메뉴 건너뛰기




Volumn 18, Issue 1, 1998, Pages 188-197

Functional dissection of YA, an essential, developmentally regulated nuclear lamina protein in Drosophila melanogaster

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR PROTEIN; NUCLEAR PROTEIN YA; UNCLASSIFIED DRUG;

EID: 2642691663     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.1.188     Document Type: Article
Times cited : (11)

References (63)
  • 1
    • 0025255158 scopus 로고
    • Zinc fingers and other metal-binding domains
    • Berg, J. M. 1990. Zinc fingers and other metal-binding domains. J. Biol. Chem. 265:6513-6516.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6513-6516
    • Berg, J.M.1
  • 2
    • 0025361318 scopus 로고
    • The segment-specific gene Krox-20 encodes a transcription factor with binding sites in the promoter region of the Hox-1.4 gene
    • Chavrier, P., C. Vesque, B. Galliot, M. Vigneron, P. Dolle, D. Duboule, and P. Charnay. 1990. The segment-specific gene Krox-20 encodes a transcription factor with binding sites in the promoter region of the Hox-1.4 gene. EMBO J. 9:1209-1218.
    • (1990) EMBO J. , vol.9 , pp. 1209-1218
    • Chavrier, P.1    Vesque, C.2    Galliot, B.3    Vigneron, M.4    Dolle, P.5    Duboule, D.6    Charnay, P.7
  • 3
    • 0023675530 scopus 로고
    • A gene encoding a protein with zinc fingers is activated during G0/G1 transition in cultured cells
    • Chavrier, P., M. Zerial, P. Lemaire, J. Almendral, R. Bravo, and P. Charnay. 1988. A gene encoding a protein with zinc fingers is activated during G0/G1 transition in cultured cells. EMBO J. 7:29-35.
    • (1988) EMBO J. , vol.7 , pp. 29-35
    • Chavrier, P.1    Zerial, M.2    Lemaire, P.3    Almendral, J.4    Bravo, R.5    Charnay, P.6
  • 4
    • 0024841735 scopus 로고
    • 'SPKK' motifs prefer to bind to DNA at A/T-rich sites
    • Churchill, M. E. A., and M. Suzuki. 1989. 'SPKK' motifs prefer to bind to DNA at A/T-rich sites. EMBO J. 8:4189-4195.
    • (1989) EMBO J. , vol.8 , pp. 4189-4195
    • Churchill, M.E.A.1    Suzuki, M.2
  • 5
    • 0026766977 scopus 로고
    • Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman, J. E. 1992. Zinc proteins: enzymes, storage proteins, transcription factors, and replication proteins. Annu. Rev. Biochem. 61:897-946.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 897-946
    • Coleman, J.E.1
  • 6
    • 0024708749 scopus 로고
    • Position effect variegation in Drosophila melanogaster: Relationship between suppression effect and the amount of Y chromosome
    • Dimitri, P., and C. Pisano. 1989. Position effect variegation in Drosophila melanogaster: relationship between suppression effect and the amount of Y chromosome. Genetics 122:793-800.
    • (1989) Genetics , vol.122 , pp. 793-800
    • Dimitri, P.1    Pisano, C.2
  • 7
    • 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 mitotic cells
    • Firmbach-Kraft, I., and R. Stick. 1993. The role of CaaX-dependent modifications in membrane association of Xenopus nuclear lamin B3 during meiosis and the fate of B3 in transfected mitotic cells. J. Cell Biol. 123:1661-1670.
    • (1993) J. Cell Biol. , vol.123 , pp. 1661-1670
    • Firmbach-Kraft, I.1    Stick, R.2
  • 9
    • 0012882392 scopus 로고
    • Nuclear lamina and organization of nuclear architecture
    • Gerace, L. 1986. Nuclear lamina and organization of nuclear architecture. Trends Biochem. Sci. 11:443-446.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 443-446
    • Gerace, L.1
  • 10
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace, L., and B. Burke. 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
  • 11
    • 0027442899 scopus 로고
    • The alpha-helical rod domain of human lamins a and C contains a chromatin binding site
    • Glass, C. A., J. R. Glass, H. Taniura, K. W. Hasel, J. M. Blevitt, and L. Gerace. 1993. The alpha-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.A.1    Glass, J.R.2    Taniura, H.3    Hasel, K.W.4    Blevitt, J.M.5    Gerace, L.6
  • 12
    • 0025005766 scopus 로고
    • Lamins A and C bind and assemble at the surface of mitotic chromosomes
    • Glass, J. R., and L. Gerace. 1990. Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111:1047-1058.
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1058
    • Glass, J.R.1    Gerace, L.2
  • 13
    • 0025888298 scopus 로고
    • Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases
    • Gonzalez, F. A., D. L. Raden, and R. J. Davis. 1991. Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases. J. Biol. Chem. 266:22159-22163.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22159-22163
    • Gonzalez, F.A.1    Raden, D.L.2    Davis, R.J.3
  • 14
    • 0025995844 scopus 로고
    • A structural taxonomy of DNA-binding domains
    • Harrison, S. C. 1991. A structural taxonomy of DNA-binding domains. Nature 353:715-719.
    • (1991) Nature , vol.353 , pp. 715-719
    • Harrison, S.C.1
  • 15
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin a that prevent nuclear lamina disassembly in mitosis
    • Heald, R., and F. McKeon. 1990. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell 61:579-590.
    • (1990) Cell , vol.61 , pp. 579-590
    • Heald, R.1    McKeon, F.2
  • 16
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins
    • Hennekes, H., and E. A. Nigg. 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.A.2
  • 17
    • 0026343513 scopus 로고
    • Interaction of Xenopus lamins A and L-II with chromatin in vitro mediated by a sequence element in the carboxy-terminal domain
    • Hoeger, T. H., G. Krohne, and J. A. Kleinschmidt. 1991. Interaction of Xenopus lamins A and L-II with chromatin in vitro mediated by a sequence element in the carboxy-terminal domain. Exp. Cell Res. 197:280-289.
    • (1991) Exp. Cell Res. , vol.197 , pp. 280-289
    • Hoeger, T.H.1    Krohne, G.2    Kleinschmidt, J.A.3
  • 18
    • 0027406964 scopus 로고
    • Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators
    • Hoey, Y., R. O. Weinzierl, G. Gill, J. L. Chen, B. D. Dynlacht, and R. Tjian. 1993. Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators. Cell 72:247-260.
    • (1993) Cell , vol.72 , pp. 247-260
    • Hoey, Y.1    Weinzierl, R.O.2    Gill, G.3    Chen, J.L.4    Dynlacht, B.D.5    Tjian, R.6
  • 19
    • 0024817731 scopus 로고
    • The CaaX motif of lamin a functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope
    • Holtz, D., R. A. Tanaka, J. Hartwig, and F. McKeon. 1989. The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell 59:969-977.
    • (1989) Cell , vol.59 , pp. 969-977
    • Holtz, D.1    Tanaka, R.A.2    Hartwig, J.3    McKeon, F.4
  • 20
    • 0028876679 scopus 로고
    • Aberrant splicing and transcription termination caused by P element insertion into the intron of a Drosophila gene
    • Horowitz, H., and C. A. Berg. 1995. Aberrant splicing and transcription termination caused by P element insertion into the intron of a Drosophila gene. Genetics 139:327-335.
    • (1995) Genetics , vol.139 , pp. 327-335
    • Horowitz, H.1    Berg, C.A.2
  • 21
    • 0025845750 scopus 로고
    • The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2
    • Kitten, G. T., and E. A. Nigg. 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.T.1    Nigg, E.A.2
  • 22
    • 0026031446 scopus 로고
    • Epitope tagging and protein surveillance
    • Kolodziej, P. A., and R. A. Young. 1991. Epitope tagging and protein surveillance. Methods Enzymol. 194:508-519.
    • (1991) Methods Enzymol. , vol.194 , pp. 508-519
    • Kolodziej, P.A.1    Young, R.A.2
  • 23
    • 0024444733 scopus 로고
    • The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope
    • Krohne, G., I. Waizenegger, and T. H. Hoeger. 1989. The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope. J. Cell Biol. 109:2003-2011.
    • (1989) J. Cell Biol. , vol.109 , pp. 2003-2011
    • Krohne, G.1    Waizenegger, I.2    Hoeger, T.H.3
  • 25
    • 0028040020 scopus 로고
    • Cytoplasmic retention of a Xenopus nuclear factor 7 before the midblastula transition uses a unique anchoring mechanism involving a retention domain and several phosphorylation sites
    • Li, X., and L. D. Etkin. 1994. Cytoplasmic retention of a Xenopus nuclear factor 7 before the midblastula transition uses a unique anchoring mechanism involving a retention domain and several phosphorylation sites. J. Cell Biol. 124:7-17.
    • (1994) J. Cell Biol. , vol.124 , pp. 7-17
    • Li, X.1    Etkin, L.D.2
  • 26
    • 0026011247 scopus 로고
    • The Drosophila maternal-effect gene fs(1)Ya encodes a cell cycle-dependent nuclear envelope component required for embryonic mitosis
    • Lin, H., and M. F. Wolfner. 1991. The Drosophila maternal-effect gene fs(1)Ya encodes a cell cycle-dependent nuclear envelope component required for embryonic mitosis. Cell 64:49-62.
    • (1991) Cell , vol.64 , pp. 49-62
    • Lin, H.1    Wolfner, M.F.2
  • 28
    • 0031569824 scopus 로고    scopus 로고
    • Formation of the male pronuclear lamina in Drosophila
    • Liu, J., H. Lin, J. M. Lopez, and M. F. Wolfner. 1997. Formation of the male pronuclear lamina in Drosophila. Dev. Biol. 184:187-196.
    • (1997) Dev. Biol. , vol.184 , pp. 187-196
    • Liu, J.1    Lin, H.2    Lopez, J.M.3    Wolfner, M.F.4
  • 29
    • 0028864348 scopus 로고
    • Mutational analyses of fs(1)Ya, an essential, developmentally regulated, nuclear envelope protein in Drosophila
    • Liu, J., K. Song, and M. F. Wolfner. 1995. Mutational analyses of fs(1)Ya, an essential, developmentally regulated, nuclear envelope protein in Drosophila. Genetics 141:1473-1481.
    • (1995) Genetics , vol.141 , pp. 1473-1481
    • Liu, J.1    Song, K.2    Wolfner, M.F.3
  • 30
    • 0028321918 scopus 로고
    • The Drosophila fs(1)Ya protein, which is needed for the first mitotic division, is in the nuclear lamina and in the envelopes of cleavage nuclei, pronuclei and nonmitotic nuclei
    • Lopez, J., K. Song, A. Hirshfeld, H. Lin, and M. F. Wolfner. 1994. The Drosophila fs(1)Ya protein, which is needed for the first mitotic division, is in the nuclear lamina and in the envelopes of cleavage nuclei, pronuclei and nonmitotic nuclei. Dev. Biol. 163:202-211.
    • (1994) Dev. Biol. , vol.163 , pp. 202-211
    • Lopez, J.1    Song, K.2    Hirshfeld, A.3    Lin, H.4    Wolfner, M.F.5
  • 32
    • 0030907906 scopus 로고    scopus 로고
    • The developmentally regulated Drosophila embryonic nuclear lamina protein 'Young Arrest' (fs(1)Ya) is capable of associating with chromatin
    • Lopez, J. M., and M. F. Wolfner. 1997. The developmentally regulated Drosophila embryonic nuclear lamina protein 'Young Arrest' (fs(1)Ya) is capable of associating with chromatin. J. Cell Sci. 110:643-651.
    • (1997) J. Cell Sci. , vol.110 , pp. 643-651
    • Lopez, J.M.1    Wolfner, M.F.2
  • 34
    • 0026559677 scopus 로고
    • Nucleoplasmic localization of prelamin A: Implications for prenylation-dependent lamin a assembly into the nuclear lamina
    • Lutz, R. J., M. A. Trujillo, K. S. Denham, L. Wenger, and M. Sinensky. 1992. Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc. Natl. Acad. Sci. USA 89:3000-3004.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3000-3004
    • Lutz, R.J.1    Trujillo, M.A.2    Denham, K.S.3    Wenger, L.4    Sinensky, M.5
  • 35
    • 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
  • 36
    • 0026094394 scopus 로고
    • The nuclear-cytoplasmic distribution of the Xenopus nuclear factor 7, xnf-7, coincides with its state of phosphorylation during early development
    • Miller, M., B. A. Reddy, M. Kloc, X. X. Li, C. Dreyer, and L. D. Etkin. 1991. The nuclear-cytoplasmic distribution of the Xenopus nuclear factor 7, xnf-7, coincides with its state of phosphorylation during early development. Development 113:569-575.
    • (1991) Development , vol.113 , pp. 569-575
    • Miller, M.1    Reddy, B.A.2    Kloc, M.3    Li, X.X.4    Dreyer, C.5    Etkin, L.D.6
  • 37
    • 0017357112 scopus 로고
    • Developmental genetics of the Drosophila egg. I. Identification of 59 sex-linked cistrons with maternal effects on embryonic development
    • Mohler, J. D. 1977. Developmental genetics of the Drosophila egg. I. Identification of 59 sex-linked cistrons with maternal effects on embryonic development. Genetics 85:259-272.
    • (1977) Genetics , vol.85 , pp. 259-272
    • Mohler, J.D.1
  • 38
    • 0029198668 scopus 로고
    • The dynamic properties and possible functions of nuclear lamins
    • Moir, R. D., T. P. Spann, and R. D. Goldman. 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    Goldman, R.D.3
  • 39
    • 0025764782 scopus 로고
    • The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SW15
    • Moll, T., G. Tebb, U. Surana, H. Robitsch, and K. Nasmyth. 1991. The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SW15. Cell 66:743-758.
    • (1991) Cell , vol.66 , pp. 743-758
    • Moll, T.1    Tebb, G.2    Surana, U.3    Robitsch, H.4    Nasmyth, K.5
  • 40
    • 0025072235 scopus 로고
    • The identification of a second cell cycle control on the HO promoter in yeast, cell cycle regulation of SW15 nuclear entry
    • Nasmyth, K., G. Adolf, D. Lydall, and A. Seddon. 1990. The identification of a second cell cycle control on the HO promoter in yeast, cell cycle regulation of SW15 nuclear entry. Cell 62:631-647.
    • (1990) Cell , vol.62 , pp. 631-647
    • Nasmyth, K.1    Adolf, G.2    Lydall, D.3    Seddon, A.4
  • 41
    • 0026813618 scopus 로고
    • Assembly-disassembly of the nuclear lamina
    • Nigg, E. 1992. Assembly-disassembly of the nuclear lamina. Curr. Opin. Cell. Biol. 4:105-109.
    • (1992) Curr. Opin. Cell. Biol. , vol.4 , pp. 105-109
    • Nigg, E.1
  • 42
    • 0001179760 scopus 로고
    • A microinjection technique for ethanol-treated eggs and a mating scheme for detection of germ line transformants
    • Park, S., and J. K. Lim. 1995. A microinjection technique for ethanol-treated eggs and a mating scheme for detection of germ line transformants. Dros. Inf. Serv. 76:197-199.
    • (1995) Dros. Inf. Serv. , vol.76 , pp. 197-199
    • Park, S.1    Lim, J.K.2
  • 43
    • 0025995937 scopus 로고
    • Different activation domains of Sp1 govern formation of multimers and mediate transcriptional synergism
    • Pascal, E., and R. Tjian. 1991. Different activation domains of Sp1 govern formation of multimers and mediate transcriptional synergism. Genes Dev. 5:1646-1656.
    • (1991) Genes Dev. , vol.5 , pp. 1646-1656
    • Pascal, E.1    Tjian, R.2
  • 44
    • 0030029383 scopus 로고    scopus 로고
    • The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
    • Paulin-Levasseur, M., D. L. Blake, M. Julien, and L. Rouleau. 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
  • 45
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter, M., J. Nakagawa, M. Doree, J. C. Labbe, and E. A. Nigg. 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
  • 46
    • 0027405725 scopus 로고
    • The k1-3 loop of the Y chromosome of Drosophila melanogaster binds a tektin-like protein
    • Pisano, C., S. Bonaccorsi, and M. Gatti. 1993. The k1-3 loop of the Y chromosome of Drosophila melanogaster binds a tektin-like protein. Genetics 133:569-579.
    • (1993) Genetics , vol.133 , pp. 569-579
    • Pisano, C.1    Bonaccorsi, S.2    Gatti, M.3
  • 47
    • 0019413560 scopus 로고
    • Monoclonal antibodies against a nuclear membrane protein of Drosophila: Localization by indirect immunofluorescence and detection of antigen using a new protein blotting procedure
    • Risau, W., H. Saumweber, and P. Symmons. 1981. Monoclonal antibodies against a nuclear membrane protein of Drosophila: localization by indirect immunofluorescence and detection of antigen using a new protein blotting procedure. Exp. Cell Res. 133:47-54.
    • (1981) Exp. Cell Res. , vol.133 , pp. 47-54
    • Risau, W.1    Saumweber, H.2    Symmons, P.3
  • 49
    • 0029585540 scopus 로고
    • In vivo assembly kinetics of fluorescently-labeled Xenopus lamin a mutants
    • Schmidt, M., and G. Krohne. 1995. In vivo assembly kinetics of fluorescently-labeled Xenopus lamin A mutants. Eur. J. Cell Biol. 68:345-354.
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 345-354
    • Schmidt, M.1    Krohne, G.2
  • 50
    • 0030042985 scopus 로고    scopus 로고
    • Finely tuned regulation of cytoplasmic retention of Xenopus nuclear factor 7 by phosphorylation of individual threonine residues
    • Shou, W., X. Li, T. Cao, J. Kuang, S. Che, and L. D. Etkin. 1996. Finely tuned regulation of cytoplasmic retention of Xenopus nuclear factor 7 by phosphorylation of individual threonine residues. Mol. Cell. Biol. 16:990-997.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 990-997
    • Shou, W.1    Li, X.2    Cao, T.3    Kuang, J.4    Che, S.5    Etkin, L.D.6
  • 51
    • 0023575750 scopus 로고
    • Biosynthesis and interconversion of Drosophila nuclear lamin isoforms during normal growth and in response to heatshock
    • Smith, D. E., Y. Gruenbaum, M. Berrios, and P. A. Fisher. 1987. Biosynthesis and interconversion of Drosophila nuclear lamin isoforms during normal growth and in response to heatshock. J. Cell Biol. 105:771-790.
    • (1987) J. Cell Biol. , vol.105 , pp. 771-790
    • Smith, D.E.1    Gruenbaum, Y.2    Berrios, M.3    Fisher, P.A.4
  • 53
    • 0001849829 scopus 로고
    • Position-effect variegation in Drosophila
    • M. Ashburner and T. R. Wright (ed.), Academic Press, New York, N.Y.
    • Spofford, J. B. 1980. Position-effect variegation in Drosophila, p. 955-1018. In M. Ashburner and T. R. Wright (ed.), Genetics and biology of Drosophila, vol. 1a. Academic Press, New York, N.Y.
    • (1980) Genetics and Biology of Drosophila , vol.1 A , pp. 955-1018
    • Spofford, J.B.1
  • 54
    • 0030198913 scopus 로고    scopus 로고
    • Intermediate filament protein polymerization: Molecular analysis of Drosophila nuclear lamin head-to-tail binding
    • Stuurman, N., B. Sasse, and P. A. Fisher. 1996. Intermediate filament protein polymerization: molecular analysis of Drosophila nuclear lamin head-to-tail binding. J. Struct. Biol. 117:1-15.
    • (1996) J. Struct. Biol. , vol.117 , pp. 1-15
    • Stuurman, N.1    Sasse, B.2    Fisher, P.A.3
  • 55
    • 0024465335 scopus 로고
    • SPKK, a new nucleic acid-binding unit of protein found in histone
    • Suzuki, M. 1989. SPKK, a new nucleic acid-binding unit of protein found in histone. EMBO J. 8:797-804.
    • (1989) EMBO J. , vol.8 , pp. 797-804
    • Suzuki, M.1
  • 56
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura, H., C. Glass, and L. Gerace. 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
  • 57
    • 0029560752 scopus 로고
    • Heterochromatin and gene expression in Drosophila
    • Weiler, K. S., and B. T. Wakimoto. 1995. Heterochromatin and gene expression in Drosophila. Annu. Rev. Genet. 29:577-605.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 577-605
    • Weiler, K.S.1    Wakimoto, B.T.2
  • 58
    • 0028968891 scopus 로고
    • The Drosophila kinesin-like protein KLP3a is a midbody component required for central spindle assembly and initiation of cytokinesis
    • Williams, B. C., M. F. Riedy, E. V. Williams, M. Gatti, and M. L. Goldberg. 1995. The Drosophila kinesin-like protein KLP3A is a midbody component required for central spindle assembly and initiation of cytokinesis. J. Cell Biol. 129:709-723.
    • (1995) J. Cell Biol. , vol.129 , pp. 709-723
    • Williams, B.C.1    Riedy, M.F.2    Williams, E.V.3    Gatti, M.4    Goldberg, M.L.5
  • 60
    • 0029160015 scopus 로고
    • Protein-protein interactions between human nuclear lamins expressed in yeast
    • Ye, Q., and H. J. Worman. 1995. Protein-protein interactions between human nuclear lamins expressed in yeast. Exp. Cell Res. 219:292-298.
    • (1995) Exp. Cell Res. , vol.219 , pp. 292-298
    • Ye, Q.1    Worman, H.J.2
  • 63
    • 0030025220 scopus 로고    scopus 로고
    • Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state
    • Zhao, K., A. Harel, N. Stuurman, U. Guedalia, and Y. Gruenbaum. 1996. Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state. FEBS Lett. 380: 161-164.
    • (1996) FEBS Lett. , vol.380 , pp. 161-164
    • Zhao, K.1    Harel, A.2    Stuurman, N.3    Guedalia, U.4    Gruenbaum, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.