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Volumn 45, Issue 1, 2005, Pages 1-16

Implications for nuclear organization and gene transcription of lamin A/C specific mutations

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EID: 28444458423     PISSN: 00652571     EISSN: None     Source Type: Book Series    
DOI: 10.1016/j.advenzreg.2005.02.016     Document Type: Article
Times cited : (5)

References (70)
  • 1
    • 0041919374 scopus 로고    scopus 로고
    • Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia
    • A.K. Agarwal, J.P. Fryns, R.J. Auchus, and A. Garg Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia Hum Mol Genet 12 2003 1995 2001
    • (2003) Hum Mol Genet , vol.12 , pp. 1995-2001
    • Agarwal, A.K.1    Fryns, J.P.2    Auchus, R.J.3    Garg, A.4
  • 2
    • 0030948576 scopus 로고    scopus 로고
    • Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains
    • V. Arranz, F. Harper, Y. Florentin, E. Puvion, M. Kress, and M. Ernoult-Lange Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains Mol Cell Biol 17 1997 2116 2126
    • (1997) Mol Cell Biol , vol.17 , pp. 2116-2126
    • Arranz, V.1    Harper, F.2    Florentin, Y.3    Puvion, E.4    Kress, M.5    Ernoult-Lange, M.6
  • 3
    • 0037447893 scopus 로고    scopus 로고
    • Effects of expressing lamin a mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells
    • K. Bechert, M. Lagos-Quintana, J. Harborth, K. Weber, and M. Osborn Effects of expressing lamin A mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells Exp Cell Res 286 2003 75 86
    • (2003) Exp Cell Res , vol.286 , pp. 75-86
    • Bechert, K.1    Lagos-Quintana, M.2    Harborth, J.3    Weber, K.4    Osborn, M.5
  • 4
    • 0033083793 scopus 로고    scopus 로고
    • Dynamic repositioning of genes in the nucleus of lymphocytes preparing for cell division
    • K.E. Brown, J. Baxter, D. Graf, M. Merkenschlager, and A.G. Fisher Dynamic repositioning of genes in the nucleus of lymphocytes preparing for cell division Mol Cell 3 1999 207 217
    • (1999) Mol Cell , vol.3 , pp. 207-217
    • Brown, K.E.1    Baxter, J.2    Graf, D.3    Merkenschlager, M.4    Fisher, A.G.5
  • 5
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • B. Burke, and C.L. Stewart Life at the edge: the nuclear envelope and human disease Nat Rev Mol Cell Biol 3 2002 575 585
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 6
    • 0034059075 scopus 로고    scopus 로고
    • Nuclear lamin A/C R482Q mutation in canadian kindreds with Dunnigan-type familial partial lipodystrophy
    • H. Cao, and R.A. Hegele Nuclear lamin A/C R482Q mutation in canadian kindreds with Dunnigan-type familial partial lipodystrophy Hum Mol Genet 9 2000 109 112
    • (2000) Hum Mol Genet , vol.9 , pp. 109-112
    • Cao, H.1    Hegele, R.A.2
  • 7
    • 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
    • C. Capanni, V. Cenni, E. Mattioli, P. Sabatelli, A. Ognibene, M. Columbaro, V.K. Parnaik, M. Wehnert, N.M. Maraldi, S. Squarzoni, and G. Lattanzi 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 291 2003 122 134
    • (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    Lattanzi, G.11
  • 9
    • 0034987343 scopus 로고    scopus 로고
    • The HIV protease inhibitor indinavir impairs sterol regulatory element-binding protein-1 intranuclear localization, inhibits preadipocyte differentiation, and induces insulin resistance
    • M. Caron, M. Auclair, C. Vigouroux, M. Glorian, C. Forest, and J. Capeau The HIV protease inhibitor indinavir impairs sterol regulatory element-binding protein-1 intranuclear localization, inhibits preadipocyte differentiation, and induces insulin resistance Diabetes 50 2001 1378 1388
    • (2001) Diabetes , vol.50 , pp. 1378-1388
    • Caron, M.1    Auclair, M.2    Vigouroux, C.3    Glorian, M.4    Forest, C.5    Capeau, J.6
  • 10
    • 0037313618 scopus 로고    scopus 로고
    • Coordinated regulation of life and death by RB
    • B.N. Chau, and J.Y. Wang Coordinated regulation of life and death by RB Nat Rev Cancer 3 2003 130 138
    • (2003) Nat Rev Cancer , vol.3 , pp. 130-138
    • Chau, B.N.1    Wang, J.Y.2
  • 11
    • 0035146907 scopus 로고    scopus 로고
    • Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina
    • M. Cohen, K.K. Lee, K.L. Wilson, and Y. Gruenbaum Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina Trends Biochem Sci 26 2001 41 47
    • (2001) Trends Biochem Sci , vol.26 , pp. 41-47
    • Cohen, M.1    Lee, K.K.2    Wilson, K.L.3    Gruenbaum, Y.4
  • 13
    • 0029582994 scopus 로고
    • The nuclear matrix and the regulation of chromatin organization and function
    • JR. Davie The nuclear matrix and the regulation of chromatin organization and function Int Rev Cytol 162 1995 191 250
    • (1995) Int Rev Cytol , vol.162 , pp. 191-250
    • Davie, J.R.1
  • 16
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin a mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • C. Favreau, E. Dubosclard, C. Ostlund, C. Vigouroux, J. Capeau, M. Wehnert, D. Higuet, H.J. Worman, J.C. Courvalin, and B. Buendia Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy Exp Cell Res 282 2003 14 23
    • (2003) Exp Cell Res , vol.282 , pp. 14-23
    • Favreau, C.1    Dubosclard, E.2    Ostlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6    Higuet, D.7    Worman, H.J.8    Courvalin, J.C.9    Buendia, B.10
  • 17
    • 0033950898 scopus 로고    scopus 로고
    • Pushing the envelope on lipodystrophy
    • J.S. Flier Pushing the envelope on lipodystrophy Nat Genet 24 2000 103 104
    • (2000) Nat Genet , vol.24 , pp. 103-104
    • Flier, J.S.1
  • 19
    • 0035834009 scopus 로고    scopus 로고
    • Nuclear relocation of a transactivator subunit precedes target gene activation
    • C. Francastel, W. Magis, and M. Groudine Nuclear relocation of a transactivator subunit precedes target gene activation Proc Natl Acad Sci USA 98 2001 12120 12125
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12120-12125
    • Francastel, C.1    Magis, W.2    Groudine, M.3
  • 21
    • 0032959251 scopus 로고    scopus 로고
    • Adipose tissue distribution pattern in patients with familial partial lipodystrophy (Dunnigan variety)
    • A. Garg, R.M. Peshock, and J.L. Fleckenstein Adipose tissue distribution pattern in patients with familial partial lipodystrophy (Dunnigan variety) J Clin Endocrinol Metab 84 1999 170 174
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 170-174
    • Garg, A.1    Peshock, R.M.2    Fleckenstein, J.L.3
  • 22
    • 0033925932 scopus 로고    scopus 로고
    • Review: Nuclear lamins-structural proteins with fundamental functions
    • Y. Gruenbaum, K.L. Wilson, A. Harel, M. Goldberg, and M. Cohen Review: nuclear lamins-structural proteins with fundamental functions J Struct Biol 129 2000 313 323
    • (2000) J Struct Biol , vol.129 , pp. 313-323
    • Gruenbaum, Y.1    Wilson, K.L.2    Harel, A.3    Goldberg, M.4    Cohen, M.5
  • 23
    • 0033973777 scopus 로고    scopus 로고
    • The envelope, please: Nuclear lamins and disease
    • R.A. Hegele The envelope, please: nuclear lamins and disease Nat Med 6 2000 136 137
    • (2000) Nat Med , vol.6 , pp. 136-137
    • Hegele, R.A.1
  • 24
    • 0035090666 scopus 로고    scopus 로고
    • Molecular basis of partial lipodystrophy and prospects for therapy
    • R.A. Hegele Molecular basis of partial lipodystrophy and prospects for therapy Trends Mol Med 7 2001 121 126
    • (2001) Trends Mol Med , vol.7 , pp. 121-126
    • Hegele, R.A.1
  • 25
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • J.M. Holaska, K.K. Lee, A.K. Kowalski, and K.L. Wilson Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro J Biol Chem 278 2003 6969 6975
    • (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
  • 26
    • 0043172367 scopus 로고    scopus 로고
    • Effect of pathogenic mis-sense mutations in lamin a on its interaction with emerin in vivo
    • I. Holt, C. Ostlund, C.L. Stewart, N. Man, H.J. Worman, and G.E. Morris Effect of pathogenic mis-sense mutations in lamin A on its interaction with emerin in vivo J Cell Sci 116 2003 3027 3035
    • (2003) J Cell Sci , vol.116 , pp. 3027-3035
    • Holt, I.1    Ostlund, C.2    Stewart, C.L.3    Man, N.4    Worman, H.J.5    Morris, G.E.6
  • 27
    • 0036864411 scopus 로고    scopus 로고
    • Sterol regulatory element-binding proteins: Transcriptional activators of lipid synthesis
    • J.D. Horton Sterol regulatory element-binding proteins: transcriptional activators of lipid synthesis Biochem Soc Trans 30 2002 1091
    • (2002) Biochem Soc Trans , vol.30 , pp. 1091
    • Horton, J.D.1
  • 28
    • 0038022718 scopus 로고    scopus 로고
    • Targeting genes and transcription factors to segregated nuclear compartments
    • Y. Isogai, and R. Tjian Targeting genes and transcription factors to segregated nuclear compartments Curr Opin Cell Biol 15 2003 296 303
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 296-303
    • Isogai, Y.1    Tjian, R.2
  • 29
    • 0034669029 scopus 로고    scopus 로고
    • Nuclear organization of DNA replication in primary mammalian cells
    • B.K. Kennedy, D.A. Barbie, M. Classon, N. Dyson, and E. Harlow Nuclear organization of DNA replication in primary mammalian cells Genes Dev 14 2000 2855 2868
    • (2000) Genes Dev , vol.14 , pp. 2855-2868
    • Kennedy, B.K.1    Barbie, D.A.2    Classon, M.3    Dyson, N.4    Harlow, E.5
  • 30
    • 0033152491 scopus 로고    scopus 로고
    • Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes
    • J. Koipally, A. Renold, J. Kim, and K. Georgopoulos Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes EMBO J 18 1999 3090 3100
    • (1999) EMBO J , vol.18 , pp. 3090-3100
    • Koipally, J.1    Renold, A.2    Kim, J.3    Georgopoulos, K.4
  • 32
    • 0037049554 scopus 로고    scopus 로고
    • Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription
    • R.I. Kumaran, B. Muralikrishna, and V.K. Parnaik Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription J Cell Biol 159 2002 783 793
    • (2002) J Cell Biol , vol.159 , pp. 783-793
    • Kumaran, R.I.1    Muralikrishna, B.2    Parnaik, V.K.3
  • 34
    • 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
    • J. Liu, T.R. Ben-Shahar, D. Riemer, M. Treinin, P. Spann, K. Weber, A. Fire, and Y. Gruenbaum Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression, and spatial organization of nuclear pore complexes Mol Biol Cell 11 2000 3937 3947
    • (2000) Mol Biol Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Ben-Shahar, T.R.2    Riemer, D.3    Treinin, M.4    Spann, P.5    Weber, K.6    Fire, A.7    Gruenbaum, Y.8
  • 35
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function (s) essential for chromosome segregation and cell division in Caenorhabditis elegans
    • J. Liu, K.K. Lee, M. Segura-Totten, E. Neufeld, K.L. Wilson, and Y. Gruenbaum MAN1 and emerin have overlapping function (s) essential for chromosome segregation and cell division in Caenorhabditis elegans Proc Natl Acad Sci USA 100 2003 4598 4603
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4598-4603
    • Liu, J.1    Lee, K.K.2    Segura-Totten, M.3    Neufeld, E.4    Wilson, K.L.5    Gruenbaum, Y.6
  • 36
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin a and SREBP1: Implications for partial lipodystrophy and other laminopathies
    • D.J. Lloyd, R.C. Trembath, and S. Shackleton A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies Hum Mol Genet 11 2002 769 777
    • (2002) Hum Mol Genet , vol.11 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 39
    • 1842854443 scopus 로고    scopus 로고
    • Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein
    • E. Markiewicz, T. Dechat, R. Foisner, R.A. Quinlan, and C.J. Hutchison Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein Mol Biol Cell 13 2002 4401 4413
    • (2002) Mol Biol Cell , vol.13 , pp. 4401-4413
    • Markiewicz, E.1    Dechat, T.2    Foisner, R.3    Quinlan, R.A.4    Hutchison, C.J.5
  • 40
    • 0035201307 scopus 로고    scopus 로고
    • The structure and function of nuclear lamins: Implications for disease
    • R.D. Moir, and T.P. Spann The structure and function of nuclear lamins: implications for disease Cell Mol Life Sci 58 2001 1748 1757
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1748-1757
    • Moir, R.D.1    Spann, T.P.2
  • 41
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins a and B1: Different pathways of assembly during nuclear envelope formation in living cells
    • R.D. Moir, M. Yoon, S. Khuon, and R.D. Goldman Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells J Cell Biol 151 2000 1155 1168
    • (2000) J Cell Biol , vol.151 , pp. 1155-1168
    • Moir, R.D.1    Yoon, M.2    Khuon, S.3    Goldman, R.D.4
  • 42
    • 0035833262 scopus 로고    scopus 로고
    • Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter
    • W.G. Muller, D. Walker, G.L. Hager, and J.G. McNally Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter J Cell Biol 154 2001 33 48
    • (2001) J Cell Biol , vol.154 , pp. 33-48
    • Muller, W.G.1    Walker, D.2    Hager, G.L.3    McNally, J.G.4
  • 44
    • 0035697055 scopus 로고    scopus 로고
    • Properties of lamin a mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy
    • C. Östlund, G. Bonne, K. Schwartz, and H.J. Worman Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy J Cell Sci 114 2001 4435 4445
    • (2001) J Cell Sci , vol.114 , pp. 4435-4445
    • Östlund, C.1    Bonne, G.2    Schwartz, K.3    Worman, H.J.4
  • 45
    • 0034100040 scopus 로고    scopus 로고
    • Half a century of "the nuclear matrix"
    • T. Pederson Half a century of "the nuclear matrix" Mol Biol Cell 11 2000 799 805
    • (2000) Mol Biol Cell , vol.11 , pp. 799-805
    • Pederson, T.1
  • 48
    • 0035696932 scopus 로고    scopus 로고
    • Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy
    • W.H. Raharjo, P. Enarson, T. Sullivan, C.L. Stewart, and B. Burke Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy J Cell Sci 114 2001 4447 4457
    • (2001) J Cell Sci , vol.114 , pp. 4447-4457
    • Raharjo, W.H.1    Enarson, P.2    Sullivan, T.3    Stewart, C.L.4    Burke, B.5
  • 49
  • 50
    • 0037194732 scopus 로고    scopus 로고
    • Chromosomal clustering of muscle-expressed genes in Caenorhabditis elegans
    • P.J. Roy, J.M. Stuart, J. Lund, and S.K. Kim Chromosomal clustering of muscle-expressed genes in Caenorhabditis elegans Nature 418 2002 975 979
    • (2002) Nature , vol.418 , pp. 975-979
    • Roy, P.J.1    Stuart, J.M.2    Lund, J.3    Kim, S.K.4
  • 52
    • 0028831126 scopus 로고
    • Lamin a precursor is localized to intranuclear foci
    • A.M. Sasseville, and Y. Raymond Lamin A precursor is localized to intranuclear foci J Cell Sci 108 1995 273 285
    • (1995) J Cell Sci , vol.108 , pp. 273-285
    • Sasseville, A.M.1    Raymond, Y.2
  • 53
    • 2342463022 scopus 로고    scopus 로고
    • BAF: Roles in chromatin, nuclear structure and retrovirus
    • M. Segura-Totten, and K.L. Wilson BAF: roles in chromatin, nuclear structure and retrovirus Trends Cell Biol 14 2004 261 266
    • (2004) Trends Cell Biol , vol.14 , pp. 261-266
    • Segura-Totten, M.1    Wilson, K.L.2
  • 54
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • M. Segura-Totten, A.K. Kowalski, R. Craigie, and K.L. Wilson Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly J Cell Biol 158 2002 475 485
    • (2002) J Cell Biol , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 56
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells
    • T. Shimi, T. Koujin, M. Segura-Totten, K.L. Wilson, T. Haraguchi, and Y. Hiraoka Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells J Struct Biol 147 2004 31 41
    • (2004) J Struct Biol , vol.147 , pp. 31-41
    • Shimi, T.1    Koujin, T.2    Segura-Totten, M.3    Wilson, K.L.4    Haraguchi, T.5    Hiraoka, Y.6
  • 58
    • 0037128211 scopus 로고    scopus 로고
    • Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription
    • T.P. Spann, A.E. Goldman, C. Wang, S. Huang, and R.D. Goldman Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription J Cell Biol 156 2002 603 608
    • (2002) J Cell Biol , vol.156 , pp. 603-608
    • Spann, T.P.1    Goldman, A.E.2    Wang, C.3    Huang, S.4    Goldman, R.D.5
  • 59
    • 0033912260 scopus 로고    scopus 로고
    • Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C
    • R.A. Speckman, A. Garg, F. Du, L. Bennett, R. Veile, E. Arioglu, S.I. Taylor, M. Lovett, and A.M. Bowcock Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C Am J Hum Genet 66 2000 1192 1198
    • (2000) Am J Hum Genet , vol.66 , pp. 1192-1198
    • Speckman, R.A.1    Garg, A.2    Du, F.3    Bennett, L.4    Veile, R.5    Arioglu, E.6    Taylor, S.I.7    Lovett, M.8    Bowcock, A.M.9
  • 62
    • 0033200389 scopus 로고    scopus 로고
    • Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation
    • Q.Q. Tang, and M.D. Lane Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation Genes Dev 13 1999 2231 2241
    • (1999) Genes Dev , vol.13 , pp. 2231-2241
    • Tang, Q.Q.1    Lane, M.D.2
  • 65
    • 16244388206 scopus 로고    scopus 로고
    • A-type lamin-linked lipodystrophies
    • C. Vigouroux, and J. Capeau A-type lamin-linked lipodystrophies Novartis Found Symp 264 2005 166 177
    • (2005) Novartis Found Symp , vol.264 , pp. 166-177
    • Vigouroux, C.1    Capeau, J.2
  • 66
    • 0035691915 scopus 로고    scopus 로고
    • Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene
    • C. Vigouroux, M. Auclair, E. Dubosclard, M. Pouchelet, J. Capeau, J.C. Courvalin, and B. Buendia Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene J Cell Sci 114 2001 4459 4468
    • (2001) J Cell Sci , vol.114 , pp. 4459-4468
    • Vigouroux, C.1    Auclair, M.2    Dubosclard, E.3    Pouchelet, M.4    Capeau, J.5    Courvalin, J.C.6    Buendia, B.7
  • 68
    • 0034176682 scopus 로고    scopus 로고
    • The nuclear envelope, muscular dystrophy and gene expression
    • K.L. Wilson The nuclear envelope, muscular dystrophy and gene expression Trends Cell Biol 10 2000 125 129
    • (2000) Trends Cell Biol , vol.10 , pp. 125-129
    • Wilson, K.L.1
  • 69
    • 0035831041 scopus 로고    scopus 로고
    • Lamins and disease: Insights into nuclear infrastructure
    • K.L. Wilson, M.S. Zastrow, and K.K. Lee Lamins and disease: insights into nuclear infrastructure Cell 104 2001 647 660
    • (2001) Cell , vol.104 , pp. 647-660
    • Wilson, K.L.1    Zastrow, M.S.2    Lee, K.K.3
  • 70
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • M.S. Zastrow, S. Vlcek, and K.L. Wilson Proteins that bind A-type lamins: integrating isolated clues J Cell Sci 117 2004 979 987
    • (2004) J Cell Sci , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3


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