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Volumn 4, Issue 2, 2013, Pages 105-114

Regulation and coordination of nuclear envelope and nuclear pore complex assembly

Author keywords

Inner nuclear membrane; Lamin; Nuclear envelope; Nuclear pore complex; Nuclear reassembly; Nucleoporin; Open mitosis

Indexed keywords

BARRIER TO AUTOINTEGRATION FACTOR; CYCLIN DEPENDENT KINASE 1; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE; KARYOPHERIN BETA; LAMIN A; LAMIN B; NUCLEOPORIN;

EID: 84875880373     PISSN: 19491034     EISSN: 19491042     Source Type: Journal    
DOI: 10.4161/nucl.23796     Document Type: Review
Times cited : (20)

References (130)
  • 1
    • 77953577950 scopus 로고    scopus 로고
    • The nuclear envelope at a glance
    • PMID:20519579
    • Wilson KL, Berk JM. The nuclear envelope at a glance. J Cell Sci 2010; 123:1973-1978; PMID:20519579; http://dx.doi.org/10.1242/jcs.019042.
    • (2010) J Cell Sci , vol.123 , pp. 1973-1978
    • Wilson, K.L.1    Berk, J.M.2
  • 2
    • 3242807744 scopus 로고
    • The nuclear envelope; its structure and relation to cytoplasmic membranes
    • PMID:13242591
    • Watson ML. The nuclear envelope; its structure and relation to cytoplasmic membranes. J Biophys Biochem Cytol 1955; 1:257-270; PMID:13242591; http://dx.doi.org/10.1083/jcb.1.3.257.
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 257-270
    • Watson, M.L.1
  • 3
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • PMID:10684247
    • Rout M P, Aitchison JD, Suprapto A, Hjertaas K, Zhao Y, Chait B T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 2000; 148:635-651; PMID:10684247; http://dx.doi. org/10.1083/jcb.148.4.635.
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 4
    • 0037008997 scopus 로고    scopus 로고
    • Proteomic analysis of the mammalian nuclear pore complex
    • PMID:12196509
    • Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ. Proteomic analysis of the mammalian nuclear pore complex. J Cell Biol 2002; 158:915-927; PMID:12196509; http://dx.doi.org/10.1083/jcb.200206106.
    • (2002) J Cell Biol , vol.158 , pp. 915-927
    • Cronshaw, J.M.1    Krutchinsky, A.N.2    Zhang, W.3    Chait, B.T.4    Matunis, M.J.5
  • 5
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • PMID:12604785
    • Denning D P, Patel SS, Uversky V, Fink AL, Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci U S A 2003; 100:2450-2455; PMID:12604785; http://dx.doi.org/10.1073/pnas.0437902100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 6
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • PMID:10611974
    • Görlich D, Kutay U. Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 1999; 15:607-660; PMID:10611974; http://dx.doi.org/10.1146/annurev.cellbio.15.1.607.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 7
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • PMID:11729264
    • Macara IG. Transport into and out of the nucleus. Microbiol Mol Biol Rev 2001; 65:570-94; PMID:11729264;http://dx.doi.org/10.1128/MMBR.65.4.570-594.2001.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 8
    • 84866148224 scopus 로고    scopus 로고
    • Heat-shock stress activates a novel nuclear import pathway mediated by Hikeshi
    • PMID:22895094
    • Imamoto N, Kose S. Heat-shock stress activates a novel nuclear import pathway mediated by Hikeshi. Nucleus 2012; 3:422-428; PMID:22895094; http://dx.doi.org/10.4161/nucl.21713.
    • (2012) Nucleus , vol.3 , pp. 422-428
    • Imamoto, N.1    Kose, S.2
  • 9
    • 0036500259 scopus 로고    scopus 로고
    • Nuclear lamins: Building blocks of nuclear architecture
    • PMID:11877373
    • Goldman RD, Gruenbaum Y, Moir RD, Shumaker DK, Spann T P. Nuclear lamins: building blocks of nuclear architecture. Genes Dev 2002; 16:533-547; PMID:11877373; http://dx.doi.org/10.1101/gad.960502.
    • (2002) Genes Dev , vol.16 , pp. 533-547
    • Goldman, R.D.1    Gruenbaum, Y.2    Moir, R.D.3    Shumaker, D.K.4    Spann, T.P.5
  • 11
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • PMID:20507227
    • Starr DA, Fridolfsson HN. Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu Rev Cell Dev Biol 2010; 26:421-444; PMID:20507227; http://dx.doi. org/10.1146/annurev-cellbio-100109-104037.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 12
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • PMID:22632968
    • Sosa BA, Rothballer A, Kutay U, Schwartz TU. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 2012; 149:1035-1047; PMID:22632968; http://dx.doi. org/10.1016/j.cell.2012.03.046.
    • (2012) Cell , vol.149 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 13
    • 0037064176 scopus 로고    scopus 로고
    • Role of ANC-1 in tethering nuclei to the actin cytoskeleton
    • PMID:12169658
    • Starr DA, Han M. Role of ANC-1 in tethering nuclei to the actin cytoskeleton. Science 2002; 298:406-409; PMID:12169658; http://dx.doi.org/10.1126/sci-ence.1075119.
    • (2002) Science , vol.298 , pp. 406-409
    • Starr, D.A.1    Han, M.2
  • 14
    • 60549099949 scopus 로고    scopus 로고
    • Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization
    • PMID:19164528
    • Roux KJ, Crisp ML, Liu Q, Kim D, Kozlov S, Stewart CL, et al. Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization. Proc Natl Acad Sci U S A 2009; 106:2194-2199; PMID:19164528; http://dx.doi.org/10.1073/pnas.0808602106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2194-2199
    • Roux, K.J.1    Crisp, M.L.2    Liu, Q.3    Kim, D.4    Kozlov, S.5    Stewart, C.L.6
  • 15
    • 28544437813 scopus 로고    scopus 로고
    • Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
    • PMID:16330710
    • Wilhelmsen K, Litjens SHM, Kuikman I, Tshimbalanga N, Janssen H, van den Bout I, et al. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J Cell Biol 2005; 171:799-810; PMID:16330710; http://dx.doi. org/10.1083/jcb.200506083.
    • (2005) J Cell Biol , vol.171 , pp. 799-810
    • Wilhelmsen, K.1    Litjens, S.H.M.2    Kuikman, I.3    Tshimbalanga, N.4    Janssen, H.5    van den Bout, I.6
  • 16
    • 0346094458 scopus 로고    scopus 로고
    • The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • PMID:14697201
    • Malone CJ, Misner L, Le Bot N, Tsai MC, Campbell JM, Ahringer J, et al. The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus. Cell 2003; 115:825-836; PMID:14697201; http://dx.doi.org/10.1016/S0092-8674(03)00985-1.
    • (2003) Cell , vol.115 , pp. 825-836
    • Malone, C.J.1    Misner, L.2    Le Bot, N.3    Tsai, M.C.4    Campbell, J.M.5    Ahringer, J.6
  • 18
    • 33750379023 scopus 로고    scopus 로고
    • The laminopathies: The functional architecture of the nucleus and its contribution to disease
    • PMID:16824021
    • Burke B, Stewart CL. The laminopathies: the functional architecture of the nucleus and its contribution to disease. Annu Rev Genomics Hum Genet 2006; 7:369-405; PMID:16824021; http://dx.doi.org/10.1146/ annurev.genom.7.080505.115732.
    • (2006) Annu Rev Genomics Hum Genet , vol.7 , pp. 369-405
    • Burke, B.1    Stewart, C.L.2
  • 19
    • 77957263769 scopus 로고    scopus 로고
    • Diseases of the nuclear envelope
    • PMID:20182615
    • Worman HJ, Ostlund C, Wang Y. Diseases of the nuclear envelope. Cold Spring Harb Perspect Biol 2010; 2:a000760; PMID:20182615; http://dx.doi.org/10.1101/cshperspect.a000760.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Worman, H.J.1    Ostlund, C.2    Wang, Y.3
  • 20
    • 79951683953 scopus 로고    scopus 로고
    • Phosphorylation of Nup98 by multiple kinases is crucial for NPC disassembly during mitotic entry
    • PMID:21335236
    • Laurell E, Beck K, Krupina K, Theerthagiri G, Bodenmiller B, Horvath P, et al. Phosphorylation of Nup98 by multiple kinases is crucial for NPC disassembly during mitotic entry. Cell 2011; 144:539-550; PMID:21335236; http://dx.doi.org/10.1016/j. cell.2011.01.012.
    • (2011) Cell , vol.144 , pp. 539-550
    • Laurell, E.1    Beck, K.2    Krupina, K.3    Theerthagiri, G.4    Bodenmiller, B.5    Horvath, P.6
  • 21
    • 0037059618 scopus 로고    scopus 로고
    • Cytoplasmic dynein as a facilitator of nuclear envelope breakdown
    • PMID:11792324
    • Salina D, Bodoor K, Eckley DM, Schroer TA, Rattner JB, Burke B. Cytoplasmic dynein as a facilitator of nuclear envelope breakdown. Cell 2002; 108:97-107; PMID:11792324; http://dx.doi.org/10.1016/S0092-8674(01)00628-6.
    • (2002) Cell , vol.108 , pp. 97-107
    • Salina, D.1    Bodoor, K.2    Eckley, D.M.3    Schroer, T.A.4    Rattner, J.B.5    Burke, B.6
  • 22
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • PMID:9298976
    • Ellenberg J, Siggia ED, Moreira JE, Smith CL, Presley JF, Worman HJ, et al. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J Cell Biol 1997; 138:1193-1206; PMID:9298976; http://dx.doi.org/10.1083/jcb.138.6.1193.
    • (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
  • 23
    • 44349165873 scopus 로고    scopus 로고
    • Spatial and temporal coordination of mitosis by Ran GTPase
    • PMID:18478030
    • Clarke PR, Zhang C. Spatial and temporal coordination of mitosis by Ran GTPase. Nat Rev Mol Cell Biol 2008; 9:464-477; PMID:18478030; http://dx.doi.org/10.1038/nrm2410.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 464-477
    • Clarke, P.R.1    Zhang, C.2
  • 24
    • 0042238022 scopus 로고    scopus 로고
    • RanGTP mediates nuclear pore complex assembly
    • PMID:12894213
    • Walther TC, Askjaer P, Gentzel M, Habermann A, Griffiths G, Wilm M, et al. RanGTP mediates nuclear pore complex assembly. Nature 2003; 424:689-694; PMID:12894213; http://dx.doi.org/10.1038/nature01898.
    • (2003) Nature , vol.424 , pp. 689-694
    • Walther, T.C.1    Askjaer, P.2    Gentzel, M.3    Habermann, A.4    Griffiths, G.5    Wilm, M.6
  • 25
    • 25444517781 scopus 로고    scopus 로고
    • Ran-GTP regulates kinet-ochore attachment in somatic cells
    • PMID:16082212
    • Arnaoutov A, Dasso M. Ran-GTP regulates kinet-ochore attachment in somatic cells. Cell Cycle 2005; 4:1161-1165; PMID:16082212; http://dx.doi.org/10.4161/cc.4.9.1979.
    • (2005) Cell Cycle , vol.4 , pp. 1161-1165
    • Arnaoutov, A.1    Dasso, M.2
  • 26
    • 70350247512 scopus 로고    scopus 로고
    • Transportin regulates major mitotic assembly events: From spindle to nuclear pore assembly
    • PMID:19641022
    • Lau CK, Delmar VA, Chan RC, Phung Q, Bernis C, Fichtman B, et al. Transportin regulates major mitotic assembly events: from spindle to nuclear pore assembly. Mol Biol Cell 2009; 20:4043-4058; PMID:19641022; http://dx.doi.org/10.1091/mbc.E09-02-0152.
    • (2009) Mol Biol Cell , vol.20 , pp. 4043-4058
    • Lau, C.K.1    Delmar, V.A.2    Chan, R.C.3    Phung, Q.4    Bernis, C.5    Fichtman, B.6
  • 27
    • 77649091127 scopus 로고    scopus 로고
    • Self-organization of intracellular gradients during mitosis
    • PMID:20181052
    • Fuller BG. Self-organization of intracellular gradients during mitosis. Cell Div 2010; 5:5; PMID:20181052; http://dx.doi.org/10.1186/1747-1028-5-5.
    • (2010) Cell Div , vol.5 , pp. 5
    • Fuller, B.G.1
  • 28
    • 34648825331 scopus 로고    scopus 로고
    • Chromosomal passengers: Conducting cell division
    • PMID:17848966
    • Ruchaud S, Carmena M, Earnshaw WC. Chromosomal passengers: conducting cell division. Nat Rev Mol Cell Biol 2007; 8:798-812; PMID:17848966; http://dx.doi.org/10.1038/nrm2257.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 798-812
    • Ruchaud, S.1    Carmena, M.2    Earnshaw, W.C.3
  • 29
    • 33645472801 scopus 로고    scopus 로고
    • A mitotic lamin B matrix induced by RanGTP required for spindle assembly
    • PMID:16543417
    • Tsai MY, Wang S, Heidinger JM, Shumaker DK, Adam SA, Goldman RD, et al. A mitotic lamin B matrix induced by RanGTP required for spindle assembly. Science 2006; 311:1887-1893; PMID:16543417; http://dx.doi.org/10.1126/science.1122771.
    • (2006) Science , vol.311 , pp. 1887-1893
    • Tsai, M.Y.1    Wang, S.2    Heidinger, J.M.3    Shumaker, D.K.4    Adam, S.A.5    Goldman, R.D.6
  • 30
    • 77954043950 scopus 로고    scopus 로고
    • Nuclear transport and the mitotic apparatus: An evolving relationship
    • PMID:20372967
    • Wozniak R, Burke B, Doye V. Nuclear transport and the mitotic apparatus: an evolving relationship. Cell Mol Life Sci 2010; 67:2215-2230; PMID:20372967; http://dx.doi.org/10.1007/s00018-010-0325-7.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2215-2230
    • Wozniak, R.1    Burke, B.2    Doye, V.3
  • 31
    • 39749150484 scopus 로고    scopus 로고
    • Kid-mediated chromosome compaction ensures proper nuclear envelope formation
    • PMID:18329364
    • Ohsugi M, Adachi K, Horai R, Kakuta S, Sudo K, Kotaki H, et al. Kid-mediated chromosome compaction ensures proper nuclear envelope formation. Cell 2008; 132:771-782; PMID:18329364; http://dx.doi. org/10.1016/j.cell.2008.01.029.
    • (2008) Cell , vol.132 , pp. 771-782
    • Ohsugi, M.1    Adachi, K.2    Horai, R.3    Kakuta, S.4    Sudo, K.5    Kotaki, H.6
  • 32
    • 59149098009 scopus 로고    scopus 로고
    • A new model for nuclear lamina organization
    • PMID:19021552
    • Goldberg M W, Fiserova J, Huttenlauch I, Stick R. A new model for nuclear lamina organization. Biochem Soc Trans 2008; 36:1339-1343; PMID:19021552; http://dx.doi.org/10.1042/BST0361339.
    • (2008) Biochem Soc Trans , vol.36 , pp. 1339-1343
    • Goldberg, M.W.1    Fiserova, J.2    Huttenlauch, I.3    Stick, R.4
  • 33
    • 84871501642 scopus 로고    scopus 로고
    • The nuclear lamins: Flexibility in function
    • PMID:23212477
    • Burke B, Stewart CL. The nuclear lamins: flexibility in function. Nat Rev Mol Cell Biol 2012; 14:13-24; PMID:23212477; http://dx.doi.org/10.1038/ nrm3488.
    • (2012) Nat Rev Mol Cell Biol , vol.14 , pp. 13-24
    • Burke, B.1    Stewart, C.L.2
  • 34
    • 0030004283 scopus 로고    scopus 로고
    • Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: Increase of lamin LI protein synthesis during meiotic maturation
    • PMID:8832400
    • Lourim D, Kempf A, Krohne G. Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: increase of lamin LI protein synthesis during meiotic maturation. J Cell Sci 1996; 109:1775-1785; PMID:8832400.
    • (1996) J Cell Sci , vol.109 , pp. 1775-1785
    • Lourim, D.1    Kempf, A.2    Krohne, G.3
  • 35
    • 0026657886 scopus 로고
    • Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract
    • PMID:1527167
    • Ulitzur N, Harel A, Feinstein N, Gruenbaum Y. Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract. J Cell Biol 1992; 119:17-25; PMID:1527167; http://dx.doi. org/10.1083/jcb.119.1.17.
    • (1992) J Cell Biol , vol.119 , pp. 17-25
    • Ulitzur, N.1    Harel, A.2    Feinstein, N.3    Gruenbaum, Y.4
  • 36
    • 0035833264 scopus 로고    scopus 로고
    • A role for nuclear lamins in nuclear envelope assembly
    • PMID:11448990
    • Lopez-Soler RI, Moir RD, Spann T P, Stick R, Goldman RD. A role for nuclear lamins in nuclear envelope assembly. J Cell Biol 2001; 154:61-70; PMID:11448990; http://dx.doi.org/10.1083/ jcb.200101025.
    • (2001) J Cell Biol , vol.154 , pp. 61-70
    • Lopez-Soler, R.I.1    Moir, R.D.2    Spann, T.P.3    Stick, R.4    Goldman, R.D.5
  • 37
    • 0025612124 scopus 로고
    • A lamin-independent pathway for nuclear envelope assembly
    • PMID:2277059
    • Newport JW, Wilson KL, Dunphy WG. A lamin-independent pathway for nuclear envelope assembly. J Cell Biol 1990; 111:2247-2259; PMID:2277059; http://dx.doi.org/10.1083/jcb.111.6.2247.
    • (1990) J Cell Biol , vol.111 , pp. 2247-2259
    • Newport, J.W.1    Wilson, K.L.2    Dunphy, W.G.3
  • 38
    • 0028972870 scopus 로고
    • Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: Evidence from cell-free egg extracts
    • PMID:8586657
    • Goldberg MW, Jenkins H, Allen T, Whitfield WG, Hutchison CJ. Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: evidence from cell-free egg extracts. J Cell Sci 1995; 108:3451-3461; PMID:8586657.
    • (1995) J Cell Sci , vol.108 , pp. 3451-3461
    • Goldberg, M.W.1    Jenkins, H.2    Allen, T.3    Whitfield, W.G.4    Hutchison, C.J.5
  • 39
    • 0035833264 scopus 로고    scopus 로고
    • A role for nuclear lamins in nuclear envelope assembly
    • PMID:11448990
    • Lopez-Soler RI, Moir RD, Spann T P, Stick R, Goldman RD. A role for nuclear lamins in nuclear envelope assembly. J Cell Biol 2001; 154:61-70; PMID:11448990; http://dx.doi.org/10.1083/ jcb.200101025.
    • (2001) J Cell Biol , vol.154 , pp. 61-70
    • Lopez-Soler, R.I.1    Moir, R.D.2    Spann, T.P.3    Stick, R.4    Goldman, R.D.5
  • 40
    • 0035972254 scopus 로고    scopus 로고
    • Mistargeting of B-type lamins at the end of mitosis: Implications on cell survival and regulation of lamins A/C expression
    • PMID:11331311
    • Steen RL, Collas P. Mistargeting of B-type lamins at the end of mitosis: implications on cell survival and regulation of lamins A/C expression. J Cell Biol 2001; 153:621-626; PMID:11331311; http://dx.doi. org/10.1083/jcb.153.3.621.
    • (2001) J Cell Biol , vol.153 , pp. 621-626
    • Steen, R.L.1    Collas, P.2
  • 41
    • 0038348529 scopus 로고    scopus 로고
    • AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase
    • PMID:12697839
    • Steen RL, Beullens M, Landsverk HB, Bollen M, Collas P. AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase. J Cell Sci 2003; 116:2237-2246; PMID:12697839; http:// dx.doi.org/10.1242/jcs.00432.
    • (2003) J Cell Sci , vol.116 , pp. 2237-2246
    • Steen, R.L.1    Beullens, M.2    Landsverk, H.B.3    Bollen, M.4    Collas, P.5
  • 42
    • 84455208122 scopus 로고    scopus 로고
    • Mouse B-type lamins are required for proper organogenesis but not by embryonic stem cells
    • PMID:22116031
    • Kim Y, Sharov AA, McDole K, Cheng M, Hao H, Fan CM, et al. Mouse B-type lamins are required for proper organogenesis but not by embryonic stem cells. Science 2011; 334:1706-1710; PMID:22116031; http://dx.doi. org/10.1126/science.1211222.
    • (2011) Science , vol.334 , pp. 1706-1710
    • Kim, Y.1    Sharov, A.A.2    McDole, K.3    Cheng, M.4    Hao, H.5    Fan, C.M.6
  • 43
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae
    • PMID:9166402
    • Lenz-Böhme B, Wismar J, Fuchs S, Reifegerste R, Buchner E, Betz H, et al. Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae. J Cell Biol 1997; 137:1001-1016; PMID:9166402; http://dx.doi.org/10.1083/jcb.137.5.1001.
    • (1997) J Cell Biol , vol.137 , pp. 1001-1016
    • Lenz-Böhme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6
  • 44
    • 0034842046 scopus 로고    scopus 로고
    • A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila
    • PMID:11533666
    • Guillemin K, Williams T, Krasnow MA. A nuclear lamin is required for cytoplasmic organization and egg polarity in Drosophila. Nat Cell Biol 2001; 3:848-851; PMID:11533666; http://dx.doi.org/10.1038/ncb0901-848.
    • (2001) Nat Cell Biol , vol.3 , pp. 848-851
    • Guillemin, K.1    Williams, T.2    Krasnow, M.A.3
  • 45
    • 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
    • PMID:11071918
    • Liu J, Rolef Ben-Shahar T, Riemer D, Treinin M, Spann P, Weber K, et al. Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes. Mol Biol Cell 2000; 11:3937-3947; PMID:11071918.
    • (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
  • 46
    • 84255196928 scopus 로고    scopus 로고
    • The role of nuclear lamin B1 in cell proliferation and senescence
    • PMID:22155925
    • Shimi T, Butin-Israeli V, Adam SA, Hamanaka RB, Goldman AE, Lucas CA, et al. The role of nuclear lamin B1 in cell proliferation and senescence. Genes Dev 2011; 25:2579-2593; PMID:22155925; http://dx.doi.org/10.1101/gad.179515.111.
    • (2011) Genes Dev , vol.25 , pp. 2579-2593
    • Shimi, T.1    Butin-Israeli, V.2    Adam, S.A.3    Hamanaka, R.B.4    Goldman, A.E.5    Lucas, C.A.6
  • 47
    • 0027275334 scopus 로고
    • Stepwise reassembly of the nuclear envelope at the end of mitosis
    • PMID:8391536
    • Chaudhary N, Courvalin JC. Stepwise reassembly of the nuclear envelope at the end of mitosis. J Cell Biol 1993; 122:295-306; PMID:8391536; http://dx.doi.org/10.1083/jcb.122.2.295.
    • (1993) J Cell Biol , vol.122 , pp. 295-306
    • Chaudhary, N.1    Courvalin, J.C.2
  • 48
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins A and B1: Different pathways of assembly during nuclear envelope formation in living cells
    • PMID:11121432
    • Moir RD, Yoon M, Khuon S, Goldman RD. Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells. J Cell Biol 2000; 151:1155-1168; PMID:11121432; http://dx.doi. org/10.1083/jcb.151.6.1155.
    • (2000) J Cell Biol , vol.151 , pp. 1155-1168
    • Moir, R.D.1    Yoon, M.2    Khuon, S.3    Goldman, R.D.4
  • 49
    • 0035833254 scopus 로고    scopus 로고
    • Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells
    • PMID:11448991
    • Daigle N, Beaudouin J, Hartnell L, Imreh G, Hallberg E, Lippincott-Schwartz J, et al. Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J Cell Biol 2001; 154:71-84; PMID:11448991; http://dx.doi.org/10.1083/ jcb.200101089.
    • (2001) J Cell Biol , vol.154 , pp. 71-84
    • Daigle, N.1    Beaudouin, J.2    Hartnell, L.3    Imreh, G.4    Hallberg, E.5    Lippincott-Schwartz, J.6
  • 50
    • 77956083200 scopus 로고    scopus 로고
    • Lamin-binding Proteins
    • PMID:20452940
    • Wilson KL, Foisner R. Lamin-binding Proteins. Cold Spring Harb Perspect Biol 2010; 2:a000554; PMID:20452940; http://dx.doi.org/10.1101/cshper-spect.a000554.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Wilson, K.L.1    Foisner, R.2
  • 51
    • 0030955703 scopus 로고    scopus 로고
    • Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis
    • PMID:9182656
    • Yang L, Guan T, Gerace L. Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis. J Cell Biol 1997; 137:1199-1210; PMID:9182656; http://dx.doi. org/10.1083/jcb.137.6.1199.
    • (1997) J Cell Biol , vol.137 , pp. 1199-1210
    • Yang, L.1    Guan, T.2    Gerace, L.3
  • 52
    • 67749124115 scopus 로고    scopus 로고
    • Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo
    • PMID:19620630
    • Anderson DJ, Vargas JD, Hsiao J P, Hetzer M W. Recruitment of functionally distinct membrane proteins to chromatin mediates nuclear envelope formation in vivo. J Cell Biol 2009; 186:183-191; PMID:19620630; http://dx.doi.org/10.1083/jcb.200901106.
    • (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
  • 53
    • 34848870027 scopus 로고    scopus 로고
    • Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum
    • PMID:17828249
    • Anderson DJ, Hetzer M W. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nat Cell Biol 2007; 9:1160-1166; PMID:17828249; http://dx.doi.org/10.1038/ ncb1636.
    • (2007) Nat Cell Biol , vol.9 , pp. 1160-1166
    • Anderson, D.J.1    Hetzer, M.W.2
  • 54
    • 2342451968 scopus 로고
    • A lamin B receptor in the nuclear envelope
    • PMID:2847165
    • Worman HJ, Yuan J, Blobel G, Georgatos SD. A lamin B receptor in the nuclear envelope. Proc Natl Acad Sci U S A 1988; 85:8531-8534; PMID:2847165; http://dx.doi.org/10.1073/pnas.85.22.8531.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8531-8534
    • Worman, H.J.1    Yuan, J.2    Blobel, G.3    Georgatos, S.D.4
  • 55
    • 0028237891 scopus 로고
    • Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane
    • PMID:8157663
    • Schuler E, Lin F, Worman HJ. Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane. J Biol Chem 1994; 269:11312-11317; PMID:8157663.
    • (1994) J Biol Chem , vol.269 , pp. 11312-11317
    • Schuler, E.1    Lin, F.2    Worman, H.J.3
  • 56
    • 0034732949 scopus 로고    scopus 로고
    • Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker
    • PMID:10828963
    • Duband-Goulet I, Courvalin JC. Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker. Biochemistry 2000; 39:6483-6488; PMID:10828963; http://dx.doi.org/10.1021/bi992908b.
    • (2000) Biochemistry , vol.39 , pp. 6483-6488
    • Duband-Goulet, I.1    Courvalin, J.C.2
  • 57
    • 77958036071 scopus 로고    scopus 로고
    • Lamin B receptor: Multi-tasking at the nuclear envelope
    • PMID:21327105
    • Olins AL, Rhodes G, Welch DBM, Zwerger M, Olins DE. Lamin B receptor: multi-tasking at the nuclear envelope. Nucleus 2010; 1:53-70; PMID:21327105.
    • (2010) Nucleus , vol.1 , pp. 53-70
    • Olins, A.L.1    Rhodes, G.2    Welch, D.B.M.3    Zwerger, M.4    Olins, D.E.5
  • 58
    • 79953296849 scopus 로고    scopus 로고
    • Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly
    • PMID:21289085
    • Funakoshi T, Clever M, Watanabe A, Imamoto N. Localization of Pom121 to the inner nuclear membrane is required for an early step of interphase nuclear pore complex assembly. Mol Biol Cell 2011; 22:1058-1069; PMID:21289085; http://dx.doi.org/10.1091/mbc. E10-07-0641.
    • (2011) Mol Biol Cell , vol.22 , pp. 1058-1069
    • Funakoshi, T.1    Clever, M.2    Watanabe, A.3    Imamoto, N.4
  • 59
    • 84859529827 scopus 로고    scopus 로고
    • The nucleoporin ELYS/Mel28 regulates nuclear envelope subdomain formation in HeLa cells
    • PMID:22555603
    • Clever M, Funakoshi T, Mimura Y, Takagi M, Imamoto N. The nucleoporin ELYS/Mel28 regulates nuclear envelope subdomain formation in HeLa cells. Nucleus 2012; 3:187-199; PMID:22555603; http:// dx.doi.org/10.4161/nucl.19595.
    • (2012) Nucleus , vol.3 , pp. 187-199
    • Clever, M.1    Funakoshi, T.2    Mimura, Y.3    Takagi, M.4    Imamoto, N.5
  • 60
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huët anomaly)
    • PMID:12118250
    • Hoffmann K, Dreger CK, Olins AL, Olins DE, Shultz LD, Lucke B, et al. Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huët anomaly). Nat Genet 2002; 31:410-414; PMID: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
  • 61
    • 0345535128 scopus 로고    scopus 로고
    • Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene
    • PMID:12618959
    • Waterham HR, Koster J, Mooyer P, Noort GG, Kelley RI, Wilcox WR, et al. Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene. Am J Hum Genet 2003; 72:1013-1017; PMID:12618959; http://dx.doi.org/10.1086/373938.
    • (2003) Am J Hum Genet , vol.72 , pp. 1013-1017
    • Waterham, H.R.1    Koster, J.2    Mooyer, P.3    Noort, G.G.4    Kelley, R.I.5    Wilcox, W.R.6
  • 62
    • 33847367253 scopus 로고    scopus 로고
    • Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta
    • PMID:17251381
    • Ma Y, Cai S, Lv Q, Jiang Q, Zhang Q, Sodmergen, et al. Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta. J Cell Sci 2007; 120:520-530; PMID:17251381; http://dx.doi.org/10.1242/jcs.03355.
    • (2007) J Cell Sci , vol.120 , pp. 520-530
    • Ma, Y.1    Cai, S.2    Lv, Q.3    Jiang, Q.4    Zhang, Q.5    Sodmergen6
  • 63
    • 0030461544 scopus 로고    scopus 로고
    • Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein
    • PMID:8991085
    • Collas P, Courvalin JC, Poccia D. Targeting of membranes to sea urchin sperm chromatin is mediated by a lamin B receptor-like integral membrane protein. J Cell Biol 1996; 135:1715-1725; PMID:8991085; http://dx.doi.org/10.1083/jcb.135.6.1715.
    • (1996) J Cell Biol , vol.135 , pp. 1715-1725
    • Collas, P.1    Courvalin, J.C.2    Poccia, D.3
  • 64
    • 0030480104 scopus 로고    scopus 로고
    • The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope
    • PMID:9003786
    • Pyrpasopoulou A, Meier J, Maison C, Simos G, Georgatos SD. The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope. EMBO J 1996; 15:7108-19; PMID:9003786.
    • (1996) EMBO J , vol.15 , pp. 7108-7119
    • Pyrpasopoulou, A.1    Meier, J.2    Maison, C.3    Simos, G.4    Georgatos, S.D.5
  • 65
    • 77958453919 scopus 로고    scopus 로고
    • Requirement for lamin B receptor and its regulation by importin beta and phosphorylation in nuclear envelope assembly during mitotic exit
    • PMID:20576617
    • Lu X, Shi Y, Lu Q, Ma Y, Luo J, Wang Q, et al. Requirement for lamin B receptor and its regulation by importin beta and phosphorylation in nuclear envelope assembly during mitotic exit. J Biol Chem 2010; 285:33281-33293; PMID:20576617; http://dx.doi. org/10.1074/jbc.M110.102368.
    • (2010) J Biol Chem , vol.285 , pp. 33281-33293
    • Lu, X.1    Shi, Y.2    Lu, Q.3    Ma, Y.4    Luo, J.5    Wang, Q.6
  • 66
    • 1842529177 scopus 로고    scopus 로고
    • Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts
    • PMID:14718546
    • Takano M, Koyama Y, Ito H, Hoshino S, Onogi H, Hagiwara M, et al. Regulation of binding of lamin B receptor to chromatin by SR protein kinase and cdc2 kinase in Xenopus egg extracts. J Biol Chem 2004; 279:13265-13271; PMID:14718546; http://dx.doi. org/10.1074/jbc.M308854200.
    • (2004) J Biol Chem , vol.279 , pp. 13265-13271
    • Takano, M.1    Koyama, Y.2    Ito, H.3    Hoshino, S.4    Onogi, H.5    Hagiwara, M.6
  • 67
    • 80052865865 scopus 로고    scopus 로고
    • Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor
    • PMID:21795390
    • Tseng LC, Chen RH. Temporal control of nuclear envelope assembly by phosphorylation of lamin B receptor. Mol Biol Cell 2011; 22:3306-3317; PMID:21795390; http://dx.doi.org/10.1091/mbc.E11-03-0199.
    • (2011) Mol Biol Cell , vol.22 , pp. 3306-3317
    • Tseng, L.C.1    Chen, R.H.2
  • 68
    • 0034681345 scopus 로고    scopus 로고
    • MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin
    • PMID:10671519
    • Lin F, Blake DL, Callebaut I, Skerjanc IS, Holmer L, McBurney MW, et al. MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin. J Biol Chem 2000; 275:4840-4847; PMID:10671519; http://dx.doi.org/10.1074/jbc.275.7.4840.
    • (2000) J Biol Chem , vol.275 , pp. 4840-4847
    • Lin, F.1    Blake, D.L.2    Callebaut, I.3    Skerjanc, I.S.4    Holmer, L.5    McBurney, M.W.6
  • 69
    • 0035881480 scopus 로고    scopus 로고
    • Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: One binds BAF and the other binds DNA
    • PMID:11500367
    • Cai M, Huang Y, Ghirlando R, Wilson KL, Craigie R, Clore GM. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. EMBO J 2001; 20:4399-407; PMID:11500367; http://dx.doi.org/10.1093/emboj/20.16.4399.
    • (2001) EMBO J , vol.20 , pp. 4399-4407
    • Cai, M.1    Huang, Y.2    Ghirlando, R.3    Wilson, K.L.4    Craigie, R.5    Clore, G.M.6
  • 70
    • 34249777825 scopus 로고    scopus 로고
    • LEM-Domain proteins: New insights into lamin-interacting proteins
    • PMID:17560279
    • Wagner N, Krohne G. LEM-Domain proteins: new insights into lamin-interacting proteins. Int Rev Cytol 2007; 261:1-46; PMID:17560279; http://dx.doi.org/10.1016/S0074-7696(07)61001-8.
    • (2007) Int Rev Cytol , vol.261 , pp. 1-46
    • Wagner, N.1    Krohne, G.2
  • 71
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • PMID:12493765
    • Holaska JM, Lee KK, Kowalski AK, Wilson KL. Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem 2003; 278:6969-6975; PMID:12493765; http://dx.doi.org/10.1074/jbc. M208811200.
    • (2003) J Biol Chem , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 72
    • 70349748587 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) condenses DNA by looping
    • PMID:19805345
    • Skoko D, Li M, Huang Y, Mizuuchi M, Cai M, Bradley CM, et al. Barrier-to-autointegration factor (BAF) condenses DNA by looping. Proc Natl Acad Sci U S A 2009; 106:16610-16615; PMID:19805345; http://dx.doi.org/10.1073/pnas.0909077106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16610-16615
    • Skoko, D.1    Li, M.2    Huang, Y.3    Mizuuchi, M.4    Cai, M.5    Bradley, C.M.6
  • 73
    • 0034255236 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex
    • PMID:10908652
    • Zheng R, Ghirlando R, Lee MS, Mizuuchi K, Krause M, Craigie R. Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc Natl Acad Sci U S A 2000; 97:8997-9002; PMID:10908652; http://dx.doi.org/10.1073/pnas.150240197.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8997-9002
    • Zheng, R.1    Ghirlando, R.2    Lee, M.S.3    Mizuuchi, K.4    Krause, M.5    Craigie, R.6
  • 74
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • PMID:12163470
    • Segura-Totten M, Kowalski AK, Craigie R, Wilson KL. Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J Cell Biol 2002; 158:475-485; PMID:12163470; http://dx.doi.org/10.1083/jcb.200202019.
    • (2002) J Cell Biol , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 75
    • 12444289583 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila
    • PMID:12902403
    • Furukawa K, Sugiyama S, Osouda S, Goto H, Inagaki M, Horigome T, et al. Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila. J Cell Sci 2003; 116:3811-3823; PMID:12902403; http://dx.doi.org/10.1242/ jcs.00682.
    • (2003) J Cell Sci , vol.116 , pp. 3811-3823
    • Furukawa, K.1    Sugiyama, S.2    Osouda, S.3    Goto, H.4    Inagaki, M.5    Horigome, T.6
  • 76
    • 14744280620 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina
    • PMID:15728376
    • Margalit A, Segura-Totten M, Gruenbaum Y, Wilson KL. Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina. Proc Natl Acad Sci U S A 2005; 102:3290-3295; PMID:15728376; http://dx.doi.org/10.1073/pnas.0408364102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3290-3295
    • Margalit, A.1    Segura-Totten, M.2    Gruenbaum, Y.3    Wilson, K.L.4
  • 77
    • 84863632575 scopus 로고    scopus 로고
    • Coordination of kinase and phosphatase activities by Lem4 enables nuclear envelope reassembly during mitosis
    • PMID:22770216
    • Asencio C, Davidson I F, Santarella-Mellwig R, Ly-Hartig TB, Mall M, Wallenfang MR, et al. Coordination of kinase and phosphatase activities by Lem4 enables nuclear envelope reassembly during mitosis. Cell 2012; 150:122-135; PMID:22770216; http://dx.doi.org/10.1016/j.cell.2012.04.043.
    • (2012) Cell , vol.150 , pp. 122-135
    • Asencio, C.1    Davidson, I.F.2    Santarella-Mellwig, R.3    Ly-Hartig, T.B.4    Mall, M.5    Wallenfang, M.R.6
  • 78
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • PMID:17851530
    • Beck M, Lucic V, Förster F, Baumeister W, Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007; 449:611-615; PMID:17851530; http://dx.doi.org/10.1038/ nature06170.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Förster, F.3    Baumeister, W.4    Medalia, O.5
  • 79
    • 84861966443 scopus 로고    scopus 로고
    • The human nuclear pore complex as revealed by cryo-electron tomography
    • PMID:22632834
    • Maimon T, Elad N, Dahan I, Medalia O. The human nuclear pore complex as revealed by cryo-electron tomography. Structure 2012; 20:998-1006; PMID:22632834; http://dx.doi.org/10.1016/j. str.2012.03.025.
    • (2012) Structure , vol.20 , pp. 998-1006
    • Maimon, T.1    Elad, N.2    Dahan, I.3    Medalia, O.4
  • 80
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • PMID:19913035
    • Frenkiel-Krispin D, Maco B, Aebi U, Medalia O. Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture. J Mol Biol 2010; 395:578-586; PMID:19913035; http://dx.doi. org/10.1016/j.jmb.2009.11.010.
    • (2010) J Mol Biol , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    Maco, B.2    Aebi, U.3    Medalia, O.4
  • 81
    • 0028786983 scopus 로고
    • Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
    • PMID:8589458
    • Guan T, Müller S, Klier G, Panté N, Blevitt JM, Haner M, et al. Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol Biol Cell 1995; 6:1591-1603; PMID:8589458.
    • (1995) Mol Biol Cell , vol.6 , pp. 1591-1603
    • Guan, T.1    Müller, S.2    Klier, G.3    Panté, N.4    Blevitt, J.M.5    Haner, M.6
  • 82
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • PMID:17082456
    • Frey S, Richter R P, Görlich D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 2006; 314:815-817; PMID:17082456; http://dx.doi. org/10.1126/science.1132516.
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Görlich, D.3
  • 83
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • PMID:17418788
    • Patel SS, Belmont BJ, Sante JM, Rexach M F. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 2007; 129:83-96; PMID:17418788; http://dx.doi.org/10.1016/j. cell.2007.01.044.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 84
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • PMID:21495847
    • Hoelz A, Debler EW, Blobel G. The structure of the nuclear pore complex. Annu Rev Biochem 2011; 80:613-643; PMID:21495847; http://dx.doi. org/10.1146/annurev-biochem-060109-151030.
    • (2011) Annu Rev Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 85
    • 84868279934 scopus 로고    scopus 로고
    • SnapShot: The nuclear envelope II
    • PMID:22939630
    • Rothballer A, Kutay U. SnapShot: the nuclear envelope II. Cell 2012; 150:1084 e1; PMID:22939630; http://dx.doi.org/10.1016/j.cell.2012.08.003.
    • (2012) Cell , vol.150 , Issue.1084
    • Rothballer, A.1    Kutay, U.2
  • 86
    • 79851490558 scopus 로고    scopus 로고
    • The nuclear pore complex and nuclear transport
    • PMID:20630994
    • Wente SR, Rout M P. The nuclear pore complex and nuclear transport. Cold Spring Harb Perspect Biol 2010; 2:a000562; PMID:20630994; http://dx.doi. org/10.1101/cshperspect.a000562.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Wente, S.R.1    Rout, M.P.2
  • 87
    • 0015160139 scopus 로고
    • Formation and distribution of nuclear pore complexes in interphase
    • PMID:5165267
    • Maul GG, Price JW, Lieberman MW. Formation and distribution of nuclear pore complexes in interphase. J Cell Biol 1971; 51:405-418; PMID:5165267; http://dx.doi.org/10.1083/jcb.51.2.405.
    • (1971) J Cell Biol , vol.51 , pp. 405-418
    • Maul, G.G.1    Price, J.W.2    Lieberman, M.W.3
  • 88
    • 0032841066 scopus 로고    scopus 로고
    • Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis
    • PMID:10362555
    • Bodoor K, Shaikh S, Salina D, Raharjo WH, Bastos R, Lohka M, et al. Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis. J Cell Sci 1999; 112:2253-2264; PMID:10362555.
    • (1999) J Cell Sci , vol.112 , pp. 2253-2264
    • Bodoor, K.1    Shaikh, S.2    Salina, D.3    Raharjo, W.H.4    Bastos, R.5    Lohka, M.6
  • 89
    • 77953724768 scopus 로고    scopus 로고
    • Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
    • PMID:20550937
    • Doucet CM, Talamas JA, Hetzer M W. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell 2010; 141:1030-1041; PMID:20550937; http://dx.doi.org/10.1016/j.cell.2010.04.036.
    • (2010) Cell , vol.141 , pp. 1030-1041
    • Doucet, C.M.1    Talamas, J.A.2    Hetzer, M.W.3
  • 90
    • 79953661699 scopus 로고    scopus 로고
    • Nuclear size, nuclear pore number and cell cycle
    • PMID:21738834
    • Maeshima K, Iino H, Hihara S, Imamoto N. Nuclear size, nuclear pore number and cell cycle. Nucleus 2011; 2:113-118; PMID:21738834; http://dx.doi.org/10.4161/nucl.2.2.15446.
    • (2011) Nucleus , vol.2 , pp. 113-118
    • Maeshima, K.1    Iino, H.2    Hihara, S.3    Imamoto, N.4
  • 91
    • 33645962474 scopus 로고    scopus 로고
    • Nuclear pores form de novo from both sides of the nuclear envelope
    • PMID:16627745
    • D'Angelo MA, Anderson DJ, Richard E, Hetzer MW. Nuclear pores form de novo from both sides of the nuclear envelope. Science 2006; 312:440-443; PMID:16627745; http://dx.doi.org/10.1126/science.1124196.
    • (2006) Science , vol.312 , pp. 440-443
    • D'Angelo, M.A.1    Anderson, D.J.2    Richard, E.3    Hetzer, M.W.4
  • 92
    • 77957660297 scopus 로고    scopus 로고
    • Nuclear pore biogenesis into an intact nuclear envelope
    • PMID:20721671
    • Doucet CM, Hetzer MW. Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma 2010; 119:469-477; PMID:20721671; http://dx.doi.org/10.1007/s00412-010-0289-2.
    • (2010) Chromosoma , vol.119 , pp. 469-477
    • Doucet, C.M.1    Hetzer, M.W.2
  • 93
    • 77956338708 scopus 로고    scopus 로고
    • Nuclear pore formation but not nuclear growth is governed by cyclin-dependent kinases (Cdks) during interphase
    • PMID:20711190
    • Maeshima K, Iino H, Hihara S, Funakoshi T, Watanabe A, Nishimura M, et al. Nuclear pore formation but not nuclear growth is governed by cyclin-dependent kinases (Cdks) during interphase. Nat Struct Mol Biol 2010; 17:1065-1071; PMID:20711190; http://dx.doi. org/10.1038/nsmb.1878.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1065-1071
    • Maeshima, K.1    Iino, H.2    Hihara, S.3    Funakoshi, T.4    Watanabe, A.5    Nishimura, M.6
  • 94
    • 79960233453 scopus 로고    scopus 로고
    • POM121 and Sun1 play a role in early steps of interphase NPC assembly
    • PMID:21727197
    • Talamas JA, Hetzer MW. POM121 and Sun1 play a role in early steps of interphase NPC assembly. J Cell Biol 2011; 194:27-37; PMID:21727197; http://dx.doi.org/10.1083/jcb.201012154.
    • (2011) J Cell Biol , vol.194 , pp. 27-37
    • Talamas, J.A.1    Hetzer, M.W.2
  • 95
    • 77955270200 scopus 로고    scopus 로고
    • NLS-mediated NPC functions of the nucleoporin Pom121
    • PMID:20624389
    • Yavuz S, Santarella-Mellwig R, Koch B, Jaedicke A, Mattaj IW, Antonin W. NLS-mediated NPC functions of the nucleoporin Pom121. FEBS Lett 2010; 584:3292-3298; PMID:20624389; http://dx.doi. org/10.1016/j.febslet.2010.07.008.
    • (2010) FEBS Lett , vol.584 , pp. 3292-3298
    • Yavuz, S.1    Santarella-Mellwig, R.2    Koch, B.3    Jaedicke, A.4    Mattaj, I.W.5    Antonin, W.6
  • 96
    • 0034759412 scopus 로고    scopus 로고
    • Steps of nuclear pore complex disassembly and reassembly during mitosis in early Drosophila embryos
    • PMID:11707513
    • Kiseleva EV, Rutherford S, Cotter LM, Allen TD, Goldberg MW. Steps of nuclear pore complex disassembly and reassembly during mitosis in early Drosophila embryos. J Cell Sci 2001; 114:3607-3618; PMID:11707513.
    • (2001) J Cell Sci , vol.114 , pp. 3607-3618
    • Kiseleva, E.V.1    Rutherford, S.2    Cotter, L.M.3    Allen, T.D.4    Goldberg, M.W.5
  • 97
    • 40849097593 scopus 로고    scopus 로고
    • Systematic kinetic analysis of mitotic dis-and reassembly of the nuclear pore in living cells
    • PMID:18316408
    • Dultz E, Zanin E, Wurzenberger C, Braun M, Rabut G, Sironi L, et al. Systematic kinetic analysis of mitotic dis-and reassembly of the nuclear pore in living cells. J Cell Biol 2008; 180:857-865; PMID:18316408; http://dx.doi.org/10.1083/jcb.200707026.
    • (2008) J Cell Biol , vol.180 , pp. 857-865
    • Dultz, E.1    Zanin, E.2    Wurzenberger, C.3    Braun, M.4    Rabut, G.5    Sironi, L.6
  • 98
    • 0023903495 scopus 로고
    • Steps in the assembly of replication-competent nuclei in a cell-free system from Xenopus eggs
    • PMID:3339085
    • Sheehan MA, Mills AD, Sleeman AM, Laskey RA, Blow JJ. Steps in the assembly of replication-competent nuclei in a cell-free system from Xenopus eggs. J Cell Biol 1988; 106:1-12; PMID:3339085; http://dx.doi. org/10.1083/jcb.106.1.1.
    • (1988) J Cell Biol , vol.106 , pp. 1-12
    • Sheehan, M.A.1    Mills, A.D.2    Sleeman, A.M.3    Laskey, R.A.4    Blow, J.J.5
  • 99
    • 0242668887 scopus 로고    scopus 로고
    • The conserved Nup107-160 complex is critical for nuclear pore complex assembly
    • PMID:12705868
    • Walther TC, Alves A, Pickersgill H, Loïodice I, Hetzer MW, Galy V, et al. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell 2003; 113:195-206; PMID:12705868; http://dx.doi. org/10.1016/S0092-8674(03)00235-6.
    • (2003) Cell , vol.113 , pp. 195-206
    • Walther, T.C.1    Alves, A.2    Pickersgill, H.3    Loïodice, I.4    Hetzer, M.W.5    Galy, V.6
  • 100
    • 80052596764 scopus 로고    scopus 로고
    • Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly
    • PMID:21825076
    • Lu L, Ladinsky MS, Kirchhausen T. Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly. J Cell Biol 2011; 194:425-440; PMID:21825076; http://dx.doi. org/10.1083/jcb.201012063.
    • (2011) J Cell Biol , vol.194 , pp. 425-440
    • Lu, L.1    Ladinsky, M.S.2    Kirchhausen, T.3
  • 101
    • 55549131172 scopus 로고    scopus 로고
    • Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly
    • PMID:18596237
    • Rasala BA, Ramos C, Harel A, Forbes DJ. Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly. Mol Biol Cell 2008; 19:3982-3996; PMID:18596237; http://dx.doi. org/10.1091/mbc.E08-01-0012.
    • (2008) Mol Biol Cell , vol.19 , pp. 3982-3996
    • Rasala, B.A.1    Ramos, C.2    Harel, A.3    Forbes, D.J.4
  • 102
    • 78049508819 scopus 로고    scopus 로고
    • Pom121 links two essential subcomplex-es of the nuclear pore complex core to the membrane
    • PMID:20974814
    • Mitchell JM, Mansfeld J, Capitanio J, Kutay U, Wozniak RW. Pom121 links two essential subcomplex-es of the nuclear pore complex core to the membrane. J Cell Biol 2010; 191:505-521; PMID:20974814; http://dx.doi.org/10.1083/jcb.201007098.
    • (2010) J Cell Biol , vol.191 , pp. 505-521
    • Mitchell, J.M.1    Mansfeld, J.2    Capitanio, J.3    Kutay, U.4    Wozniak, R.W.5
  • 103
    • 33846956769 scopus 로고    scopus 로고
    • A general amphipathic α-helical motif for sensing membrane curvature
    • PMID:17220896
    • Drin G, Casella J F, Gautier R, Boehmer T, Schwartz TU, Antonny B. A general amphipathic α-helical motif for sensing membrane curvature. Nat Struct Mol Biol 2007; 14:138-146; PMID:17220896; http://dx.doi.org/10.1038/nsmb1194.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 138-146
    • Drin, G.1    Casella, J.F.2    Gautier, R.3    Boehmer, T.4    Schwartz, T.U.5    Antonny, B.6
  • 104
    • 0036235143 scopus 로고    scopus 로고
    • Identification of a novel transcription factor, ELYS, expressed predominantly in mouse foetal haematopoietic tissues
    • PMID:11952839
    • Kimura N, Takizawa M, Okita K, Natori O, Igarashi K, Ueno M, et al. Identification of a novel transcription factor, ELYS, expressed predominantly in mouse foetal haematopoietic tissues. Genes Cells 2002; 7:435-446; PMID:11952839; http://dx.doi.org/10.1046/j.1365-2443.2002.00529.x.
    • (2002) Genes Cells , vol.7 , pp. 435-446
    • Kimura, N.1    Takizawa, M.2    Okita, K.3    Natori, O.4    Igarashi, K.5    Ueno, M.6
  • 105
    • 0038029461 scopus 로고    scopus 로고
    • Genomic organization and characterization of the mouse ELYS gene
    • PMID:12745078
    • Okita K, Nobuhisa I, Takizawa M, Ueno M, Kimura N, Taga T. Genomic organization and characterization of the mouse ELYS gene. Biochem Biophys Res Commun 2003; 305:327-332; PMID:12745078; http://dx.doi.org/10.1016/S0006-291X(03)00772-1.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 327-332
    • Okita, K.1    Nobuhisa, I.2    Takizawa, M.3    Ueno, M.4    Kimura, N.5    Taga, T.6
  • 106
    • 7944221427 scopus 로고    scopus 로고
    • Targeted disruption of the mouse ELYS gene results in embryonic death at peri-implantation development
    • PMID:15507119
    • Okita K, Kiyonari H, Nobuhisa I, Kimura N, Aizawa S, Taga T. Targeted disruption of the mouse ELYS gene results in embryonic death at peri-implantation development. Genes Cells 2004; 9:1083-1091; PMID:15507119; http://dx.doi.org/10.1111/j.1365-2443.2004.00791.x.
    • (2004) Genes Cells , vol.9 , pp. 1083-1091
    • Okita, K.1    Kiyonari, H.2    Nobuhisa, I.3    Kimura, N.4    Aizawa, S.5    Taga, T.6
  • 107
    • 33747827759 scopus 로고    scopus 로고
    • MEL-28, a novel nuclear-envelope and kineto-chore protein essential for zygotic nuclear-envelope assembly in C. elegans
    • PMID:16950114
    • Galy V, Askjaer P, Franz C, López-Iglesias C, Mattaj I W. MEL-28, a novel nuclear-envelope and kineto-chore protein essential for zygotic nuclear-envelope assembly in C. elegans. Curr Biol 2006; 16:1748-56; PMID:16950114; http://dx.doi.org/10.1016/j.cub.2006.06.067.
    • (2006) Curr Biol , vol.16 , pp. 1748-1756
    • Galy, V.1    Askjaer, P.2    Franz, C.3    López-Iglesias, C.4    Mattaj, I.W.5
  • 108
    • 33845227470 scopus 로고    scopus 로고
    • ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division
    • PMID:17098863
    • Rasala BA, Orjalo AV, Shen Z, Briggs S, Forbes DJ. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Proc Natl Acad Sci U S A 2006; 103:17801-17806; PMID:17098863; http://dx.doi.org/10.1073/pnas.0608484103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17801-17806
    • Rasala, B.A.1    Orjalo, A.V.2    Shen, Z.3    Briggs, S.4    Forbes, D.J.5
  • 109
    • 33947270331 scopus 로고    scopus 로고
    • MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly
    • PMID:17235358
    • Franz C, Walczak R, Yavuz S, Santarella R, Gentzel M, Askjaer P, et al. MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO Rep 2007; 8:165-172; PMID:17235358; http://dx.doi. org/10.1038/sj.embor.7400889.
    • (2007) EMBO Rep , vol.8 , pp. 165-172
    • Franz, C.1    Walczak, R.2    Yavuz, S.3    Santarella, R.4    Gentzel, M.5    Askjaer, P.6
  • 110
    • 34848827190 scopus 로고    scopus 로고
    • ELYS/MEL-28 chromatin association coordinates nuclear pore complex assembly and replication licensing
    • PMID:17825564
    • Gillespie PJ, Khoudoli GA, Stewart G, Swedlow JR, Blow JJ. ELYS/MEL-28 chromatin association coordinates nuclear pore complex assembly and replication licensing. Curr Biol 2007; 17:1657-1662; PMID:17825564; http://dx.doi.org/10.1016/j. cub.2007.08.041.
    • (2007) Curr Biol , vol.17 , pp. 1657-1662
    • Gillespie, P.J.1    Khoudoli, G.A.2    Stewart, G.3    Swedlow, J.R.4    Blow, J.J.5
  • 111
    • 73849084214 scopus 로고    scopus 로고
    • The Nup107-160 nucleo-porin complex promotes mitotic events via control of the localization state of the chromosome passenger complex
    • PMID:19864462
    • Platani M, Santarella-Mellwig R, Posch M, Walczak R, Swedlow JR, Mattaj IW. The Nup107-160 nucleo-porin complex promotes mitotic events via control of the localization state of the chromosome passenger complex. Mol Biol Cell 2009; 20:5260-5275; PMID:19864462; http://dx.doi.org/10.1091/mbc. E09-05-0377.
    • (2009) Mol Biol Cell , vol.20 , pp. 5260-5275
    • Platani, M.1    Santarella-Mellwig, R.2    Posch, M.3    Walczak, R.4    Swedlow, J.R.5    Mattaj, I.W.6
  • 112
    • 78649685697 scopus 로고    scopus 로고
    • Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint
    • PMID:21098116
    • Mackay DR, Makise M, Ullman KS. Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint. J Cell Biol 2010; 191:923-931; PMID:21098116; http://dx.doi. org/10.1083/jcb.201007124.
    • (2010) J Cell Biol , vol.191 , pp. 923-931
    • Mackay, D.R.1    Makise, M.2    Ullman, K.S.3
  • 113
    • 33747821629 scopus 로고    scopus 로고
    • MEL-28 is downstream of the Ran cycle and is required for nuclear-envelope function and chromatin maintenance
    • PMID:16950115
    • Fernandez AG, Piano F. MEL-28 is downstream of the Ran cycle and is required for nuclear-envelope function and chromatin maintenance. Curr Biol 2006; 16:1757-1763; PMID:16950115; http://dx.doi.org/10.1016/j. cub.2006.07.071.
    • (2006) Curr Biol , vol.16 , pp. 1757-1763
    • Fernandez, A.G.1    Piano, F.2
  • 114
    • 27144544970 scopus 로고    scopus 로고
    • Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates
    • PMID:16193066
    • Franz C, Askjaer P, Antonin W, Iglesias CL, Haselmann U, Schelder M, et al. Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates. EMBO J 2005; 24:3519-3531; PMID:16193066; http://dx.doi.org/10.1038/sj.emboj.7600825.
    • (2005) EMBO J , vol.24 , pp. 3519-3531
    • Franz, C.1    Askjaer, P.2    Antonin, W.3    Iglesias, C.L.4    Haselmann, U.5    Schelder, M.6
  • 115
    • 84872183592 scopus 로고    scopus 로고
    • The Nup155-mediated organisation of inner nuclear membrane proteins is independent of Nup155 anchoring to the metazoan nuclear pore complex
    • PMID:22718353
    • Busayavalasa K, Chen X, Farrants AK, Wagner N, Sabri N. The Nup155-mediated organisation of inner nuclear membrane proteins is independent of Nup155 anchoring to the metazoan nuclear pore complex. J Cell Sci 2012; 125:4214-8; PMID:22718353; http://dx.doi.org/10.1242/jcs.105809.
    • (2012) J Cell Sci , vol.125 , pp. 4214-4218
    • Busayavalasa, K.1    Chen, X.2    Farrants, A.K.3    Wagner, N.4    Sabri, N.5
  • 116
    • 60549094392 scopus 로고    scopus 로고
    • Early embryonic requirement for nucleoporin Nup35/ NPP-19 in nuclear assembly
    • PMID:19146848
    • Ródenas E, Klerkx E P, Ayuso C, Audhya A, Askjaer P. Early embryonic requirement for nucleoporin Nup35/ NPP-19 in nuclear assembly. Dev Biol 2009; 327:399-409; PMID:19146848; http://dx.doi.org/10.1016/j. ydbio.2008.12.024.
    • (2009) Dev Biol , vol.327 , pp. 399-409
    • Ródenas, E.1    Klerkx, E.P.2    Ayuso, C.3    Audhya, A.4    Askjaer, P.5
  • 117
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex
    • PMID:15703211
    • Hawryluk-Gara LA, Shibuya EK, Wozniak RW. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol Biol Cell 2005; 16:2382-2394; PMID:15703211; http://dx.doi.org/10.1091/mbc. E04-10-0857.
    • (2005) Mol Biol Cell , vol.16 , pp. 2382-2394
    • Hawryluk-Gara, L.A.1    Shibuya, E.K.2    Wozniak, R.W.3
  • 118
    • 44949151696 scopus 로고    scopus 로고
    • Nup53 is required for nuclear envelope and nuclear pore complex assembly
    • PMID:18256286
    • Hawryluk-Gara LA, Platani M, Santarella R, Wozniak RW, Mattaj I W. Nup53 is required for nuclear envelope and nuclear pore complex assembly. Mol Biol Cell 2008; 19:1753-1762; PMID:18256286; http://dx.doi. org/10.1091/mbc.E07-08-0820.
    • (2008) Mol Biol Cell , vol.19 , pp. 1753-1762
    • Hawryluk-Gara, L.A.1    Platani, M.2    Santarella, R.3    Wozniak, R.W.4    Mattaj, I.W.5
  • 119
    • 11344290169 scopus 로고    scopus 로고
    • The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation
    • PMID:15629719
    • Antonin W, Franz C, Haselmann U, Antony C, Mattaj I W. The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation. Mol Cell 2005; 17:83-92; PMID:15629719; http://dx.doi.org/10.1016/j.mol-cel.2004.12.010.
    • (2005) Mol Cell , vol.17 , pp. 83-92
    • Antonin, W.1    Franz, C.2    Haselmann, U.3    Antony, C.4    Mattaj, I.W.5
  • 120
    • 33646014440 scopus 로고    scopus 로고
    • The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells
    • PMID:16600873
    • Mansfeld J, Güttinger S, Hawryluk-Gara LA, Panté N, Mall M, Galy V, et al. The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells. Mol Cell 2006; 22:93-103; PMID:16600873; http://dx.doi.org/10.1016/j. molcel.2006.02.015.
    • (2006) Mol Cell , vol.22 , pp. 93-103
    • Mansfeld, J.1    Güttinger, S.2    Hawryluk-Gara, L.A.3    Panté, N.4    Mall, M.5    Galy, V.6
  • 121
    • 57349179985 scopus 로고    scopus 로고
    • Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death
    • PMID:19070573
    • Zhang X, Chen S, Yoo S, Chakrabarti S, Zhang T, Ke T, et al. Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death. Cell 2008; 135:1017-1027; PMID:19070573; http://dx.doi.org/10.1016/j.cell.2008.10.022.
    • (2008) Cell , vol.135 , pp. 1017-1027
    • Zhang, X.1    Chen, S.2    Yoo, S.3    Chakrabarti, S.4    Zhang, T.5    Ke, T.6
  • 122
    • 34948818777 scopus 로고    scopus 로고
    • Tw o distinct human POM121 genes: Requirement for the formation of nuclear pore complexes
    • PMID:17900573
    • Funakoshi T, Maeshima K, Yahata K, Sugano S, Imamoto F, Imamoto N. Tw o distinct human POM121 genes: requirement for the formation of nuclear pore complexes. FEBS Lett 2007; 581:4910-4916; PMID:17900573; http://dx.doi.org/10.1016/j.febs-let.2007.09.021.
    • (2007) FEBS Lett , vol.581 , pp. 4910-4916
    • Funakoshi, T.1    Maeshima, K.2    Yahata, K.3    Sugano, S.4    Imamoto, F.5    Imamoto, N.6
  • 123
    • 33751526510 scopus 로고    scopus 로고
    • Cell-cycle-dependent dynamics of nuclear pores: Pore-free islands and lam-ins
    • PMID:17074834
    • Maeshima K, Yahata K, Sasaki Y, Nakatomi R, Tachibana T, Hashikawa T, et al. Cell-cycle-dependent dynamics of nuclear pores: pore-free islands and lam-ins. J Cell Sci 2006; 119:4442-4451; PMID:17074834; http://dx.doi.org/10.1242/jcs.03207.
    • (2006) J Cell Sci , vol.119 , pp. 4442-4451
    • Maeshima, K.1    Yahata, K.2    Sasaki, Y.3    Nakatomi, R.4    Tachibana, T.5    Hashikawa, T.6
  • 124
    • 58049195492 scopus 로고    scopus 로고
    • The A- and B-type nuclear lamin networks: Microdomains involved in chromatin organization and transcription
    • PMID:19141474
    • Shimi T, Pfleghaar K, Kojima SI, Pack CG, Solovei I, Goldman AE, et al. The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev 2008; 22:3409-3421; PMID:19141474; http://dx.doi.org/10.1101/gad.1735208.
    • (2008) Genes Dev , vol.22 , pp. 3409-3421
    • Shimi, T.1    Pfleghaar, K.2    Kojima, S.I.3    Pack, C.G.4    Solovei, I.5    Goldman, A.E.6
  • 125
    • 84862777747 scopus 로고    scopus 로고
    • Chromosomal regions associated with prostate cancer risk localize to lamin B-deficient microdomains and exhibit reduced gene transcription
    • PMID:22025297
    • Helfand BT, Wang Y, Pfleghaar K, Shimi T, Taimen P, Shumaker DK. Chromosomal regions associated with prostate cancer risk localize to lamin B-deficient microdomains and exhibit reduced gene transcription. J Pathol 2012; 226:735-745; PMID:22025297; http://dx.doi.org/10.1002/path.3033.
    • (2012) J Pathol , vol.226 , pp. 735-745
    • Helfand, B.T.1    Wang, Y.2    Pfleghaar, K.3    Shimi, T.4    Taimen, P.5    Shumaker, D.K.6
  • 126
    • 63049132381 scopus 로고    scopus 로고
    • A-type and B-type lamins initiate layer assembly at distinct areas of the nuclear envelope in living cells
    • PMID:19210986
    • Furukawa K, Ishida K, Tsunoyama TA, Toda S, Osoda S, Horigome T, et al. A-type and B-type lamins initiate layer assembly at distinct areas of the nuclear envelope in living cells. Exp Cell Res 2009; 315:1181-1189; PMID:19210986; http://dx.doi.org/10.1016/j.yexcr.2008.12.024.
    • (2009) Exp Cell Res , vol.315 , pp. 1181-1189
    • Furukawa, K.1    Ishida, K.2    Tsunoyama, T.A.3    Toda, S.4    Osoda, S.5    Horigome, T.6
  • 127
    • 34548320825 scopus 로고    scopus 로고
    • Functional association of Sun1 with nuclear pore complexes
    • PMID:17724119
    • Liu Q, Panté N, Misteli T, Elsagga M, Crisp M, Hodzic D, et al. Functional association of Sun1 with nuclear pore complexes. J Cell Biol 2007; 178:785-798; PMID:17724119; http://dx.doi.org/10.1083/jcb.200704108.
    • (2007) J Cell Biol , vol.178 , pp. 785-798
    • Liu, Q.1    Panté, N.2    Misteli, T.3    Elsagga, M.4    Crisp, M.5    Hodzic, D.6
  • 128
    • 0034108049 scopus 로고    scopus 로고
    • Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup153 to reforming functional nuclear envelopes
    • PMID:10671368
    • Haraguchi T, Koujin T, Hayakawa T, Kaneda T, Tsutsumi C, Imamoto N, et al. Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup153 to reforming functional nuclear envelopes. J Cell Sci 2000; 113:779-794; PMID:10671368.
    • (2000) J Cell Sci , vol.113 , pp. 779-794
    • Haraguchi, T.1    Koujin, T.2    Hayakawa, T.3    Kaneda, T.4    Tsutsumi, C.5    Imamoto, N.6
  • 129
    • 50249107835 scopus 로고    scopus 로고
    • Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly
    • PMID:18628300
    • Haraguchi T, Kojidani T, Koujin T, Shimi T, Osakada H, Mori C, et al. Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly. J Cell Sci 2008; 121:2540-2554; PMID:18628300; http://dx.doi.org/10.1242/jcs.033597.
    • (2008) J Cell Sci , vol.121 , pp. 2540-2554
    • Haraguchi, T.1    Kojidani, T.2    Koujin, T.3    Shimi, T.4    Osakada, H.5    Mori, C.6
  • 130
    • 12344305602 scopus 로고    scopus 로고
    • LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly
    • PMID:15546916
    • Dechat T, Gajewski A, Korbei B, Gerlich D, Daigle N, Haraguchi T, et al. LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly. J Cell Sci 2004; 117:6117-6128; PMID:15546916; http://dx.doi.org/10.1242/ jcs.01529.
    • (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


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