
    • 0032247871 scopus 로고    scopus 로고
    • Nuclear lamin binding proteins
    • ed. H. Herrmann and J. Robin Harris. Plenum Publishing/London, UK
    • Ye, Q., Barton, R. M. and Worman, H. J. (1998). Nuclear lamin binding proteins. In Subcellular Biochemistry: Intermediate filaments (ed. H. Herrmann and J. Robin Harris), pp. 587-610. Plenum Publishing/London, UK.
    • (1998) Subcellular Biochemistry: Intermediate Filaments , pp. 587-610
    • Ye, Q.1    Barton, R.M.2    Worman, H.J.3


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