메뉴 건너뛰기




Volumn 16, Issue 1, 2009, Pages

The nuclear envelopathies and human diseases

Author keywords

[No Author keywords available]

Indexed keywords

EMERIN; LAMIN A; LAMIN B; LAMIN C; NUCLEOPORIN; PROTEIN MAD1; PROTEIN MAD2; LAMIN B1;

EID: 70449348833     PISSN: 10217770     EISSN: 14230127     Source Type: Journal    
DOI: 10.1186/1423-0127-16-96     Document Type: Review
Times cited : (47)

References (76)
  • 1
    • 60749108426 scopus 로고    scopus 로고
    • Orchestrating nuclear envelope disassembly and reassembly during mitosis
    • 10.1038/nrm2641. 19234477
    • Orchestrating nuclear envelope disassembly and reassembly during mitosis. S Guttinger E Laurell U Kutay, Nat Rev Mol Cell Biol 2009 10 178 191 10.1038/nrm2641 19234477
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 178-191
    • Guttinger, S.1    Laurell, E.2    Kutay, U.3
  • 2
    • 67650147960 scopus 로고    scopus 로고
    • The role of nuclear pores in gene regulation, development and disease
    • 10.1038/embor.2009.147. 19543230
    • The role of nuclear pores in gene regulation, development and disease. M Capelson MW Hetzer, EMBO Rep 2009 10 697 705 10.1038/embor.2009.147 19543230
    • (2009) EMBO Rep , vol.10 , pp. 697-705
    • Capelson, M.1    Hetzer, M.W.2
  • 3
    • 10944252995 scopus 로고    scopus 로고
    • The Function of Nuclear Architecture: A Genetic Approach
    • 10.1146/annurev.genet.37.110801.142705. 15568979
    • The Function of Nuclear Architecture: A Genetic Approach. A Taddei F Hediger FR Neumann SM Gasser, Annu Rev Genet 2004 38 305 345 10.1146/annurev.genet.37.110801.142705 15568979
    • (2004) Annu Rev Genet , vol.38 , pp. 305-345
    • Taddei, A.1    Hediger, F.2    Neumann, F.R.3    Gasser, S.M.4
  • 4
    • 4744370566 scopus 로고    scopus 로고
    • Visualization of a highly organized intranuclear network of filaments in living mammalian cells
    • 10.1002/cm.20023. 15362113
    • Visualization of a highly organized intranuclear network of filaments in living mammalian cells. G Nalepa JW Harper, Cell Motil Cytoskeleton 2004 59 94 108 10.1002/cm.20023 15362113
    • (2004) Cell Motil Cytoskeleton , vol.59 , pp. 94-108
    • Nalepa, G.1    Harper, J.W.2
  • 5
    • 68849119046 scopus 로고    scopus 로고
    • Laminopathies and the long strange trip from basic cell biology to therapy
    • 10.1172/JCI37679. 19587457
    • Laminopathies and the long strange trip from basic cell biology to therapy. HJ Worman LG Fong A Muchir SG Young, J Clin Invest 2009 119 1825 1836 10.1172/JCI37679 19587457
    • (2009) J Clin Invest , vol.119 , pp. 1825-1836
    • Worman, H.J.1    Fong, L.G.2    Muchir, A.3    Young, S.G.4
  • 6
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • 10.1126/science.1088176. 12958361
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics. EC Schirmer L Florens T Guan JR Yates III L Gerace, Science 2003 301 1380 1382 10.1126/science.1088176 12958361
    • (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
  • 7
    • 33845286555 scopus 로고    scopus 로고
    • Human laminopathies: Nuclei gone genetically awry
    • 10.1038/nrg1906. 17139325
    • Human laminopathies: nuclei gone genetically awry. BC Capell FS Collins, Nat Rev Genet 2006 7 940 952 10.1038/nrg1906 17139325
    • (2006) Nat Rev Genet , vol.7 , pp. 940-952
    • Capell, B.C.1    Collins, F.S.2
  • 8
    • 85047692354 scopus 로고    scopus 로고
    • How do mutations in lamins A and C cause disease?
    • 14755330
    • How do mutations in lamins A and C cause disease? HJ Worman JC Courvalin, J Clin Invest 2004 113 349 351 14755330
    • (2004) J Clin Invest , vol.113 , pp. 349-351
    • Worman, H.J.1    Courvalin, J.C.2
  • 10
    • 33845488100 scopus 로고    scopus 로고
    • Emery-Dreifuss muscular dystrophy at the nuclear envelope: 10 years on
    • 10.1007/s00018-006-6247-8. 17013557
    • Emery-Dreifuss muscular dystrophy at the nuclear envelope: 10 years on. JA Ellis, Cell Mol Life Sci 2006 63 2702 2709 10.1007/s00018-006-6247-8 17013557
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2702-2709
    • Ellis, J.A.1
  • 11
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • 10.1093/hmg/5.6.801. 8776595
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. S Manilal TM Nguyen CA Sewry GE Morris, Hum Mol Genet 1996 5 801 808 10.1093/hmg/5.6.801 8776595
    • (1996) Hum Mol Genet , vol.5 , pp. 801-808
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 12
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)
    • 12118250
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). K Hoffmann CK Dreger AL Olins DE Olins LD Shultz B Lucke H Karl R Kaps D Muller A Vaya, et al. Nat Genet 2002 31 410 414 12118250
    • (2002) Nat Genet , vol.31 , pp. 410-414
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3    Olins, D.E.4    Shultz, L.D.5    Lucke, B.6    Karl, H.7    Kaps, R.8    Muller, D.9    Vaya, A.10
  • 13
    • 33748608275 scopus 로고    scopus 로고
    • The nuclear lamina and its proposed roles in tumorigenesis: Projection on the hematologic malignancies and future targeted therapy
    • 10.1016/j.jsb.2006.02.016. 16697219
    • The nuclear lamina and its proposed roles in tumorigenesis: projection on the hematologic malignancies and future targeted therapy. M Prokocimer A Margalit Y Gruenbaum, J Struct Biol 2006 155 351 360 10.1016/j.jsb.2006.02.016 16697219
    • (2006) J Struct Biol , vol.155 , pp. 351-360
    • Prokocimer, M.1    Margalit, A.2    Gruenbaum, Y.3
  • 14
    • 0033786789 scopus 로고    scopus 로고
    • Nuclear envelope proteins and associated diseases
    • 10.1097/00019052-200010000-00005. 11073359
    • Nuclear envelope proteins and associated diseases. A Nagano K Arahata, Curr Opin Neurol 2000 13 533 539 10.1097/00019052-200010000-00005 11073359
    • (2000) Curr Opin Neurol , vol.13 , pp. 533-539
    • Nagano, A.1    Arahata, K.2
  • 15
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • 10.1083/jcb.147.5.913. 10579712
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. T Sullivan D Escalante-Alcalde H Bhatt M Anver N Bhat K Nagashima CL Stewart B Burke, J Cell Biol 1999 147 913 920 10.1083/jcb.147.5.913 10579712
    • (1999) J Cell Biol , vol.147 , pp. 913-920
    • Sullivan, T.1    Escalante-Alcalde, D.2    Bhatt, H.3    Anver, M.4    Bhat, N.5    Nagashima, K.6    Stewart, C.L.7    Burke, B.8
  • 17
    • 0037673940 scopus 로고    scopus 로고
    • A progeroid syndrome in mice is caused by defects in A-type lamins
    • 10.1038/nature01631. 12748643
    • A progeroid syndrome in mice is caused by defects in A-type lamins. LC Mounkes S Kozlov L Hernandez T Sullivan CL Stewart, Nature 2003 423 298 301 10.1038/nature01631 12748643
    • (2003) Nature , vol.423 , pp. 298-301
    • Mounkes, L.C.1    Kozlov, S.2    Hernandez, L.3    Sullivan, T.4    Stewart, C.L.5
  • 18
    • 3142696838 scopus 로고    scopus 로고
    • Lamin B1 is required for mouse development and nuclear integrity
    • 10.1073/pnas.0401424101. 15232008
    • Lamin B1 is required for mouse development and nuclear integrity. L Vergnes M Peterfy MO Bergo SG Young K Reue, Proc Natl Acad Sci USA 2004 101 10428 10433 10.1073/pnas.0401424101 15232008
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10428-10433
    • Vergnes, L.1    Peterfy, M.2    Bergo, M.O.3    Young, S.G.4    Reue, K.5
  • 19
    • 34247485356 scopus 로고    scopus 로고
    • A-type lamin networks in light of laminopathic diseases
    • 10.1016/j.bbamcr.2006.07.002. 16934891
    • A-type lamin networks in light of laminopathic diseases. S Vlcek R Foisner, Biochim Biophys Acta 2007 1773 661 674 10.1016/j.bbamcr.2006.07.002 16934891
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 661-674
    • Vlcek, S.1    Foisner, R.2
  • 20
    • 34848870304 scopus 로고    scopus 로고
    • Histone acetyltransferase hALP and nuclear membrane protein hsSUN1 function in de-condensation of mitotic chromosomes
    • 10.1074/jbc.M703098200. 17631499
    • Histone acetyltransferase hALP and nuclear membrane protein hsSUN1 function in de-condensation of mitotic chromosomes. YH Chi K Haller JM Peloponese Jr KT Jeang, J Biol Chem 2007 282 27447 27458 10.1074/jbc.M703098200 17631499
    • (2007) J Biol Chem , vol.282 , pp. 27447-27458
    • Chi, Y.H.1    Haller, K.2    Peloponese Jr., J.M.3    Jeang, K.T.4
  • 23
    • 33645962805 scopus 로고    scopus 로고
    • Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet arrangement of chromosomes
    • 10.1016/j.cell.2006.01.048. 16615890
    • Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet arrangement of chromosomes. Y Chikashige C Tsutsumi M Yamane K Okamasa T Haraguchi Y Hiraoka, Cell 2006 125 59 69 10.1016/j.cell.2006.01.048 16615890
    • (2006) Cell , vol.125 , pp. 59-69
    • Chikashige, Y.1    Tsutsumi, C.2    Yamane, M.3    Okamasa, K.4    Haraguchi, T.5    Hiraoka, Y.6
  • 24
    • 65249165924 scopus 로고    scopus 로고
    • Yeast telomerase and the SUN domain protein Mps3 anchor telomeres and repress subtelomeric recombination
    • 10.1101/gad.1787509. 19390087
    • Yeast telomerase and the SUN domain protein Mps3 anchor telomeres and repress subtelomeric recombination. H Schober H Ferreira V Kalck LR Gehlen SM Gasser, Genes Dev 2009 23 928 938 10.1101/gad.1787509 19390087
    • (2009) Genes Dev , vol.23 , pp. 928-938
    • Schober, H.1    Ferreira, H.2    Kalck, V.3    Gehlen, L.R.4    Gasser, S.M.5
  • 25
    • 65249150132 scopus 로고    scopus 로고
    • Mechanisms that regulate localization of a DNA double-strand break to the nuclear periphery
    • 10.1101/gad.1782209. 19390086
    • Mechanisms that regulate localization of a DNA double-strand break to the nuclear periphery. P Oza SL Jaspersen A Miele J Dekker CL Peterson, Genes Dev 2009 23 912 927 10.1101/gad.1782209 19390086
    • (2009) Genes Dev , vol.23 , pp. 912-927
    • Oza, P.1    Jaspersen, S.L.2    Miele, A.3    Dekker, J.4    Peterson, C.L.5
  • 26
    • 0036193442 scopus 로고    scopus 로고
    • Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans
    • 10.1091/mbc.01-06-0294. 11907270
    • Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans. KK Lee D Starr M Cohen J Liu M Han KL Wilson Y Gruenbaum, Mol Biol Cell 2002 13 892 901 10.1091/mbc.01-06-0294 11907270
    • (2002) Mol Biol Cell , vol.13 , pp. 892-901
    • Lee, K.K.1    Starr, D.2    Cohen, M.3    Liu, J.4    Han, M.5    Wilson, K.L.6    Gruenbaum, Y.7
  • 27
    • 34249313304 scopus 로고    scopus 로고
    • SUN1 is required for telomere attachment to nuclear envelope and gametogenesis in mice
    • 10.1016/j.devcel.2007.03.018. 17543860
    • SUN1 is required for telomere attachment to nuclear envelope and gametogenesis in mice. X Ding R Xu J Yu T Xu Y Zhuang M Han, Dev Cell 2007 12 863 872 10.1016/j.devcel.2007.03.018 17543860
    • (2007) Dev Cell , vol.12 , pp. 863-872
    • Ding, X.1    Xu, R.2    Yu, J.3    Xu, T.4    Zhuang, Y.5    Han, M.6
  • 29
    • 67649844282 scopus 로고    scopus 로고
    • SUN1 and SUN2 play critical but partially redundant roles in anchoring nuclei in skeletal muscle cells in mice
    • 10.1073/pnas.0812037106. 19509342
    • SUN1 and SUN2 play critical but partially redundant roles in anchoring nuclei in skeletal muscle cells in mice. K Lei X Zhang X Ding X Guo M Chen B Zhu T Xu Y Zhuang R Xu M Han, Proc Natl Acad Sci USA 2009 106 10207 10212 10.1073/pnas.0812037106 19509342
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10207-10212
    • Lei, K.1    Zhang, X.2    Ding, X.3    Guo, X.4    Chen, M.5    Zhu, B.6    Xu, T.7    Zhuang, Y.8    Xu, R.9    Han, M.10
  • 31
    • 55549086812 scopus 로고    scopus 로고
    • Loss of nucleoplasmic LAP2alpha-lamin A complexes causes erythroid and epidermal progenitor hyperproliferation
    • 10.1038/ncb1793. 18849980
    • Loss of nucleoplasmic LAP2alpha-lamin A complexes causes erythroid and epidermal progenitor hyperproliferation. N Naetar B Korbei S Kozlov MA Kerenyi D Dorner R Kral I Gotic P Fuchs TV Cohen R Bittner, et al. Nat Cell Biol 2008 10 1341 1348 10.1038/ncb1793 18849980
    • (2008) Nat Cell Biol , vol.10 , pp. 1341-1348
    • Naetar, N.1    Korbei, B.2    Kozlov, S.3    Kerenyi, M.A.4    Dorner, D.5    Kral, R.6    Gotic, I.7    Fuchs, P.8    Cohen, T.V.9    Bittner, R.10
  • 33
    • 67650147960 scopus 로고    scopus 로고
    • The role of nuclear pores in gene regulation, development and disease
    • 10.1038/embor.2009.147. 19543230
    • The role of nuclear pores in gene regulation, development and disease. M Capelson MW Hetzer, EMBO Rep 2009 10 697 705 10.1038/embor.2009.147 19543230
    • (2009) EMBO Rep , vol.10 , pp. 697-705
    • Capelson, M.1    Hetzer, M.W.2
  • 34
    • 17444411537 scopus 로고    scopus 로고
    • A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly
    • 10.1016/j.cell.2005.02.016. 15851029
    • A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly. MD Blower M Nachury R Heald K Weis, Cell 2005 121 223 234 10.1016/j.cell.2005.02.016 15851029
    • (2005) Cell , vol.121 , pp. 223-234
    • Blower, M.D.1    Nachury, M.2    Heald, R.3    Weis, K.4
  • 35
    • 30744477013 scopus 로고    scopus 로고
    • The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation
    • 10.1038/nature04221. 16355229
    • The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation. KB Jeganathan L Malureanu JM van Deursen, Nature 2005 438 1036 1039 10.1038/nature04221 16355229
    • (2005) Nature , vol.438 , pp. 1036-1039
    • Jeganathan, K.B.1    Malureanu, L.2    Van Deursen, J.M.3
  • 37
    • 0028842802 scopus 로고
    • Mad1p, a phosphoprotein component of the spindle assembly checkpoint in budding yeast
    • 10.1083/jcb.131.3.709. 7593191
    • Mad1p, a phosphoprotein component of the spindle assembly checkpoint in budding yeast. KG Hardwick AW Murray, J Cell Biol 1995 131 709 720 10.1083/jcb.131.3.709 7593191
    • (1995) J Cell Biol , vol.131 , pp. 709-720
    • Hardwick, K.G.1    Murray, A.W.2
  • 38
    • 24344459013 scopus 로고    scopus 로고
    • Interactions between Mad1p and the nuclear transport machinery in the yeast Saccharomyces cerevisiae
    • 10.1091/mbc.E05-01-0011. 16000377
    • Interactions between Mad1p and the nuclear transport machinery in the yeast Saccharomyces cerevisiae. RJ Scott CP Lusk DJ Dilworth JD Aitchison RW Wozniak, Mol Biol Cell 2005 16 4362 4374 10.1091/mbc.E05-01-0011 16000377
    • (2005) Mol Biol Cell , vol.16 , pp. 4362-4374
    • Scott, R.J.1    Lusk, C.P.2    Dilworth, D.J.3    Aitchison, J.D.4    Wozniak, R.W.5
  • 39
    • 58149093244 scopus 로고    scopus 로고
    • Requirements for protein phosphorylation and the kinase activity of polo-like kinase 1 (Plk1) for the kinetochore function of mitotic arrest deficiency protein 1 (Mad1)
    • 10.1074/jbc.M804967200. 18922800
    • Requirements for protein phosphorylation and the kinase activity of polo-like kinase 1 (Plk1) for the kinetochore function of mitotic arrest deficiency protein 1 (Mad1). YH Chi K Haller MD Ward OJ Semmes Y Li KT Jeang, J Biol Chem 2008 283 35834 35844 10.1074/jbc.M804967200 18922800
    • (2008) J Biol Chem , vol.283 , pp. 35834-35844
    • Chi, Y.H.1    Haller, K.2    Ward, M.D.3    Semmes, O.J.4    Li, Y.5    Jeang, K.T.6
  • 40
    • 0037049550 scopus 로고    scopus 로고
    • The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint
    • 10.1083/jcb.200205068. 12473689
    • The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. T Iouk O Kerscher RJ Scott MA Basrai RW Wozniak, J Cell Biol 2002 159 807 819 10.1083/jcb.200205068 12473689
    • (2002) J Cell Biol , vol.159 , pp. 807-819
    • Iouk, T.1    Kerscher, O.2    Scott, R.J.3    Basrai, M.A.4    Wozniak, R.W.5
  • 43
    • 60549094835 scopus 로고    scopus 로고
    • Spindle assembly checkpoint and p53 deficiencies cooperate for tumorigenesis in mice
    • 10.1002/ijc.24094. 19065665
    • Spindle assembly checkpoint and p53 deficiencies cooperate for tumorigenesis in mice. YH Chi JM Ward LI Cheng J Yasunaga KT Jeang, Int J Cancer 2009 124 1483 1489 10.1002/ijc.24094 19065665
    • (2009) Int J Cancer , vol.124 , pp. 1483-1489
    • Chi, Y.H.1    Ward, J.M.2    Cheng, L.I.3    Yasunaga, J.4    Jeang, K.T.5
  • 44
    • 35048828950 scopus 로고    scopus 로고
    • Aneuploidy and cancer
    • 10.1002/jcb.21484. 17661351
    • Aneuploidy and cancer. YH Chi KT Jeang, J Cell Biochem 2007 102 531 538 10.1002/jcb.21484 17661351
    • (2007) J Cell Biochem , vol.102 , pp. 531-538
    • Chi, Y.H.1    Jeang, K.T.2
  • 46
    • 33646526019 scopus 로고    scopus 로고
    • Chromosome territories - A functional nuclear landscape
    • 10.1016/j.ceb.2006.04.007. 16687245
    • Chromosome territories - a functional nuclear landscape. T Cremer M Cremer S Dietzel S Muller I Solovei S Fakan, Curr Opin Cell Biol 2006 18 307 316 10.1016/j.ceb.2006.04.007 16687245
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 307-316
    • Cremer, T.1    Cremer, M.2    Dietzel, S.3    Muller, S.4    Solovei, I.5    Fakan, S.6
  • 47
    • 34249307315 scopus 로고    scopus 로고
    • Nuclear organization of the genome and the potential for gene regulation
    • 10.1038/nature05916. 17522674
    • Nuclear organization of the genome and the potential for gene regulation. P Fraser W Bickmore, Nature 2007 447 413 417 10.1038/nature05916 17522674
    • (2007) Nature , vol.447 , pp. 413-417
    • Fraser, P.1    Bickmore, W.2
  • 48
    • 0042767995 scopus 로고    scopus 로고
    • The dynamics of chromosome organization and gene regulation
    • 10.1146/annurev.biochem.72.121801.161724. 14527325
    • The dynamics of chromosome organization and gene regulation. DL Spector, Annu Rev Biochem 2003 72 573 608 10.1146/annurev.biochem.72.121801.161724 14527325
    • (2003) Annu Rev Biochem , vol.72 , pp. 573-608
    • Spector, D.L.1
  • 50
    • 33744977019 scopus 로고    scopus 로고
    • Nuclear pore association confers optimal expression levels for an inducible yeast gene
    • 10.1038/nature04845. 16760983
    • Nuclear pore association confers optimal expression levels for an inducible yeast gene. A Taddei HG Van F Hediger V Kalck F Cubizolles H Schober SM Gasser, Nature 2006 441 774 778 10.1038/nature04845 16760983
    • (2006) Nature , vol.441 , pp. 774-778
    • Taddei, A.1    Van, H.G.2    Hediger, F.3    Kalck, V.4    Cubizolles, F.5    Schober, H.6    Gasser, S.M.7
  • 51
    • 31544471808 scopus 로고    scopus 로고
    • Nup-PI: The nucleopore-promoter interaction of genes in yeast
    • 10.1016/j.molcel.2005.12.012. 16455493
    • Nup-PI: the nucleopore-promoter interaction of genes in yeast. M Schmid G Arib C Laemmli J Nishikawa T Durussel UK Laemmli, Mol Cell 2006 21 379 391 10.1016/j.molcel.2005.12.012 16455493
    • (2006) Mol Cell , vol.21 , pp. 379-391
    • Schmid, M.1    Arib, G.2    Laemmli, C.3    Nishikawa, J.4    Durussel, T.5    Laemmli, U.K.6
  • 52
    • 33748289518 scopus 로고    scopus 로고
    • Characterization of the Drosophila melanogaster genome at the nuclear lamina
    • DOI 10.1038/ng1852, PII NG1852
    • Characterization of the Drosophila melanogaster genome at the nuclear lamina. H Pickersgill B Kalverda WE de W Talhout M Fornerod SB van, Nat Genet 2006 38 1005 1014 10.1038/ng1852 16878134 (Pubitemid 44325925)
    • (2006) Nature Genetics , vol.38 , Issue.9 , pp. 1005-1014
    • Pickersgill, H.1    Kalverda, B.2    De Wit, E.3    Talhout, W.4    Fornerod, M.5    Van Steensel, B.6
  • 53
    • 40749122641 scopus 로고    scopus 로고
    • Transcriptional repression mediated by repositioning of genes to the nuclear lamina
    • 10.1038/nature06727. 18272965
    • Transcriptional repression mediated by repositioning of genes to the nuclear lamina. KL Reddy JM Zullo E Bertolino H Singh, Nature 2008 452 243 247 10.1038/nature06727 18272965
    • (2008) Nature , vol.452 , pp. 243-247
    • Reddy, K.L.1    Zullo, J.M.2    Bertolino, E.3    Singh, H.4
  • 54
    • 26444589253 scopus 로고    scopus 로고
    • The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
    • 10.1242/jcs.02521. 16129885
    • The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. R Somech S Shaklai O Geller N Amariglio AJ Simon G Rechavi EN Gal-Yam, J Cell Sci 2005 118 4017 4025 10.1242/jcs.02521 16129885
    • (2005) J Cell Sci , vol.118 , pp. 4017-4025
    • Somech, R.1    Shaklai, S.2    Geller, O.3    Amariglio, N.4    Simon, A.J.5    Rechavi, G.6    Gal-Yam, E.N.7
  • 56
    • 54949154104 scopus 로고    scopus 로고
    • Model of human aging: Recent findings on Werner's and Hutchinson-Gilford progeria syndromes
    • 18982914
    • Model of human aging: recent findings on Werner's and Hutchinson-Gilford progeria syndromes. SL Ding CY Shen, Clin Interv Aging 2008 3 431 444 18982914
    • (2008) Clin Interv Aging , vol.3 , pp. 431-444
    • Ding, S.L.1    Shen, C.Y.2
  • 57
    • 0037470542 scopus 로고    scopus 로고
    • Aging and genome maintenance: Lessons from the mouse?
    • 10.1126/science.1079161. 12610296
    • Aging and genome maintenance: lessons from the mouse? P Hasty J Campisi J Hoeijmakers SH van J Vijg, Science 2003 299 1355 1359 10.1126/science.1079161 12610296
    • (2003) Science , vol.299 , pp. 1355-1359
    • Hasty, P.1    Campisi, J.2    Hoeijmakers, J.3    Van, S.H.4    Vijg, J.5
  • 60
    • 59449095581 scopus 로고    scopus 로고
    • Suppression of proliferative defects associated with processing-defective lamin A mutants by hTERT or inactivation of p53
    • 10.1091/mbc.E08-05-0492. 18843043
    • Suppression of proliferative defects associated with processing-defective lamin A mutants by hTERT or inactivation of p53. BA Kudlow MN Stanfel CR Burtner ED Johnston BK Kennedy, Mol Biol Cell 2008 19 5238 5248 10.1091/mbc.E08-05-0492 18843043
    • (2008) Mol Biol Cell , vol.19 , pp. 5238-5248
    • Kudlow, B.A.1    Stanfel, M.N.2    Burtner, C.R.3    Johnston, E.D.4    Kennedy, B.K.5
  • 61
    • 12344305602 scopus 로고    scopus 로고
    • LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly
    • 10.1242/jcs.01529. 15546916
    • LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly. T Dechat A Gajewski B Korbei D Gerlich N Daigle T Haraguchi K Furukawa J Ellenberg R Foisner, J Cell Sci 2004 117 6117 6128 10.1242/jcs.01529 15546916
    • (2004) J Cell Sci , vol.117 , pp. 6117-6128
    • Dechat, T.1    Gajewski, A.2    Korbei, B.3    Gerlich, D.4    Daigle, N.5    Haraguchi, T.6    Furukawa, K.7    Ellenberg, J.8    Foisner, R.9
  • 62
    • 67749124115 scopus 로고    scopus 로고
    • Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo
    • 10.1083/jcb.200901106. 19620630
    • Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. DJ Anderson JD Vargas JP Hsiao MW Hetzer, J Cell Biol 2009 186 183 191 10.1083/jcb.200901106 19620630
    • (2009) J Cell Biol , vol.186 , pp. 183-191
    • Anderson, D.J.1    Vargas, J.D.2    Hsiao, J.P.3    Hetzer, M.W.4
  • 67
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • 10.1093/hmg/9.9.1453. 10814726
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). A Muchir G Bonne AJ van der Kooi MM van F Baas PA Bolhuis VM de K Schwartz, Hum Mol Genet 2000 9 1453 1459 10.1093/hmg/9.9.1453 10814726
    • (2000) Hum Mol Genet , vol.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    Van Der Kooi, A.J.3    Van, M.M.4    Baas, F.5    Bolhuis, P.A.6    De, V.M.7    Schwartz, K.8
  • 68
    • 0033518282 scopus 로고    scopus 로고
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease
    • 10.1056/NEJM199912023412302. 10580070
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. D Fatkin C MacRae T Sasaki MR Wolff M Porcu M Frenneaux J Atherton HJ Vidaillet Jr S Spudich GU De, et al. N Engl J Med 1999 341 1715 1724 10.1056/NEJM199912023412302 10580070
    • (1999) N Engl J Med , vol.341 , pp. 1715-1724
    • Fatkin, D.1    MacRae, C.2    Sasaki, T.3    Wolff, M.R.4    Porcu, M.5    Frenneaux, M.6    Atherton, J.7    Vidaillet Jr., H.J.8    Spudich, S.9    De, G.U.10
  • 69
    • 0036178210 scopus 로고    scopus 로고
    • Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse
    • 10.1086/339274. 11799477
    • Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. A De Sandre-Giovannoli M Chaouch S Kozlov JM Vallat M Tazir N Kassouri P Szepetowski T Hammadouche A Vandenberghe CL Stewart, et al. Am J Hum Genet 2002 70 726 736 10.1086/339274 11799477
    • (2002) Am J Hum Genet , vol.70 , pp. 726-736
    • De Sandre-Giovannoli, A.1    Chaouch, M.2    Kozlov, S.3    Vallat, J.M.4    Tazir, M.5    Kassouri, N.6    Szepetowski, P.7    Hammadouche, T.8    Vandenberghe, A.9    Stewart, C.L.10
  • 70
    • 0034059075 scopus 로고    scopus 로고
    • Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy
    • Nuclear lamin A/C R482Q mutation in canadian kindreds with Dunnigan-type familial partial lipodystrophy. H Cao RA Hegele, Hum Mol Genet 2000 9 109 112 10.1093/hmg/9.1.109 10587585 (Pubitemid 30145295)
    • (2000) Human Molecular Genetics , vol.9 , Issue.1 , pp. 109-112
    • Cao, H.1    Hegele, R.A.2
  • 71
    • 0033912260 scopus 로고    scopus 로고
    • Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C
    • 10.1086/302836. 10739751
    • Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C. RA Speckman A Garg F Du L Bennett R Veile E Arioglu SI Taylor M Lovett AM Bowcock, Am J Hum Genet 2000 66 1192 1198 10.1086/302836 10739751
    • (2000) Am J Hum Genet , vol.66 , pp. 1192-1198
    • Speckman, R.A.1    Garg, A.2    Du, F.3    Bennett, L.4    Veile, R.5    Arioglu, E.6    Taylor, S.I.7    Lovett, M.8    Bowcock, A.M.9
  • 74
    • 0037342243 scopus 로고    scopus 로고
    • A new clinical condition linked to a novel mutation in lamins A and C with generalized lipoatrophy, insulin-resistant diabetes, disseminated leukomelanodermic papules, liver steatosis, and cardiomyopathy
    • 10.1210/jc.2002-021506. 12629077
    • A new clinical condition linked to a novel mutation in lamins A and C with generalized lipoatrophy, insulin-resistant diabetes, disseminated leukomelanodermic papules, liver steatosis, and cardiomyopathy. F Caux E Dubosclard O Lascols B Buendia O Chazouilleres A Cohen JC Courvalin L Laroche J Capeau C Vigouroux, et al. J Clin Endocrinol Metab 2003 88 1006 1013 10.1210/jc.2002-021506 12629077
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 1006-1013
    • Caux, F.1    Dubosclard, E.2    Lascols, O.3    Buendia, B.4    Chazouilleres, O.5    Cohen, A.6    Courvalin, J.C.7    Laroche, L.8    Capeau, J.9    Vigouroux, C.10
  • 75
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • 10.1038/ng1294-323. 7894480
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. S Bione E Maestrini S Rivella M Mancini S Regis G Romeo D Toniolo, Nat Genet 1994 8 323 327 10.1038/ng1294-323 7894480
    • (1994) Nat Genet , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 76
    • 0037081564 scopus 로고    scopus 로고
    • The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype
    • 11839786
    • The cell cycle dependent mislocalisation of emerin may contribute to the Emery-Dreifuss muscular dystrophy phenotype. EA Fairley A Riddell JA Ellis J Kendrick-Jones, J Cell Sci 2002 115 341 354 11839786
    • (2002) J Cell Sci , vol.115 , pp. 341-354
    • Fairley, E.A.1    Riddell, A.2    Ellis, J.A.3    Kendrick-Jones, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.