메뉴 건너뛰기




Volumn 85, Issue 6, 2006, Pages 501-517

Phosphorylation of the p34cdc2 target site on goldfish germinal vesicle lamin B3 before oocyte maturation

Author keywords

Germinal vesicle; Intermediate filament; Nuclear matrix; Protein kinase; Protein phosphatase

Indexed keywords

CYCLIN DEPENDENT KINASE 1; LAMIN B; PHOSPHOPROTEIN PHOSPHATASE; POLYCLONAL ANTIBODY; PROTEIN KINASE; SERINE;

EID: 33646565689     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2006.02.002     Document Type: Article
Times cited : (8)

References (66)
  • 1
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi U., Cohn J., Buhle L., and Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323 (1986) 560-564
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 2
    • 0029041375 scopus 로고
    • Mapping the cell's nucleus
    • Baskin Y. Mapping the cell's nucleus. Science 268 (1995) 1564-1565
    • (1995) Science , vol.268 , pp. 1564-1565
    • Baskin, Y.1
  • 3
    • 0027752440 scopus 로고
    • Lamin distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy topography
    • Belmont A.S., Zhai Y., and Thilenius A. Lamin distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy topography. J. Cell Biol. 123 (1993) 1671-1685
    • (1993) J. Cell Biol. , vol.123 , pp. 1671-1685
    • Belmont, A.S.1    Zhai, Y.2    Thilenius, A.3
  • 4
    • 0021842623 scopus 로고
    • Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis
    • Benavente R., Krohne G., and Franke W.W. Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis. Cell 41 (1985) 177-190
    • (1985) Cell , vol.41 , pp. 177-190
    • Benavente, R.1    Krohne, G.2    Franke, W.W.3
  • 5
    • 0032414848 scopus 로고    scopus 로고
    • The new paradigm: integrating genomic function and nuclear structure
    • Berezney R., and Wei X. The new paradigm: integrating genomic function and nuclear structure. J. Cell. Biochem. Suppl. 30/31 (1998) 238-242
    • (1998) J. Cell. Biochem. Suppl. , vol.30-31 , pp. 238-242
    • Berezney, R.1    Wei, X.2
  • 7
    • 0027416334 scopus 로고
    • Internal lamin structures within G1 nuclei of human dermal fibroblasts
    • Bridger J.M., Kill I.R., O' Farrell M., and Hutchison C.J. Internal lamin structures within G1 nuclei of human dermal fibroblasts. J. Cell Sci. 104 (1993) 297-306
    • (1993) J. Cell Sci. , vol.104 , pp. 297-306
    • Bridger, J.M.1    Kill, I.R.2    O' Farrell, M.3    Hutchison, C.J.4
  • 8
    • 0032925541 scopus 로고    scopus 로고
    • Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly
    • Collas P. Sequential PKC- and Cdc2-mediated phosphorylation events elicit zebrafish nuclear envelope disassembly. J. Cell Sci. 112 (1999) 977-987
    • (1999) J. Cell Sci. , vol.112 , pp. 977-987
    • Collas, P.1
  • 9
    • 0030771437 scopus 로고    scopus 로고
    • Protein kinase C-mediated interphase lamin B phosphorylation and solublization
    • Collas P., Thompson L., Fields A.P., Poccia D.L., and Courvalin J.-C. Protein kinase C-mediated interphase lamin B phosphorylation and solublization. J. Biol. Chem. 272 (1997) 21274-21280
    • (1997) J. Biol. Chem. , vol.272 , pp. 21274-21280
    • Collas, P.1    Thompson, L.2    Fields, A.P.3    Poccia, D.L.4    Courvalin, J.-C.5
  • 10
    • 0025808241 scopus 로고
    • DNA replication occurs at discrete sites in pseudonuclei assembled from purified DNA in vitro
    • Cox L.S., and Laskey R. DNA replication occurs at discrete sites in pseudonuclei assembled from purified DNA in vitro. Cell 66 (1991) 271-275
    • (1991) Cell , vol.66 , pp. 271-275
    • Cox, L.S.1    Laskey, R.2
  • 11
    • 0023678444 scopus 로고
    • Monoclonal antibodies specific for thiophosphorylated proteins recognize Xenopus MPF
    • Cyert M.S., Scherson T., and Kirschner M.W. Monoclonal antibodies specific for thiophosphorylated proteins recognize Xenopus MPF. Dev. Biol. 129 (1988) 209-216
    • (1988) Dev. Biol. , vol.129 , pp. 209-216
    • Cyert, M.S.1    Scherson, T.2    Kirschner, M.W.3
  • 12
    • 0026452236 scopus 로고
    • Host cell factors controlling vimentin organization in the Xenopus oocyte
    • Dent J.A., Cary R.B., Bechant J.B., Domingo R., and Klymkowsky M.W. Host cell factors controlling vimentin organization in the Xenopus oocyte. J. Cell Biol. 119 (1992) 855-866
    • (1992) J. Cell Biol. , vol.119 , pp. 855-866
    • Dent, J.A.1    Cary, R.B.2    Bechant, J.B.3    Domingo, R.4    Klymkowsky, M.W.5
  • 15
    • 0025945045 scopus 로고
    • Identification of phosphorylation sites on murine nuclear lamin C by RP-HPLC and microsequencing
    • Eggert M., Radomski N., Tripier D., Traub D., and Jost E. Identification of phosphorylation sites on murine nuclear lamin C by RP-HPLC and microsequencing. FEBS Lett. 292 (1991) 205-209
    • (1991) FEBS Lett. , vol.292 , pp. 205-209
    • Eggert, M.1    Radomski, N.2    Tripier, D.3    Traub, D.4    Jost, E.5
  • 17
    • 0023942696 scopus 로고
    • Phosphorylation of lamin B at the nuclear membrane by activated protein kinase C
    • Fields A.P., Pettit G.R., and May W.S. Phosphorylation of lamin B at the nuclear membrane by activated protein kinase C. J. Biol. Chem. 263 (1988) 8253-8260
    • (1988) J. Biol. Chem. , vol.263 , pp. 8253-8260
    • Fields, A.P.1    Pettit, G.R.2    May, W.S.3
  • 18
    • 0028283501 scopus 로고
    • Intermediate filament proteins: structure, dynamics, function and disease
    • Fuchs E., and Weber K. Intermediate filament proteins: structure, dynamics, function and disease. Annu. Rev. Biochem. 63 (1994) 345-382
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 19
    • 0027712787 scopus 로고
    • Confocal immunofluorescence microscopy of microtubules in oocytes, eggs, and embryos of algae and amphibians
    • Gard D., and Kropf D. Confocal immunofluorescence microscopy of microtubules in oocytes, eggs, and embryos of algae and amphibians. Methods Cell Biol. 37 (1993) 147-169
    • (1993) Methods Cell Biol. , vol.37 , pp. 147-169
    • Gard, D.1    Kropf, D.2
  • 20
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L., and Burke B. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4 (1988) 335-374
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 21
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald R., and McKeon F. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61 (1990) 579-589
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 23
    • 0026568833 scopus 로고
    • The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins
    • Heitlinger E., Peter M., Lustig A., Villiger W., Nigg E.A., and Aebi U. The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins. J. Struct. Biol. 108 (1992) 74-89
    • (1992) J. Struct. Biol. , vol.108 , pp. 74-89
    • Heitlinger, E.1    Peter, M.2    Lustig, A.3    Villiger, W.4    Nigg, E.A.5    Aebi, U.6
  • 25
    • 0027502241 scopus 로고
    • Identification of protein kinase C (PKC) phosphorylation sites on human lamin B
    • Hocevar B.A., Burns D.J., and Fields A.P. Identification of protein kinase C (PKC) phosphorylation sites on human lamin B. J. Biol. Chem. 268 (1993) 7545-7552
    • (1993) J. Biol. Chem. , vol.268 , pp. 7545-7552
    • Hocevar, B.A.1    Burns, D.J.2    Fields, A.P.3
  • 26
    • 0036176397 scopus 로고    scopus 로고
    • Conservation of the gene structure and membrane-targeting signals of germ cell-specific lamin LIII in amphibian and fish
    • Hofemeister H., Kuhn C., Franke W.W., Weber K., and Stick R. Conservation of the gene structure and membrane-targeting signals of germ cell-specific lamin LIII in amphibian and fish. Eur. J. Cell Biol. 81 (2002) 51-60
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 51-60
    • Hofemeister, H.1    Kuhn, C.2    Franke, W.W.3    Weber, K.4    Stick, R.5
  • 27
    • 0027460452 scopus 로고
    • The cell's nucleus shapes up
    • Hoffman M. The cell's nucleus shapes up. Science 259 (1993) 1257-1259
    • (1993) Science , vol.259 , pp. 1257-1259
    • Hoffman, M.1
  • 28
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak P., Sasseville A.M.-J., Raymod Y., and Cook P.R. Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci. 108 (1995) 635-644
    • (1995) J. Cell Sci. , vol.108 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.-J.2    Raymod, Y.3    Cook, P.R.4
  • 29
    • 0028151022 scopus 로고
    • Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis
    • Inagaki M. Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis. J. Cell Biol. 269 (1994) 31097-31106
    • (1994) J. Cell Biol. , vol.269 , pp. 31097-31106
    • Inagaki, M.1
  • 31
    • 0021418551 scopus 로고
    • In vitro estradiol-17β and testosterone production by ovarian follicles of the goldfish, Carassius auratus
    • Kagawa H., Young G., and Nagahama Y. In vitro estradiol-17β and testosterone production by ovarian follicles of the goldfish, Carassius auratus. Gen. Comp. Endocrinol. 54 (1984) 139-143
    • (1984) Gen. Comp. Endocrinol. , vol.54 , pp. 139-143
    • Kagawa, H.1    Young, G.2    Nagahama, Y.3
  • 32
    • 0029080459 scopus 로고
    • Molecular cloning and immunological analysis of goldfish cyclin A during oocyte maturation
    • Katsu Y., Yamashita M., Hirai T., Tokumoto T., Kajiura H., and Nagahama Y. Molecular cloning and immunological analysis of goldfish cyclin A during oocyte maturation. Dev. Biol. 170 (1995) 616-625
    • (1995) Dev. Biol. , vol.170 , pp. 616-625
    • Katsu, Y.1    Yamashita, M.2    Hirai, T.3    Tokumoto, T.4    Kajiura, H.5    Nagahama, Y.6
  • 33
    • 0029417112 scopus 로고
    • S-phase phosphorylation of lamin B2
    • Kill I.R., and Hutchison C.J. S-phase phosphorylation of lamin B2. FEBS Lett. 377 (1995) 26-30
    • (1995) FEBS Lett. , vol.377 , pp. 26-30
    • Kill, I.R.1    Hutchison, C.J.2
  • 34
    • 0019781276 scopus 로고
    • Cell type-specific differences in protein composition of nuclear pore complex-lamina structures in oocytes and erythrocytes of Xenopus laevis
    • Krohne G., Dabauvalle M.-C., and Franke W. Cell type-specific differences in protein composition of nuclear pore complex-lamina structures in oocytes and erythrocytes of Xenopus laevis. J. Mol. Biol. 151 (1981) 121-141
    • (1981) J. Mol. Biol. , vol.151 , pp. 121-141
    • Krohne, G.1    Dabauvalle, M.-C.2    Franke, W.3
  • 35
    • 0024064963 scopus 로고
    • Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm
    • Loewinger L., and McKeon F. Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm. EMBO J. 7 (1988) 2301-2309
    • (1988) EMBO J. , vol.7 , pp. 2301-2309
    • Loewinger, L.1    McKeon, F.2
  • 37
    • 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. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319 (1986) 463-468
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 38
    • 0024388420 scopus 로고
    • Replication occurs at discrete foci spaced throughout nuclei replicating in vitro
    • Mills A.D., Blow J.J., White J.G., Amos W.B., Wilcock D., and Laskey R.A. Replication occurs at discrete foci spaced throughout nuclei replicating in vitro. J. Cell Sci. 94 (1989) 471-477
    • (1989) J. Cell Sci. , vol.94 , pp. 471-477
    • Mills, A.D.1    Blow, J.J.2    White, J.G.3    Amos, W.B.4    Wilcock, D.5    Laskey, R.A.6
  • 39
    • 0031834613 scopus 로고    scopus 로고
    • The cellular organization of gene expression
    • Misteli T., and Spector D.L. The cellular organization of gene expression. Curr. Opin. Cell Biol. 10 (1998) 323-331
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 323-331
    • Misteli, T.1    Spector, D.L.2
  • 40
    • 0028247078 scopus 로고
    • Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication
    • Moir D.M., Montag-Lowry M., and Goldman R.D. Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J. Cell Biol. 125 (1994) 1201-1212
    • (1994) J. Cell Biol. , vol.125 , pp. 1201-1212
    • Moir, D.M.1    Montag-Lowry, M.2    Goldman, R.D.3
  • 41
    • 0026612335 scopus 로고
    • p34cdc2 kinase-mediated release of lamins from nuclear ghosts is inhibited by cAMP-dependent protein kinase
    • Molloy S., and Little M. p34cdc2 kinase-mediated release of lamins from nuclear ghosts is inhibited by cAMP-dependent protein kinase. Exp. Cell Res. 201 (1992) 494-499
    • (1992) Exp. Cell Res. , vol.201 , pp. 494-499
    • Molloy, S.1    Little, M.2
  • 42
    • 0029558856 scopus 로고
    • The architectural organization of nuclear metabolism
    • Nickerson J.A., Blencowe B.J., and Penman S. The architectural organization of nuclear metabolism. Int. Rev. Cytol. 162 (1995) 67-123
    • (1995) Int. Rev. Cytol. , vol.162 , pp. 67-123
    • Nickerson, J.A.1    Blencowe, B.J.2    Penman, S.3
  • 43
    • 0026813618 scopus 로고
    • Assembly disassembly of the nuclear lamina
    • Nigg E.A. Assembly disassembly of the nuclear lamina. Curr. Opin. Cell Biol. 4 (1992) 105-109
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 105-109
    • Nigg, E.A.1
  • 44
    • 0027480379 scopus 로고
    • Dynamics of neuronal intermediate filaments
    • Okabe S., Miyasaka H., and Hirokawa N. Dynamics of neuronal intermediate filaments. J. Cell Biol. 121 (1993) 375-386
    • (1993) J. Cell Biol. , vol.121 , pp. 375-386
    • Okabe, S.1    Miyasaka, H.2    Hirokawa, N.3
  • 45
    • 0021955147 scopus 로고
    • Phosphorylation of the nuclear lamins during interphase and mitosis
    • Ottaviano Y., and Gerace L. Phosphorylation of the nuclear lamins during interphase and mitosis. J. Biol. Chem. 260 (1985) 624-632
    • (1985) J. Biol. Chem. , vol.260 , pp. 624-632
    • Ottaviano, Y.1    Gerace, L.2
  • 47
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Dorée M., Labbé J.C., and Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61 (1990) 591-602
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Dorée, M.3    Labbé, J.C.4    Nigg, E.A.5
  • 48
    • 0025736038 scopus 로고
    • Disassembly of in vitro-formed lamin head-to-tail polymers by cdc2 kinase
    • Peter M., Heitlinger E., Häner M., Aebi U., and Nigg E.A. Disassembly of in vitro-formed lamin head-to-tail polymers by cdc2 kinase. EMBO J. 10 (1991) 1535-1544
    • (1991) EMBO J. , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Häner, M.3    Aebi, U.4    Nigg, E.A.5
  • 49
    • 0001597369 scopus 로고    scopus 로고
    • Metalloenzymes and signal transduction: the protein serine/threonine phosphatases, a novel class of binuclear metal-containing enzymes
    • Rusnak F., Yu L., and Mertz P. Metalloenzymes and signal transduction: the protein serine/threonine phosphatases, a novel class of binuclear metal-containing enzymes. J. Biol. Inorg. Chem. 1 (1996) 388-396
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 388-396
    • Rusnak, F.1    Yu, L.2    Mertz, P.3
  • 50
    • 0033528715 scopus 로고    scopus 로고
    • Phosphorylation of the major Drosophila lamin in vivo: Site identification during both M-phase (meiosis) and interphase by electrospray ionization tandem mass spectrometry
    • Schneider U., Mini T., Jenö P., Fisher P.A., and Stuurman N. Phosphorylation of the major Drosophila lamin in vivo: Site identification during both M-phase (meiosis) and interphase by electrospray ionization tandem mass spectrometry. Biochemistry 38 (1999) 4620-4632
    • (1999) Biochemistry , vol.38 , pp. 4620-4632
    • Schneider, U.1    Mini, T.2    Jenö, P.3    Fisher, P.A.4    Stuurman, N.5
  • 51
    • 0030063171 scopus 로고    scopus 로고
    • Detection of protein kinase activity specifically activated at metaphase-anaphase transition
    • Sekimata M., Tsujimura K., Tanaka J., Takeuchi Y., Inagaki N., and Inagaki M. Detection of protein kinase activity specifically activated at metaphase-anaphase transition. J. Cell Biol. 133 (1996) 141-149
    • (1996) J. Cell Biol. , vol.133 , pp. 141-149
    • Sekimata, M.1    Tsujimura, K.2    Tanaka, J.3    Takeuchi, Y.4    Inagaki, N.5    Inagaki, M.6
  • 52
    • 0025803568 scopus 로고
    • Recent insight into assembly, dynamics, and function of intermediate filament networks
    • Skalli O., and Goldman R.D. Recent insight into assembly, dynamics, and function of intermediate filament networks. Cell Motil. Cytoskeleton 19 (1991) 67-79
    • (1991) Cell Motil. Cytoskeleton , vol.19 , pp. 67-79
    • Skalli, O.1    Goldman, R.D.2
  • 53
    • 0027613753 scopus 로고
    • Nuclear organization of pre-mRNA processing
    • Spector D.L. Nuclear organization of pre-mRNA processing. Curr. Opin. Cell Biol. 5 (1993) 442-447
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 442-447
    • Spector, D.L.1
  • 54
    • 0024095062 scopus 로고
    • lll of Xenopus laevis
    • lll of Xenopus laevis. EMBO J. 7 (1988) 3189-3197
    • (1988) EMBO J. , vol.7 , pp. 3189-3197
    • Stick, R.1
  • 55
    • 0021859643 scopus 로고
    • Changes in the nuclear lamina composition during early development of Xenopus laevis
    • Stick R., and Hausen P. Changes in the nuclear lamina composition during early development of Xenopus laevis. Cell 41 (1985) 191-200
    • (1985) Cell , vol.41 , pp. 191-200
    • Stick, R.1    Hausen, P.2
  • 56
    • 0031037074 scopus 로고    scopus 로고
    • Identification of a conserved phosphorylation site modulating nuclear lamin polymerization
    • Stuurman N. Identification of a conserved phosphorylation site modulating nuclear lamin polymerization. FEBS Lett. 401 (1997) 171-174
    • (1997) FEBS Lett. , vol.401 , pp. 171-174
    • Stuurman, N.1
  • 57
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: their structure, assembly, and interactions
    • Stuurman N., Heins S., and Aebi U. Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 122 (1998) 42-66
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 58
    • 0028290651 scopus 로고
    • Association of casein kinase 2 with nuclear matrix
    • Tawfic S., and Ahmed K. Association of casein kinase 2 with nuclear matrix. J. Biol. Chem. 269 (1994) 7489-7493
    • (1994) J. Biol. Chem. , vol.269 , pp. 7489-7493
    • Tawfic, S.1    Ahmed, K.2
  • 61
    • 0025285068 scopus 로고
    • Identification of cell cycle-regulated phosphorylation on nuclear lamin C
    • Ward G.E., and Kirschner M.W. Identification of cell cycle-regulated phosphorylation on nuclear lamin C. Cell 61 (1990) 561-577
    • (1990) Cell , vol.61 , pp. 561-577
    • Ward, G.E.1    Kirschner, M.W.2
  • 62
    • 0026065461 scopus 로고
    • Preservation of specific RNA distribution within the chromatin-depleted nuclear substructure demonstrated by in situ hybridization coupled with biochemical fractionation
    • Xing Y.G., and Lawrence J.B. Preservation of specific RNA distribution within the chromatin-depleted nuclear substructure demonstrated by in situ hybridization coupled with biochemical fractionation. J. Cell Biol. 112 (1991) 1055-1063
    • (1991) J. Cell Biol. , vol.112 , pp. 1055-1063
    • Xing, Y.G.1    Lawrence, J.B.2
  • 63
    • 0035735529 scopus 로고    scopus 로고
    • Somatic lamins in germinal vesicles of goldfish (Carassius auratus) vitellogenic oocytes
    • Yamaguchi A., and Nagahama Y. Somatic lamins in germinal vesicles of goldfish (Carassius auratus) vitellogenic oocytes. Cell Struct. Funct. 26 (2001) 693-703
    • (2001) Cell Struct. Funct. , vol.26 , pp. 693-703
    • Yamaguchi, A.1    Nagahama, Y.2
  • 64
    • 0035064147 scopus 로고    scopus 로고
    • Identification and cDNA cloning of germinal vesicle lamin B3 in goldfish (Carassius auratus) oocytes
    • Yamaguchi A., Yamashita M., Yoshikuni M., and Nagahama Y. Identification and cDNA cloning of germinal vesicle lamin B3 in goldfish (Carassius auratus) oocytes. Eur. J. Biochem. 268 (2001) 932-939
    • (2001) Eur. J. Biochem. , vol.268 , pp. 932-939
    • Yamaguchi, A.1    Yamashita, M.2    Yoshikuni, M.3    Nagahama, Y.4
  • 66
    • 0028967060 scopus 로고
    • Molecular mechanisms of the activation of maturation-promoting factor during goldfish oocyte maturation
    • Yamashita M., Kajiura H., Tanaka T., Onoe S., and Nagahama Y. Molecular mechanisms of the activation of maturation-promoting factor during goldfish oocyte maturation. Dev. Biol. 168 (1995) 62-75
    • (1995) Dev. Biol. , vol.168 , pp. 62-75
    • Yamashita, M.1    Kajiura, H.2    Tanaka, T.3    Onoe, S.4    Nagahama, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.