메뉴 건너뛰기




Volumn 120, Issue 1, 2007, Pages 77-85

Specific and conserved sequences in D. melanogaster and C. elegans lamins and histone H2A mediate the attachment of lamins to chromosomes

Author keywords

Chromatin; Histone; NLS; Nuclear envelope; Trail domain

Indexed keywords

ALANINE; ARGININE; HISTONE H2A; HISTONE H2B; IMMUNOGLOBULIN; LAMIN; THREONINE;

EID: 33846847699     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03325     Document Type: Article
Times cited : (58)

References (69)
  • 2
    • 33846844376 scopus 로고    scopus 로고
    • The lamin Dm(0) allele Ari3 acts as an enhancer of position effect variegation of the w (m4) allele in Drosophila
    • in press
    • Bao, X., Girton, J., Johansen, J. and Johansen, K. M. (2006). The lamin Dm(0) allele Ari3 acts as an enhancer of position effect variegation of the w (m4) allele in Drosophila. Genetics in press.
    • (2006) Genetics
    • Bao, X.1    Girton, J.2    Johansen, J.3    Johansen, K.M.4
  • 3
    • 0029967125 scopus 로고    scopus 로고
    • DNA from Drosophila melanogaster beta-heterochromatin binds specifically to nuclear lamins in vitro and the nuclear envelope in situ
    • Baricheva, E. A., Berrios, M., Bogachev, S. S., Borisevich, I. V., Lapik, E. R., Sharakhov, I. V., Stuurman, N. and Fisher, P. A. (1996). DNA from Drosophila melanogaster beta-heterochromatin binds specifically to nuclear lamins in vitro and the nuclear envelope in situ. Gene 171, 171-176.
    • (1996) Gene , vol.171 , pp. 171-176
    • Baricheva, E.A.1    Berrios, M.2    Bogachev, S.S.3    Borisevich, I.V.4    Lapik, E.R.5    Sharakhov, I.V.6    Stuurman, N.7    Fisher, P.A.8
  • 4
    • 0027752440 scopus 로고
    • Lamin B distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy tomography
    • Belmont, A. S., Zhai, Y. and Thilenius, A. (1993). Lamin B distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy tomography. J. Cell Biol. 123, 1671-1685.
    • (1993) J. Cell Biol. , vol.123 , pp. 1671-1685
    • Belmont, A.S.1    Zhai, Y.2    Thilenius, A.3
  • 5
    • 0038094501 scopus 로고    scopus 로고
    • Nucleosomes unfold completely at a transcriptionally active promoter
    • Boeger, H., Griesenbeck, J., Strattan, J. S. and Kornberg, R. D. (2003). Nucleosomes unfold completely at a transcriptionally active promoter. Mol. Cell 11, 1587-1598.
    • (2003) Mol. Cell , vol.11 , pp. 1587-1598
    • Boeger, H.1    Griesenbeck, J.2    Strattan, J.S.3    Kornberg, R.D.4
  • 6
    • 2942574467 scopus 로고    scopus 로고
    • Removal of promoter nucleosomes by disassembly rather than sliding in vivo
    • Boeger, H., Griesenbeck, J., Strattan, J. S. and Kornberg, R. D. (2004). Removal of promoter nucleosomes by disassembly rather than sliding in vivo. Mol. Cell 14, 667-673.
    • (2004) Mol. Cell , vol.14 , pp. 667-673
    • Boeger, H.1    Griesenbeck, J.2    Strattan, J.S.3    Kornberg, R.D.4
  • 7
    • 0027285880 scopus 로고
    • A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein
    • Bossie, C. A. and Sanders, M. M. (1993). A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein. J. Cell Sci. 104, 1263-1272.
    • (1993) J. Cell Sci. , vol.104 , pp. 1263-1272
    • Bossie, C.A.1    Sanders, M.M.2
  • 10
    • 33645053801 scopus 로고    scopus 로고
    • Lysine residues in N-terminal and C-terminal regions of human historic H2A are targets for biotinylation by biotinidase
    • Chew, Y., Camporeale, G., Kothapalli, N., Sarath, G. and Zempleni, J. (2006). Lysine residues in N-terminal and C-terminal regions of human historic H2A are targets for biotinylation by biotinidase. J. Nutr Biochem. 17, 225-233.
    • (2006) J. Nutr Biochem. , vol.17 , pp. 225-233
    • Chew, Y.1    Camporeale, G.2    Kothapalli, N.3    Sarath, G.4    Zempleni, J.5
  • 11
    • 0035146907 scopus 로고    scopus 로고
    • Transcriptional repression, apoptosis, human disease and the functional evolution ofthe nuclear lamina
    • Cohen, M., Lee, K. K., Wilson, K. L. and Gruenbaum, Y. (2001). Transcriptional repression, apoptosis, human disease and the functional evolution ofthe nuclear lamina. Trends Bioc. Sci. 26, 41-47.
    • (2001) Trends Bioc. Sci. , vol.26 , pp. 41-47
    • Cohen, M.1    Lee, K.K.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 13
    • 0034331073 scopus 로고    scopus 로고
    • Finding nuclear localization signals
    • Cokol, M., Nair, R. and Rost, B. (2000). Finding nuclear localization signals. EMBO Rep. 1, 411-415.
    • (2000) EMBO Rep. , vol.1 , pp. 411-415
    • Cokol, M.1    Nair, R.2    Rost, B.3
  • 14
    • 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
  • 15
    • 0035189722 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins and the nuclear lamina
    • Foisner, R. (2001). Inner nuclear membrane proteins and the nuclear lamina. J Cell Sci. 114, 3791-3792.
    • (2001) J Cell Sci. , vol.114 , pp. 3791-3792
    • Foisner, R.1
  • 16
    • 22144448593 scopus 로고    scopus 로고
    • Historic H2A phosphorylation in DNA double-strand break repair
    • Foster, E. and Downs, J. (2005). Historic H2A phosphorylation in DNA double-strand break repair. FEBS Lett. 272, 3231-3240.
    • (2005) FEBS Lett. , vol.272 , pp. 3231-3240
    • Foster, E.1    Downs, J.2
  • 17
    • 0016401871 scopus 로고
    • Structure, biochemistry, and function of the Nuclear envelope
    • Franke, W. W. (1974). Structure, biochemistry, and function of the Nuclear envelope. Philos. Trans. R. Soc. Land. B 268, 67-93.
    • (1974) Philos. Trans. R. Soc. Land. B , vol.268 , pp. 67-93
    • Franke, W.W.1
  • 18
    • 2342466617 scopus 로고    scopus 로고
    • Matefin, a C. elegans germ-line specific SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development
    • Fridkin, A., Mills, E., Margalit, A., Neufeld, E., Lee, K. K., Feinstein, N., Cohen, M., Wilson, K. L. and Gruenbaum, Y. (2004). Matefin, a C. elegans germ-line specific SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development. Proc. Natl. Acad. Sci. USA 101, 6987-6992.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6987-6992
    • Fridkin, A.1    Mills, E.2    Margalit, A.3    Neufeld, E.4    Lee, K.K.5    Feinstein, N.6    Cohen, M.7    Wilson, K.L.8    Gruenbaum, Y.9
  • 19
    • 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
  • 20
    • 0025005766 scopus 로고
    • Lamins A and C bind and assemble at the surface of mitotic chromosomes
    • Glass, J. R. and Gerace, L. (1990). Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111, 1047-1057.
    • (1990) J. Cell Biol. , vol.111 , pp. 1047-1057
    • Glass, J.R.1    Gerace, L.2
  • 24
    • 30044434950 scopus 로고    scopus 로고
    • A-type lamin complexes and regenerative potential: A step towards understanding laminopathic diseases?
    • Gotzmann, J. and Foisner, R. (2005). A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases? Histochem. Cell Biol. 125, 33-41.
    • (2005) Histochem. Cell Biol. , vol.125 , pp. 33-41
    • Gotzmann, J.1    Foisner, R.2
  • 25
    • 0023840620 scopus 로고
    • Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene
    • Gruenbaum, Y., Landesman, Y., Drees, B., Bare, J. W., Saumweber, H., Paddy, M. R., Sedat, J. W., Smith, D. E., Benton, B. M. and Fisher, P. A. (1988). Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene. J. Cell Biol. 106, 585-596.
    • (1988) J. Cell Biol. , vol.106 , pp. 585-596
    • Gruenbaum, Y.1    Landesman, Y.2    Drees, B.3    Bare, J.W.4    Saumweber, H.5    Paddy, M.R.6    Sedat, J.W.7    Smith, D.E.8    Benton, B.M.9    Fisher, P.A.10
  • 28
    • 0034842046 scopus 로고    scopus 로고
    • A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila
    • Guillemin, K., Williams, T. and Krasnow, M. A. (2001). A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila. Nat. Cell Biol. 3, 848-851.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 848-851
    • Guillemin, K.1    Williams, T.2    Krasnow, M.A.3
  • 29
    • 17144363594 scopus 로고    scopus 로고
    • Deimination of historic H2A and H4 at arginine 3 in HL-60 granulocytes
    • Hagiwara, T., Hidaka, Y. and Yamada, M. (2005). Deimination of historic H2A and H4 at arginine 3 in HL-60 granulocytes. Biochemistry 44, 5827-5834.
    • (2005) Biochemistry , vol.44 , pp. 5827-5834
    • Hagiwara, T.1    Hidaka, Y.2    Yamada, M.3
  • 30
    • 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
  • 31
    • 0024355616 scopus 로고
    • Persistence of major nuclear envelope antigens in an envelope-like structure during mitosis in Drosophila melanogaster embryos
    • Harel, A., Zlotkin, E., Nainudel, E. S., Feinstein, N., Fisher, P. A. and Gruenbaum, Y. (1989). Persistence of major nuclear envelope antigens in an envelope-like structure during mitosis in Drosophila melanogaster embryos. J. Cell Sci. 94, 463-470.
    • (1989) J. Cell Sci. , vol.94 , pp. 463-470
    • Harel, A.1    Zlotkin, E.2    Nainudel, E.S.3    Feinstein, N.4    Fisher, P.A.5    Gruenbaum, Y.6
  • 32
    • 33746578389 scopus 로고    scopus 로고
    • Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy
    • Hegele, R. A., Cao, H., Liu, D. M., Costain, G. A., Charlton-Menys, V., Rodger, N. W. and Durrington, P. N. (2006). Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy. Am. J Hum. Genet. 79, 383-389.
    • (2006) Am. J Hum. Genet. , vol.79 , pp. 383-389
    • Hegele, R.A.1    Cao, H.2    Liu, D.M.3    Costain, G.A.4    Charlton-Menys, V.5    Rodger, N.W.6    Durrington, P.N.7
  • 33
    • 0042329786 scopus 로고    scopus 로고
    • Intermediate filaments: Novel assembly models and exciting new functions for nuclear lamins
    • Herrmann, H. and Foisner, R. (2003). Intermediate filaments: novel assembly models and exciting new functions for nuclear lamins. Cell Mol. Life Sci. 60, 1607-1612.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1607-1612
    • Herrmann, H.1    Foisner, R.2
  • 34
    • 0024241247 scopus 로고
    • Amino acid sequence and molecular characterization of murine lamin B as deduced from CDNA clones
    • Hoger, T. H., Krohne, G. and Franke, W. W. (1988). Amino acid sequence and molecular characterization of murine lamin B as deduced from CDNA clones. Eur. J. Cell Biol. 47, 283-290.
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 283-290
    • Hoger, T.H.1    Krohne, G.2    Franke, W.W.3
  • 35
    • 0026343513 scopus 로고
    • Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain
    • Hoger, T. H., Krohne, G. and Kleinschmidt, J. A. (1991). Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain. Esp. Cell Res. 197, 280-289.
    • (1991) Esp. Cell Res. , vol.197 , pp. 280-289
    • Hoger, T.H.1    Krohne, G.2    Kleinschmidt, J.A.3
  • 38
    • 33745125712 scopus 로고    scopus 로고
    • Tumor suppressor menin: The essential role of nuclear localization signal domains in coordinating gene expression
    • La, P., Desmond, A., Hou, Z., Silva, A. C., Schnepp, R. W. and Hua, X. (2006). Tumor suppressor menin: the essential role of nuclear localization signal domains in coordinating gene expression. Oncogene 25, 3537-3546.
    • (2006) Oncogene , vol.25 , pp. 3537-3546
    • La, P.1    Desmond, A.2    Hou, Z.3    Silva, A.C.4    Schnepp, R.W.5    Hua, X.6
  • 39
    • 0029739422 scopus 로고    scopus 로고
    • All four core historic N-termini contain sequences required for the repression of basal transcription in yeast
    • Lenfant, F., Mann, R. K., Thomsen, B., Ling, X. and Grunstein, M. (1996). All four core historic N-termini contain sequences required for the repression of basal transcription in yeast. EMBO J. 15, 3974-3985.
    • (1996) EMBO J. , vol.15 , pp. 3974-3985
    • Lenfant, F.1    Mann, R.K.2    Thomsen, B.3    Ling, X.4    Grunstein, M.5
  • 40
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin dm(0) gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae
    • Lenz-Bohme, B., Wismar, J., Fuchs, S., Reifegerste, R., Buchner, E., Betz, H. and Schmitt, B. (1997). Insertional mutation of the Drosophila nuclear lamin dm(0) gene results in defective nuclear envelopes, 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-Bohme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6    Schmitt, B.7
  • 41
    • 0028168825 scopus 로고
    • Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove
    • Luderus, M. E., den Blaautwen, J., de Smit, O., Compton, D. A. and van Driel, R. (1994). Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove. Mol. Cell. Biol. 14, 6297-6305.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6297-6305
    • Luderus, M.E.1    den Blaautwen, J.2    de Smit, O.3    Compton, D.A.4    van Driel, R.5
  • 42
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Möder, A. W., Richmond, R. K., Sargent, D. F. and Richmond, T. J. (1997). Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Möder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 43
    • 0029969424 scopus 로고    scopus 로고
    • Specific interactions of chromatin with the nuclear envelope: Positional determination within the nucleus in Drosophila melanogaster
    • Marshall, W. F., Dernburg, A. F., Harmon, B., Agard, D. A. and Sedat, J. W. (1996). Specific interactions of chromatin with the nuclear envelope: positional determination within the nucleus in Drosophila melanogaster. Mol. Biol. Cell 7, 825-842.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 825-842
    • Marshall, W.F.1    Dernburg, A.F.2    Harmon, B.3    Agard, D.A.4    Sedat, J.W.5
  • 45
    • 0242383489 scopus 로고    scopus 로고
    • Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery
    • Mattout-Drubezki, A. and Gruenbaum, Y. (2003). Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery. Cell Mol. Life Sci. 60, 2053-2063.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 2053-2063
    • Mattout-Drubezki, A.1    Gruenbaum, Y.2
  • 46
    • 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. (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319, 463-468.
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 48
    • 6044256118 scopus 로고    scopus 로고
    • Histories and historic modifications
    • Peterson, C. and Laniel, M. (2004). Histories and historic modifications. Curr Biol. 14, 546-551.
    • (2004) Curr Biol. , vol.14 , pp. 546-551
    • Peterson, C.1    Laniel, M.2
  • 51
    • 0029939581 scopus 로고    scopus 로고
    • Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae
    • Recht, J., Dunn, B., Raff, A. and Osley, M. A. (1996). Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae. Mol. Biol. Cell 16, 2545-2553.
    • (1996) Mol. Biol. Cell , vol.16 , pp. 2545-2553
    • Recht, J.1    Dunn, B.2    Raff, A.3    Osley, M.A.4
  • 52
    • 0027729310 scopus 로고
    • A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; CDNA cloning and gene organization
    • Riemer, D., Dodemont, H. and Weber, K. (1993). A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; CDNA cloning and gene organization. Eur J. Cell Biol. 62, 214-223.
    • (1993) Eur J. Cell Biol. , vol.62 , pp. 214-223
    • Riemer, D.1    Dodemont, H.2    Weber, K.3
  • 53
    • 0031965429 scopus 로고    scopus 로고
    • In vivo association of lamins with nucleic acids in Drosophila melanogaster
    • Rzepecki, R., Bogachev, S. S., Kokoza, E., Stuurman, N. and Fisher, P. A. (1998). In vivo association of lamins with nucleic acids in Drosophila melanogaster. J Cell Sci. 111, 121-129.
    • (1998) J Cell Sci. , vol.111 , pp. 121-129
    • Rzepecki, R.1    Bogachev, S.S.2    Kokoza, E.3    Stuurman, N.4    Fisher, P.A.5
  • 54
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and Von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 55
    • 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., Jeno, P., Fisher, P. A. and Stuurman, N. (1999). 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, 4620-4632.
    • (1999) Biochemistry , vol.38 , pp. 4620-4632
    • Schneider, U.1    Mini, T.2    Jeno, P.3    Fisher, P.A.4    Stuurman, N.5
  • 56
    • 0025302814 scopus 로고
    • The in vitro DNA-binding properties of purified nuclear lamin proteins and vimentin
    • Shoeman, R. L. and Traub, P. (1990). The in vitro DNA-binding properties of purified nuclear lamin proteins and vimentin. J. Biol. Chem. 265, 9055-9061.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9055-9061
    • Shoeman, R.L.1    Traub, P.2
  • 58
    • 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
  • 60
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura, H., Glass, C. and Gerace, L. (1995). A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J Cell Biol. 131, 33-44.
    • (1995) J Cell Biol. , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 61
    • 33645528413 scopus 로고    scopus 로고
    • A tripartite DNA-binding element, comprised of the nuclear localization signal and two AT-hook motifs, mediates the association of LEDGF/p75 with chromatin in vivo
    • Turlure, F., Maertens, G., Rahman, S., Cherepanov, P. and Engelman, A. (2006). A tripartite DNA-binding element, comprised of the nuclear localization signal and two AT-hook motifs, mediates the association of LEDGF/p75 with chromatin in vivo. Nucleic Acids Res. 34, 1653-1675.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1653-1675
    • Turlure, F.1    Maertens, G.2    Rahman, S.3    Cherepanov, P.4    Engelman, A.5
  • 62
    • 18744413894 scopus 로고    scopus 로고
    • Fate of the nuclear lamina during Caenorhabditis elegans apoptosis
    • Tzur, Y. B., Hersh, B. M., Horvitz, H. R. and Gruenbaum, Y. (2002). Fate of the nuclear lamina during Caenorhabditis elegans apoptosis. J. Struct. Biol. 137, 146-153.
    • (2002) J. Struct. Biol. , vol.137 , pp. 146-153
    • Tzur, Y.B.1    Hersh, B.M.2    Horvitz, H.R.3    Gruenbaum, Y.4
  • 63
    • 1442345760 scopus 로고    scopus 로고
    • The lamin B receptor of Drosophila melanogaster
    • Wagner, N., Weber, D., Seitz, S. and Krohne, G. (2004). The lamin B receptor of Drosophila melanogaster. J. Cell Sci. 117, 2015-2028.
    • (2004) J. Cell Sci. , vol.117 , pp. 2015-2028
    • Wagner, N.1    Weber, D.2    Seitz, S.3    Krohne, G.4
  • 65
    • 25144515509 scopus 로고    scopus 로고
    • Nuclear envelope, nuclear lamina, and inherited disease
    • Worman, H. J. and Courvalin, J. C. (2005). Nuclear envelope, nuclear lamina, and inherited disease. Int. Rev. Cytol. 246, 231-279.
    • (2005) Int. Rev. Cytol. , vol.246 , pp. 231-279
    • Worman, H.J.1    Courvalin, J.C.2
  • 66
    • 0038531105 scopus 로고    scopus 로고
    • Multiple roles for Saccharomyces cerevisiae historic H2A in telomere position effect, Spt phenotypes and double-strand-break repair
    • Wyatt, H. R., Liaw, H., Green, G. R. and Lustig, A. J. (2003). Multiple roles for Saccharomyces cerevisiae historic H2A in telomere position effect, Spt phenotypes and double-strand-break repair. Genetics 164, 47-64.
    • (2003) Genetics , vol.164 , pp. 47-64
    • Wyatt, H.R.1    Liaw, H.2    Green, G.R.3    Lustig, A.J.4
  • 68
    • 0141483484 scopus 로고    scopus 로고
    • Identification of novel historic post-translational modifications by peptide mass fingerprinting
    • Zhang, L., Eugeni, E., Parthun, M. and Freitas, M. (2003). Identification of novel historic post-translational modifications by peptide mass fingerprinting. Chromosoma 112, 77-86.
    • (2003) Chromosoma , vol.112 , pp. 77-86
    • Zhang, L.1    Eugeni, E.2    Parthun, M.3    Freitas, M.4
  • 69
    • 0027306750 scopus 로고
    • SAR-dependent mobilization of historic H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin
    • Zhao, K., Kas, E., Gonzalez, E. and Laemmli, U. K. (1993). SAR-dependent mobilization of historic H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin. EMBO J. 12, 3237-3247.
    • (1993) EMBO J. , vol.12 , pp. 3237-3247
    • Zhao, K.1    Kas, E.2    Gonzalez, E.3    Laemmli, U.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.