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Volumn 246, Issue , 2005, Pages 231-279

Nuclear envelope, nuclear lamina, and inherited disease

Author keywords

Aging; Cardiomyopathy; Lamin; Lipodystrophy; Muscular dystrophy; Nuclear envelope; Peripheral neuropathy; Progeria

Indexed keywords

CYTOPLASM PROTEIN; LAMIN; LAMIN A; LAMIN B; MUTANT PROTEIN; NUCLEAR PROTEIN;

EID: 25144515509     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(05)46006-4     Document Type: Review
Times cited : (99)

References (306)
  • 1
    • 0038319891 scopus 로고
    • Isolation of nuclear pore complexes in association with a lamina
    • Aaronson R.P., and Blobel G. Isolation of nuclear pore complexes in association with a lamina Proc. Natl. Acad. Sci. USA 72 1975 1007 1011
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1007-1011
    • Aaronson, R.P.1    Blobel, G.2
  • 2
    • 0031009827 scopus 로고    scopus 로고
    • Chromatin dynamics in interphase nuclei and its implications for nuclear structure
    • Abney J.R., Cutler B., Fillbach M.L., Axelrod D., and Scalettar B.A. Chromatin dynamics in interphase nuclei and its implications for nuclear structure J. Cell Biol. 137 1997 1459 1468
    • (1997) J. Cell Biol. , vol.137 , pp. 1459-1468
    • Abney, J.R.1    Cutler, B.2    Fillbach, M.L.3    Axelrod, D.4    Scalettar, B.A.5
  • 3
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi U., Cohn J., Buhle L., and Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments Nature 323 1986 560 564
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 4
    • 0041919374 scopus 로고    scopus 로고
    • Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia
    • Agarwal A.K., Fryns J.P., Auchus R.J., and Garg A. 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
  • 5
    • 0030297086 scopus 로고    scopus 로고
    • Change of karyoskeleton during mammalian spermatogenesis: Expression pattern of nuclear lamin C2 and its regulation
    • Alsheimer M., and Benavente R. Change of karyoskeleton during mammalian spermatogenesis: Expression pattern of nuclear lamin C2 and its regulation Exp. Cell Res. 228 1996 181 188
    • (1996) Exp. Cell Res. , vol.228 , pp. 181-188
    • Alsheimer, M.1    Benavente, R.2
  • 8
    • 0019467367 scopus 로고
    • Homozygous form of the Pelger-Huët leukocyte anomaly in man
    • Aznar J., and Vaya A. Homozygous form of the Pelger-Huët leukocyte anomaly in man Acta Haematol. 66 1981 59 62
    • (1981) Acta Haematol. , vol.66 , pp. 59-62
    • Aznar, J.1    Vaya, A.2
  • 10
    • 0033571036 scopus 로고    scopus 로고
    • Mutations in ooc-5 and ooc-3 disrupt oocyte formation and the reestablishment of asymmetric PAR protein localization in two-cell Caenorhabditis elegans embryos
    • Basham S.E., and Rose L.S. Mutations in ooc-5 and ooc-3 disrupt oocyte formation and the reestablishment of asymmetric PAR protein localization in two-cell Caenorhabditis elegans embryos Dev. Biol. 215 1999 253 263
    • (1999) Dev. Biol. , vol.215 , pp. 253-263
    • Basham, S.E.1    Rose, L.S.2
  • 11
    • 0035202870 scopus 로고    scopus 로고
    • The Caenorhabditis elegans polarity gene ooc-5 encodes a torsin-related protein of the AAA ATPase superfamily
    • Basham S.E., and Rose L.S. The Caenorhabditis elegans polarity gene ooc-5 encodes a torsin-related protein of the AAA ATPase superfamily Development 128 2001 4645 4656
    • (2001) Development , vol.128 , pp. 4645-4656
    • Basham, S.E.1    Rose, L.S.2
  • 12
    • 0037059611 scopus 로고    scopus 로고
    • Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina
    • Beaudouin J., Gerlich D., Daigle N., Eils R., and Ellenberg J. Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina Cell 108 2002 83 96
    • (2002) Cell , vol.108 , pp. 83-96
    • Beaudouin, J.1    Gerlich, D.2    Daigle, N.3    Eils, R.4    Ellenberg, J.5
  • 13
    • 0037447893 scopus 로고    scopus 로고
    • Effects of expressing lamin a mutant protein causing Emery-Dreifuss muscular dystrophy and familial partial lipodystrophy in HeLa cells
    • Bechert K., Lagos-Quintana M., Harborth J., Weber K., and Osborn M. 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
  • 14
    • 0024094640 scopus 로고
    • Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei
    • Beck L.A., Hosick T.J., and Sinensky M. Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei J. Cell Biol. 107 1988 1307 1316
    • (1988) J. Cell Biol. , vol.107 , pp. 1307-1316
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 15
    • 0025362748 scopus 로고
    • Isoprenylation is required for the processing of the lamin a precursor
    • Beck L.A., Hosick T.J., and Sinensky M. Isoprenylation is required for the processing of the lamin A precursor J. Cell Biol. 110 1990 1489 -99.
    • (1990) J. Cell Biol. , vol.110 , pp. 1489
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 16
    • 0038701027 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Navigating the channel
    • Bednenko J., Cingolani G., and Gerace L. Nucleocytoplasmic transport: Navigating the channel Traffic 4 2003 127 135
    • (2003) Traffic , vol.4 , pp. 127-135
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 21
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G., and Toniolo D. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy Nat. Genet. 8 1994 323 327
    • (1994) Nat. Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 24
    • 0036133645 scopus 로고    scopus 로고
    • 82nd ENMC international workshop, 5th international Emery-Dreifuss muscular dystrophy (EDMD) workshop, 1st Workshop of the MYO-CLUSTER project EUROMEN (European muscle envelope nucleopathies), 15-16 September 2000, Naarden, the Netherlands
    • Bonne G., Capeau J., De Visser M., Duboc D., Merlini L., Morris G.E., Muntoni F., Recan D., Sewry C., Squarzoni S., Stewart C., Talim B., van der Kooi A., Worman H., and Schwartz K. 82nd ENMC international workshop, 5th international Emery-Dreifuss muscular dystrophy (EDMD) workshop, 1st Workshop of the MYO-CLUSTER project EUROMEN (European muscle envelope nucleopathies), 15-16 September 2000, Naarden, The Netherlands Neuromuscul. Disord. 12 2002 187 194
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 187-194
    • Bonne, G.1    Capeau, J.2    De Visser, M.3    Duboc, D.4    Merlini, L.5    Morris, G.E.6    Muntoni, F.7    Recan, D.8    Sewry, C.9    Squarzoni, S.10    Stewart, C.11    Talim, B.12    Van Der Kooi, A.13    Worman, H.14    Schwartz, K.15
  • 26
    • 0035253606 scopus 로고    scopus 로고
    • The spatial organization of human chromosomes within the nuclei of normal and emerin-mutant cells
    • Boyle S., Gilchrist S., Bridger J.M., Mahy N.L., Ellis J.A., and Bickmore W.A. The spatial organization of human chromosomes within the nuclei of normal and emerin-mutant cells Hum. Mol. Genet. 10 2001 211 219
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 211-219
    • Boyle, S.1    Gilchrist, S.2    Bridger, J.M.3    Mahy, N.L.4    Ellis, J.A.5    Bickmore, W.A.6
  • 27
    • 0034620567 scopus 로고    scopus 로고
    • Lamin A/C gene mutation associated with dilated cardiomyopathy with variable skeletal muscle involvement
    • Brodsky G.L., Muntoni F., Miocic S., Sinagra G., Sewry C., and Mestroni L. Lamin A/C gene mutation associated with dilated cardiomyopathy with variable skeletal muscle involvement Circulation 101 2000 473 476
    • (2000) Circulation , vol.101 , pp. 473-476
    • Brodsky, G.L.1    Muntoni, F.2    Miocic, S.3    Sinagra, G.4    Sewry, C.5    Mestroni, L.6
  • 29
    • 7944232477 scopus 로고    scopus 로고
    • Decreased mechanical stiffness in LMNA-/- cells is caused by defective nucleo-cytoskeletal integrity: Implications for the development of laminopathies
    • Broers J.L., Peeters E.A., Kuijpers H.J., Endert J., Bouten C.V., Oomens C.W., Baaijens F.P., and Ramaekers F.C. Decreased mechanical stiffness in LMNA-/- cells is caused by defective nucleo-cytoskeletal integrity: Implications for the development of laminopathies Hum. Mol. Genet. 13 2004 2567 2580
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2567-2580
    • Broers, J.L.1    Peeters, E.A.2    Kuijpers, H.J.3    Endert, J.4    Bouten, C.V.5    Oomens, C.W.6    Baaijens, F.P.7    Ramaekers, F.C.8
  • 30
    • 14644442325 scopus 로고    scopus 로고
    • Both lamin a and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization
    • Broers J.L., Kuijpers H.J., Östlund C., Worman H.J., Endert J., and Ramaekers F.C. Both lamin A and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization Exp. Cell Res. 304 2005 582 592
    • (2005) Exp. Cell Res. , vol.304 , pp. 582-592
    • Broers, J.L.1    Kuijpers, H.J.2    Östlund, C.3    Worman, H.J.4    Endert, J.5    Ramaekers, F.C.6
  • 31
  • 32
    • 0018372184 scopus 로고
    • Human mutations affecting aging - a review
    • Brown W.T. Human mutations affecting aging - a review Mech. Aging Dev. 9 1979 325 336
    • (1979) Mech. Aging Dev. , vol.9 , pp. 325-336
    • Brown, W.T.1
  • 33
    • 0031561731 scopus 로고    scopus 로고
    • Domain-specific disassembly and reassembly of nuclear membranes during mitosis
    • Buendia B., and Courvalin J.C. Domain-specific disassembly and reassembly of nuclear membranes during mitosis Exp. Cell Res. 230 1997 133 144
    • (1997) Exp. Cell Res. , vol.230 , pp. 133-144
    • Buendia, B.1    Courvalin, J.C.2
  • 34
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • Burke B., and Stewart C.L. 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
  • 35
    • 0000108041 scopus 로고
    • Ein fall von dermatofibrosis lenticularis disseminata
    • Buschke A., and Ollendorff H. Ein fall von dermatofibrosis lenticularis disseminata Derm. Wochenschr. 86 1928 257 262
    • (1928) Derm. Wochenschr. , vol.86 , pp. 257-262
    • Buschke, A.1    Ollendorff, H.2
  • 36
    • 0035881480 scopus 로고    scopus 로고
    • Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: One binds BAF and the other binds DNA
    • Cai M., Huang Y., Ghirlando R., Wilson K.L., Craigie R., and Clore G.M. Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: One binds BAF and the other binds DNA EMBO J. 20 2001 4399 4407
    • (2001) EMBO J. , vol.20 , pp. 4399-4407
    • Cai, M.1    Huang, Y.2    Ghirlando, R.3    Wilson, K.L.4    Craigie, R.5    Clore, G.M.6
  • 37
    • 0014343407 scopus 로고
    • Melorheostosis. a report of the clinical, roentgenographic, and pathological findings in fourteen cases
    • Campbell C.J., Papademetriou T., and Bonfiglio M. Melorheostosis. A report of the clinical, roentgenographic, and pathological findings in fourteen cases J. Bone Joint Surg. Am. 50 1968 1281 1304
    • (1968) J. Bone Joint Surg. Am. , vol.50 , pp. 1281-1304
    • Campbell, C.J.1    Papademetriou, T.2    Bonfiglio, M.3
  • 39
    • 0034059075 scopus 로고    scopus 로고
    • Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy
    • Cao H., and Hegele R.A. 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
  • 40
    • 0038376023 scopus 로고    scopus 로고
    • LMNA is mutated in Hutchinson-Gilford progeria (MIM 176670) but not in Wiedemann-Rautenstrauch progeroid syndrome (MIM 264090)
    • Cao H., and Hegele R.A. LMNA is mutated in Hutchinson-Gilford progeria (MIM 176670) but not in Wiedemann-Rautenstrauch progeroid syndrome (MIM 264090) J. Hum. Genet. 48 2003 271 274
    • (2003) J. Hum. Genet. , vol.48 , pp. 271-274
    • Cao, H.1    Hegele, R.A.2
  • 41
    • 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
    • Capanni C., Cenni V., Mattioli E., Sabatelli P., Ognibene A., Columbaro M., Parnaik V.K., Wehnert M., Maraldi N.M., Squarzoni S., and Lattanzi G. 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
  • 44
    • 0027275334 scopus 로고
    • Stepwise reassembly of the nuclear envelope at the end of mitosis
    • Chaudhary N., and Courvalin J.C. Stepwise reassembly of the nuclear envelope at the end of mitosis J. Cell Biol. 122 1993 295 306
    • (1993) J. Cell Biol. , vol.122 , pp. 295-306
    • Chaudhary, N.1    Courvalin, J.C.2
  • 46
    • 0025991903 scopus 로고
    • Symmetry of bone lesions in osteopoikilosis: Report of 4 cases
    • Chigira M., Kato K., Mashio K., and Shinozaki T. Symmetry of bone lesions in osteopoikilosis: Report of 4 cases Acta Orthof. Scand. 62 1991 495 496
    • (1991) Acta Orthof. Scand. , vol.62 , pp. 495-496
    • Chigira, M.1    Kato, K.2    Mashio, K.3    Shinozaki, T.4
  • 47
    • 0036006293 scopus 로고    scopus 로고
    • Chromatin motion is constrained by association with nuclear compartments in human cells
    • Chubb J.R., Boyle S., Perry P., and Bickmore W.A. Chromatin motion is constrained by association with nuclear compartments in human cells Curr. Biol. 12 2002 439 445
    • (2002) Curr. Biol. , vol.12 , pp. 439-445
    • Chubb, J.R.1    Boyle, S.2    Perry, P.3    Bickmore, W.A.4
  • 49
    • 0035146907 scopus 로고    scopus 로고
    • Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina
    • Cohen M., Lee K.K., Wilson K.L., and Gruenbaum Y. 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
  • 50
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn R.D., and Campbell K.P. Molecular basis of muscular dystrophies Muscle Nerve 23 2000 1456 1471
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 52
    • 0026783801 scopus 로고
    • The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase
    • Courvalin J.C., Segil N., Blobel G., and Worman H.J. The lamin B receptor of the inner nuclear membrane undergoes mitosis-specific phosphorylation and is a substrate for p34cdc2-type protein kinase J. Biol. Chem. 267 1992 19035 19038
    • (1992) J. Biol. Chem. , vol.267 , pp. 19035-19038
    • Courvalin, J.C.1    Segil, N.2    Blobel, G.3    Worman, H.J.4
  • 53
    • 0035316574 scopus 로고    scopus 로고
    • Chromosome territories, nuclear architecture and gene regulation in mammalian cells
    • Cremer T., and Cremer C. Chromosome territories, nuclear architecture and gene regulation in mammalian cells Nat. Rev. Genet. 2 2001 292 301
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 292-301
    • Cremer, T.1    Cremer, C.2
  • 55
    • 36348978046 scopus 로고    scopus 로고
    • The nuclear pore complex: Disease associations and functional correlations
    • Cronshaw J.M., and Matunis M.J. The nuclear pore complex: Disease associations and functional correlations Trends Endocrinol. Metab. 15 2004 34 39
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 34-39
    • Cronshaw, J.M.1    Matunis, M.J.2
  • 57
    • 8344274464 scopus 로고    scopus 로고
    • Genome-scale expression profiling of Hutchinson-Gilford progeria syndrome reveals widespread transcriptional misregulation leading to mesodermal/mesenchymal defects and accelerated atherosclerosis
    • Csoka A.B., English S.B., Simkevich C.P., Ginzinger D.G., Butte A.J., Schatten G.P., Rothman F.G., and Sedivy J.M. Genome-scale expression profiling of Hutchinson-Gilford progeria syndrome reveals widespread transcriptional misregulation leading to mesodermal/mesenchymal defects and accelerated atherosclerosis Aging Cell 3 2004 235 243
    • (2004) Aging Cell , vol.3 , pp. 235-243
    • Csoka, A.B.1    English, S.B.2    Simkevich, C.P.3    Ginzinger, D.G.4    Butte, A.J.5    Schatten, G.P.6    Rothman, F.G.7    Sedivy, J.M.8
  • 59
    • 0025746706 scopus 로고
    • Insulin-resistant diabetes mellitus and hypermetabolism in mandibuloacral dysplasia: A newly recognized form of partial lipodystrophy
    • Cutler D.L., Kaufmann S., and Freidenberg G.R. Insulin-resistant diabetes mellitus and hypermetabolism in mandibuloacral dysplasia: A newly recognized form of partial lipodystrophy J. Clin. Endocrinol. Metab. 73 1991 1056 1061
    • (1991) J. Clin. Endocrinol. Metab. , vol.73 , pp. 1056-1061
    • Cutler, D.L.1    Kaufmann, S.2    Freidenberg, G.R.3
  • 61
    • 0038054542 scopus 로고    scopus 로고
    • Muscular dystrophies: Genes to pathogenesis
    • Dalkilic I., and Kunkel L.M. Muscular dystrophies: Genes to pathogenesis Curr. Opin. Genet. Dev. 13 2003 231 238
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 231-238
    • Dalkilic, I.1    Kunkel, L.M.2
  • 63
    • 0015319601 scopus 로고
    • The Hutchinson-Gilford progeria syndrome
    • DeBusk F.L. The Hutchinson-Gilford progeria syndrome J. Pediat. 80 1972 697 724
    • (1972) J. Pediat. , vol.80 , pp. 697-724
    • Debusk, F.L.1
  • 66
    • 0036860727 scopus 로고    scopus 로고
    • The spatio-temporal organization of DNA replication sites is identical in primary, immortalized and transformed mammalian cells
    • Dimitrova D.S., and Berezney R. The spatio-temporal organization of DNA replication sites is identical in primary, immortalized and transformed mammalian cells J. Cell Sci. 115 2002 4037 4051
    • (2002) J. Cell Sci. , vol.115 , pp. 4037-4051
    • Dimitrova, D.S.1    Berezney, R.2
  • 67
    • 0025053673 scopus 로고
    • Gene structure of nuclear lamin LIII of Xenopus laevis; A model for the evolution of if proteins from a lamin-like ancestor
    • Doring V., and Stick R. Gene structure of nuclear lamin LIII of Xenopus laevis; a model for the evolution of IF proteins from a lamin-like ancestor EMBO J. 9 1990 4073 4081
    • (1990) EMBO J. , vol.9 , pp. 4073-4081
    • Doring, V.1    Stick, R.2
  • 68
    • 0036848357 scopus 로고    scopus 로고
    • In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C
    • Dreuillet C., Tillit J., Kress M., and Ernoult-Lange M. In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C Nucleic Acids Res. 30 2002 4634 4642
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4634-4642
    • Dreuillet, C.1    Tillit, J.2    Kress, M.3    Ernoult-lange, M.4
  • 69
    • 0034732949 scopus 로고    scopus 로고
    • Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker
    • Duband-Goulet I., and Courvalin J.C. Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker Biochemistry 39 2000 6483 6488
    • (2000) Biochemistry , vol.39 , pp. 6483-6488
    • Duband-goulet, I.1    Courvalin, J.C.2
  • 70
    • 0015979147 scopus 로고
    • Familial lipoatrophic diabetes with dominant transmission. a new syndrome
    • Dunnigan M.G., Cochrane M.A., Kelly A., and Scott J.W. Familial lipoatrophic diabetes with dominant transmission. A new syndrome Q. J. Med. 43 1974 33 48
    • (1974) Q. J. Med. , vol.43 , pp. 33-48
    • Dunnigan, M.G.1    Cochrane, M.A.2    Kelly, A.3    Scott, J.W.4
  • 71
    • 0017134119 scopus 로고
    • A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei
    • Dwyer N., and Blobel G. A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei J. Cell Biol. 70 1976 581 591
    • (1976) J. Cell Biol. , vol.70 , pp. 581-591
    • Dwyer, N.1    Blobel, G.2
  • 72
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg J., Siggia E.D., Moreira J.E., Smith C.L., Presley J.F., Worman H.J., and Lippincott-Schwartz J. Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis J. Cell Biol. 138 1997 1193 1206
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-schwartz, J.7
  • 73
    • 0031969698 scopus 로고    scopus 로고
    • Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype
    • Ellis J.A., Craxton M., Yates J.R., and Kendrick-Jones J. Aberrant intracellular targeting and cell cycle-dependent phosphorylation of emerin contribute to the Emery-Dreifuss muscular dystrophy phenotype J. Cell Sci. 111 1998 781 792
    • (1998) J. Cell Sci. , vol.111 , pp. 781-792
    • Ellis, J.A.1    Craxton, M.2    Yates, J.R.3    Kendrick-jones, J.4
  • 74
    • 0032939360 scopus 로고    scopus 로고
    • Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy
    • Ellis J.A., Yates J.R., Kendrick-Jones J., and Brown C.A. Changes at P183 of emerin weaken its protein-protein interactions resulting in X-linked Emery-Dreifuss muscular dystrophy Hum. Genet. 104 1999 262 268
    • (1999) Hum. Genet. , vol.104 , pp. 262-268
    • Ellis, J.A.1    Yates, J.R.2    Kendrick-jones, J.3    Brown, C.A.4
  • 75
    • 0033988181 scopus 로고    scopus 로고
    • Two distal mutations in the gene encoding emerin have profoundly different effects on emerin protein expression
    • Ellis J.A., Brown C.A., Tilley L.D., Kendrick-Jones J., Spence J.E., and Yates J.R. Two distal mutations in the gene encoding emerin have profoundly different effects on emerin protein expression Neuromuscul. Disord. 10 2000 24 30
    • (2000) Neuromuscul. Disord. , vol.10 , pp. 24-30
    • Ellis, J.A.1    Brown, C.A.2    Tilley, L.D.3    Kendrick-jones, J.4    Spence, J.E.5    Yates, J.R.6
  • 77
    • 0024419522 scopus 로고
    • Emery-Dreifuss syndrome
    • Emery A.E. Emery-Dreifuss syndrome J. Med. Genet. 26 1989 637 641
    • (1989) J. Med. Genet. , vol.26 , pp. 637-641
    • Emery, A.E.1
  • 80
    • 0026411318 scopus 로고
    • The genetics of idiopathic torsion dystonia
    • Fahn S. The genetics of idiopathic torsion dystonia Int. J. Neurol. 25 1991 70 80
    • (1991) Int. J. Neurol. , vol.25 , pp. 70-80
    • Fahn, S.1
  • 81
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: Nucleocytoplasmic transport and beyond
    • Fahrenkrog B., and Aebi U. The nuclear pore complex: Nucleocytoplasmic transport and beyond Nat. Rev. Mol. Cell Biol. 4 2003 757 -66.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 757
    • Fahrenkrog, B.1    Aebi, U.2
  • 82
    • 0032771080 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane
    • Fairley E.A., Kendrick-Jones J., and Ellis J.A. The Emery-Dreifuss muscular dystrophy phenotype arises from aberrant targeting and binding of emerin at the inner nuclear membrane J. Cell Sci. 112 1999 2571 2582
    • (1999) J. Cell Sci. , vol.112 , pp. 2571-2582
    • Fairley, E.A.1    Kendrick-jones, J.2    Ellis, J.A.3
  • 85
    • 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
    • Favreau C., Dubosclard E., Östlund C., Vigouroux C., Capeau J., Wehnert M., Higuet D., Worman H.J., Courvalin J.C., and Buendia B. 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    Östlund, 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
  • 86
    • 0842347426 scopus 로고    scopus 로고
    • Expression of a mutant lamin a that causes Emery-Dreifuss muscular dystrophy inhibits in vitro differentiation of C2C12 myoblasts
    • Favreau C., Higuet D., Courvalin J.C., and Buendia B. Expression of a mutant lamin A that causes Emery-Dreifuss muscular dystrophy inhibits in vitro differentiation of C2C12 myoblasts Mol. Cell Biol. 24 2004 1481 1492
    • (2004) Mol. Cell Biol. , vol.24 , pp. 1481-1492
    • Favreau, C.1    Higuet, D.2    Courvalin, J.C.3    Buendia, B.4
  • 87
    • 0013925189 scopus 로고
    • On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates
    • Fawcett D.W. On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates Am. J. Anat. 119 1966 129 145
    • (1966) Am. J. Anat. , vol.119 , pp. 129-145
    • Fawcett, D.W.1
  • 88
    • 0020398795 scopus 로고
    • An autosomal-dominant dystrophy with humeropelvic distribution and cardiomyopathy
    • Fenichel G.M., Sul Y.C., Kilroy A.W., and Blouin R. An autosomal-dominant dystrophy with humeropelvic distribution and cardiomyopathy Neurology 32 1982 1399 1401
    • (1982) Neurology , vol.32 , pp. 1399-1401
    • Fenichel, G.M.1    Sul, Y.C.2    Kilroy, A.W.3    Blouin, R.4
  • 89
    • 0037624625 scopus 로고    scopus 로고
    • Architectural abnormalities in muscle nuclei. Ultrastructural differences between X-linked and autosomal dominant forms of EDMD
    • Fidzianska A, and Hausmanowa-Petrusewicz I. Architectural abnormalities in muscle nuclei. Ultrastructural differences between X-linked and autosomal dominant forms of EDMD J. Neurol. Sci. 210 2003 47 51
    • (2003) J. Neurol. Sci. , vol.210 , pp. 47-51
    • Fidzianska, A.1    Hausmanowa-petrusewicz, I.2
  • 90
    • 0023032014 scopus 로고
    • CDNA sequencing of nuclear lamins a and C reveals primary and secondary structural homology to intermediate filament proteins
    • Fisher D.Z., Chaudhary N., and Blobel G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins Proc. Natl. Acad. Sci. USA 83 1986 6450 6454
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 91
    • 0020064097 scopus 로고
    • Isolation and characterization of a proteinaceous subnuclear fraction composed of nuclear matrix, peripheral lamina, and nuclear pore complexes from embryos of Drosophila melanogaster
    • Fisher P.A., Berrios M., and Blobel G. Isolation and characterization of a proteinaceous subnuclear fraction composed of nuclear matrix, peripheral lamina, and nuclear pore complexes from embryos of Drosophila melanogaster J. Cell Biol. 92 1982 674 686
    • (1982) J. Cell Biol. , vol.92 , pp. 674-686
    • Fisher, P.A.1    Berrios, M.2    Blobel, G.3
  • 92
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R., and Gerace L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation Cell 73 1993 1267 1279
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 96
    • 2342466617 scopus 로고    scopus 로고
    • Matefin, a Caenorhabditis elegans germ line-specific SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development
    • Fridkin A., Mills E., Margalit A., Neufeld E., Lee K.K., Feinstein N., Cohen M., Wilson K.L., and Gruenbaum Y. Matefin, a Caenorhabditis elegans germ line-specific SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development Proc. Natl. Acad. Sci. USA 101 2004 6987 6992
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6987-6992
    • Fridkin, A.1    Mills, E.2    Margalit, A.3    Neufeld, E.4    Lee, K.K.5    Feinstein, N.6    Cohen, M.7    Wilson, K.L.8    Gruenbaum, Y.9
  • 97
    • 0027509502 scopus 로고
    • CDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells
    • Furukawa K., and Hotta Y. cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells EMBO J. 12 1993 97 106
    • (1993) EMBO J. , vol.12 , pp. 97-106
    • Furukawa, K.1    Hotta, Y.2
  • 98
    • 0028342511 scopus 로고
    • Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice
    • Furukawa K., Inagaki H., and Hotta Y. Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice Exp. Cell Res. 212 1994 426 430
    • (1994) Exp. Cell Res. , vol.212 , pp. 426-430
    • Furukawa, K.1    Inagaki, H.2    Hotta, Y.3
  • 99
    • 0035145898 scopus 로고    scopus 로고
    • Phenotypic heterogeneity in patients with familial partial lipodystrophy (Dunnigan variety) related to the site of missense mutations in lamin A/C gene
    • Garg A., Vinaitheerthan M., Weatherall P.T., and Bowcock A.M. Phenotypic heterogeneity in patients with familial partial lipodystrophy (Dunnigan variety) related to the site of missense mutations in lamin A/C gene J. Clin. Endocrinol. Metab. 86 2001 59 65
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 59-65
    • Garg, A.1    Vinaitheerthan, M.2    Weatherall, P.T.3    Bowcock, A.M.4
  • 100
    • 0036098280 scopus 로고    scopus 로고
    • Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamin A/C gene
    • Garg A., Speckman R.A., and Bowcock A.M. Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamin A/C gene Am. J. Med. 112 2002 549 555
    • (2002) Am. J. Med. , vol.112 , pp. 549-555
    • Garg, A.1    Speckman, R.A.2    Bowcock, A.M.3
  • 101
    • 0018093261 scopus 로고
    • Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution
    • Gerace L., Blum A., and Blobel G. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution J. Cell Biol. 79 1978 546 566
    • (1978) J. Cell Biol. , vol.79 , pp. 546-566
    • Gerace, L.1    Blum, A.2    Blobel, G.3
  • 102
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace L., and Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis Cell 19 1980 277 287
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 103
    • 2942643929 scopus 로고    scopus 로고
    • TorsinA and torsion dystonia: Unraveling the architecture of the nuclear envelope
    • Gerace L. TorsinA and torsion dystonia: Unraveling the architecture of the nuclear envelope Proc. Natl. Acad. Sci. USA 101 2004 8839 8840
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8839-8840
    • Gerace, L.1
  • 105
    • 0037578194 scopus 로고
    • Ateleiosis and progeria: Continuous youth and premature old age
    • Gilford H. Ateleiosis and progeria: Continuous youth and premature old age BMJ 2 1904 914 918
    • (1904) BMJ , vol.2 , pp. 914-918
    • Gilford, H.1
  • 106
    • 0026659229 scopus 로고
    • Buschke-Ollendorff syndrome associated with elevated elastin production by affected skin fibroblasts in culture
    • Giro M.G., Duvic M., Smith L.T., Kennedy R., Rapini R., Arnett F.C., and Davidson J.M. Buschke-Ollendorff syndrome associated with elevated elastin production by affected skin fibroblasts in culture J. Invest. Dermatol. 99 1992 129 137
    • (1992) J. Invest. Dermatol. , vol.99 , pp. 129-137
    • Giro, M.G.1    Duvic, M.2    Smith, L.T.3    Kennedy, R.4    Rapini, R.5    Arnett, F.C.6    Davidson, J.M.7
  • 107
    • 0027442899 scopus 로고
    • The alpha-helical rod domain of human lamins a and C contains a chromatin binding site
    • Glass C.A., Glass J.R., Taniura H., Hasel K.W., Blevitt J.M., and Gerace L. The alpha-helical rod domain of human lamins A and C contains a chromatin binding site EMBO J. 12 1993 4413 4424
    • (1993) EMBO J. , vol.12 , pp. 4413-4424
    • Glass, C.A.1    Glass, J.R.2    Taniura, H.3    Hasel, K.W.4    Blevitt, J.M.5    Gerace, L.6
  • 109
    • 0022453107 scopus 로고
    • Keratin-like proteins that coisolate with intermediate filaments of BHK-21 cells are nuclear lamins
    • Goldman A.E., Maul G., Steinert P.M., Yang H.Y., and Goldman R.D. Keratin-like proteins that coisolate with intermediate filaments of BHK-21 cells are nuclear lamins Proc. Natl. Acad. Sci. USA 83 1986 3839 3843
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3839-3843
    • Goldman, A.E.1    Maul, G.2    Steinert, P.M.3    Yang, H.Y.4    Goldman, R.D.5
  • 112
    • 1642290757 scopus 로고    scopus 로고
    • Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia
    • Gonzalez-Alegre P., and Paulson H.L. Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia J. Neurosci. 24 2004 2593 2601
    • (2004) J. Neurosci. , vol.24 , pp. 2593-2601
    • Gonzalez-alegre, P.1    Paulson, H.L.2
  • 113
    • 1642433201 scopus 로고    scopus 로고
    • Mislocalization to the nuclear envelope: An effect of the dystonia-causing torsinA mutation
    • Goodchild R.E., and Dauer W.T. Mislocalization to the nuclear envelope: An effect of the dystonia-causing torsinA mutation Proc. Natl. Acad. Sci. USA 101 2004 847 852
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 847-852
    • Goodchild, R.E.1    Dauer, W.T.2
  • 114
    • 15444374750 scopus 로고    scopus 로고
    • The AAA+ protein torsonA interacts with a conserved domain present in LAP1 and a novel ER protein
    • Goodchild R.E., and Dauer W.T. The AAA+ protein torsonA interacts with a conserved domain present in LAP1 and a novel ER protein J. Cell Biol. 168 2005 855 862
    • (2005) J. Cell Biol. , vol.168 , pp. 855-862
    • Goodchild, R.E.1    Dauer, W.T.2
  • 116
    • 14944383792 scopus 로고    scopus 로고
    • RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: Implications for Hutchinson-Gilford progeria syndrome
    • Gruber J., Lampe T., Osborn M., and Weber K. RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: Implications for Hutchinson-Gilford progeria syndrome J. Cell Sci. 118 2005 689 696
    • (2005) J. Cell Sci. , vol.118 , pp. 689-696
    • Gruber, J.1    Lampe, T.2    Osborn, M.3    Weber, K.4
  • 117
    • 0036500323 scopus 로고    scopus 로고
    • The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans
    • Gruenbaum Y., Lee K.K., Liu J., Cohen M., and Wilson K.L. The expression, lamin-dependent localization and RNAi depletion phenotype for emerin in C. elegans J. Cell Sci. 115 2002 923 929
    • (2002) J. Cell Sci. , vol.115 , pp. 923-929
    • Gruenbaum, Y.1    Lee, K.K.2    Liu, J.3    Cohen, M.4    Wilson, K.L.5
  • 119
    • 0025374930 scopus 로고
    • Lamins a and C are not expressed at early stages of human lymphocyte differentiation
    • Guilly M.N., Kolb J.P., Gosti F., Godeau F., and Courvalin J.C. Lamins A and C are not expressed at early stages of human lymphocyte differentiation Exp. Cell Res. 189 1990 145 147
    • (1990) Exp. Cell Res. , vol.189 , pp. 145-147
    • Guilly, M.N.1    Kolb, J.P.2    Gosti, F.3    Godeau, F.4    Courvalin, J.C.5
  • 120
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg E., Wozniak R.W., and Blobel G. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region J. Cell Biol. 122 1993 513 521
    • (1993) J. Cell Biol. , vol.122 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 122
    • 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 J.M., Yamane M., Koujin T., Hashiguchi N., Mori C., Wilson K.L., and Hiraoka Y. 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 2004 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    Mori, C.6    Wilson, K.L.7    Hiraoka, Y.8
  • 123
    • 0035694237 scopus 로고    scopus 로고
    • Identification of essential genes in cultured mammalian cells using small interfering RNAs
    • Harborth J., Elbashir S.M., Bechert K., Tuschl T., and Weber K. Identification of essential genes in cultured mammalian cells using small interfering RNAs J. Cell Sci. 114 2001 4557 4565
    • (2001) J. Cell Sci. , vol.114 , pp. 4557-4565
    • Harborth, J.1    Elbashir, S.M.2    Bechert, K.3    Tuschl, T.4    Weber, K.5
  • 124
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and Is required for the assembly of a Nup93-containing complex
    • Hawryluk-Gara L.A., Shibuya E.K., and Wozniak R.W. Vertebrate Nup53 interacts with the nuclear lamina and Is required for the assembly of a Nup93-containing complex Mol. Biol. Cell 16 2005 2382 2394
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2382-2394
    • Hawryluk-gara, L.A.1    Shibuya, E.K.2    Wozniak, R.W.3
  • 125
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin a that prevent nuclear lamina disassembly in mitosis
    • Heald R., and McKeon F. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis Cell 61 1990 579 589
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.2
  • 127
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann H., and Aebi U. Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds Annu. Rev. Biochem. 73 2004 749 789
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 130
    • 0025165401 scopus 로고
    • Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin
    • Höger T.H., Zatloukal K., Waizenegger I., and Krohne G. Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin Chromosoma 99 1990 379 390
    • (1990) Chromosoma , vol.99 , pp. 379-390
    • Höger, T.H.1    Zatloukal, K.2    Waizenegger, I.3    Krohne, G.4
  • 131
    • 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 J.M., Lee K.K., Kowalski A.K., and Wilson K.L. 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
  • 132
    • 19344378383 scopus 로고    scopus 로고
    • Emerin caps the pointed end of actin filaments: Evidence for an actin cortical network at the nuclear inner membrane
    • Holaska J.M., Kowalski A.K., and Wilson K.L. Emerin caps the pointed end of actin filaments: Evidence for an actin cortical network at the nuclear inner membrane PLoS Biol. 2 2004 E231
    • (2004) PLoS Biol. , vol.2 , pp. 231
    • Holaska, J.M.1    Kowalski, A.K.2    Wilson, K.L.3
  • 133
    • 0032535470 scopus 로고    scopus 로고
    • The human lamin B receptor/sterol reductase multigene family
    • Holmer L., Pezhman A., and Worman H.J. The human lamin B receptor/sterol reductase multigene family Genomics 54 1998 469 476
    • (1998) Genomics , vol.54 , pp. 469-476
    • Holmer, L.1    Pezhman, A.2    Worman, H.J.3
  • 134
    • 0043172367 scopus 로고    scopus 로고
    • Effect of pathogenic mis-sense mutations in lamin a on its interaction with emerin in vivo
    • Holt I., Östlund C., Stewart C.L., Man N., Worman H.J., and Morris G.E. 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    Östlund, C.2    Stewart, C.L.3    Man, N.4    Worman, H.J.5    Morris, G.E.6
  • 135
    • 0035153087 scopus 로고    scopus 로고
    • Lamins in disease: Why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?
    • Hutchison C.J., Alvarez-Reyes M., and Vaughan O.A. Lamins in disease: Why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes? J. Cell Sci. 114 2001 9 19
    • (2001) J. Cell Sci. , vol.114 , pp. 9-19
    • Hutchison, C.J.1    Alvarez-reyes, M.2    Vaughan, O.A.3
  • 136
    • 7944219648 scopus 로고    scopus 로고
    • A-type lamins: Guardians of the soma?
    • Hutchison C.J., and Worman H.J. A-type lamins: guardians of the soma? Nat. Cell Biol. 6 2004 1062 1067
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1062-1067
    • Hutchison, C.J.1    Worman, H.J.2
  • 137
    • 0038253709 scopus 로고
    • Case of congenital absence of hair, with atrophic condition of the skin and its appendages, in a boy whose mother had been almost wholly bald from alopecia areata from the age of six
    • Hutchinson J. Case of congenital absence of hair, with atrophic condition of the skin and its appendages, in a boy whose mother had been almost wholly bald from alopecia areata from the age of six Lancet I 1886 923
    • (1886) Lancet , vol.1 , pp. 923
    • Hutchinson, J.1
  • 138
    • 0344431581 scopus 로고
    • Ueber eine bisher unbekannte familiaere Anomalie der Leukocyten
    • Huët G.J. Ueber eine bisher unbekannte familiaere Anomalie der Leukocyten Klin. Wochenschr. 11 1932 1264 1266
    • (1932) Klin. Wochenschr. , vol.11 , pp. 1264-1266
    • Huët, G.J.1
  • 139
    • 0030681031 scopus 로고    scopus 로고
    • Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression
    • Imai S., Nishibayashi S., Takao K., Tomifuji M., Fujino T., Hasegawa M., and Takano T. Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression Mol. Biol. Cell 8 1997 2407 2419
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2407-2419
    • Imai, S.1    Nishibayashi, S.2    Takao, K.3    Tomifuji, M.4    Fujino, T.5    Hasegawa, M.6    Takano, T.7
  • 140
    • 0031028991 scopus 로고    scopus 로고
    • Dunnigan-Köbberling syndrome: An autosomal dominant form of partial lipodystrophy
    • Jackson S.N., Howlett T.A., McNally P.G., O'Rahilly S., and Trembath R.C. Dunnigan-Köbberling syndrome: An autosomal dominant form of partial lipodystrophy Q. J. Med. 90 1997 27 36
    • (1997) Q. J. Med. , vol.90 , pp. 27-36
    • Jackson, S.N.1    Howlett, T.A.2    McNally, P.G.3    O'Rahilly, S.4    Trembath, R.C.5
  • 144
    • 0034669029 scopus 로고    scopus 로고
    • Nuclear organization of DNA replication in primary mammalian cells
    • Kennedy B.K., Barbie D.A., Classon M., Dyson N., and Harlow E. 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
  • 145
    • 0031054691 scopus 로고    scopus 로고
    • In vitro assay and characterization of the farnesylation-dependent prelamin a endoprotease
    • Kilic F., Dalton M.B., Burrell S.K., Mayer J.P., Patterson S.D., and Sinensky M. In vitro assay and characterization of the farnesylation-dependent prelamin A endoprotease J. Biol. Chem. 272 1997 5298 5304
    • (1997) J. Biol. Chem. , vol.272 , pp. 5298-5304
    • Kilic, F.1    Dalton, M.B.2    Burrell, S.K.3    Mayer, J.P.4    Patterson, S.D.5    Sinensky, M.6
  • 146
  • 147
    • 0016702194 scopus 로고
    • Lipodystrophy of the extremities. a dominantly inherited syndrome associated with lipatrophic diabetes
    • Köbberling J., Willms B., Kattermann R., and Creutzfeldt W. Lipodystrophy of the extremities. A dominantly inherited syndrome associated with lipatrophic diabetes Humangenetik 29 1975 111 120
    • (1975) Humangenetik , vol.29 , pp. 111-120
    • Köbberling, J.1    Willms, B.2    Kattermann, R.3    Creutzfeldt, W.4
  • 148
    • 5744240629 scopus 로고    scopus 로고
    • A Drosophila model of early onset torsion dystonia suggests impairment in TGF-beta signaling
    • Koh Y.H., Rehfeld K., and Ganetzky B. A Drosophila model of early onset torsion dystonia suggests impairment in TGF-beta signaling Hum. Mol. Genet. 13 2004 2019 2030
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2019-2030
    • Koh, Y.H.1    Rehfeld, K.2    Ganetzky, B.3
  • 150
    • 0021350949 scopus 로고
    • A monoclonal antibody against nuclear lamina proteins reveals cell type-specificity in Xenopus laevis
    • Krohne G., Debus E., Osborn M., Weber K., and Franke W.W. A monoclonal antibody against nuclear lamina proteins reveals cell type-specificity in Xenopus laevis Exp. Cell Res. 150 1984 47 59
    • (1984) Exp. Cell Res. , vol.150 , pp. 47-59
    • Krohne, G.1    Debus, E.2    Osborn, M.3    Weber, K.4    Franke, W.W.5
  • 151
    • 0023505969 scopus 로고
    • Nuclear lamin LI of Xenopus laevis: CDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily
    • Krohne G., Wolin S.L., McKeon F.D., Franke W.W., and Kirschner M.W. Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily EMBO J. 6 1987 3801 3808
    • (1987) EMBO J. , vol.6 , pp. 3801-3808
    • Krohne, G.1    Wolin, S.L.2    McKeon, F.D.3    Franke, W.W.4    Kirschner, M.W.5
  • 152
    • 0037049554 scopus 로고    scopus 로고
    • Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription
    • Kumaran R.I., Muralikrishna B., and Parnaik V.K. 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
  • 155
    • 0033000856 scopus 로고    scopus 로고
    • Molecular characterization and developmentally regulated expression of Xenopus lamina-associated polypeptide 2 (XLAP2)
    • Lang C., Paulin-Levasseur M., Gajewski A., Alsheimer M., Benavente R., and Krohne G. Molecular characterization and developmentally regulated expression of Xenopus lamina-associated polypeptide 2 (XLAP2) J. Cell Sci. 112 1999 749 759
    • (1999) J. Cell Sci. , vol.112 , pp. 749-759
    • Lang, C.1    Paulin-levasseur, M.2    Gajewski, A.3    Alsheimer, M.4    Benavente, R.5    Krohne, G.6
  • 156
    • 0023603590 scopus 로고
    • Lamins a and C appear during retinoic acid-induced differentiation of mouse embryonal carcinoma cells
    • Lebel S., Lampron C., Royal A., and Raymond Y. Lamins A and C appear during retinoic acid-induced differentiation of mouse embryonal carcinoma cells J. Cell Biol. 105 1987 1099 1104
    • (1987) J. Cell Biol. , vol.105 , pp. 1099-1104
    • Lebel, S.1    Lampron, C.2    Royal, A.3    Raymond, Y.4
  • 157
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin a and DNA-bridging protein BAF
    • Lee K.K., Haraguchi T., Lee R.S., Koujin T., Hiraoka Y., and Wilson K.L. Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF J. Cell Sci. 114 2001 4567 4573
    • (2001) J. Cell Sci. , vol.114 , pp. 4567-4573
    • Lee, K.K.1    Haraguchi, T.2    Lee, R.S.3    Koujin, T.4    Hiraoka, Y.5    Wilson, K.L.6
  • 160
    • 0027257461 scopus 로고
    • Structural organization of the human gene encoding nuclear lamin a and nuclear lamin C
    • Lin F., and Worman H.J. Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C J. Biol. Chem. 268 1993 16321 16326
    • (1993) J. Biol. Chem. , vol.268 , pp. 16321-16326
    • Lin, F.1    Worman, H.J.2
  • 161
    • 0028980880 scopus 로고
    • Structural organization of the human gene (LMNB1) encoding nuclear lamin B1
    • Lin F., and Worman H.J. Structural organization of the human gene (LMNB1) encoding nuclear lamin B1 Genomics 27 1995 230 236
    • (1995) Genomics , vol.27 , pp. 230-236
    • Lin, F.1    Worman, H.J.2
  • 163
    • 13544264752 scopus 로고    scopus 로고
    • MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling
    • Lin F., Morrison J.M., Wu W., and Worman H.J. MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling Hum. Mol. Genet. 14 2005 437 445
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 437-445
    • Lin, F.1    Morrison, J.M.2    Wu, W.3    Worman, H.J.4
  • 164
    • 0025332706 scopus 로고
    • Immunoaffinity purification and functional characterization of interphase and meiotic Drosophila nuclear lamin isoforms
    • Lin L., and Fisher P.A. Immunoaffinity purification and functional characterization of interphase and meiotic Drosophila nuclear lamin isoforms J. Biol. Chem. 265 1990 12596 12601
    • (1990) J. Biol. Chem. , vol.265 , pp. 12596-12601
    • Lin, L.1    Fisher, P.A.2
  • 165
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans
    • Liu J., Lee K.K., Segura-Totten M., Neufeld E., Wilson K.L., and Gruenbaum Y. 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
  • 166
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin a and SREBP1: Implications for partial lipodystrophy and other laminopathies
    • Lloyd D.J., Trembath R.C., and Shackleton S. 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
  • 168
    • 0028168825 scopus 로고
    • Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove
    • Luderus M.E., den Blaauwen J.L., de Smit O.J., Compton D.A., and van Driel R. Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove Mol. Cell. Biol. 14 1994 6297 6305
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6297-6305
    • Luderus, M.E.1    Den Blaauwen, J.L.2    De Smit, O.J.3    Compton, D.A.4    Van Driel, R.5
  • 170
    • 0032772929 scopus 로고    scopus 로고
    • UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development
    • Malone C.J., Fixsen W.D., Horvitz H.R., and Han M. UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development Development 126 1999 3171 3181
    • (1999) Development , vol.126 , pp. 3171-3181
    • Malone, C.J.1    Fixsen, W.D.2    Horvitz, H.R.3    Han, M.4
  • 171
    • 0346094458 scopus 로고    scopus 로고
    • The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • Malone C.J., Misner L., Le Bot N., Tsai M.C., Campbell J.M., Ahringer J., and White J.G. The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus Cell 115 2003 825 836
    • (2003) Cell , vol.115 , pp. 825-836
    • Malone, C.J.1    Misner, L.2    Le Bot, N.3    Tsai, M.C.4    Campbell, J.M.5    Ahringer, J.6    White, J.G.7
  • 172
    • 0027976913 scopus 로고
    • The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein
    • Mancini M.A., Shan B., Nickerson J.A., Penman S., and Lee W.H. The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein Proc. Natl. Acad. Sci. USA 91 1994 418 422
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 418-422
    • Mancini, M.A.1    Shan, B.2    Nickerson, J.A.3    Penman, S.4    Lee, W.H.5
  • 173
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • Manilal S., Nguyen T.M., Sewry C.A., and Morris G.E. The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein Hum. Mol. Genet. 5 1996 801 808
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 801-808
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 175
    • 14044265165 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro
    • Markiewicz E., Ledran M., and Hutchison C.J. Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro J. Cell Sci. 118 2005 409 420
    • (2005) J. Cell Sci. , vol.118 , pp. 409-420
    • Markiewicz, E.1    Ledran, M.2    Hutchison, C.J.3
  • 177
    • 0141530040 scopus 로고    scopus 로고
    • A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation
    • Maske C.P., Hollinshead M.S., Higbee N.C., Bergo M.O., Young S.G., and Vaux D.J. A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation J. Cell Biol. 162 2003 1223 1232
    • (2003) J. Cell Biol. , vol.162 , pp. 1223-1232
    • Maske, C.P.1    Hollinshead, M.S.2    Higbee, N.C.3    Bergo, M.O.4    Young, S.G.5    Vaux, D.J.6
  • 178
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • McKeon F.D., Kirschner M.W., and Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins Nature 319 1986 463 468
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 179
    • 0026016285 scopus 로고
    • The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs
    • Meier J., Campbell K.H., Ford C.C., Stick R., and Hutchison C.J. The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs J. Cell Sci. 98 1991 271 279
    • (1991) J. Cell Sci. , vol.98 , pp. 271-279
    • Meier, J.1    Campbell, K.H.2    Ford, C.C.3    Stick, R.4    Hutchison, C.J.5
  • 181
    • 0034640884 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization blocks the elongation phase of DNA replication
    • Moir R.D., Spann T.P., Herrmann H., and Goldman R.D. Disruption of nuclear lamin organization blocks the elongation phase of DNA replication J. Cell Biol. 149 2000 1179 1192
    • (2000) J. Cell Biol. , vol.149 , pp. 1179-1192
    • Moir, R.D.1    Spann, T.P.2    Herrmann, H.3    Goldman, R.D.4
  • 182
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins a and B1: Different pathways of assembly during nuclear envelope formation in living cells
    • Moir R.D., Yoon M., Khuon S., and Goldman R.D. 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
  • 183
    • 0037673940 scopus 로고    scopus 로고
    • A progeroid syndrome in mice is caused by defects in A-type lamins
    • Mounkes L.C., Kozlov S., Hernandez L., Sullivan T., and Stewart C.L. A progeroid syndrome in mice is caused by defects in A-type lamins Nature 423 2003 298 301
    • (2003) Nature , vol.423 , pp. 298-301
    • Mounkes, L.C.1    Kozlov, S.2    Hernandez, L.3    Sullivan, T.4    Stewart, C.L.5
  • 184
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • Muchir A., Bonne G., van der Kooi A.J., van Meegen M., Baas F., Bolhuis P.A., de Visser M., and Schwartz K. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B) Hum. Mol. Genet. 9 2000 1453 1459
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    Van Der Kooi, A.J.3    Van Meegen, M.4    Baas, F.5    Bolhuis, P.A.6    De Visser, M.7    Schwartz, K.8
  • 185
    • 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
    • Muchir A., van Engelen B.G., Lammens M., Mislow J.M., McNally E., Schwartz K., and 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. 291 2003 352 362
    • (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
  • 190
    • 0346216789 scopus 로고    scopus 로고
    • Expression of emerin and lamins in muscle of patients with different forms of Emery-Dreifuss muscular dystrophy
    • Niebroj-Dobosz I., Fidzianska A., and Hausmanowa-Petrusewicz I. Expression of emerin and lamins in muscle of patients with different forms of Emery-Dreifuss muscular dystrophy Acta Myol. 22 2003 52 57
    • (2003) Acta Myol. , vol.22 , pp. 52-57
    • Niebroj-dobosz, I.1    Fidzianska, A.2    Hausmanowa-petrusewicz, I.3
  • 195
    • 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 E.C., Nishimoto T., and Gerace L. Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore J. Cell Biol. 167 2004 1051 1062
    • (2004) J. Cell Biol. , vol.167 , pp. 1051-1062
    • Ohba, T.1    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 196
    • 0037959860 scopus 로고    scopus 로고
    • XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos
    • Osada S., Ohmori S.Y., and Taira M. XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos Development 130 2003 1783 1794
    • (2003) Development , vol.130 , pp. 1783-1794
    • Osada, S.1    Ohmori, S.Y.2    Taira, M.3
  • 198
    • 0035697055 scopus 로고    scopus 로고
    • Properties of lamin a mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy
    • Östlund C., Bonne G., Schwartz K., and Worman H.J. 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
  • 199
    • 0028064990 scopus 로고
    • Complex formation between lamin a and the retinoblastoma gene product: Identification of the domain on lamin a required for its interaction
    • Ozaki T., Saijo M., Murakami K., Enomoto H., Taya Y., and Sakiyama S. Complex formation between lamin A and the retinoblastoma gene product: Identification of the domain on lamin A required for its interaction Oncogene 9 1994 2649 2653
    • (1994) Oncogene , vol.9 , pp. 2649-2653
    • Ozaki, T.1    Saijo, M.2    Murakami, K.3    Enomoto, H.4    Taya, Y.5    Sakiyama, S.6
  • 202
    • 0021206298 scopus 로고
    • Mandibuloacral dysplasia: A rare progeroid syndrome. Two brothers confirm autosomal recessive inheritance
    • Pallotta R., and Morgese G. Mandibuloacral dysplasia: A rare progeroid syndrome. Two brothers confirm autosomal recessive inheritance Clin. Genet. 26 1984 133 138
    • (1984) Clin. Genet. , vol.26 , pp. 133-138
    • Pallotta, R.1    Morgese, G.2
  • 203
    • 18144411595 scopus 로고    scopus 로고
    • The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the TGFbeta superfamily of cytokines
    • Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., and Luo K. The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the TGFbeta superfamily of cytokines J. Biol. Chem. 280 2005 15992 16001
    • (2005) J. Biol. Chem. , vol.280 , pp. 15992-16001
    • Pan, D.1    Estevez-salmeron, L.D.2    Stroschein, S.L.3    Zhu, X.4    He, J.5    Zhou, S.6    Luo, K.7
  • 204
    • 0742305345 scopus 로고    scopus 로고
    • The functions of Klarsicht and nuclear lamin in developmentally regulated nuclear migrations of photoreceptor cells in the Drosophila eye
    • Patterson K., Molofsky A.B., Robinson C., Acosta S., Cater C., and Fischer J.A. The functions of Klarsicht and nuclear lamin in developmentally regulated nuclear migrations of photoreceptor cells in the Drosophila eye Mol. Biol. Cell 15 2004 600 610
    • (2004) Mol. Biol. Cell , vol.15 , pp. 600-610
    • Patterson, K.1    Molofsky, A.B.2    Robinson, C.3    Acosta, S.4    Cater, C.5    Fischer, J.A.6
  • 205
    • 0030029383 scopus 로고    scopus 로고
    • The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells
    • Paulin-Levasseur M., Blake D.L., Julien M., and Rouleau L. The MAN antigens are non-lamin constituents of the nuclear lamina in vertebrate cells Chromosoma 104 1996 367 379
    • (1996) Chromosoma , vol.104 , pp. 367-379
    • Paulin-levasseur, M.1    Blake, D.L.2    Julien, M.3    Rouleau, L.4
  • 206
    • 0012800504 scopus 로고
    • Demonstratie van een paar zeldzaam voorkomende typen van bloedlichaampjes en bespreking der patienten
    • Pelger K. Demonstratie van een paar zeldzaam voorkomende typen van bloedlichaampjes en bespreking der patienten Ned. Tijdschr. Geneeskd. 72 1928 1178
    • (1928) Ned. Tijdschr. Geneeskd. , vol.72 , pp. 1178
    • Pelger, K.1
  • 208
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Doree M., Labbe J.C., and Nigg E.A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase Cell 61 1990 591 602
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 209
    • 0031932459 scopus 로고    scopus 로고
    • Localization of the gene for familial partial lipodystrophy (Dunnigan variety) to chromosome 1q21-22
    • Peters J.M., Barnes R., Bennett L., Gitomer W.M., Bowcock A.M., and Garg A. Localization of the gene for familial partial lipodystrophy (Dunnigan variety) to chromosome 1q21-22 Nat. Genet. 18 1998 292 295
    • (1998) Nat. Genet. , vol.18 , pp. 292-295
    • Peters, J.M.1    Barnes, R.2    Bennett, L.3    Gitomer, W.M.4    Bowcock, A.M.5    Garg, A.6
  • 211
    • 12344326099 scopus 로고    scopus 로고
    • The lamin CxxM motif promotes nuclear membrane growth
    • Prufert K., Vogel A., and Krohne G. The lamin CxxM motif promotes nuclear membrane growth J. Cell Sci. 117 2004 6105 6116
    • (2004) J. Cell Sci. , vol.117 , pp. 6105-6116
    • Prufert, K.1    Vogel, A.2    Krohne, G.3
  • 212
    • 2342513330 scopus 로고    scopus 로고
    • Dynamics of nuclear pore complex organization through the cell cycle
    • Rabut G., Lenart P., and Ellenberg J. Dynamics of nuclear pore complex organization through the cell cycle Curr. Opin. Cell Biol. 16 2004 314 321
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 314-321
    • Rabut, G.1    Lenart, P.2    Ellenberg, J.3
  • 214
    • 0035696932 scopus 로고    scopus 로고
    • Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy
    • Raharjo W.H., Enarson P., Sullivan T., Stewart C.L., and Burke B. 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
  • 215
    • 12344259997 scopus 로고    scopus 로고
    • Intranuclear membrane structure formations by CaaX-containing nuclear proteins
    • Ralle T., Grund C., Franke W.W., and Stick R. Intranuclear membrane structure formations by CaaX-containing nuclear proteins J. Cell Sci. 117 2004 6095 6104
    • (2004) J. Cell Sci. , vol.117 , pp. 6095-6104
    • Ralle, T.1    Grund, C.2    Franke, W.W.3    Stick, R.4
  • 216
    • 0347927630 scopus 로고    scopus 로고
    • SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1
    • Raju G.P., Dimova N., Klein P.S., and Huang H.C. SANE, a novel LEM domain protein, regulates bone morphogenetic protein signaling through interaction with Smad1 J. Biol. Chem. 278 2003 428 437
    • (2003) J. Biol. Chem. , vol.278 , pp. 428-437
    • Raju, G.P.1    Dimova, N.2    Klein, P.S.3    Huang, H.C.4
  • 219
    • 0027729310 scopus 로고
    • A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; CDNA cloning and gene organization
    • Riemer D., Dodemont H., and Weber K. A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; cDNA cloning and gene organization Eur. J. Cell Biol. 62 1993 214 223
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 214-223
    • Riemer, D.1    Dodemont, H.2    Weber, K.3
  • 220
    • 0028344919 scopus 로고
    • The organization of the gene for Drosophila lamin C: Limited homology with vertebrate lamin genes and lack of homology versus the Drosophila lamin Dmo gene
    • Riemer D., and Weber K. The organization of the gene for Drosophila lamin C: limited homology with vertebrate lamin genes and lack of homology versus the Drosophila lamin Dmo gene Eur. J. Cell Biol. 63 1994 299 306
    • (1994) Eur. J. Cell Biol. , vol.63 , pp. 299-306
    • Riemer, D.1    Weber, K.2
  • 221
    • 0024561417 scopus 로고
    • Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study
    • Rober R.A., Weber K., and Osborn M. Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study Development 105 1989 365 378
    • (1989) Development , vol.105 , pp. 365-378
    • Rober, R.A.1    Weber, K.2    Osborn, M.3
  • 222
    • 0025272702 scopus 로고
    • Cells of the cellular immune and hemopoietic system of the mouse lack lamins A/C: Distinction versus other somatic cells
    • Rober R.A., Sauter H., Weber K., and Osborn M. Cells of the cellular immune and hemopoietic system of the mouse lack lamins A/C: Distinction versus other somatic cells J. Cell Sci. 95 1990 587 598
    • (1990) J. Cell Sci. , vol.95 , pp. 587-598
    • Rober, R.A.1    Sauter, H.2    Weber, K.3    Osborn, M.4
  • 223
  • 227
    • 0141864610 scopus 로고    scopus 로고
    • Molecular mechanisms, diagnosis, and rational approaches to management of and therapy for Charcot-Marie-Tooth disease and related peripheral neuropathies
    • Saifi G.M., Szigeti K., Snipes G.J., Garcia C.A., and Lupski J.R. Molecular mechanisms, diagnosis, and rational approaches to management of and therapy for Charcot-Marie-Tooth disease and related peripheral neuropathies J. Investig. Med. 51 2003 261 283
    • (2003) J. Investig. Med. , vol.51 , pp. 261-283
    • Saifi, G.M.1    Szigeti, K.2    Snipes, G.J.3    Garcia, C.A.4    Lupski, J.R.5
  • 231
    • 17644373758 scopus 로고    scopus 로고
    • Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome
    • Scaffidi P., and Misteli T. Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome Nat. Med. 11 2005 440 445
    • (2005) Nat. Med. , vol.11 , pp. 440-445
    • Scaffidi, P.1    Misteli, T.2
  • 232
    • 0017225494 scopus 로고
    • Experimental disintegration of the nuclear envelope. Evidence for pore-connecting fibrils
    • Scheer U., Kartenbeck J., Trendelenburg M.F., Stadler J., and Franke W.W. Experimental disintegration of the nuclear envelope. Evidence for pore-connecting fibrils J. Cell Biol. 69 1976 1 18
    • (1976) J. Cell Biol. , vol.69 , pp. 1-18
    • Scheer, U.1    Kartenbeck, J.2    Trendelenburg, M.F.3    Stadler, J.4    Franke, W.W.5
  • 233
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer E.C., Florens L., Guan T., Yates J.R., 3rd, and Gerace L. Nuclear membrane proteins with potential disease links found by subtractive proteomics Science 301 2003 1380 1382
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates III, J.R.4    Gerace, L.5
  • 234
    • 5644250530 scopus 로고    scopus 로고
    • The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths
    • Schirmer E.C., and Gerace L. The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths J. Biol. Chem. 279 2004 42811 42817
    • (2004) J. Biol. Chem. , vol.279 , pp. 42811-42817
    • Schirmer, E.C.1    Gerace, L.2
  • 235
    • 0028237891 scopus 로고
    • Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane
    • Schuler E., Lin F., and Worman H.J. Characterization of the human gene encoding LBR, an integral protein of the nuclear envelope inner membrane J. Biol. Chem. 269 1994 11312 11317
    • (1994) J. Biol. Chem. , vol.269 , pp. 11312-11317
    • Schuler, E.1    Lin, F.2    Worman, H.J.3
  • 237
    • 0024263203 scopus 로고
    • Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina
    • Senior A., and Gerace L. Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina J. Cell Biol. 107 1988 2029 2036
    • (1988) J. Cell Biol. , vol.107 , pp. 2029-2036
    • Senior, A.1    Gerace, L.2
  • 239
    • 0033960712 scopus 로고    scopus 로고
    • Immunocytochemical analysis of human muscular dystrophy
    • Sewry C.A. Immunocytochemical analysis of human muscular dystrophy Microsc. Res. Tech. 48 2000 142 154
    • (2000) Microsc. Res. Tech. , vol.48 , pp. 142-154
    • Sewry, C.A.1
  • 243
    • 0344874046 scopus 로고    scopus 로고
    • Mandibuloacral dysplasia caused by homozygosity for the R527H mutation in lamin A/C
    • Shen J.J., Brown C.A., Lupski J.R., and Potocki L. Mandibuloacral dysplasia caused by homozygosity for the R527H mutation in lamin A/C J. Med. Genet. 40 2003 854 857
    • (2003) J. Med. Genet. , vol.40 , pp. 854-857
    • Shen, J.J.1    Brown, C.A.2    Lupski, J.R.3    Potocki, L.4
  • 245
    • 0031838013 scopus 로고    scopus 로고
    • Human lamin B receptor exhibits sterol C14-reductase activity in Saccharomyces cerevisiae
    • Silve S., Dupuy P.H., Ferrara P., and Loison G. Human lamin B receptor exhibits sterol C14-reductase activity in Saccharomyces cerevisiae Biochim. Biophys. Acta 1392 1998 233 244
    • (1998) Biochim. Biophys. Acta , vol.1392 , pp. 233-244
    • Silve, S.1    Dupuy, P.H.2    Ferrara, P.3    Loison, G.4
  • 246
    • 0036171687 scopus 로고    scopus 로고
    • Body fat distribution and metabolic derangements in patients with familial partial lipodystrophy associated with mandibuloacral dysplasia
    • Simha V., and Garg A. Body fat distribution and metabolic derangements in patients with familial partial lipodystrophy associated with mandibuloacral dysplasia J. Clin. Endocrinol. Metab. 87 2002 776 785
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 776-785
    • Simha, V.1    Garg, A.2
  • 247
    • 0037564014 scopus 로고    scopus 로고
    • Genetic and phenotypic heterogeneity in patients with mandibuloacral dysplasia-associated lipodystrophy
    • Simha V., Agarwal A.K., Oral E.A., Fryns J.P., and Garg A. Genetic and phenotypic heterogeneity in patients with mandibuloacral dysplasia-associated lipodystrophy J. Clin. Endocrinol. Metab. 88 2003 2821 2824
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 2821-2824
    • Simha, V.1    Agarwal, A.K.2    Oral, E.A.3    Fryns, J.P.4    Garg, A.5
  • 249
    • 0034254413 scopus 로고    scopus 로고
    • Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: Evidence from cell-free extracts of Xenopus eggs
    • Smythe C., Jenkins H.E., and Hutchison C.J. Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: Evidence from cell-free extracts of Xenopus eggs EMBO J. 19 2000 3918 3931
    • (2000) EMBO J. , vol.19 , pp. 3918-3931
    • Smythe, C.1    Jenkins, H.E.2    Hutchison, C.J.3
  • 250
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B., and Worman H.J. The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal J. Cell Biol. 120 1993 1093 1100
    • (1993) J. Cell Biol. , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 251
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • Soullam B., and Worman H.J. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane J. Cell Biol. 130 1995 15 27
    • (1995) J. Cell Biol. , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.J.2
  • 252
    • 0030863126 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis
    • Spann T.P., Moir R.D., Goldman A.E., Stick R., and Goldman R.D. Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis J. Cell Biol. 136 1997 1201 1212
    • (1997) J. Cell Biol. , vol.136 , pp. 1201-1212
    • Spann, T.P.1    Moir, R.D.2    Goldman, A.E.3    Stick, R.4    Goldman, R.D.5
  • 253
    • 0037128211 scopus 로고    scopus 로고
    • Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription
    • Spann T.P., Goldman A.E., Wang C., Huang S., and Goldman R.D. 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
  • 254
    • 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
    • Speckman R.A., Garg A., Du F., Bennett L., Veile R., Arioglu E., Taylor S.I., Lovett M., and Bowcock A.M. 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
  • 255
    • 0037064176 scopus 로고    scopus 로고
    • Role of ANC-1 in tethering nuclei to the actin cytoskeleton
    • Starr D.A., and Han M. Role of ANC-1 in tethering nuclei to the actin cytoskeleton Science 298 2002 406 409
    • (2002) Science , vol.298 , pp. 406-409
    • Starr, D.A.1    Han, M.2
  • 256
    • 0037439661 scopus 로고    scopus 로고
    • ANChors away: An actin based mechanism of nuclear positioning
    • Starr D.A., and Han M. ANChors away: An actin based mechanism of nuclear positioning J. Cell Sci. 116 2003 211 216
    • (2003) J. Cell Sci. , vol.116 , pp. 211-216
    • Starr, D.A.1    Han, M.2
  • 257
    • 0023646768 scopus 로고
    • Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B
    • Stewart C., and Burke B. Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B Cell 51 1987 383 392
    • (1987) Cell , vol.51 , pp. 383-392
    • Stewart, C.1    Burke, B.2
  • 258
    • 0024095062 scopus 로고
    • CDNA cloning of the developmentally regulated lamin LIII of Xenopus laevis
    • Stick R. cDNA cloning of the developmentally regulated lamin LIII of Xenopus laevis EMBO J. 7 1988 3189 3197
    • (1988) EMBO J. , vol.7 , pp. 3189-3197
    • Stick, R.1
  • 259
    • 0026670970 scopus 로고
    • The gene structure of Xenopus nuclear lamin A: A model for the evolution of A-type from B-type lamins by exon shuffling
    • Stick R. The gene structure of Xenopus nuclear lamin A: A model for the evolution of A-type from B-type lamins by exon shuffling Chromosoma 101 1992 566 574
    • (1992) Chromosoma , vol.101 , pp. 566-574
    • Stick, R.1
  • 260
    • 0027936303 scopus 로고
    • The gene structure of B-type nuclear lamins of Xenopus laevis: Implications for the evolution of the vertebrate lamin family
    • Stick R. The gene structure of B-type nuclear lamins of Xenopus laevis: Implications for the evolution of the vertebrate lamin family Chromosome Res. 2 1994 376 382
    • (1994) Chromosome Res. , vol.2 , pp. 376-382
    • Stick, R.1
  • 262
    • 0030909575 scopus 로고    scopus 로고
    • Muscular dystrophies and the dystrophin-glycoprotein complex
    • Straub V., and Campbell K.P. Muscular dystrophies and the dystrophin-glycoprotein complex Curr. Opin. Neurol. 10 1997 168 175
    • (1997) Curr. Opin. Neurol. , vol.10 , pp. 168-175
    • Straub, V.1    Campbell, K.P.2
  • 264
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam M., and Wente S.R. Peering through the pore: Nuclear pore complex structure, assembly, and function Dev. Cell 4 2003 775 789
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 265
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura H., Glass C., and Gerace L. A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones J. Cell Biol. 131 1995 33 44
    • (1995) J. Cell Biol. , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 268
    • 0033083786 scopus 로고    scopus 로고
    • Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy
    • Tsuchiya Y., Hase A., Ogawa M., Yorifuji H., and Arahata K. Distinct regions specify the nuclear membrane targeting of emerin, the responsible protein for Emery-Dreifuss muscular dystrophy Eur. J. Biochem. 259 1999 859 865
    • (1999) Eur. J. Biochem. , vol.259 , pp. 859-865
    • Tsuchiya, Y.1    Hase, A.2    Ogawa, M.3    Yorifuji, H.4    Arahata, K.5
  • 269
    • 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., and Arahata K. CDNA microarray analysis of gene expression in fibroblasts of patients with X-linked Emery-Dreifuss muscular dystrophy Muscle Nerve 25 2002 898 901
    • (2002) Muscle Nerve , vol.25 , pp. 898-901
    • Tsukahara, T.1    Tsujino, S.2    Arahata, K.3
  • 276
    • 0035691915 scopus 로고    scopus 로고
    • Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene
    • Vigouroux C., Auclair M., Dubosclard E., Pouchelet M., Capeau J., Courvalin J.C., and Buendia B. 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
  • 278
    • 0025285068 scopus 로고
    • Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C
    • Ward G.E., and Kirschner M.W. Identification of cell cycle-regulated phosphorylation sites on nuclear lamin C Cell 61 1990 561 577
    • (1990) Cell , vol.61 , pp. 561-577
    • Ward, G.E.1    Kirschner, M.W.2
  • 279
    • 1442345760 scopus 로고    scopus 로고
    • The lamin B receptor of Drosophila melanogaster
    • Wagner N., Weber D., Seitz S., and Krohne G. The lamin B receptor of Drosophila melanogaster J. Cell Sci. 117 2004 2015 2028
    • (2004) J. Cell Sci. , vol.117 , pp. 2015-2028
    • Wagner, N.1    Weber, D.2    Seitz, S.3    Krohne, G.4
  • 280
    • 0345535128 scopus 로고    scopus 로고
    • Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene
    • Waterham H.R., Koster J., Mooyer P., Noort G.G., Kelley R.I., Wilcox W.R., Wanders R.J., Hennekam R.C., and Oosterwijk J.C. Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene Am. J. Hum. Genet. 72 2003 1013 1017
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1013-1017
    • Waterham, H.R.1    Koster, J.2    Mooyer, P.3    Noort, G.G.4    Kelley, R.I.5    Wilcox, W.R.6    Wanders, R.J.7    Hennekam, R.C.8    Oosterwijk, J.C.9
  • 281
    • 0024828257 scopus 로고
    • Maturation of nuclear lamin a involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; Implications for the structure of the nuclear lamina
    • Weber K., Plessmann U., and Traub P. Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina FEBS Lett. 257 1989 411 414
    • (1989) FEBS Lett. , vol.257 , pp. 411-414
    • Weber, K.1    Plessmann, U.2    Traub, P.3
  • 282
    • 0029665691 scopus 로고    scopus 로고
    • Köbberling-Dunnigan syndrome: A rare cause of generalized muscular hypertrophy
    • Wildermuth S., Spranger S., Spranger M., Raue F., and Meinck H.M. Köbberling-Dunnigan syndrome: A rare cause of generalized muscular hypertrophy Muscle Nerve 19 1996 843 847
    • (1996) Muscle Nerve , vol.19 , pp. 843-847
    • Wildermuth, S.1    Spranger, S.2    Spranger, M.3    Raue, F.4    Meinck, H.M.5
  • 284
    • 0035831041 scopus 로고    scopus 로고
    • Lamins and disease: Insights into nuclear infrastructure
    • Wilson K.L., Zastrow M.S., and Lee K.K. Lamins and disease: Insights into nuclear infrastructure Cell 104 2001 647 650
    • (2001) Cell , vol.104 , pp. 647-650
    • Wilson, K.L.1    Zastrow, M.S.2    Lee, K.K.3
  • 285
    • 0023917971 scopus 로고
    • Evidence for modification of lamin B by a product of mevalonic acid
    • Wolda S.L., and Glomset J.A. Evidence for modification of lamin B by a product of mevalonic acid J. Biol. Chem. 263 1988 5997 6000
    • (1988) J. Biol. Chem. , vol.263 , pp. 5997-6000
    • Wolda, S.L.1    Glomset, J.A.2
  • 286
    • 0035919768 scopus 로고    scopus 로고
    • Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy
    • Wolff N., Gilquin B., Courchay K., Callebaut I., Worman H.J., and Zinn-Justin S. Structural analysis of emerin, an inner nuclear membrane protein mutated in X-linked Emery-Dreifuss muscular dystrophy FEBS Lett. 501 2001 171 176
    • (2001) FEBS Lett. , vol.501 , pp. 171-176
    • Wolff, N.1    Gilquin, B.2    Courchay, K.3    Callebaut, I.4    Worman, H.J.5    Zinn-justin, S.6
  • 288
    • 0036899615 scopus 로고    scopus 로고
    • The nuclear lamina and inherited disease
    • Worman H.J., and Courvalin J.C. The nuclear lamina and inherited disease Trends Cell Biol. 12 2002 591 598
    • (2002) Trends Cell Biol. , vol.12 , pp. 591-598
    • Worman, H.J.1    Courvalin, J.C.2
  • 289
    • 85047692354 scopus 로고    scopus 로고
    • How do mutations in lamins a and C cause disease?
    • Worman H.J., and Courvalin J.C. How do mutations in lamins A and C cause disease? J. Clin. Invest. 113 2004 349 351
    • (2004) J. Clin. Invest. , vol.113 , pp. 349-351
    • Worman, H.J.1    Courvalin, J.C.2
  • 290
    • 0023807582 scopus 로고
    • Nuclear lamina heterogeneity in mammalian cells. Differential expression of the major lamins and variations in lamin B phosphorylation
    • Worman H.J., Lazaridis I., and Georgatos S.D. Nuclear lamina heterogeneity in mammalian cells. Differential expression of the major lamins and variations in lamin B phosphorylation J. Biol. Chem. 263 1988 12135 12141
    • (1988) J. Biol. Chem. , vol.263 , pp. 12135-12141
    • Worman, H.J.1    Lazaridis, I.2    Georgatos, S.D.3
  • 292
    • 0025149541 scopus 로고
    • The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains
    • Worman H.J., Evans C.D., and Blobel G. The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains J. Cell Biol. 111 1990 1535 1542
    • (1990) J. Cell Biol. , vol.111 , pp. 1535-1542
    • Worman, H.J.1    Evans, C.D.2    Blobel, G.3
  • 293
    • 0024360678 scopus 로고
    • Primary structure analysis of an integral membrane glycoprotein of the nuclear pore
    • Wozniak R.W., Bartnik E., and Blobel G. Primary structure analysis of an integral membrane glycoprotein of the nuclear pore J. Cell Biol. 108 1989 2083 2092
    • (1989) J. Cell Biol. , vol.108 , pp. 2083-2092
    • Wozniak, R.W.1    Bartnik, E.2    Blobel, G.3
  • 294
    • 0028313943 scopus 로고
    • POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope
    • Wozniak R.W., Blobel G., and Rout M.P. POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope J. Cell Biol. 125 1994 31 42
    • (1994) J. Cell Biol. , vol.125 , pp. 31-42
    • Wozniak, R.W.1    Blobel, G.2    Rout, M.P.3
  • 295
    • 0036538599 scopus 로고    scopus 로고
    • Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane
    • Wu W., Lin F., and Worman H.J. Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane J. Cell Sci. 115 2002 1361 1371
    • (2002) J. Cell Sci. , vol.115 , pp. 1361-1371
    • Wu, W.1    Lin, F.2    Worman, H.J.3
  • 296
    • 0029917273 scopus 로고    scopus 로고
    • Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization
    • Wydner K.L., McNeil J.A., Lin F., Worman H.J., and Lawrence J.B. Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization Genomics 32 1996 474 478
    • (1996) Genomics , vol.32 , pp. 474-478
    • Wydner, K.L.1    McNeil, J.A.2    Lin, F.3    Worman, H.J.4    Lawrence, J.B.5
  • 297
    • 0030955703 scopus 로고    scopus 로고
    • Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis
    • Yang L., Guan T., and Gerace L. Integral membrane proteins of the nuclear envelope are dispersed throughout the endoplasmic reticulum during mitosis J. Cell Biol. 137 1997 1199 1210
    • (1997) J. Cell Biol. , vol.137 , pp. 1199-1210
    • Yang, L.1    Guan, T.2    Gerace, L.3
  • 298
    • 0028363978 scopus 로고
    • Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane
    • Ye Q., and Worman H.J. Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane J. Biol. Chem. 269 1994 11306 11311
    • (1994) J. Biol. Chem. , vol.269 , pp. 11306-11311
    • Ye, Q.1    Worman, H.J.2
  • 299
    • 0029160015 scopus 로고
    • Protein-protein interactions between human nuclear lamins expressed in yeast
    • Ye Q., and Worman H.J. Protein-protein interactions between human nuclear lamins expressed in yeast Exp. Cell Res. 219 1995 292 298
    • (1995) Exp. Cell Res. , vol.219 , pp. 292-298
    • Ye, Q.1    Worman, H.J.2
  • 300
    • 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., and Worman H.J. Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1 J. Biol. Chem. 271 1996 14653 14656
    • (1996) J. Biol. Chem. , vol.271 , pp. 14653-14656
    • Ye, Q.1    Worman, H.J.2
  • 301
    • 0030987777 scopus 로고    scopus 로고
    • Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR
    • Ye Q., Callebaut I., Pezhman A., Courvalin J.C., and Worman H.J. Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR J. Biol. Chem. 272 1997 14983 14989
    • (1997) J. Biol. Chem. , vol.272 , pp. 14983-14989
    • Ye, Q.1    Callebaut, I.2    Pezhman, A.3    Courvalin, J.C.4    Worman, H.J.5
  • 302
    • 14344265557 scopus 로고    scopus 로고
    • Spectrin repeat proteins in the nucleus
    • Young K.G., and Kothary R. Spectrin repeat proteins in the nucleus BioEssays 27 2005 144 152
    • (2005) BioEssays , vol.27 , pp. 144-152
    • Young, K.G.1    Kothary, R.2
  • 303
    • 0015068895 scopus 로고
    • New syndrome manifested by mandibular hypoplasia, acroosteolysis, stiff joints and cutaneous atrophy (mandibuloacral dysplasia) in two unrelated boys
    • Young L.W., Radebaugh J.F., Rubin P., Sensenbrenner J.A., Fiorelli G., and McKusick V.A. New syndrome manifested by mandibular hypoplasia, acroosteolysis, stiff joints and cutaneous atrophy (mandibuloacral dysplasia) in two unrelated boys Birth Defects Orig. Artic. Ser. 7 1971 291 297
    • (1971) Birth Defects Orig. Artic. Ser. , vol.7 , pp. 291-297
    • Young, L.W.1    Radebaugh, J.F.2    Rubin, P.3    Sensenbrenner, J.A.4    Fiorelli, G.5    McKusick, V.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.