메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

Net23/sting promotes chromatin compaction from the nuclear envelope

Author keywords

[No Author keywords available]

Indexed keywords

INTERFERON; MEMBRANE PROTEIN; NUCLEAR ENVELOPE TRANSMEMBRANE PROTEIN 23; UNCLASSIFIED DRUG; CHROMATIN; HISTONE; MPYS PROTEIN, HUMAN;

EID: 84911431532     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0111851     Document Type: Article
Times cited : (20)

References (75)
  • 1
    • 84891533416 scopus 로고    scopus 로고
    • Tissue specificity in the nuclear envelope supports its functional complexity
    • de Las Heras JI, Meinke P, Batrakou DG, Srsen V, Zuleger N, et al. (2013) Tissue specificity in the nuclear envelope supports its functional complexity. Nucleus 4: 460-477.
    • (2013) Nucleus , vol.4 , pp. 460-477
    • De Las Heras, J.I.1    Meinke, P.2    Batrakou, D.G.3    Srsen, V.4    Zuleger, N.5
  • 3
    • 0034864629 scopus 로고    scopus 로고
    • Skeletal muscle pathology in autosomal dominant Emery-Dreifuss muscular dystrophy with lamin A/C mutations
    • Sewry CA, Brown SC, Mercuri E, Bonne G, Feng L, et al. (2001) Skeletal muscle pathology in autosomal dominant Emery-Dreifuss muscular dystrophy with lamin A/C mutations. Neuropathol Appl Neurobiol 27: 281-290.
    • (2001) Neuropathol Appl Neurobiol , vol.27 , pp. 281-290
    • Sewry, C.A.1    Brown, S.C.2    Mercuri, E.3    Bonne, G.4    Feng, L.5
  • 4
    • 0344629215 scopus 로고    scopus 로고
    • Loss of lamin A/C expression revealed by immuno-electron microscopy in dilated cardiomyopathy with atrioventricular block caused by LMNA gene defects
    • Verga L, Concardi M, Pilotto A, Bellini O, Pasotti M, et al. (2003) Loss of lamin A/C expression revealed by immuno-electron microscopy in dilated cardiomyopathy with atrioventricular block caused by LMNA gene defects. Virchows Arch 443: 664-671.
    • (2003) Virchows Arch , vol.443 , pp. 664-671
    • Verga, L.1    Concardi, M.2    Pilotto, A.3    Bellini, O.4    Pasotti, M.5
  • 5
    • 0345084450 scopus 로고    scopus 로고
    • Ultrastructural abnormality of sarcolemmal nuclei in Emery-Dreifuss muscular dystrophy (EDMD)
    • Fidzianska A, Toniolo D, Hausmanowa-Petrusewicz I (1998) Ultrastructural abnormality of sarcolemmal nuclei in Emery-Dreifuss muscular dystrophy (EDMD). J Neurol Sci 159: 88-93.
    • (1998) J Neurol Sci , vol.159 , pp. 88-93
    • Fidzianska, A.1    Toniolo, D.2    Hausmanowa-Petrusewicz, I.3
  • 7
    • 0032770324 scopus 로고    scopus 로고
    • Nuclear changes in a case of X-linked Emery-Dreifuss muscular dystrophy
    • Ognibene A, Sabatelli P, Petrini S, Squarzoni S, Riccio M, et al. (1999) Nuclear changes in a case of X-linked Emery-Dreifuss muscular dystrophy. Muscle Nerve 22: 864-869.
    • (1999) Muscle Nerve , vol.22 , pp. 864-869
    • Ognibene, A.1    Sabatelli, P.2    Petrini, S.3    Squarzoni, S.4    Riccio, M.5
  • 8
    • 33747893889 scopus 로고    scopus 로고
    • Pathology and nuclear abnormalities in hearts of transgenic mice expressing M371K lamin A encoded by an LMNA mutation causing Emery-Dreifuss muscular dystrophy
    • Wang Y, Herron AJ, Worman HJ (2006) Pathology and nuclear abnormalities in hearts of transgenic mice expressing M371K lamin A encoded by an LMNA mutation causing Emery-Dreifuss muscular dystrophy. Hum Mol Genet 15: 2479-2489.
    • (2006) Hum Mol Genet , vol.15 , pp. 2479-2489
    • Wang, Y.1    Herron, A.J.2    Worman, H.J.3
  • 9
    • 28344440157 scopus 로고    scopus 로고
    • Alterations of nuclear envelope and chromatin organization in mandibuloacral dysplasia, a rare form of laminopathy
    • Filesi I, Gullotta F, Lattanzi G, D'Apice MR, Capanni C, et al. (2005) Alterations of nuclear envelope and chromatin organization in mandibuloacral dysplasia, a rare form of laminopathy. Physiol Genomics 23: 150-158.
    • (2005) Physiol Genomics , vol.23 , pp. 150-158
    • Filesi, I.1    Gullotta, F.2    Lattanzi, G.3    D'Apice, M.R.4    Capanni, C.5
  • 10
    • 2942643923 scopus 로고    scopus 로고
    • Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome
    • Goldman RD, Shumaker DK, Erdos MR, Eriksson M, Goldman AE, et al. (2004) Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci U S A 101: 8963-8968.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8963-8968
    • Goldman, R.D.1    Shumaker, D.K.2    Erdos, M.R.3    Eriksson, M.4    Goldman, A.E.5
  • 12
    • 28344445866 scopus 로고    scopus 로고
    • Rescue of heterochromatin organization in Hutchinson-Gilford progeria by drug treatment
    • Columbaro M, Capanni C, Mattioli E, Novelli G, Parnaik VK, et al. (2005) Rescue of heterochromatin organization in Hutchinson-Gilford progeria by drug treatment. Cell Mol Life Sci 62: 2669-2678.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2669-2678
    • Columbaro, M.1    Capanni, C.2    Mattioli, E.3    Novelli, G.4    Parnaik, V.K.5
  • 13
  • 14
    • 33745016642 scopus 로고    scopus 로고
    • Mutant nuclear lamin A leads to progressive alterations of epigenetic control in premature aging
    • Shumaker DK, Dechat T, Kohlmaier A, Adam SA, Bozovsky MR, et al. (2006) Mutant nuclear lamin A leads to progressive alterations of epigenetic control in premature aging. Proc Natl Acad Sci U S A 103: 8703-8708.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8703-8708
    • Shumaker, D.K.1    Dechat, T.2    Kohlmaier, A.3    Adam, S.A.4    Bozovsky, M.R.5
  • 15
    • 32144431571 scopus 로고    scopus 로고
    • Loss of emerin at the nuclear envelope disrupts the Rb1/E2F and MyoD pathways during muscle regeneration
    • Melcon G, Kozlov S, Cutler DA, Sullivan T, Hernandez L, et al. (2006) Loss of emerin at the nuclear envelope disrupts the Rb1/E2F and MyoD pathways during muscle regeneration. Human Molecular Genetics 15: 637-651.
    • (2006) Human Molecular Genetics , vol.15 , pp. 637-651
    • Melcon, G.1    Kozlov, S.2    Cutler, D.A.3    Sullivan, T.4    Hernandez, L.5
  • 16
    • 0036263036 scopus 로고    scopus 로고
    • CDNA microarray analysis of gene expression in fibroblasts of patients with X-linked Emery-Dreifuss muscular dystrophy
    • Tsukahara T, Tsujino S, Arahata K (2002) CDNA microarray analysis of gene expression in fibroblasts of patients with X-linked Emery-Dreifuss muscular dystrophy. Muscle Nerve 25: 898-901.
    • (2002) Muscle Nerve , vol.25 , pp. 898-901
    • Tsukahara, T.1    Tsujino, S.2    Arahata, K.3
  • 17
    • 36849011520 scopus 로고
    • Biochemical activities of the cell nucleus
    • Suppl
    • Mirsky AE, Allfrey V (1960) Biochemical activities of the cell nucleus. Dis Nerv Syst 21(2) Suppl: 23-28.
    • (1960) Dis Nerv Syst , vol.21 , Issue.2 , pp. 23-28
    • Mirsky, A.E.1    Allfrey, V.2
  • 18
    • 0015196030 scopus 로고
    • The effect of PHA stimulation of human peripheral blood lymphocytes upon cellular content of euchromatin and heterochromatin
    • Hirschhorn R, Decsy MI, Troll W (1971) The effect of PHA stimulation of human peripheral blood lymphocytes upon cellular content of euchromatin and heterochromatin. Cell Immunol 2: 696-701.
    • (1971) Cell Immunol , vol.2 , pp. 696-701
    • Hirschhorn, R.1    Decsy, M.I.2    Troll, W.3
  • 19
    • 0037023361 scopus 로고    scopus 로고
    • Subnuclear compartmentalization of immunoglobulin loci during lymphocyte development
    • Kosak ST, Skok JA, Medina KL, Riblet R, Le Beau MM, et al. (2002) Subnuclear compartmentalization of immunoglobulin loci during lymphocyte development. Science 296: 158-162.
    • (2002) Science , vol.296 , pp. 158-162
    • Kosak, S.T.1    Skok, J.A.2    Medina, K.L.3    Riblet, R.4    Le Beau, M.M.5
  • 20
    • 31644436473 scopus 로고    scopus 로고
    • Neural induction promotes large-scale chromatin reorganisation of the Mash1 locus
    • Williams RR, Azuara V, Perry P, Sauer S, Dvorkina M, et al. (2006) Neural induction promotes large-scale chromatin reorganisation of the Mash1 locus. J Cell Sci 119: 132-140.
    • (2006) J Cell Sci , vol.119 , pp. 132-140
    • Williams, R.R.1    Azuara, V.2    Perry, P.3    Sauer, S.4    Dvorkina, M.5
  • 21
    • 4544255977 scopus 로고    scopus 로고
    • Transcription-dependent spatial arrangements of CFTR and adjacent genes in human cell nuclei
    • Zink D, Amaral MD, Englmann A, Lang S, Clarke LA, et al. (2004) Transcription-dependent spatial arrangements of CFTR and adjacent genes in human cell nuclei. J Cell Biol 166: 815-825.
    • (2004) J Cell Biol , vol.166 , pp. 815-825
    • Zink, D.1    Amaral, M.D.2    Englmann, A.3    Lang, S.4    Clarke, L.A.5
  • 22
    • 33748289518 scopus 로고    scopus 로고
    • Characterization of the Drosophila melanogaster genome at the nuclear lamina
    • Pickersgill H, Kalverda B, de Wit E, Talhout W, Fornerod M, et al. (2006) Characterization of the Drosophila melanogaster genome at the nuclear lamina. Nat Genet 38: 1005-1014.
    • (2006) Nat Genet , vol.38 , pp. 1005-1014
    • Pickersgill, H.1    Kalverda, B.2    De Wit, E.3    Talhout, W.4    Fornerod, M.5
  • 23
    • 34547771741 scopus 로고    scopus 로고
    • SUUR joins separate subsets of PcG, HP1 and B-type lamin targets in Drosophila
    • Pindyurin AV, Moorman C, de Wit E, Belyakin SN, Belyaeva ES, et al. (2007) SUUR joins separate subsets of PcG, HP1 and B-type lamin targets in Drosophila. J Cell Sci 120: 2344-2351.
    • (2007) J Cell Sci , vol.120 , pp. 2344-2351
    • Pindyurin, A.V.1    Moorman, C.2    De Wit, E.3    Belyakin, S.N.4    Belyaeva, E.S.5
  • 24
    • 40349113413 scopus 로고    scopus 로고
    • Global histone acetylation induces functional genomic reorganization at mammalian nuclear pore complexes
    • Brown CR, Kennedy CJ, Delmar VA, Forbes DJ, Silver PA (2008) Global histone acetylation induces functional genomic reorganization at mammalian nuclear pore complexes. Genes & Development 22: 627-639.
    • (2008) Genes & Development , vol.22 , pp. 627-639
    • Brown, C.R.1    Kennedy, C.J.2    Delmar, V.A.3    Forbes, D.J.4    Silver, P.A.5
  • 25
    • 2942586676 scopus 로고    scopus 로고
    • The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope
    • Makatsori D, Kourmouli N, Polioudaki H, Shultz LD, McLean K, et al. (2004) The inner nuclear membrane protein lamin B receptor forms distinct microdomains and links epigenetically marked chromatin to the nuclear envelope. J Biol Chem 279: 25567-25573.
    • (2004) J Biol Chem , vol.279 , pp. 25567-25573
    • Makatsori, D.1    Kourmouli, N.2    Polioudaki, H.3    Shultz, L.D.4    McLean, K.5
  • 26
    • 0025056506 scopus 로고
    • On the cell-free association of lamins A and C with metaphase chromosomes
    • Burke B (1990) On the cell-free association of lamins A and C with metaphase chromosomes. Exp Cell Res 186: 169-176.
    • (1990) Exp Cell Res , vol.186 , pp. 169-176
    • Burke, B.1
  • 27
    • 0026343513 scopus 로고
    • Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain
    • Hoger TH, Krohne G, Kleinschmidt JA (1991) Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain. Exp Cell Res 197: 280-289.
    • (1991) Exp Cell Res , vol.197 , pp. 280-289
    • Hoger, T.H.1    Krohne, G.2    Kleinschmidt, J.A.3
  • 28
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura H, Glass C, Gerace L (1995) A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J Cell Biol 131: 33-44.
    • (1995) J Cell Biol , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 30
    • 0036889312 scopus 로고    scopus 로고
    • Esc1, a nuclear periphery protein required for Sir4-based plasmid anchoring and partitioning
    • Andrulis ED, Zappulla DC, Ansari A, Perrod S, Laiosa CV, et al. (2002) Esc1, a nuclear periphery protein required for Sir4-based plasmid anchoring and partitioning. Mol Cell Biol 22: 8292-8301.
    • (2002) Mol Cell Biol , vol.22 , pp. 8292-8301
    • Andrulis, E.D.1    Zappulla, D.C.2    Ansari, A.3    Perrod, S.4    Laiosa, C.V.5
  • 31
    • 17544383469 scopus 로고    scopus 로고
    • Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1
    • Ye Q, Worman HJ (1996) Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J Biol Chem 271: 14653-14656.
    • (1996) J Biol Chem , vol.271 , pp. 14653-14656
    • Ye, Q.1    Worman, H.J.2
  • 32
    • 0034756597 scopus 로고    scopus 로고
    • Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1
    • Polioudaki H, Kourmouli N, Drosou V, Bakou A, Theodoropoulos PA, et al. (2001) Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1. EMBO Rep 2: 920-925.
    • (2001) EMBO Rep , vol.2 , pp. 920-925
    • Polioudaki, H.1    Kourmouli, N.2    Drosou, V.3    Bakou, A.4    Theodoropoulos, P.A.5
  • 33
    • 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
    • Somech R, Shaklai S, Geller O, Amariglio N, Simon AJ, et al. (2005) The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J Cell Sci 118: 4017-4025.
    • (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
  • 34
    • 0031559831 scopus 로고    scopus 로고
    • Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2
    • Furukawa K, Glass C, Kondo T (1997) Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2. Biochem Biophys Res Commun 238: 240-246.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 240-246
    • Furukawa, K.1    Glass, C.2    Kondo, T.3
  • 36
    • 84862689455 scopus 로고    scopus 로고
    • The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity
    • Demmerle J, Koch AJ, Holaska JM (2012) The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity. J Biol Chem 287: 22080-22088.
    • (2012) J Biol Chem , vol.287 , pp. 22080-22088
    • Demmerle, J.1    Koch, A.J.2    Holaska, J.M.3
  • 37
    • 1542284570 scopus 로고    scopus 로고
    • Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy
    • Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, et al. (2004) Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Biochem 271: 1035-1045.
    • (2004) Eur J Biochem , vol.271 , pp. 1035-1045
    • Haraguchi, T.1    Holaska, J.M.2    Yamane, M.3    Koujin, T.4    Hashiguchi, N.5
  • 38
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • Holaska JM, Lee K, Kowalski AK, Wilson KL (2003) Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem 278: 6969-6975.
    • (2003) J Biol Chem , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 39
    • 84891808429 scopus 로고    scopus 로고
    • Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis
    • Demmerle J, Koch AJ, Holaska JM (2013) Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis. Chromosome Res 21: 765-779.
    • (2013) Chromosome Res , vol.21 , pp. 765-779
    • Demmerle, J.1    Koch, A.J.2    Holaska, J.M.3
  • 40
    • 84862639469 scopus 로고    scopus 로고
    • DNA sequence-dependent compartmentalization and silencing of chromatin at the nuclear lamina
    • Zullo JM, Demarco IA, Pique-Regi R, Gaffney DJ, Epstein CB, et al. (2012) DNA sequence-dependent compartmentalization and silencing of chromatin at the nuclear lamina. Cell 149: 1474-1487.
    • (2012) Cell , vol.149 , pp. 1474-1487
    • Zullo, J.M.1    Demarco, I.A.2    Pique-Regi, R.3    Gaffney, D.J.4    Epstein, C.B.5
  • 41
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer EC, Florens L, Guan T, Yates JR, Gerace L (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301: 1380-1382.
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3
  • 42
    • 53349178089 scopus 로고    scopus 로고
    • STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling
    • Ishikawa H, Barber GN (2008) STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling. Nature 455: 674-678.
    • (2008) Nature , vol.455 , pp. 674-678
    • Ishikawa, H.1    Barber, G.N.2
  • 43
    • 49449115516 scopus 로고    scopus 로고
    • MPYS, a novel membrane tetraspanner, is associated with major histocompatibility complex class II and mediates transduction of apoptotic signals
    • Jin L, Waterman PM, Jonscher KR, Short CM, Reisdorph NA, et al. (2008) MPYS, a novel membrane tetraspanner, is associated with major histocompatibility complex class II and mediates transduction of apoptotic signals. Mol Cell Biol 28: 5014-5026.
    • (2008) Mol Cell Biol , vol.28 , pp. 5014-5026
    • Jin, L.1    Waterman, P.M.2    Jonscher, K.R.3    Short, C.M.4    Reisdorph, N.A.5
  • 44
    • 77950609706 scopus 로고    scopus 로고
    • Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope
    • Malik P, Korfali N, Srsen V, Lazou V, Batrakou DG, et al. (2010) Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope. Cell Mol Life Sci 67: 1353-1369.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 1353-1369
    • Malik, P.1    Korfali, N.2    Srsen, V.3    Lazou, V.4    Batrakou, D.G.5
  • 45
    • 66649109939 scopus 로고    scopus 로고
    • ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
    • Sun W, Li Y, Chen L, Chen H, You F, et al. (2009) ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization. Proc Natl Acad Sci U S A 106: 8653-8658.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8653-8658
    • Sun, W.1    Li, Y.2    Chen, L.3    Chen, H.4    You, F.5
  • 46
    • 53349168904 scopus 로고    scopus 로고
    • The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation
    • Zhong B, Yang Y, Li S, Wang YY, Li Y, et al. (2008) The adaptor protein MITA links virus-sensing receptors to IRF3 transcription factor activation. Immunity 29: 538-550.
    • (2008) Immunity , vol.29 , pp. 538-550
    • Zhong, B.1    Yang, Y.2    Li, S.3    Wang, Y.Y.4    Li, Y.5
  • 47
    • 84885956378 scopus 로고    scopus 로고
    • Epigenomic control of the innate immune response
    • Stender JD, Glass CK (2013) Epigenomic control of the innate immune response. Curr Opin Pharmacol 13: 582-587.
    • (2013) Curr Opin Pharmacol , vol.13 , pp. 582-587
    • Stender, J.D.1    Glass, C.K.2
  • 48
    • 33749051214 scopus 로고    scopus 로고
    • Keeping up NF-kappaB appearances: Epigenetic control of immunity or inflammation-triggered epigenetics
    • Vanden Berghe W, Ndlovu MN, Hoya-Arias R, Dijsselbloem N, Gerlo S, et al. (2006) Keeping up NF-kappaB appearances: epigenetic control of immunity or inflammation-triggered epigenetics. Biochem Pharmacol 72: 1114-1131.
    • (2006) Biochem Pharmacol , vol.72 , pp. 1114-1131
    • Vanden Berghe, W.1    Ndlovu, M.N.2    Hoya-Arias, R.3    Dijsselbloem, N.4    Gerlo, S.5
  • 49
    • 0032559796 scopus 로고    scopus 로고
    • Selective entrapment of extrachromosomally amplified DNA by nuclear budding and micronucleation during S phase
    • Shimizu N, Itoh N, Utiyama H, Wahl GM (1998) Selective entrapment of extrachromosomally amplified DNA by nuclear budding and micronucleation during S phase. J Cell Biol 140: 1307-1320.
    • (1998) J Cell Biol , vol.140 , pp. 1307-1320
    • Shimizu, N.1    Itoh, N.2    Utiyama, H.3    Wahl, G.M.4
  • 50
    • 45149084413 scopus 로고    scopus 로고
    • Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions
    • Guelen L, Pagie L, Brasset E, Meuleman W, Faza MB, et al. (2008) Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions. Nature 453: 948-951.
    • (2008) Nature , vol.453 , pp. 948-951
    • Guelen, L.1    Pagie, L.2    Brasset, E.3    Meuleman, W.4    Faza, M.B.5
  • 51
    • 84875703872 scopus 로고    scopus 로고
    • Single-cell dynamics of genome-nuclear lamina interactions
    • Kind J, Pagie L, Ortabozkoyun H, Boyle S, de Vries SS, et al. (2013) Single-cell dynamics of genome-nuclear lamina interactions. Cell 153: 178-192.
    • (2013) Cell , vol.153 , pp. 178-192
    • Kind, J.1    Pagie, L.2    Ortabozkoyun, H.3    Boyle, S.4    De Vries, S.S.5
  • 52
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26: 239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 53
    • 84861191874 scopus 로고    scopus 로고
    • Breaking the HAC Barrier: Histone H3K9 acetyl/methyl balance regulates CENP-A assembly
    • Ohzeki J, Bergmann JH, Kouprina N, Noskov VN, Nakano M, et al. (2012) Breaking the HAC Barrier: histone H3K9 acetyl/methyl balance regulates CENP-A assembly. EMBO J 31: 2391-2402.
    • (2012) Embo J , vol.31 , pp. 2391-2402
    • Ohzeki, J.1    Bergmann, J.H.2    Kouprina, N.3    Noskov, V.N.4    Nakano, M.5
  • 54
    • 0348134932 scopus 로고    scopus 로고
    • Staurosporine-induced apoptosis in human cornea epithelial cells in vitro
    • Hartel S, Zorn-Kruppa M, Tykhonova S, Alajuuma P, Engelke M, et al. (2003) Staurosporine-induced apoptosis in human cornea epithelial cells in vitro. Cytometry A 55: 15-23.
    • (2003) Cytometry A , vol.55 , pp. 15-23
    • Hartel, S.1    Zorn-Kruppa, M.2    Tykhonova, S.3    Alajuuma, P.4    Engelke, M.5
  • 55
    • 84878944044 scopus 로고    scopus 로고
    • Readout of epigenetic modifications
    • Patel DJ, Wang Z (2013) Readout of epigenetic modifications. Annu Rev Biochem 82: 81-118.
    • (2013) Annu Rev Biochem , vol.82 , pp. 81-118
    • Patel, D.J.1    Wang, Z.2
  • 56
    • 84896292088 scopus 로고    scopus 로고
    • An H3K9/S10 methyl-phospho switch modulates Polycomb and Pol II binding at repressed genes during differentiation
    • Sabbattini P, Sjoberg M, Nikic S, Frangini A, Holmqvist PH, et al. (2014) An H3K9/S10 methyl-phospho switch modulates Polycomb and Pol II binding at repressed genes during differentiation. Mol Biol Cell 25: 904-915.
    • (2014) Mol Biol Cell , vol.25 , pp. 904-915
    • Sabbattini, P.1    Sjoberg, M.2    Nikic, S.3    Frangini, A.4    Holmqvist, P.H.5
  • 57
    • 4444334462 scopus 로고    scopus 로고
    • Trichostatin A-induced histone acetylation causes decondensation of interphase chromatin
    • Toth KF, Knoch TA, Wachsmuth M, Frank-Stohr M, Stohr M, et al. (2004) Trichostatin A-induced histone acetylation causes decondensation of interphase chromatin. J Cell Sci 117: 4277-4287.
    • (2004) J Cell Sci , vol.117 , pp. 4277-4287
    • Toth, K.F.1    Knoch, T.A.2    Wachsmuth, M.3    Frank-Stohr, M.4    Stohr, M.5
  • 58
    • 84861722003 scopus 로고    scopus 로고
    • Histone H3 lysine 9 di-methylation as an epigenetic signature of the interferon response
    • Fang TC, Schaefer U, Mecklenbrauker I, Stienen A, Dewell S, et al. (2012) Histone H3 lysine 9 di-methylation as an epigenetic signature of the interferon response. J Exp Med 209: 661-669.
    • (2012) J Exp Med , vol.209 , pp. 661-669
    • Fang, T.C.1    Schaefer, U.2    Mecklenbrauker, I.3    Stienen, A.4    Dewell, S.5
  • 59
    • 79251554670 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors impair innate immune responses to Toll-like receptor agonists and to infection
    • Roger T, Lugrin J, Le Roy D, Goy G, Mombelli M, et al. (2011) Histone deacetylase inhibitors impair innate immune responses to Toll-like receptor agonists and to infection. Blood 117: 1205-1217.
    • (2011) Blood , vol.117 , pp. 1205-1217
    • Roger, T.1    Lugrin, J.2    Le Roy, D.3    Goy, G.4    Mombelli, M.5
  • 60
    • 84876085954 scopus 로고    scopus 로고
    • STING recognition of cytoplasmic DNA instigates cellular defense
    • Abe T, Harashima A, Xia T, Konno H, Konno K, et al. (2013) STING recognition of cytoplasmic DNA instigates cellular defense. Mol Cell 50: 5-15.
    • (2013) Mol Cell , vol.50 , pp. 5-15
    • Abe, T.1    Harashima, A.2    Xia, T.3    Konno, H.4    Konno, K.5
  • 61
    • 84885169498 scopus 로고    scopus 로고
    • Cutting edge: DNA sensing via the STING adaptor in myeloid dendritic cells induces potent tolerogenic responses
    • Huang L, Li L, Lemos H, Chandler PR, Pacholczyk G, et al. (2013) Cutting edge: DNA sensing via the STING adaptor in myeloid dendritic cells induces potent tolerogenic responses. J Immunol 191: 3509-3513.
    • (2013) J Immunol , vol.191 , pp. 3509-3513
    • Huang, L.1    Li, L.2    Lemos, H.3    Chandler, P.R.4    Pacholczyk, G.5
  • 62
    • 84868107436 scopus 로고    scopus 로고
    • HDT701, a histone H4 deacetylase, negatively regulates plant innate immunity by modulating histone H4 acetylation of defense-related genes in rice
    • Ding B, Bellizzi Mdel R, Ning Y, Meyers BC, Wang GL (2012) HDT701, a histone H4 deacetylase, negatively regulates plant innate immunity by modulating histone H4 acetylation of defense-related genes in rice. Plant Cell 24: 3783-3794.
    • (2012) Plant Cell , vol.24 , pp. 3783-3794
    • Ding, B.1    Bellizzi Mdel, R.2    Ning, Y.3    Meyers, B.C.4    Wang, G.L.5
  • 63
    • 84902170924 scopus 로고    scopus 로고
    • Activation of the STING adaptor attenuates experimental autoimmune encephalitis
    • Lemos H, Huang L, Chandler PR, Mohamed E, Souza GR, et al. (2014) Activation of the STING Adaptor Attenuates Experimental Autoimmune Encephalitis. J Immunol.
    • (2014) J Immunol
    • Lemos, H.1    Huang, L.2    Chandler, P.R.3    Mohamed, E.4    Souza, G.R.5
  • 64
    • 84859501317 scopus 로고    scopus 로고
    • Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways
    • Malik P, Tabarraei A, Kehlenbach RH, Korfali N, Iwasawa R, et al. (2012) Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways. J Biol Chem 287: 12277-12292.
    • (2012) J Biol Chem , vol.287 , pp. 12277-12292
    • Malik, P.1    Tabarraei, A.2    Kehlenbach, R.H.3    Korfali, N.4    Iwasawa, R.5
  • 65
    • 11244316478 scopus 로고    scopus 로고
    • Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
    • Ohba T, Schirmer EC, Nishimoto T, Gerace L (2004) Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore. J Cell Biol 167: 1051-1062.
    • (2004) J Cell Biol , vol.167 , pp. 1051-1062
    • Ohba, T.1    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 66
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B, Worman HJ (1993) The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J Cell Biol 120: 1093-1100.
    • (1993) J Cell Biol , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 67
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • Soullam B, Worman HJ (1995) Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. Journal of Cell Biology 130: 15-27.
    • (1995) Journal Of Cell Biology , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.J.2
  • 68
    • 79955502505 scopus 로고    scopus 로고
    • System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics
    • Zuleger N, Kelly DA, Richardson AC, Kerr AR, Goldberg MW, et al. (2011) System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics. J Cell Biol 193: 109-123.
    • (2011) J Cell Biol , vol.193 , pp. 109-123
    • Zuleger, N.1    Kelly, D.A.2    Richardson, A.C.3    Kerr, A.R.4    Goldberg, M.W.5
  • 69
    • 67349231939 scopus 로고    scopus 로고
    • Interaction between the inner nuclear membrane lamin B receptor and the heterochromatic methyl binding protein, MeCP2
    • Guarda A, Bolognese F, Bonapace IM, Badaracco G (2009) Interaction between the inner nuclear membrane lamin B receptor and the heterochromatic methyl binding protein, MeCP2. Exp Cell Res 315: 1895-1903.
    • (2009) Exp Cell Res , vol.315 , pp. 1895-1903
    • Guarda, A.1    Bolognese, F.2    Bonapace, I.M.3    Badaracco, G.4
  • 70
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de novo point mutations in lamin a cause Hutchinson-Gilford progeria syndrome
    • Eriksson M, Brown WT, Gordon LB, Glynn MW, Singer J, et al. (2003) Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 423: 293-298.
    • (2003) Nature , vol.423 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3    Glynn, M.W.4    Singer, J.5
  • 72
    • 0032568321 scopus 로고    scopus 로고
    • Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells
    • Kanda T, Sullivan KF, Wahl GM (1998) Histone-GFP fusion protein enables sensitive analysis of chromosome dynamics in living mammalian cells. Curr Biol 8: 377-385.
    • (1998) Curr Biol , vol.8 , pp. 377-385
    • Kanda, T.1    Sullivan, K.F.2    Wahl, G.M.3
  • 73
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • Sullivan T, Escalante-Alcalde D, Bhatt H, Anver M, Bhat N, et al. (1999) Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J Cell Biol 147: 913-920.
    • (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
  • 74
    • 0032701521 scopus 로고    scopus 로고
    • Disruption of p53 in human cancer cells alters the responses to therapeutic agents
    • Bunz F, Hwang PM, Torrance C, Waldman T, Zhang Y, et al. (1999) Disruption of p53 in human cancer cells alters the responses to therapeutic agents. J Clin Invest 104: 263-269.
    • (1999) J Clin Invest , vol.104 , pp. 263-269
    • Bunz, F.1    Hwang, P.M.2    Torrance, C.3    Waldman, T.4    Zhang, Y.5
  • 75
    • 0035972145 scopus 로고    scopus 로고
    • Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization
    • Schirmer EC, Guan T, Gerace L (2001) Involvement of the lamin rod domain in heterotypic lamin interactions important for nuclear organization. J Cell Biol 153: 479-489.
    • (2001) J Cell Biol , vol.153 , pp. 479-489
    • Schirmer, E.C.1    Guan, T.2    Gerace, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.