메뉴 건너뛰기




Volumn 5, Issue 5, 2014, Pages 427-440

Diverse lamin-dependent mechanisms interact to control chromatin dynamics: Focus on laminopathies

Author keywords

Chromatin; Emery Dreifuss muscular dystrophy; Familial partial lipodystrophy; Hutchinson Gilford progeria; LADs; Laminopathies; Lamins; Mandibuloacral dysplasia; Nuclear envelope proteins

Indexed keywords

HISTONE DEACETYLASE; LAMIN; CHROMATIN; LAMIN A; LAMIN B;

EID: 84964313439     PISSN: 19491034     EISSN: 19491042     Source Type: Journal    
DOI: 10.4161/nucl.36289     Document Type: Review
Times cited : (90)

References (134)
  • 1
    • 79952555799 scopus 로고    scopus 로고
    • Laminopathies and lamin-associated signaling pathways
    • PMID:21400569
    • Maraldi NM, Capanni C, Cenni V, Fini M, Lattanzi G. Laminopathies and lamin-associated signaling pathways. J Cell Biochem 2011; 112:979-92; PMID:21400569; http://dx.doi.org/10.1002/jcb.22992
    • (2011) J Cell Biochem , vol.112 , pp. 979-992
    • Maraldi, N.M.1    Capanni, C.2    Cenni, V.3    Fini, M.4    Lattanzi, G.5
  • 3
    • 20444396818 scopus 로고    scopus 로고
    • Dynamic properties of germ line-specific lamin B3: The role of the shortened rod domain
    • PMID:16106909
    • Schütz W, Benavente R, Alsheimer M. Dynamic properties of germ line-specific lamin B3: the role of the shortened rod domain. Eur J Cell Biol 2005; 84:649-62; PMID:16106909; http://dx.doi.org/10.1016/j.ejcb.2005.03.001
    • (2005) Eur J Cell Biol , vol.84 , pp. 649-662
    • Schütz, W.1    Benavente, R.2    Alsheimer, M.3
  • 5
    • 84857099433 scopus 로고    scopus 로고
    • Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24
    • PMID:22355414
    • Barrowman J, Hamblet C, Kane MS, Michaelis S. Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24. PLoS One 2012; 7:e32120; PMID:22355414; http://dx.doi.org/10.1371/journal.pone.0032120
    • (2012) PLoS One , vol.7
    • Barrowman, J.1    Hamblet, C.2    Kane, M.S.3    Michaelis, S.4
  • 6
    • 77953023624 scopus 로고    scopus 로고
    • Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging
    • PMID:20458013
    • Ragnauth CD, Warren DT, Liu Y, McNair R, Tajsic T, Fig N, Shroff R, Skepper J, Shanahan CM. Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging. Circulation 2010; 121:2200-10; PMID:20458013; http://dx.doi.org/10.1161/CIRCULATIONAHA.109.902056
    • (2010) Circulation , vol.121 , pp. 2200-2210
    • Ragnauth, C.D.1    Warren, D.T.2    Liu, Y.3    McNair, R.4    Tajsic, T.5    Fig, N.6    Shroff, R.7    Skepper, J.8    Shanahan, C.M.9
  • 10
    • 84857683190 scopus 로고    scopus 로고
    • The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C
    • PMID:22393432
    • Zaremba-Czogalla M, Piekarowicz K, Wachowicz K, Kozioł K, Dubinska-Magiera M, Rzepecki R. The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C. PLoS One 2012; 7:e32649; PMID:22393432; http://dx.doi.org/10.1371/journal.pone.0032649
    • (2012) PLoS One , vol.7
    • Zaremba-Czogalla, M.1    Piekarowicz, K.2    Wachowicz, K.3    Kozioł, K.4    Dubinska-Magiera, M.5    Rzepecki, R.6
  • 11
    • 84875911766 scopus 로고    scopus 로고
    • Disruption of lamin B1 and lamin B2 processing and localization by farnesyltransferase inhibitors
    • PMID:23475125
    • Adam SA, Butin-Israeli V, Cleland MM, Shimi T, Goldman RD. Disruption of lamin B1 and lamin B2 processing and localization by farnesyltransferase inhibitors. Nucleus 2013; 4:142-50; PMID:23475125; http://dx.doi.org/10.4161/nucl.24089
    • (2013) Nucleus , vol.4 , pp. 142-150
    • Adam, S.A.1    Butin-Israeli, V.2    Cleland, M.M.3    Shimi, T.4    Goldman, R.D.5
  • 16
    • 81855169436 scopus 로고    scopus 로고
    • Prelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells
    • PMID:22103510
    • Lattanzi G. Prelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells. Biochem Soc Trans 2011; 39:1698-704; PMID:22103510; http://dx.doi.org/10.1042/BST20110657
    • (2011) Biochem Soc Trans , vol.39 , pp. 1698-1704
    • Lattanzi, G.1
  • 17
    • 84876714439 scopus 로고    scopus 로고
    • Nuclear damages and oxidative stress: New perspectives for laminopathies
    • PMID:23361241
    • Lattanzi G, Marmiroli S, Facchini A, Maraldi NM. Nuclear damages and oxidative stress: new perspectives for laminopathies. Eur J Histochem 2012; 56:e45; PMID:23361241; http://dx.doi.org/10.4081/ejh.2012.e45
    • (2012) Eur J Histochem , vol.56
    • Lattanzi, G.1    Marmiroli, S.2    Facchini, A.3    Maraldi, N.M.4
  • 23
    • 84863814698 scopus 로고    scopus 로고
    • The role of nuclear matrix proteins binding to matrix attachment regions (Mars) in prostate cancer cell differentiation
    • PMID:22808207
    • Barboro P, Repaci E, D’Arrigo C, Balbi C. The role of nuclear matrix proteins binding to matrix attachment regions (Mars) in prostate cancer cell differentiation. PLoS One 2012; 7:e40617; PMID:22808207; http://dx.doi.org/10.1371/journal.pone.0040617
    • (2012) PLoS One , vol.7
    • Barboro, P.1    Repaci, E.2    D’arrigo, C.3    Balbi, C.4
  • 24
    • 80054693830 scopus 로고    scopus 로고
    • Identification of new in vivo phosphosites on lamin Dm - the evidence of heterogeneity of phosphorylation sites in different Drosophila tissues
    • PMID:21989239
    • Zaremba-Czogalla M, Gagat P, Kozioł K, Dubinska-Magiera M, Sikora J, Dadlez M, Rzepecki R. Identification of new in vivo phosphosites on lamin Dm - the evidence of heterogeneity of phosphorylation sites in different Drosophila tissues. Nucleus 2011; 2:478-88; PMID:21989239; http://dx.doi.org/10.4161/nucl.2.5.17864
    • (2011) Nucleus , vol.2 , pp. 478-488
    • Zaremba-Czogalla, M.1    Gagat, P.2    Kozioł, K.3    Dubinska-Magiera, M.4    Sikora, J.5    Dadlez, M.6    Rzepecki, R.7
  • 25
    • 47549109045 scopus 로고    scopus 로고
    • Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies
    • PMID:18606848
    • Zhang YQ, Sarge KD. Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. J Cell Biol 2008; 182:35-9; PMID:18606848; http://dx.doi.org/10.1083/jcb.200712124
    • (2008) J Cell Biol , vol.182 , pp. 35-39
    • Zhang, Y.Q.1    Sarge, K.D.2
  • 27
    • 84873353657 scopus 로고    scopus 로고
    • tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations
    • PMID:23243001
    • Simon DN, Domaradzki T, Hofmann WA, Wilson KL. Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations. Mol Biol Cell 2013; 24:342-50; PMID:23243001; http://dx.doi.org/10.1091/mbc.E12-07-0527
    • (2013) Mol Biol Cell , vol.24 , pp. 342-350
    • Simon, D.N.1    Domaradzki, T.2    Hofmann, W.A.3    Wilson, K.L.4    Lamin, A.5
  • 29
    • 84875190548 scopus 로고    scopus 로고
    • Nuclear positioning
    • PMID:23498944
    • Gundersen GG, Worman HJ. Nuclear positioning. Cell 2013; 152:1376-89; PMID:23498944; http://dx.doi.org/10.1016/j.cell.2013.02.031
    • (2013) Cell , vol.152 , pp. 1376-1389
    • Gundersen, G.G.1    Worman, H.J.2
  • 30
    • 84873302358 scopus 로고    scopus 로고
    • LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation
    • PMID:23374351
    • Solovei I, Wang AS, Thanisch K, Schmidt CS, Krebs S, Zwerger M, Cohen TV, Devys D, Foisner R, Peichl L, et al. LBR and lamin A/C sequentially tether peripheral heterochromatin and inversely regulate differentiation. Cell 2013; 152:584-98; PMID:23374351; http://dx.doi.org/10.1016/j.cell.2013.01.009
    • (2013) Cell , vol.152 , pp. 584-598
    • Solovei, I.1    Wang, A.S.2    Thanisch, K.3    Schmidt, C.S.4    Krebs, S.5    Zwerger, M.6    Cohen, T.V.7    Devys, D.8    Foisner, R.9    Peichl, L.10
  • 31
    • 77956278711 scopus 로고    scopus 로고
    • Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein
    • PMID:20498703
    • Chaturvedi P, Parnaik VK. Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein, FBXW10. PLoS One 2010; 5:e10620; PMID:20498703; http://dx.doi.org/10.1371/journal.pone.0010620
    • (2010) FBXW10. PLoS One , vol.5
    • Chaturvedi, P.1    Parnaik, V.K.2
  • 32
    • 84880071424 scopus 로고    scopus 로고
    • High mobility group protein N5 (HMGN5) and lamina-associated polypeptide 2α (LAP2α) interact and reciprocally affect their genome-wide chromatin organization
    • PMID:23673662
    • Zhang S, Schones DE, Malicet C, Rochman M, Zhou M, Foisner R, Bustin M. High mobility group protein N5 (HMGN5) and lamina-associated polypeptide 2α (LAP2α) interact and reciprocally affect their genome-wide chromatin organization. J Biol Chem 2013; 288:18104-9; PMID:23673662; http://dx.doi.org/10.1074/jbc.C113.469544
    • (2013) J Biol Chem , vol.288 , pp. 18104-18109
    • Zhang, S.1    Schones, D.E.2    Malicet, C.3    Rochman, M.4    Zhou, M.5    Foisner, R.6    Bustin, M.7
  • 33
    • 74449093801 scopus 로고    scopus 로고
    • HMGN5/NSBP1: A new member of the HMGN protein family that affects chromatin structure and function
    • PMID:20123071
    • Rochman M, Malicet C, Bustin M. HMGN5/NSBP1: a new member of the HMGN protein family that affects chromatin structure and function. Biochim Biophys Acta 2010; 1799:86-92; PMID:20123071; http://dx.doi.org/10.1016/j.bbagrm.2009.09.012
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 86-92
    • Rochman, M.1    Malicet, C.2    Bustin, M.3
  • 34
    • 84856922144 scopus 로고    scopus 로고
    • Barrier-to-Autointegration Factor influences specific histone modifications
    • PMID:22127260
    • Montes de Oca R, Andreassen PR, Wilson KL. Barrier-to-Autointegration Factor influences specific histone modifications. Nucleus 2011; 2:580-90; PMID:22127260; http://dx.doi.org/10.4161/nucl.2.6.17960
    • (2011) Nucleus , vol.2 , pp. 580-590
    • Montes De Oca, R.1    Andreassen, P.R.2    Wilson, K.L.3
  • 36
    • 84862689455 scopus 로고    scopus 로고
    • The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity
    • PMID:22570481
    • Demmerle J, Koch AJ, Holaska JM. The nuclear envelope protein emerin binds directly to histone deacetylase 3 (HDAC3) and activates HDAC3 activity. J Biol Chem 2012; 287:22080-8; PMID:22570481; http://dx.doi.org/10.1074/jbc.M111.325308
    • (2012) J Biol Chem , vol.287 , pp. 22080-22088
    • Demmerle, J.1    Koch, A.J.2    Holaska, J.M.3
  • 37
    • 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
    • PMID:24062260
    • Demmerle J, Koch AJ, Holaska JM. Emerin and histone deacetylase 3 (HDAC3) cooperatively regulate expression and nuclear positions of MyoD, Myf5, and Pax7 genes during myogenesis. Chromosome Res 2013; 21:765-79; PMID:24062260; http://dx.doi.org/10.1007/s10577-013-9381-9
    • (2013) Chromosome Res , vol.21 , pp. 765-779
    • Demmerle, J.1    Koch, A.J.2    Holaska, J.M.3
  • 38
    • 84873375779 scopus 로고    scopus 로고
    • Constitutive nuclear lamina-genome interactions are highly conserved and associated with A/T-rich sequence
    • PMID:23124521
    • Meuleman W, Peric-Hupkes D, Kind J, Beaudry JB, Pagie L, Kellis M, Reinders M, Wessels L, van Steensel B. Constitutive nuclear lamina-genome interactions are highly conserved and associated with A/T-rich sequence. Genome Res 2013; 23:270-80; PMID:23124521; http://dx.doi.org/10.1101/gr.141028.112
    • (2013) Genome Res , vol.23 , pp. 270-280
    • Meuleman, W.1    Peric-Hupkes, D.2    Kind, J.3    Beaudry, J.B.4    Pagie, L.5    Kellis, M.6    Reinders, M.7    Wessels, L.8    Van Steensel, B.9
  • 39
    • 33748289518 scopus 로고    scopus 로고
    • Characterization of the Drosophila melanogaster genome at the nuclear lamina
    • PMID:16878134
    • Pickersgill H, Kalverda B, de Wit E, Talhout W, Fornerod M, van Steensel B. Characterization of the Drosophila melanogaster genome at the nuclear lamina. Nat Genet 2006; 38:1005-14; PMID:16878134; http://dx.doi.org/10.1038/ng1852
    • (2006) Nat Genet , vol.38 , pp. 1005-1014
    • Pickersgill, H.1    Kalverda, B.2    De Wit, E.3    Talhout, W.4    Fornerod, M.5    Van Steensel, B.6
  • 41
    • 84882642434 scopus 로고    scopus 로고
    • Redistribution of the Lamin B1 genomic binding profile affects rearrangement of heterochromatic domains and SAHF formation during senescence
    • PMID:23964094
    • Sadaie M, Salama R, Carroll T, Tomimatsu K, Chandra T, Young AR, Narita M, Pérez-Mancera PA, Bennett DC, Chong H, et al. Redistribution of the Lamin B1 genomic binding profile affects rearrangement of heterochromatic domains and SAHF formation during senescence. Genes Dev 2013; 27:1800-8; PMID:23964094; http://dx.doi.org/10.1101/gad.217281.113
    • (2013) Genes Dev , vol.27 , pp. 1800-1808
    • Sadaie, M.1    Salama, R.2    Carroll, T.3    Tomimatsu, K.4    Chandra, T.5    Young, A.R.6    Narita, M.7    Pérez-Mancera, P.A.8    Bennett, D.C.9    Chong, H.10
  • 42
    • 84897042327 scopus 로고    scopus 로고
    • Nucleolus and nuclear periphery: Velcro for heterochromatin
    • PMID:24690547
    • Padeken J, Heun P. Nucleolus and nuclear periphery: velcro for heterochromatin. Curr Opin Cell Biol 2014; 28:54-60; PMID:24690547; http://dx.doi.org/10.1016/j.ceb.2014.03.001
    • (2014) Curr Opin Cell Biol , vol.28 , pp. 54-60
    • Padeken, J.1    Heun, P.2
  • 43
    • 84899815048 scopus 로고    scopus 로고
    • Stochastic genome-nuclear lamina interactions: Modulating roles of Lamin A and BAF
    • PMID:24717229
    • Kind J, van Steensel B. Stochastic genome-nuclear lamina interactions: modulating roles of Lamin A and BAF. Nucleus 2014; 5:124-30; PMID:24717229; http://dx.doi.org/10.4161/nucl.28825
    • (2014) Nucleus , vol.5 , pp. 124-130
    • Kind, J.1    Van Steensel, B.2
  • 44
    • 77958029730 scopus 로고    scopus 로고
    • D4Z4 as a prototype of CTCF and lamins-dependent insulator in human cells
    • PMID:21327102
    • Ottaviani A, Schluth-Bolard C, Gilson E, Magdinier F. D4Z4 as a prototype of CTCF and lamins-dependent insulator in human cells. Nucleus 2010; 1:30-6; PMID:21327102
    • (2010) Nucleus , vol.1 , pp. 30-36
    • Ottaviani, A.1    Schluth-Bolard, C.2    Gilson, E.3    Magdinier, F.4
  • 46
  • 52
    • 80155174987 scopus 로고    scopus 로고
    • A new pathway that regulates 53BP1 stability implicates cathepsin L and vitamin D in DNA repair
    • PMID:21750527
    • Gonzalez-Suarez I, Redwood AB, Grotsky DA, Neumann MA, Cheng EH, Stewart CL, Dusso A, Gonzalo S. A new pathway that regulates 53BP1 stability implicates cathepsin L and vitamin D in DNA repair. EMBO J 2011; 30:3383-96; PMID:21750527; http://dx.doi.org/10.1038/emboj.2011.225
    • (2011) EMBO J , vol.30 , pp. 3383-3396
    • Gonzalez-Suarez, I.1    Redwood, A.B.2    Grotsky, D.A.3    Neumann, M.A.4    Cheng, E.H.5    Stewart, C.L.6    Dusso, A.7    Gonzalo, S.8
  • 54
    • 84880805342 scopus 로고    scopus 로고
    • Regulation of nucleotide excision repair by nuclear lamin b1
    • PMID:23894423
    • Butin-Israeli V, Adam SA, Goldman RD. Regulation of nucleotide excision repair by nuclear lamin b1. PLoS One 2013; 8:e69169; PMID:23894423; http://dx.doi.org/10.1371/journal.pone.0069169
    • (2013) PLoS One , vol.8
    • Butin-Israeli, V.1    Adam, S.A.2    Goldman, R.D.3
  • 57
    • 84877071045 scopus 로고    scopus 로고
    • A-type lamins maintain the positional stability of DNA damage repair foci in mammalian nuclei
    • PMID:23658700
    • Mahen R, Hattori H, Lee M, Sharma P, Jeyasekharan AD, Venkitaraman AR. A-type lamins maintain the positional stability of DNA damage repair foci in mammalian nuclei. PLoS One 2013; 8:e61893; PMID:23658700; http://dx.doi.org/10.1371/journal.pone.0061893
    • (2013) PLoS One , vol.8
    • Mahen, R.1    Hattori, H.2    Lee, M.3    Sharma, P.4    Jeyasekharan, A.D.5    Venkitaraman, A.R.6
  • 59
    • 78649658934 scopus 로고    scopus 로고
    • ERK1/2 MAP kinases promote cell cycle entry by rapid, kinase-independent disruption of retinoblastoma-lamin A complexes
    • PMID:21115804
    • Rodríguez J, Calvo F, González JM, Casar B, Andrés V, Crespo P. ERK1/2 MAP kinases promote cell cycle entry by rapid, kinase-independent disruption of retinoblastoma-lamin A complexes. J Cell Biol 2010; 191:967-79; PMID:21115804; http://dx.doi.org/10.1083/jcb.201004067
    • (2010) J Cell Biol , vol.191 , pp. 967-979
    • Rodríguez, J.1    Calvo, F.2    González, J.M.3    Casar, B.4    Andrés, V.5    Crespo, P.6
  • 60
    • 65549171487 scopus 로고    scopus 로고
    • Phosphorylation-dependent binding of human transcription factor MOK2 to lamin A/C
    • PMID:19490114
    • Harper M, Tillit J, Kress M, Ernoult-Lange M. Phosphorylation-dependent binding of human transcription factor MOK2 to lamin A/C. FEBS J 2009; 276:3137-47; PMID:19490114; http://dx.doi.org/10.1111/j.1742-4658.2009.07032.x
    • (2009) FEBS J , vol.276 , pp. 3137-3147
    • Harper, M.1    Tillit, J.2    Kress, M.3    Ernoult-Lange, M.4
  • 62
    • 59849092583 scopus 로고    scopus 로고
    • Lamin B1 controls oxidative stress responses via Oct-1
    • PMID:19139261
    • Malhas AN, Lee CF, Vaux DJ. Lamin B1 controls oxidative stress responses via Oct-1. J Cell Biol 2009; 184:45-55; PMID:19139261; http://dx.doi.org/10.1083/jcb.200804155
    • (2009) J Cell Biol , vol.184 , pp. 45-55
    • Malhas, A.N.1    Lee, C.F.2    Vaux, D.J.3
  • 63
    • 34848872591 scopus 로고    scopus 로고
    • The inner nuclear envelope as a transcription factor resting place
    • PMID:17906672
    • Heessen S, Fornerod M. The inner nuclear envelope as a transcription factor resting place. EMBO Rep 2007; 8:914-9; PMID:17906672; http://dx.doi.org/10.1038/sj.embor.7401075
    • (2007) EMBO Rep , vol.8 , pp. 914-919
    • Heessen, S.1    Fornerod, M.2
  • 65
    • 38849198553 scopus 로고    scopus 로고
    • Mislocalization of human transcription factor MOK2 in the presence of pathogenic mutations of lamin A/C
    • PMID:17760566
    • Dreuillet C, Harper M, Tillit J, Kress M, Ernoult-Lange M. Mislocalization of human transcription factor MOK2 in the presence of pathogenic mutations of lamin A/C. Biol Cell 2008; 100:51-61; PMID:17760566; http://dx.doi.org/10.1042/BC20070053
    • (2008) Biol Cell , vol.100 , pp. 51-61
    • Dreuillet, C.1    Harper, M.2    Tillit, J.3    Kress, M.4    Ernoult-Lange, M.5
  • 67
    • 84867266933 scopus 로고    scopus 로고
    • Familial partial lipodystrophy, mandibuloacral dysplasia and restrictive dermopathy feature barrier-to-autointegration factor (BAF) nuclear redistribution
    • PMID:22935701
    • Capanni C, Squarzoni S, Cenni V, D’Apice MR, Gambineri A, Novelli G, Wehnert M, Pasquali R, Maraldi NM, Lattanzi G. Familial partial lipodystrophy, mandibuloacral dysplasia and restrictive dermopathy feature barrier-to-autointegration factor (BAF) nuclear redistribution. Cell Cycle 2012; 11:3568-77; PMID:22935701; http://dx.doi.org/10.4161/cc.21869
    • (2012) Cell Cycle , vol.11 , pp. 3568-3577
    • Capanni, C.1    Squarzoni, S.2    Cenni, V.3    D’apice, M.R.4    Gambineri, A.5    Novelli, G.6    Wehnert, M.7    Pasquali, R.8    Maraldi, N.M.9    Lattanzi, G.10
  • 68
    • 84873531288 scopus 로고    scopus 로고
    • Lamin A/C is expressed in pluripotent mouse embryonic stem cells
    • PMID:23324457
    • Eckersley-Maslin MA, Bergmann JH, Lazar Z, Spector DL. Lamin A/C is expressed in pluripotent mouse embryonic stem cells. Nucleus 2013; 4:53-60; PMID:23324457; http://dx.doi.org/10.4161/nucl.23384
    • (2013) Nucleus , vol.4 , pp. 53-60
    • Eckersley-Maslin, M.A.1    Bergmann, J.H.2    Lazar, Z.3    Spector, D.L.4
  • 69
    • 80052215353 scopus 로고    scopus 로고
    • An absence of both lamin B1 and lamin B2 in keratinocytes has no effect on cell proliferation or the development of skin and hair
    • PMID:21659336
    • Yang SH, Chang SY, Yin L, Tu Y, Hu Y, Yoshinaga Y, de Jong PJ, Fong LG, Young SG. An absence of both lamin B1 and lamin B2 in keratinocytes has no effect on cell proliferation or the development of skin and hair. Hum Mol Genet 2011; 20:3537-44; PMID:21659336; http://dx.doi.org/10.1093/hmg/ddr266
    • (2011) Hum Mol Genet , vol.20 , pp. 3537-3544
    • Yang, S.H.1    Chang, S.Y.2    Yin, L.3    Tu, Y.4    Hu, Y.5    Yoshinaga, Y.6    De Jong, P.J.7    Fong, L.G.8    Young, S.G.9
  • 70
    • 84889087314 scopus 로고    scopus 로고
    • Proliferation and differentiation of mouse embryonic stem cells lacking all lamins
    • PMID:23979018
    • Kim Y, Zheng X, Zheng Y. Proliferation and differentiation of mouse embryonic stem cells lacking all lamins. Cell Res 2013; 23:1420-3; PMID:23979018; http://dx.doi.org/10.1038/cr.2013.118
    • (2013) Cell Res , vol.23 , pp. 1420-1423
    • Kim, Y.1    Zheng, X.2    Zheng, Y.3
  • 71
    • 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, Gaiano N, Ko MS, Zheng Y. Mouse B-type lamins are required for proper organogenesis but not by embryonic stem cells. Science 2011; 334:1706-10; 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    Gaiano, N.7    Ko, M.S.8    Zheng, Y.9
  • 72
    • 77950394590 scopus 로고    scopus 로고
    • Abnormal development of the cerebral cortex and cerebellum in the setting of lamin B2 deficiency
    • PMID:20145110
    • Coffinier C, Chang SY, Nobumori C, Tu Y, Farber EA, Toth JI, Fong LG, Young SG. Abnormal development of the cerebral cortex and cerebellum in the setting of lamin B2 deficiency. Proc Natl Acad Sci U S A 2010; 107:5076-81; PMID:20145110; http://dx.doi.org/10.1073/pnas.0908790107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5076-5081
    • Coffinier, C.1    Chang, S.Y.2    Nobumori, C.3    Tu, Y.4    Farber, E.A.5    Toth, J.I.6    Fong, L.G.7    Young, S.G.8
  • 73
    • 84863334769 scopus 로고    scopus 로고
    • Histone modifications and lamin A regulate chromatin protein dynamics in early embryonic stem cell differentiation
    • PMID:22713752
    • Melcer S, Hezroni H, Rand E, Nissim-Rafinia M, Skoultchi A, Stewart CL, Bustin M, Meshorer E. Histone modifications and lamin A regulate chromatin protein dynamics in early embryonic stem cell differentiation. Nat Commun 2012; 3:910; PMID:22713752; http://dx.doi.org/10.1038/ncomms1915
    • (2012) Nat Commun , vol.3 , pp. 910
    • Melcer, S.1    Hezroni, H.2    Rand, E.3    Nissim-Rafinia, M.4    Skoultchi, A.5    Stewart, C.L.6    Bustin, M.7    Meshorer, E.8
  • 74
    • 84873372317 scopus 로고    scopus 로고
    • Correlated spatio-temporal fluctuations in chromatin compaction states characterize stem cells
    • PMID:23442906
    • Talwar S, Kumar A, Rao M, Menon GI, Shivashankar GV. Correlated spatio-temporal fluctuations in chromatin compaction states characterize stem cells. Biophys J 2013; 104:553-64; PMID:23442906; http://dx.doi.org/10.1016/j.bpj.2012.12.033
    • (2013) Biophys J , vol.104 , pp. 553-564
    • Talwar, S.1    Kumar, A.2    Rao, M.3    Menon, G.I.4    Shivashankar, G.V.5
  • 75
    • 79954626173 scopus 로고    scopus 로고
    • Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome
    • PMID:21346760
    • Liu GH, Barkho BZ, Ruiz S, Diep D, Qu J, Yang SL, Panopoulos AD, Suzuki K, Kurian L, Walsh C, et al. Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome. Nature 2011; 472:221-5; PMID:21346760; http://dx.doi.org/10.1038/nature09879
    • (2011) Nature , vol.472 , pp. 221-225
    • Liu, G.H.1    Barkho, B.Z.2    Ruiz, S.3    Diep, D.4    Qu, J.5    Yang, S.L.6    Panopoulos, A.D.7    Suzuki, K.8    Kurian, L.9    Walsh, C.10
  • 76
    • 78650995671 scopus 로고    scopus 로고
    • A human iPSC model of Hutchinson Gilford Progeria reveals vascular smooth muscle and mesenchymal stem cell defects
    • PMID:21185252
    • Zhang J, Lian Q, Zhu G, Zhou F, Sui L, Tan C, Mutalif RA, Navasankari R, Zhang Y, Tse HF, et al. A human iPSC model of Hutchinson Gilford Progeria reveals vascular smooth muscle and mesenchymal stem cell defects. Cell Stem Cell 2011; 8:31-45; PMID:21185252; http://dx.doi.org/10.1016/j.stem.2010.12.002
    • (2011) Cell Stem Cell , vol.8 , pp. 31-45
    • Zhang, J.1    Lian, Q.2    Zhu, G.3    Zhou, F.4    Sui, L.5    Tan, C.6    Mutalif, R.A.7    Navasankari, R.8    Zhang, Y.9    Tse, H.F.10
  • 77
    • 84877642990 scopus 로고    scopus 로고
    • An inhibitory role of progerin in the gene induction network of adipocyte differentiation from iPS cells
    • PMID:23596277
    • Xiong ZM, LaDana C, Wu D, Cao K. An inhibitory role of progerin in the gene induction network of adipocyte differentiation from iPS cells. Aging (Albany NY) 2013; 5:288-303; PMID:23596277
    • (2013) Aging (Albany NY) , vol.5 , pp. 288-303
    • Xiong, Z.M.1    Ladana, C.2    Wu, D.3    Cao, K.4
  • 78
    • 84901473315 scopus 로고    scopus 로고
    • Lamina-associated polypeptide (LAP)2α and nucleoplasmic lamins in adult stem cell regulation and disease
    • PMID:24374133
    • Gesson K, Vidak S, Foisner R. Lamina-associated polypeptide (LAP)2α and nucleoplasmic lamins in adult stem cell regulation and disease. Semin Cell Dev Biol 2014; 29:116-24; PMID:24374133; http://dx.doi.org/10.1016/j.semcdb.2013.12.009
    • (2014) Semin Cell Dev Biol , vol.29 , pp. 116-124
    • Gesson, K.1    Vidak, S.2    Foisner, R.3
  • 80
    • 79959693815 scopus 로고    scopus 로고
    • Biophysical regulation of histone acetylation in mesenchymal stem cells
    • PMID:21504726
    • Li Y, Chu JS, Kurpinski K, Li X, Bautista DM, Yang L, Sung KL, Li S. Biophysical regulation of histone acetylation in mesenchymal stem cells. Biophys J 2011; 100:1902-9; PMID:21504726; http://dx.doi.org/10.1016/j.bpj.2011.03.008
    • (2011) Biophys J , vol.100 , pp. 1902-1909
    • Li, Y.1    Chu, J.S.2    Kurpinski, K.3    Li, X.4    Bautista, D.M.5    Yang, L.6    Sung, K.L.7    Li, S.8
  • 81
    • 65249097788 scopus 로고    scopus 로고
    • Dynamic complexes of A-type lamins and emerin influence adipogenic capacity of the cell via nucleocytoplasmic distribution of beta-catenin
    • PMID:19126678
    • Tilgner K, Wojciechowicz K, Jahoda C, Hutchison C, Markiewicz E. Dynamic complexes of A-type lamins and emerin influence adipogenic capacity of the cell via nucleocytoplasmic distribution of beta-catenin. J Cell Sci 2009; 122:401-13; PMID:19126678; http://dx.doi.org/10.1242/jcs.026179
    • (2009) J Cell Sci , vol.122 , pp. 401-413
    • Tilgner, K.1    Wojciechowicz, K.2    Jahoda, C.3    Hutchison, C.4    Markiewicz, E.5
  • 86
    • 84905270580 scopus 로고    scopus 로고
    • Loss of lamin B1 results in prolongation of S phase and decondensation of chromosome territories
    • PMID:24732130
    • Camps J, Wangsa D, Falke M, Brown M, Case CM, Erdos MR, Ried T. Loss of lamin B1 results in prolongation of S phase and decondensation of chromosome territories. FASEB J 2014; 28:3423-34; PMID:24732130; http://dx.doi.org/10.1096/fj.14-250456
    • (2014) FASEB J , vol.28 , pp. 3423-3434
    • Camps, J.1    Wangsa, D.2    Falke, M.3    Brown, M.4    Case, C.M.5    Erdos, M.R.6    Ried, T.7
  • 87
    • 84882682843 scopus 로고    scopus 로고
    • Lamin B1 depletion in senescent cells triggers large-scale changes in gene expression and the chromatin landscape
    • PMID:23934658
    • Shah PP, Donahue G, Otte GL, Capell BC, Nelson DM, Cao K, Aggarwala V, Cruickshanks HA, Rai TS, McBryan T, et al. Lamin B1 depletion in senescent cells triggers large-scale changes in gene expression and the chromatin landscape. Genes Dev 2013; 27:1787-99; PMID:23934658; http://dx.doi.org/10.1101/gad.223834.113
    • (2013) Genes Dev , vol.27 , pp. 1787-1799
    • Shah, P.P.1    Donahue, G.2    Otte, G.L.3    Capell, B.C.4    Nelson, D.M.5    Cao, K.6    Aggarwala, V.7    Cruickshanks, H.A.8    Rai, T.S.9    McBryan, T.10
  • 88
    • 84879808450 scopus 로고    scopus 로고
    • Prelamin A accelerates vascular calcification via activation of the DNA damage response and senescence-associated secretory phenotype in vascular smooth muscle cells
    • PMID:23564641
    • Liu Y, Drozdov I, Shroff R, Beltran LE, Shanahan CM. Prelamin A accelerates vascular calcification via activation of the DNA damage response and senescence-associated secretory phenotype in vascular smooth muscle cells. Circ Res 2013; 112:e99-109; PMID:23564641; http://dx.doi.org/10.1161/CIRCRESAHA.111.300543
    • (2013) Circ Res , vol.112 , pp. e99-e109
    • Liu, Y.1    Drozdov, I.2    Shroff, R.3    Beltran, L.E.4    Shanahan, C.M.5
  • 89
    • 84857995837 scopus 로고    scopus 로고
    • Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation
    • PMID:22246186
    • Barascu A, Le Chalony C, Pennarun G, Genet D, Imam N, Lopez B, Bertrand P. Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation. EMBO J 2012; 31:1080-94; PMID:22246186; http://dx.doi.org/10.1038/emboj.2011.492
    • (2012) EMBO J , vol.31 , pp. 1080-1094
    • Barascu, A.1    Le Chalony, C.2    Pennarun, G.3    Genet, D.4    Imam, N.5    Lopez, B.6    Bertrand, P.7
  • 93
    • 0242365630 scopus 로고    scopus 로고
    • Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: Altered intermolecular interaction with emerin and implications for gene transcription
    • PMID:14597414
    • Capanni C, Cenni V, Mattioli E, Sabatelli P, Ognibene A, Columbaro M, Parnaik VK, Wehnert M, Maraldi NM, Squarzoni S, et al. Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. Exp Cell Res 2003; 291:122-34; PMID:14597414; http://dx.doi.org/10.1016/S0014-4827(03)00395-1
    • (2003) Exp Cell Res , vol.291 , pp. 122-134
    • Capanni, C.1    Cenni, V.2    Mattioli, E.3    Sabatelli, P.4    Ognibene, A.5    Columbaro, M.6    Parnaik, V.K.7    Wehnert, M.8    Maraldi, N.M.9    Squarzoni, S.10
  • 95
    • 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 S, Pack CG, Solovei I, Goldman AE, Adam SA, Shumaker DK, Kinjo M, Cremer T, et al. The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev 2008; 22:3409-21; 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.3    Pack, C.G.4    Solovei, I.5    Goldman, A.E.6    Adam, S.A.7    Shumaker, D.K.8    Kinjo, M.9    Cremer, T.10
  • 96
    • 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, Furukawa K, Ellenberg J, Foisner R. LAP2alpha and BAF transiently localize to telomeres and specific regions on chromatin during nuclear assembly. J Cell Sci 2004; 117:6117-28; 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    Furukawa, K.7    Ellenberg, J.8    Foisner, R.9
  • 97
    • 40749104851 scopus 로고    scopus 로고
    • Chromatin dynamics and gene positioning
    • PMID:18358806
    • Kumaran RI, Thakar R, Spector DL. Chromatin dynamics and gene positioning. Cell 2008; 132:929-34; PMID:18358806; http://dx.doi.org/10.1016/j.cell.2008.03.004
    • (2008) Cell , vol.132 , pp. 929-934
    • Kumaran, R.I.1    Thakar, R.2    Spector, D.L.3
  • 98
    • 23944437599 scopus 로고    scopus 로고
    • Lamins A and C are differentially dysfunctional in autosomal dominant Emery-Dreifuss muscular dystrophy
    • PMID:16218190
    • Motsch I, Kaluarachchi M, Emerson LJ, Brown CA, Brown SC, Dabauvalle MC, Ellis JA. Lamins A and C are differentially dysfunctional in autosomal dominant Emery-Dreifuss muscular dystrophy. Eur J Cell Biol 2005; 84:765-81; PMID:16218190; http://dx.doi.org/10.1016/j.ejcb.2005.04.004
    • (2005) Eur J Cell Biol , vol.84 , pp. 765-781
    • Motsch, I.1    Kaluarachchi, M.2    Emerson, L.J.3    Brown, C.A.4    Brown, S.C.5    Dabauvalle, M.C.6    Ellis, J.A.7
  • 99
    • 0036837219 scopus 로고    scopus 로고
    • Functional domains of the nucleus: Implications for Emery-Dreifuss muscular dystrophy
    • PMID:12398831
    • Maraldi NM, Lattanzi G, Sabatelli P, Ognibene A, Squarzoni S. Functional domains of the nucleus: implications for Emery-Dreifuss muscular dystrophy. Neuromuscul Disord 2002; 12:815-23; PMID:12398831; http://dx.doi.org/10.1016/S0960-8966(02)00067-6
    • (2002) Neuromuscul Disord , vol.12 , pp. 815-823
    • Maraldi, N.M.1    Lattanzi, G.2    Sabatelli, P.3    Ognibene, A.4    Squarzoni, S.5
  • 101
    • 33947357081 scopus 로고    scopus 로고
    • Primary laminopathy fibroblasts display altered genome organization and apoptosis
    • PMID:17274801
    • Meaburn KJ, Cabuy E, Bonne G, Levy N, Morris GE, Novelli G, Kill IR, Bridger JM. Primary laminopathy fibroblasts display altered genome organization and apoptosis. Aging Cell 2007; 6:139-53; PMID:17274801; http://dx.doi.org/10.1111/j.1474-9726.2007.00270.x
    • (2007) Aging Cell , vol.6 , pp. 139-153
    • Meaburn, K.J.1    Cabuy, E.2    Bonne, G.3    Levy, N.4    Morris, G.E.5    Novelli, G.6    Kill, I.R.7    Bridger, J.M.8
  • 102
    • 0344309291 scopus 로고    scopus 로고
    • Nuclear envelope alterations in fibroblasts from LGMD1B patients carrying nonsense Y259X heterozygous or homozygous mutation in lamin A/C gene
    • PMID:14644157
    • Muchir A, van Engelen BG, Lammens M, Mislow JM, McNally E, Schwartz K, Bonne G. Nuclear envelope alterations in fibroblasts from LGMD1B patients carrying nonsense Y259X heterozygous or homozygous mutation in lamin A/C gene. Exp Cell Res 2003; 291:352-62; PMID:14644157; http://dx.doi.org/10.1016/j.yexcr.2003.07.002
    • (2003) Exp Cell Res , vol.291 , pp. 352-362
    • Muchir, A.1    Van Engelen, B.G.2    Lammens, M.3    Mislow, J.M.4    McNally, E.5    Schwartz, K.6    Bonne, G.7
  • 103
    • 28844466695 scopus 로고    scopus 로고
    • Familial Cardiomyopathy Registry Research Group. Thymopoietin (lamina-associated polypeptide 2) gene mutation associated with dilated cardiomyopathy
    • PMID:16247757
    • Taylor MR, Slavov D, Gajewski A, Vlcek S, Ku L, Fain PR, Carniel E, Di Lenarda A, Sinagra G, Boucek MM, et al.; Familial Cardiomyopathy Registry Research Group. Thymopoietin (lamina-associated polypeptide 2) gene mutation associated with dilated cardiomyopathy. Hum Mutat 2005; 26:566-74; PMID:16247757; http://dx.doi.org/10.1002/humu.20250
    • (2005) Hum Mutat , vol.26 , pp. 566-574
    • Taylor, M.R.1    Slavov, D.2    Gajewski, A.3    Vlcek, S.4    Ku, L.5    Fain, P.R.6    Carniel, E.7    Di Lenarda, A.8    Sinagra, G.9    Boucek, M.M.10
  • 105
    • 79952061789 scopus 로고    scopus 로고
    • Uncoordinated transcription and compromised muscle function in the lmna-null mouse model of Emery- Emery-Dreyfuss muscular dystrophy
    • PMID:21364987
    • Gnocchi VF, Scharner J, Huang Z, Brady K, Lee JS, White RB, Morgan JE, Sun YB, Ellis JA, Zammit PS. Uncoordinated transcription and compromised muscle function in the lmna-null mouse model of Emery- Emery-Dreyfuss muscular dystrophy. PLoS One 2011; 6:e16651; PMID:21364987; http://dx.doi.org/10.1371/journal.pone.0016651
    • (2011) PLoS One , vol.6
    • Gnocchi, V.F.1    Scharner, J.2    Huang, Z.3    Brady, K.4    Lee, J.S.5    White, R.B.6    Morgan, J.E.7    Sun, Y.B.8    Ellis, J.A.9    Zammit, P.S.10
  • 106
    • 84884587480 scopus 로고    scopus 로고
    • Doubly heterozygous LMNA and TTN mutations revealed by exome sequencing in a severe form of dilated cardiomyopathy. European journal of human genetics
    • Roncarati R, Viviani Anselmi C, Krawitz P, Lattanzi G, von Kodolitsch Y, Perrot A, et al. Doubly heterozygous LMNA and TTN mutations revealed by exome sequencing in a severe form of dilated cardiomyopathy. European journal of human genetics. Eur J Hum Genet 2013; http://dx.doi.org/10.1038/ejhg.2013.16
    • (2013) Eur J Hum Genet
    • Roncarati, R.1    Viviani Anselmi, C.2    Krawitz, P.3    Lattanzi, G.4    Von Kodolitsch, Y.5    Perrot, A.6
  • 107
    • 68549083365 scopus 로고    scopus 로고
    • Impaired nuclear functions lead to increased senescence and inefficient differentiation in human myoblasts with a dominant p.R545C mutation in the LMNA gene
    • PMID:19589617
    • Kandert S, Wehnert M, Müller CR, Buendia B, Dabauvalle MC. Impaired nuclear functions lead to increased senescence and inefficient differentiation in human myoblasts with a dominant p.R545C mutation in the LMNA gene. Eur J Cell Biol 2009; 88:593-608; PMID:19589617; http://dx.doi.org/10.1016/j.ejcb.2009.06.002
    • (2009) Eur J Cell Biol , vol.88 , pp. 593-608
    • Kandert, S.1    Wehnert, M.2    Müller, C.R.3    Buendia, B.4    Dabauvalle, M.C.5
  • 109
    • 84896697545 scopus 로고    scopus 로고
    • Genome-wide analysis links emerin to neuromuscular junction activity in Caenorhabditis elegans
    • PMID:24490688
    • González-Aguilera C, Ikegami K, Ayuso C, de Luis A, Iñiguez M, Cabello J, Lieb JD, Askjaer P. Genome-wide analysis links emerin to neuromuscular junction activity in Caenorhabditis elegans. Genome Biol 2014; 15:R21; PMID:24490688; http://dx.doi.org/10.1186/gb-2014-15-2-r21
    • (2014) Genome Biol , vol.15 , pp. R21
    • González-Aguilera, C.1    Ikegami, K.2    Ayuso, C.3    De Luis, A.4    Iñiguez, M.5    Cabello, J.6    Lieb, J.D.7    Askjaer, P.8
  • 110
    • 43249124368 scopus 로고    scopus 로고
    • Expression of the myodystrophic R453W mutation of lamin A in C2C12 myoblasts causes promoter-specific and global epigenetic defects
    • PMID:18396274
    • Håkelien AM, Delbarre E, Gaustad KG, Buendia B, Collas P. Expression of the myodystrophic R453W mutation of lamin A in C2C12 myoblasts causes promoter-specific and global epigenetic defects. Exp Cell Res 2008; 314:1869-80; PMID:18396274; http://dx.doi.org/10.1016/j.yexcr.2008.02.018
    • (2008) Exp Cell Res , vol.314 , pp. 1869-1880
    • Håkelien, A.M.1    Delbarre, E.2    Gaustad, K.G.3    Buendia, B.4    Collas, P.5
  • 112
    • 0037161026 scopus 로고    scopus 로고
    • Association between altered expression of adipogenic factor SREBP1 in lipoatrophic adipose tissue from HIV-1-infected patients and abnormal adipocyte differentiation and insulin resistance
    • PMID:11937183
    • Bastard JP, Caron M, Vidal H, Jan V, Auclair M, Vigouroux C, Luboinski J, Laville M, Maachi M, Girard PM, et al. Association between altered expression of adipogenic factor SREBP1 in lipoatrophic adipose tissue from HIV-1-infected patients and abnormal adipocyte differentiation and insulin resistance. Lancet 2002; 359:1026-31; PMID:11937183; http://dx.doi.org/10.1016/S0140-6736(02)08094-7
    • (2002) Lancet , vol.359 , pp. 1026-1031
    • Bastard, J.P.1    Caron, M.2    Vidal, H.3    Jan, V.4    Auclair, M.5    Vigouroux, C.6    Luboinski, J.7    Laville, M.8    Maachi, M.9    Girard, P.M.10
  • 113
    • 84873730295 scopus 로고    scopus 로고
    • Sp1 transcription factor interaction with accumulated prelamin a impairs adipose lineage differentiation in human mesenchymal stem cells: Essential role of sp1 in the integrity of lipid vesicles
    • PMID:23197810
    • Ruiz de Eguino G, Infante A, Schlangen K, Aransay AM, Fullaondo A, Soriano M, García-Verdugo JM, Martín AG, Rodríguez CI. Sp1 transcription factor interaction with accumulated prelamin a impairs adipose lineage differentiation in human mesenchymal stem cells: essential role of sp1 in the integrity of lipid vesicles. Stem Cells Transl Med 2012; 1:309-21; PMID:23197810; http://dx.doi.org/10.5966/sctm.2011-0010
    • (2012) Stem Cells Transl Med , vol.1 , pp. 309-321
    • Ruiz De Eguino, G.1    Infante, A.2    Schlangen, K.3    Aransay, A.M.4    Fullaondo, A.5    Soriano, M.6    García-Verdugo, J.M.7    Martín, A.G.8    Rodríguez, C.I.9
  • 114
    • 84905274646 scopus 로고    scopus 로고
    • Mineralocorticoid receptor antagonism induces browning of white adipose tissue through impairment of autophagy and prevents adipocyte dysfunction in high-fat-diet-fed mice
    • PMID:24806198
    • Armani A, Cinti F, Marzolla V, Morgan J, Cranston GA, Antelmi A, Carpinelli G, Canese R, Pagotto U, Quarta C, et al. Mineralocorticoid receptor antagonism induces browning of white adipose tissue through impairment of autophagy and prevents adipocyte dysfunction in high-fat-diet-fed mice. FASEB J 2014; 28:3745-57; PMID:24806198; http://dx.doi.org/10.1096/fj.13-245415
    • (2014) FASEB J , vol.28 , pp. 3745-3757
    • Armani, A.1    Cinti, F.2    Marzolla, V.3    Morgan, J.4    Cranston, G.A.5    Antelmi, A.6    Carpinelli, G.7    Canese, R.8    Pagotto, U.9    Quarta, C.10
  • 115
    • 84894086580 scopus 로고    scopus 로고
    • Deregulation of Fragile X-related protein 1 by the lipodystrophic lamin A p.R482W mutation elicits a myogenic gene expression program in preadipocytes
    • PMID:24108105
    • Oldenburg AR, Delbarre E, Thiede B, Vigouroux C, Collas P. Deregulation of Fragile X-related protein 1 by the lipodystrophic lamin A p.R482W mutation elicits a myogenic gene expression program in preadipocytes. Hum Mol Genet 2014; 23:1151-62; PMID:24108105; http://dx.doi.org/10.1093/hmg/ddt509
    • (2014) Hum Mol Genet , vol.23 , pp. 1151-1162
    • Oldenburg, A.R.1    Delbarre, E.2    Thiede, B.3    Vigouroux, C.4    Collas, P.5
  • 117
    • 84873349707 scopus 로고    scopus 로고
    • Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome
    • PMID:23152449
    • McCord RP, Nazario-Toole A, Zhang H, Chines PS, Zhan Y, Erdos MR, Collins FS, Dekker J, Cao K. Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome. Genome Res 2013; 23:260-9; PMID:23152449; http://dx.doi.org/10.1101/gr.138032.112
    • (2013) Genome Res , vol.23 , pp. 260-269
    • McCord, R.P.1    Nazario-Toole, A.2    Zhang, H.3    Chines, P.S.4    Zhan, Y.5    Erdos, M.R.6    Collins, F.S.7    Dekker, J.8    Cao, K.9
  • 118
    • 77954176613 scopus 로고    scopus 로고
    • Loss of a DNA binding site within the tail of prelamin A contributes to altered heterochromatin anchorage by progerin
    • PMID:20580717
    • Bruston F, Delbarre E, Ostlund C, Worman HJ, Buendia B, Duband-Goulet I. Loss of a DNA binding site within the tail of prelamin A contributes to altered heterochromatin anchorage by progerin. FEBS Lett 2010; 584:2999-3004; PMID:20580717; http://dx.doi.org/10.1016/j.febslet.2010.05.032
    • (2010) FEBS Lett , vol.584 , pp. 2999-3004
    • Bruston, F.1    Delbarre, E.2    Ostlund, C.3    Worman, H.J.4    Buendia, B.5    Duband-Goulet, I.6
  • 119
    • 84870506099 scopus 로고    scopus 로고
    • Resveratrol rescues SIRT1-dependent adult stem cell decline and alleviates progeroid features in laminopathy-based progeria
    • PMID:23217256
    • Liu B, Ghosh S, Yang X, Zheng H, Liu X, Wang Z, Jin G, Zheng B, Kennedy BK, Suh Y, et al. Resveratrol rescues SIRT1-dependent adult stem cell decline and alleviates progeroid features in laminopathy-based progeria. Cell Metab 2012; 16:738-50; PMID:23217256; http://dx.doi.org/10.1016/j.cmet.2012.11.007
    • (2012) Cell Metab , vol.16 , pp. 738-750
    • Liu, B.1    Ghosh, S.2    Yang, X.3    Zheng, H.4    Liu, X.5    Wang, Z.6    Jin, G.7    Zheng, B.8    Kennedy, B.K.9    Suh, Y.10
  • 120
    • 36248954501 scopus 로고    scopus 로고
    • SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation
    • PMID:18004385
    • Vaquero A, Scher M, Erdjument-Bromage H, Tempst P, Serrano L, Reinberg D. SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature 2007; 450:440-4; PMID:18004385; http://dx.doi.org/10.1038/nature06268
    • (2007) Nature , vol.450 , pp. 440-444
    • Vaquero, A.1    Scher, M.2    Erdjument-Bromage, H.3    Tempst, P.4    Serrano, L.5    Reinberg, D.6
  • 121
    • 84878738557 scopus 로고    scopus 로고
    • Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model
    • PMID:23695662
    • Liu B, Wang Z, Zhang L, Ghosh S, Zheng H, Zhou Z. Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model. Nat Commun 2013; 4:1868; PMID:23695662; http://dx.doi.org/10.1038/ncomms2885
    • (2013) Nat Commun , vol.4 , pp. 1868
    • Liu, B.1    Wang, Z.2    Zhang, L.3    Ghosh, S.4    Zheng, H.5    Zhou, Z.6
  • 123
    • 80053150156 scopus 로고    scopus 로고
    • The accumulation of un-repairable DNA damage in laminopathy progeria fibroblasts is caused by ROS generation and is prevented by treatment with N-acetyl cysteine
    • PMID:21807766
    • Richards SA, Muter J, Ritchie P, Lattanzi G, Hutchison CJ. The accumulation of un-repairable DNA damage in laminopathy progeria fibroblasts is caused by ROS generation and is prevented by treatment with N-acetyl cysteine. Hum Mol Genet 2011; 20:3997-4004; PMID:21807766; http://dx.doi.org/10.1093/hmg/ddr327
    • (2011) Hum Mol Genet , vol.20 , pp. 3997-4004
    • Richards, S.A.1    Muter, J.2    Ritchie, P.3    Lattanzi, G.4    Hutchison, C.J.5
  • 125
    • 79955641987 scopus 로고    scopus 로고
    • Osteoblasts from a mandibuloacral dysplasia patient induce human blood precursors to differentiate into active osteoclasts
    • PMID:21419220
    • Avnet S, Pallotta R, Perut F, Baldini N, Pittis MG, Saponari A, Lucarelli E, Dozza B, Greggi T, Maraldi NM, et al. Osteoblasts from a mandibuloacral dysplasia patient induce human blood precursors to differentiate into active osteoclasts. Biochim Biophys Acta 2011; 1812:711-8; PMID:21419220; http://dx.doi.org/10.1016/j.bbadis.2011.03.006
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 711-718
    • Avnet, S.1    Pallotta, R.2    Perut, F.3    Baldini, N.4    Pittis, M.G.5    Saponari, A.6    Lucarelli, E.7    Dozza, B.8    Greggi, T.9    Maraldi, N.M.10
  • 127
    • 84858335346 scopus 로고    scopus 로고
    • Replication factor C1, the large subunit of replication factor C, is proteolytically truncated in Hutchinson-Gilford progeria syndrome
    • PMID:22168243
    • Tang H, Hilton B, Musich PR, Fang DZ, Zou Y. Replication factor C1, the large subunit of replication factor C, is proteolytically truncated in Hutchinson-Gilford progeria syndrome. Aging Cell 2012; 11:363-5; PMID:22168243; http://dx.doi.org/10.1111/j.1474-9726.2011.00779.x
    • (2012) Aging Cell , vol.11 , pp. 363-365
    • Tang, H.1    Hilton, B.2    Musich, P.R.3    Fang, D.Z.4    Zou, Y.5
  • 129
    • 84881259855 scopus 로고    scopus 로고
    • The contrasting roles of lamin B1 in cellular aging and human disease
    • PMID:23873483
    • Dreesen O, Ong PF, Chojnowski A, Colman A. The contrasting roles of lamin B1 in cellular aging and human disease. Nucleus 2013; 4:283-90; PMID:23873483; http://dx.doi.org/10.4161/nucl.25808
    • (2013) Nucleus , vol.4 , pp. 283-290
    • Dreesen, O.1    Ong, P.F.2    Chojnowski, A.3    Colman, A.4
  • 130
    • 84857997652 scopus 로고    scopus 로고
    • B-type lamins and their elusive roles in metazoan cell proliferation and senescence
    • PMID:22343942
    • Hutchison CJ. B-type lamins and their elusive roles in metazoan cell proliferation and senescence. EMBO J 2012; 31:1058-9; PMID:22343942; http://dx.doi.org/10.1038/emboj.2012.39
    • (2012) EMBO J , vol.31 , pp. 1058-1059
    • Hutchison, C.J.1
  • 132
    • 79959359806 scopus 로고    scopus 로고
    • Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein
    • PMID:21327084
    • Clayton P, Fischer B, Mann A, Mansour S, Rossier E, Veen M, Lang C, Baasanjav S, Kieslich M, Brossuleit K, et al. Mutations causing Greenberg dysplasia but not Pelger anomaly uncouple enzymatic from structural functions of a nuclear membrane protein. Nucleus 2010; 1:354-66; PMID:21327084; http://dx.doi.org/10.4161/nucl.1.4.12435
    • (2010) Nucleus , vol.1 , pp. 354-366
    • Clayton, P.1    Fischer, B.2    Mann, A.3    Mansour, S.4    Rossier, E.5    Veen, M.6    Lang, C.7    Baasanjav, S.8    Kieslich, M.9    Brossuleit, K.10
  • 133
    • 84856951638 scopus 로고    scopus 로고
    • DelK32-lamin A/C has abnormal location and induces incomplete tissue maturation and severe metabolic defects leading to premature death
    • PMID:22090424
    • Bertrand AT, Renou L, Papadopoulos A, Beuvin M, Lacène E, Massart C, Ottolenghi C, Decostre V, Maron S, Schlossarek S, et al. DelK32-lamin A/C has abnormal location and induces incomplete tissue maturation and severe metabolic defects leading to premature death. Hum Mol Genet 2012; 21:1037-48; PMID:22090424; http://dx.doi.org/10.1093/hmg/ddr534
    • (2012) Hum Mol Genet , vol.21 , pp. 1037-1048
    • Bertrand, A.T.1    Renou, L.2    Papadopoulos, A.3    Beuvin, M.4    Lacène, E.5    Massart, C.6    Ottolenghi, C.7    Decostre, V.8    Maron, S.9    Schlossarek, S.10
  • 134
    • 84867736667 scopus 로고    scopus 로고
    • Nuclear lamina defects cause ATM-dependent NF-κB activation and link accelerated aging to a systemic inflammatory response
    • PMID:23019125
    • Osorio FG, Bárcena C, Soria-Valles C, Ramsay AJ, de Carlos F, Cobo J, Fueyo A, Freije JM, López-Otín C. Nuclear lamina defects cause ATM-dependent NF-κB activation and link accelerated aging to a systemic inflammatory response. Genes Dev 2012; 26:2311-24; PMID:23019125; http://dx.doi.org/10.1101/gad.197954.112
    • (2012) Genes Dev , vol.26 , pp. 2311-2324
    • Osorio, F.G.1    Bárcena, C.2    Soria-Valles, C.3    Ramsay, A.J.4    De Carlos, F.5    Cobo, J.6    Fueyo, A.7    Freije, J.M.8    López-Otín, C.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.