메뉴 건너뛰기




Volumn 21, Issue 7, 2012, Pages 1544-1556

LMNA variants cause cytoplasmic distribution of nuclear pore proteins in drosophila and human muscle

Author keywords

[No Author keywords available]

Indexed keywords

LAMIN A; LAMIN B; LAMIN C; LMNA PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84858170389     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr592     Document Type: Article
Times cited : (37)

References (79)
  • 1
    • 33845286555 scopus 로고    scopus 로고
    • Human laminopathies: nuclei gone genetically awry
    • Capell, B.C. and Collins, F.S. (2006) Human laminopathies: nuclei gone genetically awry. Nat. Rev. Genet., 7, 940-952.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 940-952
    • Capell, B.C.1    Collins, F.S.2
  • 5
    • 0035197961 scopus 로고    scopus 로고
    • The plant nuclear envelope
    • Meier, I. (2001) The plant nuclear envelope. Cell. Mol. Life Sci., 58, 1774-1780.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1774-1780
    • Meier, I.1
  • 7
    • 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
  • 9
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L. and Blobel, G. (1980) The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell, 19, 277-287.
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 10
    • 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
  • 11
    • 0028980645 scopus 로고
    • Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins
    • Riemer, D., Stuurman, N., Berrios, M., Hunter, C., Fisher, P.A. and Weber, K. (1995) Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins. J. Cell Sci., 108 (Pt 10), 3189-3198.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 10 , pp. 3189-3198
    • Riemer, D.1    Stuurman, N.2    Berrios, M.3    Hunter, C.4    Fisher, P.A.5    Weber, K.6
  • 12
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: their structure, assembly, and interactions
    • Stuurman, N., Heins, S. and Aebi, U. (1998) Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol., 122, 42-66.
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 13
    • 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
  • 14
    • 0028342511 scopus 로고
    • Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice
    • Furukawa, K., Inagaki, H. and Hotta, Y. (1994) Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice. Exp. Cell Res., 212, 426-430.
    • (1994) Exp. Cell Res. , vol.212 , pp. 426-430
    • Furukawa, K.1    Inagaki, H.2    Hotta, Y.3
  • 16
    • 33751060219 scopus 로고    scopus 로고
    • Identification of a novel, highly variable aminoterminal amino acid sequence element in the nuclear intermediate filament protein lamin B(2) from higher vertebrates
    • Schumacher, J., Reichenzeller, M., Kempf, T., Schnolzer, M. and Herrmann, H. (2006) Identification of a novel, highly variable aminoterminal amino acid sequence element in the nuclear intermediate filament protein lamin B(2) from higher vertebrates. FEBS Lett., 580, 6211-6216.
    • (2006) FEBS Lett. , vol.580 , pp. 6211-6216
    • Schumacher, J.1    Reichenzeller, M.2    Kempf, T.3    Schnolzer, M.4    Herrmann, H.5
  • 17
    • 34248391873 scopus 로고    scopus 로고
    • The nuclear envelope, a key structure in cellular integrity and gene expression
    • Verstraeten, V.L., Broers, J.L., Ramaekers, F.C. and van Steensel, M.A. (2007) The nuclear envelope, a key structure in cellular integrity and gene expression. Curr. Med. Chem., 14, 1231-1248.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1231-1248
    • Verstraeten, V.L.1    Broers, J.L.2    Ramaekers, F.C.3    van Steensel, M.A.4
  • 18
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins
    • Fisher, D.Z., Chaudhary, N. and Blobel, G. (1986) cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl Acad. Sci. USA, 83, 6450-6454.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 20
    • 0035694237 scopus 로고    scopus 로고
    • Identification of essential genes in cultured mammalian cells using small interfering RNAs
    • Harborth, J., Elbashir, S.M., Bechert, K., Tuschl, T. and Weber, K. (2001) Identification of essential genes in cultured mammalian cells using small interfering RNAs. J. Cell. Sci., 114, 4557-4565.
    • (2001) J. Cell. Sci. , vol.114 , pp. 4557-4565
    • Harborth, J.1    Elbashir, S.M.2    Bechert, K.3    Tuschl, T.4    Weber, K.5
  • 21
    • 0025317917 scopus 로고
    • In vitro posttranslational modification of lamin B cloned from a human T-cell line
    • Pollard, K.M., Chan, E.K., Grant, B.J., Sullivan, K.F., Tan, E.M. and Glass, C.A. (1990) In vitro posttranslational modification of lamin B cloned from a human T-cell line. Mol. Cell Biol., 10, 2164-2175.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 2164-2175
    • Pollard, K.M.1    Chan, E.K.2    Grant, B.J.3    Sullivan, K.F.4    Tan, E.M.5    Glass, C.A.6
  • 22
    • 0020640611 scopus 로고
    • Mitotic architecture of the cell: the filament networks of the nucleus and cytoplasm
    • Capco, D.G. and Penman, S. (1983) Mitotic architecture of the cell: the filament networks of the nucleus and cytoplasm. J. Cell Biol., 96, 896-906.
    • (1983) J. Cell Biol. , vol.96 , pp. 896-906
    • Capco, D.G.1    Penman, S.2
  • 23
    • 0033749567 scopus 로고    scopus 로고
    • Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes
    • Liu, J., Rolef Ben-Shahar, T., Riemer, D., Treinin, M., Spann, P., Weber, K., Fire, A. and Gruenbaum, Y. (2000) Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol. Biol. Cell, 11, 3937-3947.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Rolef Ben-Shahar, T.2    Riemer, D.3    Treinin, M.4    Spann, P.5    Weber, K.6    Fire, A.7    Gruenbaum, Y.8
  • 24
    • 0037220989 scopus 로고    scopus 로고
    • Nuclear positioning: the means is at the ends
    • Morris, N.R. (2003) Nuclear positioning: the means is at the ends. Curr. Opin. Cell Biol., 15, 54-59.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 54-59
    • Morris, N.R.1
  • 25
    • 0025306949 scopus 로고
    • Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery
    • Paddy, M.R., Belmont, A.S., Saumweber, H., Agard, D.A. and Sedat, J.W. (1990) Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery. Cell, 62, 89-106.
    • (1990) Cell , vol.62 , pp. 89-106
    • Paddy, M.R.1    Belmont, A.S.2    Saumweber, H.3    Agard, D.A.4    Sedat, J.W.5
  • 26
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer, E.C., Florens, L., Guan, T., Yates, J.R. III and Gerace, L. (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science, 301, 1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates III, J.R.4    Gerace, L.5
  • 27
    • 30444450095 scopus 로고    scopus 로고
    • KASH 'n Karry: the KASH domain family of cargo-specific cytoskeletal adaptor proteins
    • Starr, D.A. and Fischer, J.A. (2005) KASH 'n Karry: the KASH domain family of cargo-specific cytoskeletal adaptor proteins. Bioessays, 27, 1136-1146.
    • (2005) Bioessays , vol.27 , pp. 1136-1146
    • Starr, D.A.1    Fischer, J.A.2
  • 29
    • 33846140462 scopus 로고    scopus 로고
    • KASH-domain proteins in nuclear migration, anchorage and other processes
    • Wilhelmsen, K., Ketema, M., Truong, H. and Sonnenberg, A. (2006) KASH-domain proteins in nuclear migration, anchorage and other processes. J. Cell Sci., 119, 5021-5029.
    • (2006) J. Cell Sci. , vol.119 , pp. 5021-5029
    • Wilhelmsen, K.1    Ketema, M.2    Truong, H.3    Sonnenberg, A.4
  • 30
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak, P., Sasseville, A.M., Raymond, Y. and Cook, P.R. (1995) Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci., 108 (Pt 2), 635-644.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 2 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 31
    • 3042829496 scopus 로고    scopus 로고
    • A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation
    • Johnson, B.R., Nitta, R.T., Frock, R.L., Mounkes, L., Barbie, D.A., Stewart, C.L., Harlow, E. and Kennedy, B.K. (2004) A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation. Proc. Natl Acad. Sci. USA, 101, 9677-9682.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9677-9682
    • Johnson, B.R.1    Nitta, R.T.2    Frock, R.L.3    Mounkes, L.4    Barbie, D.A.5    Stewart, C.L.6    Harlow, E.7    Kennedy, B.K.8
  • 33
    • 0034669029 scopus 로고    scopus 로고
    • Nuclear organization of DNA replication in primary mammalian cells
    • Kennedy, B.K., Barbie, D.A., Classon, M., Dyson, N. and Harlow, E. (2000) Nuclear organization of DNA replication in primary mammalian cells. Genes Dev., 14, 2855-2868.
    • (2000) Genes Dev , vol.14 , pp. 2855-2868
    • Kennedy, B.K.1    Barbie, D.A.2    Classon, M.3    Dyson, N.4    Harlow, E.5
  • 34
    • 4544228141 scopus 로고    scopus 로고
    • The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
    • Dahl, K.N., Kahn, S.M., Wilson, K.L. and Discher, D.E. (2004) The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. J. Cell Sci., 117, 4779-4786.
    • (2004) J. Cell Sci. , vol.117 , pp. 4779-4786
    • Dahl, K.N.1    Kahn, S.M.2    Wilson, K.L.3    Discher, D.E.4
  • 35
    • 34247505044 scopus 로고    scopus 로고
    • Role of nuclear lamina-cytoskeleton interactions in the maintenance of cellular strength
    • Houben, F., Ramaekers, F.C., Snoeckx, L.H. and Broers, J.L. (2007) Role of nuclear lamina-cytoskeleton interactions in the maintenance of cellular strength. Biochim. Biophys. Acta, 1773, 675-686.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 675-686
    • Houben, F.1    Ramaekers, F.C.2    Snoeckx, L.H.3    Broers, J.L.4
  • 36
    • 30044434950 scopus 로고    scopus 로고
    • A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases? Histochem
    • Gotzmann, J. and Foisner, R. (2006) A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases? Histochem. Cell Biol., 125, 33-41.
    • (2006) Cell Biol , vol.125 , pp. 33-41
    • Gotzmann, J.1    Foisner, R.2
  • 37
    • 47949122432 scopus 로고    scopus 로고
    • Adult stem cell maintenance and tissue regeneration in the ageing context: the role for A-type lamins as intrinsic modulators of ageing in adult stem cells and their niches
    • Pekovic, V. and Hutchison, C.J. (2008) Adult stem cell maintenance and tissue regeneration in the ageing context: the role for A-type lamins as intrinsic modulators of ageing in adult stem cells and their niches. J. Anat., 213, 5-25.
    • (2008) J. Anat. , vol.213 , pp. 5-25
    • Pekovic, V.1    Hutchison, C.J.2
  • 38
    • 34250166469 scopus 로고    scopus 로고
    • Lamins and lamin-associated proteins in aging and disease
    • Vlcek, S. and Foisner, R. (2007) Lamins and lamin-associated proteins in aging and disease. Curr. Opin. Cell Biol., 19, 298-304.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 298-304
    • Vlcek, S.1    Foisner, R.2
  • 43
    • 0036741796 scopus 로고    scopus 로고
    • GAL4 system in Drosophila: a fly geneticist's Swiss army knife
    • Duffy, J.B. (2002) GAL4 system in Drosophila: a fly geneticist's Swiss army knife. Genesis, 34, 1-15.
    • (2002) Genesis , vol.34 , pp. 1-15
    • Duffy, J.B.1
  • 44
    • 77956601360 scopus 로고    scopus 로고
    • The role of Drosophila Lamin C in muscle function and gene expression
    • Dialynas, G., Speese, S., Budnik, V., Geyer, P.K. and Wallrath, L.L. (2010) The role of Drosophila Lamin C in muscle function and gene expression. Development, 137, 3067-3077.
    • (2010) Development , vol.137 , pp. 3067-3077
    • Dialynas, G.1    Speese, S.2    Budnik, V.3    Geyer, P.K.4    Wallrath, L.L.5
  • 45
    • 36448957153 scopus 로고    scopus 로고
    • dTrf2 is required for transcriptional and developmental responses to ecdysone during Drosophila metamorphosis
    • Bashirullah, A., Lam, G., Yin, V.P. and Thummel, C.S. (2007) dTrf2 is required for transcriptional and developmental responses to ecdysone during Drosophila metamorphosis. Dev. Dyn., 236, 3173-3179.
    • (2007) Dev. Dyn. , vol.236 , pp. 3173-3179
    • Bashirullah, A.1    Lam, G.2    Yin, V.P.3    Thummel, C.S.4
  • 46
    • 34547861803 scopus 로고    scopus 로고
    • Drosophila Klaroid encodes a SUN domain protein required for Klarsicht localization to the nuclear envelope and nuclear migration in the eye
    • Kracklauer, M.P., Banks, S.M., Xie, X., Wu, Y. and Fischer, J.A. (2007) Drosophila Klaroid encodes a SUN domain protein required for Klarsicht localization to the nuclear envelope and nuclear migration in the eye. Fly (Austin), 1, 75-85.
    • (2007) Fly (Austin) , vol.1 , pp. 75-85
    • Kracklauer, M.P.1    Banks, S.M.2    Xie, X.3    Wu, Y.4    Fischer, J.A.5
  • 47
    • 0023449881 scopus 로고
    • Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway
    • Davis, L.I. and Blobel, G. (1987) Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. Proc. Natl Acad. Sci. USA, 84, 7552-7556.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7552-7556
    • Davis, L.I.1    Blobel, G.2
  • 48
    • 0021987228 scopus 로고
    • Monoclonal antibodies prepared against the major Drosophila nuclear Matrix-pore complex-lamina glycoprotein bind specifically to the nuclear envelope in situ
    • Filson, A.J., Lewis, A., Blobel, G. and Fisher, P.A. (1985) Monoclonal antibodies prepared against the major Drosophila nuclear Matrix-pore complex-lamina glycoprotein bind specifically to the nuclear envelope in situ. J. Biol. Chem., 260, 3164-3172.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3164-3172
    • Filson, A.J.1    Lewis, A.2    Blobel, G.3    Fisher, P.A.4
  • 49
    • 0024445456 scopus 로고
    • Distribution patterns of HP1, a heterochromatin-associated nonhistone chromosomal protein of Drosophila
    • James, T.C., Eissenberg, J.C., Craig, C., Dietrich, V., Hobson, A. and Elgin, S.C. (1989) Distribution patterns of HP1, a heterochromatin-associated nonhistone chromosomal protein of Drosophila. Eur. J. Cell Biol., 50, 170-180.
    • (1989) Eur. J. Cell Biol. , vol.50 , pp. 170-180
    • James, T.C.1    Eissenberg, J.C.2    Craig, C.3    Dietrich, V.4    Hobson, A.5    Elgin, S.C.6
  • 50
    • 0018874238 scopus 로고
    • Arrangement of chromatin in the nucleus
    • Comings, D.E. (1980) Arrangement of chromatin in the nucleus. Hum. Genet., 53, 131-143.
    • (1980) Hum. Genet. , vol.53 , pp. 131-143
    • Comings, D.E.1
  • 51
    • 0029937208 scopus 로고    scopus 로고
    • Genetic modification of heterochromatic association and nuclear organization in Drosophila
    • Csink, A.K. and Henikoff, S. (1996) Genetic modification of heterochromatic association and nuclear organization in Drosophila. Nature, 381, 529-531.
    • (1996) Nature , vol.381 , pp. 529-531
    • Csink, A.K.1    Henikoff, S.2
  • 52
    • 0027135889 scopus 로고
    • Macromolecular domains within the cell nucleus
    • Spector, D.L. (1993) Macromolecular domains within the cell nucleus. Annu. Rev. Cell Biol., 9, 265-315.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 265-315
    • Spector, D.L.1
  • 55
    • 0030778575 scopus 로고    scopus 로고
    • Assembly of A- and B-type lamins studied in vivo with the baculovirus system
    • Klapper, M., Exner, K., Kempf, A., Gehrig, C., Stuurman, N., Fisher, P.A. and Krohne, G. (1997) Assembly of A- and B-type lamins studied in vivo with the baculovirus system. J. Cell Sci., 110 (Pt 20), 2519-2532.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 20 , pp. 2519-2532
    • Klapper, M.1    Exner, K.2    Kempf, A.3    Gehrig, C.4    Stuurman, N.5    Fisher, P.A.6    Krohne, G.7
  • 57
    • 0037684765 scopus 로고    scopus 로고
    • The nucleoskeleton: lamins and actin are major players in essential nuclear functions
    • Shumaker, D.K., Kuczmarski, E.R. and Goldman, R.D. (2003) The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr. Opin. Cell Biol., 15, 358-366.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 358-366
    • Shumaker, D.K.1    Kuczmarski, E.R.2    Goldman, R.D.3
  • 59
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg, J., Siggia, E.D., Moreira, J.E., Smith, C.L., Presley, J.F., Worman, H.J. and Lippincott-Schwartz, J. (1997) Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol., 138, 1193-1206.
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 60
    • 0033021606 scopus 로고    scopus 로고
    • Intracellular trafficking of emerin, the Emery- Dreifuss muscular dystrophy protein
    • Ostlund, C., Ellenberg, J., Hallberg, E., Lippincott-Schwartz, J. and Worman, H.J. (1999) Intracellular trafficking of emerin, the Emery- Dreifuss muscular dystrophy protein. J. Cell Sci., 112 (Pt 11), 1709-1719.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 11 , pp. 1709-1719
    • Ostlund, C.1    Ellenberg, J.2    Hallberg, E.3    Lippincott-Schwartz, J.4    Worman, H.J.5
  • 61
    • 32244448250 scopus 로고    scopus 로고
    • Dependence of diffusional mobility of integral inner nuclear membrane proteins on A-type lamins
    • Ostlund, C., Sullivan, T., Stewart, C.L. and Worman, H.J. (2006) Dependence of diffusional mobility of integral inner nuclear membrane proteins on A-type lamins. Biochemistry, 45, 1374-1382.
    • (2006) Biochemistry , vol.45 , pp. 1374-1382
    • Ostlund, C.1    Sullivan, T.2    Stewart, C.L.3    Worman, H.J.4
  • 62
    • 0025666495 scopus 로고
    • Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina
    • Powell, L. and Burke, B. (1990) Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina. J. Cell Biol., 111, 2225-2234.
    • (1990) J. Cell Biol. , vol.111 , pp. 2225-2234
    • Powell, L.1    Burke, B.2
  • 63
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: integrating isolated clues
    • Zastrow, M.S., Vlcek, S. and Wilson, K.L. (2004) Proteins that bind A-type lamins: integrating isolated clues. J. Cell Sci., 117, 979-987.
    • (2004) J. Cell Sci. , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 65
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • Haque, F., Lloyd, D.J., Smallwood, D.T., Dent, C.L., Shanahan, C.M., Fry, A.M., Trembath, R.C. and Shackleton, S. (2006) SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol. Cell Biol., 26, 3738-3751.
    • (2006) Mol. Cell Biol. , vol.26 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Trembath, R.C.7    Shackleton, S.8
  • 68
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies
    • Lloyd, D.J., Trembath, R.C. and Shackleton, S. (2002) A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum. Mol. Genet., 11, 769-777.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 70
    • 80054702906 scopus 로고    scopus 로고
    • Distinct association of the nuclear pore protein Nup153 with A- and B-type lamins
    • Al-Haboubi, T., Shumaker, D.K., Koser, J., Wehnert, M. and Fahrenkrog, B. (2011) Distinct association of the nuclear pore protein Nup153 with A- and B-type lamins. Nucleus, 2, 500-509.
    • (2011) Nucleus , vol.2 , pp. 500-509
    • Al-Haboubi, T.1    Shumaker, D.K.2    Koser, J.3    Wehnert, M.4    Fahrenkrog, B.5
  • 72
    • 0037624625 scopus 로고    scopus 로고
    • Architectural abnormalities in muscle nuclei: ultrastructural differences between X-linked and autosomal dominant forms of EDMD
    • Fidzianska, A. and Hausmanowa-Petrusewicz, I. (2003) Architectural abnormalities in muscle nuclei: ultrastructural differences between X-linked and autosomal dominant forms of EDMD. J. Neurol. Sci., 210, 47-51.
    • (2003) J. Neurol. Sci. , vol.210 , pp. 47-51
    • Fidzianska, A.1    Hausmanowa-Petrusewicz, I.2
  • 73
    • 0345084450 scopus 로고    scopus 로고
    • Ultrastructural abnormality of sarcolemmal nuclei in Emery-Dreifuss muscular dystrophy (EDMD)
    • Fidzianska, A., Toniolo, D. and Hausmanowa-Petrusewicz, I. (1998) Ultrastructural abnormality of sarcolemmal nuclei in Emery-Dreifuss muscular dystrophy (EDMD). J. Neurol. Sci., 159, 88-93.
    • (1998) J. Neurol. Sci. , vol.159 , pp. 88-93
    • Fidzianska, A.1    Toniolo, D.2    Hausmanowa-Petrusewicz, I.3
  • 74
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. and Perrimon, N. (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development, 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 75
    • 0028691986 scopus 로고
    • Raising large quantities of Drosophila for biochemical experiments
    • Shaffer, C.D., Wuller, J.M. and Elgin, S.C. (1994) Raising large quantities of Drosophila for biochemical experiments. Methods Cell Biol., 44, 99-108.
    • (1994) Methods Cell Biol , vol.44 , pp. 99-108
    • Shaffer, C.D.1    Wuller, J.M.2    Elgin, S.C.3
  • 76
    • 0033529567 scopus 로고    scopus 로고
    • Regulation of DLG localization at synapses by CaMKII-dependent phosphorylation
    • Koh, Y.H., Popova, E., Thomas, U., Griffith, L.C. and Budnik, V. (1999) Regulation of DLG localization at synapses by CaMKII-dependent phosphorylation. Cell, 98, 353-363.
    • (1999) Cell , vol.98 , pp. 353-363
    • Koh, Y.H.1    Popova, E.2    Thomas, U.3    Griffith, L.C.4    Budnik, V.5
  • 77
    • 0025513585 scopus 로고
    • Morphological plasticity of motor axons in Drosophila mutants with altered excitability
    • Budnik, V., Zhong, Y. and Wu, C.F. (1990) Morphological plasticity of motor axons in Drosophila mutants with altered excitability. J. Neurosci., 10, 3754-3768.
    • (1990) J. Neurosci. , vol.10 , pp. 3754-3768
    • Budnik, V.1    Zhong, Y.2    Wu, C.F.3
  • 78
    • 0026499832 scopus 로고
    • The urate oxidase gene of Drosophila pseudoobscura and Drosophila melanogaster: evolutionary changes of sequence and regulation
    • Friedman, T.B., Burnett, J.B., Lootens, S., Steinman, R. and Wallrath, L.L. (1992) The urate oxidase gene of Drosophila pseudoobscura and Drosophila melanogaster: evolutionary changes of sequence and regulation. J. Mol. Evol., 34, 62-77.
    • (1992) J. Mol. Evol. , vol.34 , pp. 62-77
    • Friedman, T.B.1    Burnett, J.B.2    Lootens, S.3    Steinman, R.4    Wallrath, L.L.5
  • 79
    • 52049104416 scopus 로고    scopus 로고
    • Sensory mechanisms controlling the timing of larval developmental and behavioral transitions require the Drosophila DEG/ ENaC subunit
    • Ainsley, J.A., Kim, M.J., Wegman, L.J., Pettus, J.M. and Johnson, W.A. (2008) Sensory mechanisms controlling the timing of larval developmental and behavioral transitions require the Drosophila DEG/ ENaC subunit, Pickpocket1. Dev. Biol., 322, 46-55.
    • (2008) Pickpocket1. Dev. Biol. , vol.322 , pp. 46-55
    • Ainsley, J.A.1    Kim, M.J.2    Wegman, L.J.3    Pettus, J.M.4    Johnson, W.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.