메뉴 건너뛰기




Volumn 16, Issue 1, 2011, Pages 114-148

Laminopathies: The molecular background of the disease and the prospects for its treatment

Author keywords

Emerin; Gene therapy; Lamin; Laminopathies; Nuclear lamina

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ANTHRA[1,9 CD]PYRAZOL 6(2H) ONE; ANTISENSE OLIGONUCLEOTIDE; BETA CATENIN; EMERIN; LAMIN A; LAMIN C; LEPTIN; NEUROFILAMENT L PROTEIN; NEUROFILAMENT PROTEIN; PROGESTERONE; RECOMBINANT LEPTIN; SHORT HAIRPIN RNA; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 79953821298     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-010-0038-9     Document Type: Review
Times cited : (38)

References (146)
  • 1
    • 68849119046 scopus 로고    scopus 로고
    • Laminopathies and the long strange trip from basic cell biology to therapy
    • Worman, H.J., Fong, L.G., Muchir, A. and Young, S.G. Laminopathies and the long strange trip from basic cell biology to therapy. J. Clin. Invest. 119 (2009) 1825-1836.
    • (2009) J. Clin. Invest. , vol.119 , pp. 1825-1836
    • Worman, H.J.1    Fong, L.G.2    Muchir, A.3    Young, S.G.4
  • 4
    • 77957264815 scopus 로고    scopus 로고
    • The Nuclear Envelope. Cold Spring Harb
    • cshperspect
    • Hetzer, M.W. The Nuclear Envelope. Cold Spring Harb. Perspect Biol. (2010) cshperspect.a000539.
    • (2010) Perspect Biol
    • Hetzer, M.W.1
  • 7
    • 41649097238 scopus 로고    scopus 로고
    • Nuclear lamins: Major factors in the structural organization and function of the nucleus and chromatin
    • Dechat, T., Pfleghaar, K., Sengupta, K., Shimi, T., Shumaker, D.K., Solimando, L. and Goldman, R.D. Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin. Genes Dev. 22 (2008) 832-853.
    • (2008) Genes Dev , vol.22 , pp. 832-853
    • Dechat, T.1    Pfleghaar, K.2    Sengupta, K.3    Shimi, T.4    Shumaker, D.K.5    Solimando, L.6    Goldman, R.D.7
  • 8
    • 77956273850 scopus 로고    scopus 로고
    • Dynamics of lamin-A processing following precursor accumulation
    • Liu, Q., Kim, D.I., Syme, J., LuValle, P., Burke, B. and Roux, K.J. Dynamics of lamin-A processing following precursor accumulation. PLoS One 5 (2010) e10874.
    • (2010) PLoS One , vol.5
    • Liu, Q.1    Kim, D.I.2    Syme, J.3    Luvalle, P.4    Burke, B.5    Roux, K.J.6
  • 13
    • 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
  • 15
    • 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
  • 17
    • 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
  • 19
  • 24
    • 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
  • 34
    • 34249699119 scopus 로고    scopus 로고
    • Phenomics and lamins: From disease to therapy
    • Hegele, R.A. and Oshima, J. Phenomics and lamins: from disease to therapy. Exp. Cell Res. 313 (2007) 2134-2143.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2134-2143
    • Hegele, R.A.1    Oshima, J.2
  • 35
    • 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
  • 38
    • 0345535128 scopus 로고    scopus 로고
    • Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3betahydroxysterol delta14-reductase deficiency due to mutations in the lamin B receptor gene
    • Waterham, H.R., Koster, J., Mooyer, P., van Noort, G., Kelley, R.I., Wilcox, W.R., Wanders, R.J.A., Hennekam, R.C.M. and Oosterwijk, J.C. Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3betahydroxysterol delta14-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    van Noort, G.4    Kelley, R.I.5    Wilcox, W.R.6    Wanders, R.J.A.7    Hennekam, R.C.M.8    Oosterwijk, J.C.9
  • 39
    • 79960756795 scopus 로고    scopus 로고
    • Buschke-Ollendorff Syndrome with Striking Phenotypic Variation Resulting from a Novel c.2203C>T Nonsense Mutation in LEMD3
    • DOI: 10.1111/j.1525-1470.2010
    • Yuste-Chaves, M., Cañueto, J., Santos-Briz, A., Ciria, S., González- Sarmiento, R. and Unamuno, P. Buschke-Ollendorff Syndrome with Striking Phenotypic Variation Resulting from a Novel c.2203C>T Nonsense Mutation in LEMD3. Pediatr. Dermatol. (2010) DOI: 10.1111/j.1525-1470.2010
    • (2010) Pediatr. Dermatol.
    • Yuste-Chaves, M.1    Cañueto, J.2    Santos-Briz, A.3    Ciria, S.4    González-Sarmiento, R.5    Unamuno, P.6
  • 41
    • 34249742648 scopus 로고    scopus 로고
    • The position of the mutation within the LMNA gene determines the type and extent of tissue involvement in laminopathies
    • Landires, I., Pascale, J.M. and Motta, J. The position of the mutation within the LMNA gene determines the type and extent of tissue involvement in laminopathies. Clin. Genet. 71 (2007) 592-593.
    • (2007) Clin. Genet. , vol.71 , pp. 592-593
    • Landires, I.1    Pascale, J.M.2    Motta, J.3
  • 42
    • 76449114620 scopus 로고    scopus 로고
    • Genotypephenotype correlations in laminopathies: How does fate translate?
    • Scharner, J., Gnocchi, V.F., Ellis, J.A. and Zammit, P.S. Genotypephenotype correlations in laminopathies: how does fate translate? BMC Dev. Biol. 38 (2010) 257-262.
    • (2010) BMC Dev. Biol. , vol.38 , pp. 257-262
    • Scharner, J.1    Gnocchi, V.F.2    Ellis, J.A.3    Zammit, P.S.4
  • 43
    • 77956588049 scopus 로고    scopus 로고
    • Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail
    • Simon, D.N., Zastrow, M.S. and Wilson, K.L. Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail. Nucleus 1 (2010) 264-272.
    • (2010) Nucleus , vol.1 , pp. 264-272
    • Simon, D.N.1    Zastrow, M.S.2    Wilson, K.L.3
  • 45
    • 77956230877 scopus 로고    scopus 로고
    • Muscular dystrophies: An update on pathology and diagnosis
    • Sewry, C. Muscular dystrophies: an update on pathology and diagnosis. Acta Neuropathol. 120 (2010) 343-358.
    • (2010) Acta Neuropathol , vol.120 , pp. 343-358
    • Sewry, C.1
  • 46
    • 0036962351 scopus 로고    scopus 로고
    • The nuclear lamins and nuclear envelope
    • Rzepecki, R. The nuclear lamins and nuclear envelope. Cel. Mol. Biol. Lett. 7 (2002) 1019-1035.
    • (2002) Cel. Mol. Biol. Lett. , vol.7 , pp. 1019-1035
    • Rzepecki, R.1
  • 51
    • 59149103623 scopus 로고    scopus 로고
    • Molecular signatures of Emery-Dreifuss muscular dystrophy
    • Wheeler, M.A. and Ellis, J.A. Molecular signatures of Emery-Dreifuss muscular dystrophy. Biochem. Soc. Trans. 36 (2008) 1354-1358.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1354-1358
    • Wheeler, M.A.1    Ellis, J.A.2
  • 58
    • 72149096260 scopus 로고    scopus 로고
    • In the middle of it all: Mutual mechanical regulation between the nucleus and the cytoskeleton
    • Dahl, K.N., Booth-Gauthier, E.A. and Ladoux, B. In the middle of it all: mutual mechanical regulation between the nucleus and the cytoskeleton. J. Biomech. 43 (2010) 2-8.
    • (2010) J. Biomech. , vol.43 , pp. 2-8
    • Dahl, K.N.1    Booth-Gauthier, E.A.2    Ladoux, B.3
  • 61
    • 34547642520 scopus 로고    scopus 로고
    • An emerin "proteome": Purification of distinct emerincontaining complexes from HeLa cells suggests molecular basis for diverse rolesincluding gene regulation, mRNA splicing, signaling, mechanosensing, and nu clear architecture
    • Holaska, J.M. and Wilson, K.L. An emerin "proteome": purification of distinct emerincontaining complexes from HeLa cells suggests molecular basis for diverse rolesincluding gene regulation, mRNA splicing, signaling, mechanosensing, and nu clear architecture. Biochemistry 46 (2007) 8897-8908.
    • (2007) Biochemistry , vol.46 , pp. 8897-8908
    • Holaska, J.M.1    Wilson, K.L.2
  • 62
    • 76149084859 scopus 로고    scopus 로고
    • Role of A-type lamins in signaling, transcription, and chromatin organization
    • Andrés, V. and González, J.M. Role of A-type lamins in signaling, transcription, and chromatin organization. J. Cell Biol. 187 (2009) 945-957.
    • (2009) J. Cell Biol. , vol.187 , pp. 945-957
    • Andrés, V.1    González, J.M.2
  • 64
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • Kim, E.K. and Choi, E.J. Pathological roles of MAPK signaling pathways in human diseases. Biochim. Biophys. Acta 1802 (2010) 396-405.
    • (2010) Biochim. Biophys. Acta. , vol.1802 , pp. 396-405
    • Kim, E.K.1    Choi, E.J.2
  • 65
    • 58149186768 scopus 로고    scopus 로고
    • Fast regulation of AP-1 activity through interaction of lamin A/C, ERK1/2, and c-Fos at the nuclear envelope
    • González, J.M., Navarro-Puche, A., Casar, B., Crespo, P. and Andrés, V. Fast regulation of AP-1 activity through interaction of lamin A/C, ERK1/2, and c-Fos at the nuclear envelope. J. Cell Biol. 183 (2008) 653-666.
    • (2008) J. Cell Biol. , vol.183 , pp. 653-666
    • González, J.M.1    Navarro-Puche, A.2    Casar, B.3    Crespo, P.4    Andrés, V.5
  • 66
    • 34547851806 scopus 로고    scopus 로고
    • Activation of MAPK in hearts of EMD null mice: Similarities between mouse models of X-linked and autosomal dominant Emery Dreifuss muscular dystrophy
    • Muchir, A., Pavlidis, P., Bonne, G., Hayashi, Y.K. and Worman, H.J. Activation of MAPK in hearts of EMD null mice: similarities between mouse models of X-linked and autosomal dominant Emery Dreifuss muscular dystrophy. Hum. Mol. Genet. 16 (2007) 1884-1895.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1884-1895
    • Muchir, A.1    Pavlidis, P.2    Bonne, G.3    Hayashi, Y.K.4    Worman, H.J.5
  • 67
    • 34248198298 scopus 로고    scopus 로고
    • Activation of MAPK pathways links LMNA mutations to cardiomyopathy in Emery-Dreifuss muscular dystrophy
    • Muchir, A., Pavlidis, P., Decostre, V., Herron, A.J., Arimura, T., Bonne, G. and Worman, H.J. Activation of MAPK pathways links LMNA mutations to cardiomyopathy in Emery-Dreifuss muscular dystrophy. J. Clin. Invest. 117 (2007) 1282-1293.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1282-1293
    • Muchir, A.1    Pavlidis, P.2    Decostre, V.3    Herron, A.J.4    Arimura, T.5    Bonne, G.6    Worman, H.J.7
  • 68
    • 57849157294 scopus 로고    scopus 로고
    • Reduced expression of A-type lamins and emerin activates extracellular signal-regulated kinase in cultured cells
    • Muchir, A., Wu, W. and Worman, H.J. Reduced expression of A-type lamins and emerin activates extracellular signal-regulated kinase in cultured cells. Biochim. Biophys. Acta 1792 (2009) 75-81.
    • (2009) Biochim. Biophys. Acta. , vol.1792 , pp. 75-81
    • Muchir, A.1    Wu, W.2    Worman, H.J.3
  • 70
    • 58049209788 scopus 로고    scopus 로고
    • Inhibition of extracellular signal-regulated kinase signaling to prevent cardiomyopathy caused by mutation in the gene encoding A-type lamins
    • Muchir, A., Shan, J., Bonne, G., Lehnart, S.E. and Worman, H.J. Inhibition of extracellular signal-regulated kinase signaling to prevent cardiomyopathy caused by mutation in the gene encoding A-type lamins. Hum. Mol. Genet. 18 (2009) 241-247.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 241-247
    • Muchir, A.1    Shan, J.2    Bonne, G.3    Lehnart, S.E.4    Worman, H.J.5
  • 71
    • 77953810973 scopus 로고    scopus 로고
    • Pharmacological inhibition of c-Jun N-terminal kinase signaling prevents cardiomyopathy caused by mutation in LMNA gene
    • Wu, W., Shan, J., Bonne, G., Worman, H.J. and Muchir, A. Pharmacological inhibition of c-Jun N-terminal kinase signaling prevents cardiomyopathy caused by mutation in LMNA gene. Biochim. Biophys. Acta 1802 (2010) 632-638.
    • (2010) Biochim. Biophys. Acta. , vol.1802 , pp. 632-638
    • Wu, W.1    Shan, J.2    Bonne, G.3    Worman, H.J.4    Muchir, A.5
  • 72
    • 67650230896 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling: Components, mechanisms, and diseases
    • MacDonald, B.T., Tamai, K. and He, X. Wnt/beta-catenin signaling: components, mechanisms, and diseases. Dev. Cell 17 (2009) 9-26.
    • (2009) Dev. Cell. , vol.17 , pp. 9-26
    • Macdonald, B.T.1    Tamai, K.2    He, X.3
  • 74
    • 33847367723 scopus 로고    scopus 로고
    • Wnt signalling: Variety at the core
    • Hoppler, S. and Kavanagh, C.L. Wnt signalling: variety at the core. J. Cell Sci. 120 (2007) 385-393.
    • (2007) J. Cell Sci. , vol.120 , pp. 385-393
    • Hoppler, S.1    Kavanagh, C.L.2
  • 75
    • 0035038243 scopus 로고    scopus 로고
    • Recruitment of ß-catenin to cadherin-mediated intercellular adhesions is involved in myogenic induction
    • Goichberg, P., Shtutman, M., Ben-Zeev, A. and Geiger, B. Recruitment of ß-catenin to cadherin-mediated intercellular adhesions is involved in myogenic induction. J. Cell Sci. 114 (2001) 1309-1319.
    • (2001) J. Cell Sci. , vol.114 , pp. 1309-1319
    • Goichberg, P.1    Shtutman, M.2    Ben-Zeev, A.3    Geiger, B.4
  • 76
    • 46649089157 scopus 로고    scopus 로고
    • ß-catenin promotes self-renewal of skeletal-muscle satellite cells
    • Perez-Ruiz, A., Ono, Y., Gnocchi, V.F. and Zammit, P.S. ß-catenin promotes self-renewal of skeletal-muscle satellite cells J. Cell Sci. 121 (2008) 1373-1382.
    • (2008) J.Cell Sci. , vol.121 , pp. 1373-1382
    • Perez-Ruiz, A.1    Ono, Y.2    Gnocchi, V.F.3    Zammit, P.S.4
  • 77
    • 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
  • 78
    • 3042829496 scopus 로고    scopus 로고
    • A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation
    • Johnson, B.R. A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation. Proc. Natl. Acad. Sci. USA 101 (2004) 9677-9682.
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 9677-9682
    • Johnson, B.R.1
  • 79
    • 1842854443 scopus 로고    scopus 로고
    • Lamin A/C binding protein LAP2 alpha is required for nuclear anchorage of retinoblastoma protein
    • Markiewicz, E., Dechat, T., Foisner, R., Quinlan, R.A. and Hutchison, C.J. Lamin A/C binding protein LAP2 alpha is required for nuclear anchorage of retinoblastoma protein. Mol. Biol. Cell. 13 (2002) 4401-4413.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 4401-4413
    • Markiewicz, E.1    Dechat, T.2    Foisner, R.3    Quinlan, R.A.4    Hutchison, C.J.5
  • 80
    • 32644447630 scopus 로고    scopus 로고
    • Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation
    • Frock, R.L., Kudlow, B.A., Evans, A.M., Jameson, S.A., Hauschka, S.D. and Kennedy, B.K. Lamin A/C and emerin are critical for skeletal muscle satellite cell differentiation. Genes Dev. 20 (2006) 486-500.
    • (2006) Genes Dev , vol.20 , pp. 486-500
    • Frock, R.L.1    Kudlow, B.A.2    Evans, A.M.3    Jameson, S.A.4    Hauschka, S.D.5    Kennedy, B.K.6
  • 81
    • 66849126054 scopus 로고    scopus 로고
    • Lamin complexes in the nuclear interior control progenitor cell proliferation and tissue homeostasis
    • Naetar, N. and Foisner, R. Lamin complexes in the nuclear interior control progenitor cell proliferation and tissue homeostasis. Cell Cycle 8 (2009) 1488-1493.
    • (2009) Cell Cycle , vol.8 , pp. 1488-1493
    • Naetar, N.1    Foisner, R.2
  • 82
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-beta signals
    • Massagué, J. How cells read TGF-beta signals. Nat. Rev. Mol. Cell Biol. 1 (2000) 169-178.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massagué, J.1
  • 85
    • 58849128158 scopus 로고    scopus 로고
    • Nuclear changes in skeletal muscle extend to satellite cells in autosomal dominant Emery-Dreifuss muscular dystrophy/limb-girdle muscular dystrophy 1B
    • Park, Y.E., Hayashi, Y.K., Goto, K., Komaki, H., Hayashi, Y., Inuzuka, T., Noguchi, S., Nonaka, I. and Nishino, I. Nuclear changes in skeletal muscle extend to satellite cells in autosomal dominant Emery-Dreifuss muscular dystrophy/limb-girdle muscular dystrophy 1B. Neuromuscul. Disord. 19 (2008) 29-36.
    • (2008) Neuromuscul. Disord. , vol.19 , pp. 29-36
    • Park, Y.E.1    Hayashi, Y.K.2    Goto, K.3    Komaki, H.4    Hayashi, Y.5    Inuzuka, T.6    Noguchi, S.7    Nonaka, I.8    Nishino, I.9
  • 86
    • 42049090788 scopus 로고    scopus 로고
    • Gone with the Wnt/Notch: Stem cells in laminopathies, progeria, and aging
    • Meshorer, E. and Gruenbaum, Y. Gone with the Wnt/Notch: stem cells in laminopathies, progeria, and aging. J. Cell Biol. 181 (2008) 9-13.
    • (2008) J. Cell Biol. , vol.181 , pp. 9-13
    • Meshorer, E.1    Gruenbaum, Y.2
  • 87
    • 37549069749 scopus 로고    scopus 로고
    • No place like home: Anatomy and function of the stem cell niche
    • Jones, D.L. and Wagers, A.J. No place like home: anatomy and function of the stem cell niche. Nat. Rev. Mol. Cell. Biol. 9 (2008) 11-21.
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 11-21
    • Jones, D.L.1    Wagers, A.J.2
  • 88
    • 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
  • 89
    • 77954626396 scopus 로고    scopus 로고
    • Successful surgical repair for Emery-Dreifuss muscular dystrophy valvular disease with longterm follow-up
    • Takai, H., Yamada, T., Tada, S. and Matsumaru, I. Successful surgical repair for Emery-Dreifuss muscular dystrophy valvular disease with longterm follow-up. Interac. Cardiovasc. Thorac. Surg. 10 (2010) 811-812.
    • (2010) Interac. Cardiovasc. Thorac. Surg. , vol.10 , pp. 811-812
    • Takai, H.1    Yamada, T.2    Tada, S.3    Matsumaru, I.4
  • 91
    • 67649188781 scopus 로고    scopus 로고
    • Increased expression of the Hutchinson-Gilford progeria syndrome truncated lamin A transcript during cell aging
    • Rodriguez, S., Coppedè, F., Sagelius, H. and Eriksson, M. Increased expression of the Hutchinson-Gilford progeria syndrome truncated lamin A transcript during cell aging. Eur. J. Hum. Genet. 17 (2009) 928-937.
    • (2009) Eur. J. Hum. Genet. , vol.17 , pp. 928-937
    • Rodriguez, S.1    Coppedè, F.2    Sagelius, H.3    Eriksson, M.4
  • 93
    • 26444463068 scopus 로고    scopus 로고
    • Inhibiting farnesylation reverses the nuclear morphology defect in a HeLa cell model for Hutchinson-Gilford progeria syndrome
    • Mallampalli, M.P., Huyer, G., Bendale, P., Gelb, M.H. and Michaelis, S. Inhibiting farnesylation reverses the nuclear morphology defect in a HeLa cell model for Hutchinson-Gilford progeria syndrome. Proc. Natl. Acad. Sci. USA 102 (2005) 14416-14421.
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 14416-14421
    • Mallampalli, M.P.1    Huyer, G.2    Bendale, P.3    Gelb, M.H.4    Michaelis, S.5
  • 96
    • 39049111972 scopus 로고    scopus 로고
    • Treatment with a farnesyltransferase inhibitor improves survival in mice with a Hutchinson- Gilford progeria syndrome mutation
    • Yang, S.H., Qiao, X., Fong, L.G. and Youn, S.G. Treatment with a farnesyltransferase inhibitor improves survival in mice with a Hutchinson- Gilford progeria syndrome mutation. Biochim. Biophys. Acta 1781 (2008) 36-39.
    • (2008) Biochim. Biophys. Acta. , vol.1781 , pp. 36-39
    • Yang, S.H.1    Qiao, X.2    Fong, L.G.3    Youn, S.G.4
  • 97
    • 55849129996 scopus 로고    scopus 로고
    • Progerin elicits disease phenotypes of progeria in mice whether or not it is farnesylated
    • Yang, S.H., Andres, D.A., Spielmann, H.P., Young, S.G. and Fong, L.G. Progerin elicits disease phenotypes of progeria in mice whether or not it is farnesylated. J. Clin. Invest. 118 (2008) 3291-3300.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3291-3300
    • Yang, S.H.1    Andres, D.A.2    Spielmann, H.P.3    Young, S.G.4    Fong, L.G.5
  • 101
    • 34548713556 scopus 로고    scopus 로고
    • Human lipodystrophies linked to mutations in A-type lamins and to HIV protease inhibitor therapy are both associated with pre-lamin A accumulation, oxidative stress and premature cellular senescence
    • Caron, M., Auclair, M., Donadille, B., Béréziat, V., Guerci, B., Laville, M., Narbonne, H., Bodemer, C., Lascols, O., Capeau, J. and Vigouroux, C. Human lipodystrophies linked to mutations in A-type lamins and to HIV protease inhibitor therapy are both associated with pre-lamin A accumulation, oxidative stress and premature cellular senescence. Cell Death Differ. 14 (2007) 1759-1767.
    • (2007) Cell Death Differ , vol.14 , pp. 1759-1767
    • Caron, M.1    Auclair, M.2    Donadille, B.3    Béréziat, V.4    Guerci, B.5    Laville, M.6    Narbonne, H.7    Bodemer, C.8    Lascols, O.9    Capeau, J.10    Vigouroux, C.11
  • 102
    • 34548063171 scopus 로고    scopus 로고
    • HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead to an accumulation of pre-lamin A in cells
    • Coffinier, C., Hudon, S.E., Farber, E.A., Chang, S.Y., Hrycyna, C.A., Young, S.G. and Fong, L.G. HIV protease inhibitors block the zinc metalloproteinase ZMPSTE24 and lead to an accumulation of pre-lamin A in cells. Proc. Natl. Acad. Sci.USA 104 (2007) 13432-13437.
    • (2007) Proc. Natl. Acad. Sci.USA. , vol.104 , pp. 13432-13437
    • Coffinier, C.1    Hudon, S.E.2    Farber, E.A.3    Chang, S.Y.4    Hrycyna, C.A.5    Young, S.G.6    Fong, L.G.7
  • 103
    • 30744473703 scopus 로고    scopus 로고
    • Correction of cellular phenotypes of Hutchinson-Gilford Progeria cells by RNA interference
    • Huang, S., Chen, L., Libina, N., Janes, J., Martin, G.M., Campisi, J. and Oshima, J. Correction of cellular phenotypes of Hutchinson-Gilford Progeria cells by RNA interference. Hum. Genet. (2005) 1-7.
    • (2005) Hum. Genet. , pp. 1-7
    • Huang, S.1    Chen, L.2    Libina, N.3    Janes, J.4    Martin, G.M.5    Campisi, J.6    Oshima, J.7
  • 107
    • 43149124203 scopus 로고    scopus 로고
    • Lamin A-dependent misregulation of adult stem cells associated with accelerated ageing
    • Scaffidi, P. and Misteli, T. Lamin A-dependent misregulation of adult stem cells associated with accelerated ageing. Nat. Cell Biol. 10 (2008) 452-459.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 452-459
    • Scaffidi, P.1    Misteli, T.2
  • 108
    • 33646745137 scopus 로고    scopus 로고
    • Lamin A-dependent nuclear defects in human aging
    • Scaffidi, P. and Misteli, T. Lamin A-dependent nuclear defects in human aging. Science 312 (2006) 1059-1063.
    • (2006) Science , vol.312 , pp. 1059-1063
    • Scaffidi, P.1    Misteli, T.2
  • 110
    • 34548148047 scopus 로고    scopus 로고
    • Thematic review series: Adipocyte Biology. Lipodystrophies: Windows on adipose biology and metabolism
    • Hegele, R.A., Joy, T.R., Al-Attar, S.A. and Rutt, B.K. Thematic review series: Adipocyte Biology. Lipodystrophies: windows on adipose biology and metabolism. J. Lipid Res. 48 (2007) 1433-1444.
    • (2007) J. Lipid Res. , vol.48 , pp. 1433-1444
    • Hegele, R.A.1    Joy, T.R.2    Al-Attar, S.A.3    Rutt, B.K.4
  • 111
    • 65249097788 scopus 로고    scopus 로고
    • Dynamic complexes of A-type lamins and emerin influence adipogenic capacity of the cell via nucleocytoplasmic distribution of {beta}-catenin
    • Tilgner, K., Wojciechowicz, K., Jahoda, C., Hutchison, C. and Markiewicz, E. Dynamic complexes of A-type lamins and emerin influence adipogenic capacity of the cell via nucleocytoplasmic distribution of {beta}-catenin. J. Cell Sci. 122 (2009) 401-413.
    • (2009) J. Cell Sci. , vol.122 , pp. 401-413
    • Tilgner, K.1    Wojciechowicz, K.2    Jahoda, C.3    Hutchison, C.4    Markiewicz, E.5
  • 113
    • 2942547652 scopus 로고    scopus 로고
    • Glucose induces de novo lipogenesis in rat muscle satellite cells through a sterol-regulatory-element-binding-protein- 1c-dependent pathway
    • Guillet-Deniau, I., Pichard, A.-L., Kone, A., Esnous, C., Nieruchalski, M., Girard, J. and Prip-Buus, C. Glucose induces de novo lipogenesis in rat muscle satellite cells through a sterol-regulatory-element-binding-protein- 1c-dependent pathway. J. Cell Sci. 117 (2004) 1937-1944.
    • (2004) J. Cell Sci. , vol.117 , pp. 1937-1944
    • Guillet-Deniau, I.1    Pichard, A.-L.2    Kone, A.3    Esnous, C.4    Nieruchalski, M.5    Girard, J.6    Prip-Buus, C.7
  • 114
    • 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
  • 115
    • 21344447493 scopus 로고    scopus 로고
    • Long-term efficacy of leptin replacement in patients with generalized lipodystrophy
    • Javor, E.D., Cochran, E.K., Musso, C., Young, J.R., Depaoli, A.M. and Gorden, P. Long-term efficacy of leptin replacement in patients with generalized lipodystrophy. Diabetes 54 (2005) 1994-2002.
    • (2005) Diabetes , vol.54 , pp. 1994-2002
    • Javor, E.D.1    Cochran, E.K.2    Musso, C.3    Young, J.R.4    Depaoli, A.M.5    Gorden, P.6
  • 116
    • 33947283865 scopus 로고    scopus 로고
    • Longterm efficacy of leptin replacement in patients with Dunnigan-type familial partial lipodystrophy
    • Park, J.Y., Javor, E.D., Cochran, E.K., DePaoli, A.M. and Gorden, P. Longterm efficacy of leptin replacement in patients with Dunnigan-type familial partial lipodystrophy. Metabolism 56 (2007) 508-516.
    • (2007) Metabolism , vol.56 , pp. 508-516
    • Park, J.Y.1    Javor, E.D.2    Cochran, E.K.3    Depaoli, A.M.4    Gorden, P.5
  • 117
    • 51349153839 scopus 로고    scopus 로고
    • SREBP1 interaction with pre-lamin A forms: A pathogenic mechanism for lipodystrophic laminopathies
    • Maraldi, N.M., Capanni, C., Lattanzi, G., Camozzi, D., Facchini, A. and Manzoli, F.A. SREBP1 interaction with pre-lamin A forms: a pathogenic mechanism for lipodystrophic laminopathies. Adv. Enzyme Regul. 48 (2008) 209-223.
    • (2008) Adv. Enzyme Regul. , vol.48 , pp. 209-223
    • Maraldi, N.M.1    Capanni, C.2    Lattanzi, G.3    Camozzi, D.4    Facchini, A.5    Manzoli, F.A.6
  • 120
    • 33847342966 scopus 로고    scopus 로고
    • The nuclear lamina. Both a structural framework and a platform for genome organization
    • Bridger, J.M., Foeger, N., Kill, I.R. and Herrmann, H. The nuclear lamina. Both a structural framework and a platform for genome organization. FEBS J. 274 (2007) 1354-1361.
    • (2007) FEBS J , vol.274 , pp. 1354-1361
    • Bridger, J.M.1    Foeger, N.2    Kill, I.R.3    Herrmann, H.4
  • 121
    • 77956083200 scopus 로고    scopus 로고
    • Lamin-binding Proteins. Cold Spring Harb Perspect
    • Wilson, K.L. and Foisner, R. Lamin-binding Proteins. Cold Spring Harb Perspect. Biol. 2 (2010) a000554.
    • (2010) Biol , pp. 2
    • Wilson, K.L.1    Foisner, R.2
  • 122
    • 0036424455 scopus 로고    scopus 로고
    • In vivo phosphorylation of Drosophila melanogaster nuclear lamins during both interphase and mitosis
    • Rzepecki, R. and Fisher, P.A. In vivo phosphorylation of Drosophila melanogaster nuclear lamins during both interphase and mitosis. Cell. Mol. Biol. Lett. 7 (2002) 859-876.
    • (2002) Cell. Mol. Biol. Lett. , vol.7 , pp. 859-876
    • Rzepecki, R.1    Fisher, P.A.2
  • 123
    • 47549109045 scopus 로고    scopus 로고
    • Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies
    • Zhang, Y.Q. and Sarge, K.D. Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. J. Cell Biol. 182 (2008) 35-39.
    • (2008) J. Cell Biol. , vol.182 , pp. 35-39
    • Zhang, Y.Q.1    Sarge, K.D.2
  • 125
    • 70350418612 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of nuclear-membrane protein emerin by Src, Abl and other kinases
    • Tifft, K.E., Bradbury, K.A. and Wilson, K.L. Tyrosine phosphorylation of nuclear-membrane protein emerin by Src, Abl and other kinases. J. Cell Sci. 122 (2009) 3780-3790.
    • (2009) J. Cell Sci. , vol.122 , pp. 3780-3790
    • Tifft, K.E.1    Bradbury, K.A.2    Wilson, K.L.3
  • 130
    • 26444595257 scopus 로고    scopus 로고
    • Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice
    • Mounkes, L.C., Kozlov, S.V., Rottman, J.N. and Stewart, C.L. Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice. Hum. Mol. Genet. 14 (2006) 2167-2180.
    • (2006) Hum. Mol. Genet. , vol.14 , pp. 2167-2180
    • Mounkes, L.C.1    Kozlov, S.V.2    Rottman, J.N.3    Stewart, C.L.4
  • 131
    • 33747893889 scopus 로고    scopus 로고
    • Pathology and nuclear abnormalities in hearts of transgenic mice expressing M371K lamin A encoded by an LMNA mutation causing Emery-Dreifuss muscular dystrophy
    • Wang, Y., Herron, A.J. and Worman, H.J. Pathology and nuclear abnormalities in hearts of transgenic mice expressing M371K lamin A encoded by an LMNA mutation causing Emery-Dreifuss muscular dystrophy. Hum. Mol. Genet. 15 (2006) 2479-2489.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2479-2489
    • Wang, Y.1    Herron, A.J.2    Worman, H.J.3
  • 135
    • 0036791026 scopus 로고    scopus 로고
    • Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a pre-lamin A processing defect
    • Bergo, M.O. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a pre-lamin A processing defect. Proc. Natl. Acad. Sci. USA 99 (2002) 13049-13054.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 13049-13054
    • Bergo, M.O.1
  • 136
    • 10944256054 scopus 로고    scopus 로고
    • In vivo contribution of murine mesenchymal stem cells into multiple cell-types under minimal damage conditions
    • Anjos-Afonso, F., Siapati, E.K. and Bonnet, D. In vivo contribution of murine mesenchymal stem cells into multiple cell-types under minimal damage conditions. J. Cell Sci. 117 (2004) 5655-5664.
    • (2004) J. Cell Sci. , vol.117 , pp. 5655-5664
    • Anjos-Afonso, F.1    Siapati, E.K.2    Bonnet, D.3
  • 137
    • 4344610581 scopus 로고    scopus 로고
    • Regeneration of skeletal muscle from transplanted immortalised myoblasts is oligoclonal
    • Cousins, J.C., Woodward, K.J., Gross, J.G., Partridge, T.A. and Morgan, J.E. Regeneration of skeletal muscle from transplanted immortalised myoblasts is oligoclonal. J. Cell Sci. 117 (2004) 3259-3269.
    • (2004) J. Cell Sci. , vol.117 , pp. 3259-3269
    • Cousins, J.C.1    Woodward, K.J.2    Gross, J.G.3    Partridge, T.A.4    Morgan, J.E.5
  • 138
    • 4344645792 scopus 로고    scopus 로고
    • Marrow-isolated adult multilineage inducible (MIAMI) cells, a unique population of postnatal young and old human cells with extensive expansion and differentiation potential
    • DIppolito, G., Diabira, S., Howard, G.A., Menei, P., Roos, B.A. and Schiller, P.C. Marrow-isolated adult multilineage inducible (MIAMI) cells, a unique population of postnatal young and old human cells with extensive expansion and differentiation potential. J. Cell Sci. 117 (2004) 2971-2981.
    • (2004) J. Cell Sci. , vol.117 , pp. 2971-2981
    • Dippolito, G.1    Diabira, S.2    Howard, G.A.3    Menei, P.4    Roos, B.A.5    Schiller, P.C.6
  • 139
    • 33846467107 scopus 로고    scopus 로고
    • Mechanisms of action of mesenchymal stem cells in cardiac repair: Potential influences on the cardiac stem cell niche
    • Mazhari, R. and Hare, J.M. Mechanisms of action of mesenchymal stem cells in cardiac repair: potential influences on the cardiac stem cell niche. Nat. Clin. Pract. Cardiovasc. Med. 4 (2007) S21-26.
    • (2007) Nat. Clin. Pract. Cardiovasc. Med. , vol.4
    • Mazhari, R.1    Hare, J.M.2
  • 141
    • 77949433853 scopus 로고    scopus 로고
    • Potential of mesenchymal stem cells for the therapy of autoimmune diseases
    • Pistoia, V. and Raffaghello, L. Potential of mesenchymal stem cells for the therapy of autoimmune diseases. Expert Rev. Clin. Immunol. 6 (2010) 211-218.
    • (2010) Expert Rev. Clin. Immunol. , vol.6 , pp. 211-218
    • Pistoia, V.1    Raffaghello, L.2
  • 142
    • 77953728022 scopus 로고    scopus 로고
    • Genetically modified mesenchymal stem cells and their clinical potential in acute cardiovascular disease
    • Griffin, M., Greiser, U., Barry, F., O'Brien, T. and Ritter, T. Genetically modified mesenchymal stem cells and their clinical potential in acute cardiovascular disease. Discov. Med. 9 (2010) 219-223.
    • (2010) Discov. Med. , vol.9 , pp. 219-223
    • Griffin, M.1    Greiser, U.2    Barry, F.3    O'Brien, T.4    Ritter, T.5
  • 143
    • 12344337753 scopus 로고    scopus 로고
    • Stem cell antigen-1 is necessary for cell-cycle withdrawal and myoblast differentiation in C2C12 cells
    • Epting, C.L., Lopez, J.E., Shen, X., Liu, L., Bristow, J. and Bernstein, H.S. Stem cell antigen-1 is necessary for cell-cycle withdrawal and myoblast differentiation in C2C12 cells. J. Cell Sci. 117 (2004) 6185-6195.
    • (2004) J. Cell Sci. , vol.117 , pp. 6185-6195
    • Epting, C.L.1    Lopez, J.E.2    Shen, X.3    Liu, L.4    Bristow, J.5    Bernstein, H.S.6
  • 144
    • 2942547646 scopus 로고    scopus 로고
    • Role of bone marrow cell trafficking in replenishing skeletal muscle SP and MP cell populations
    • Rivier, F., Alkan, O., Flint, A.F., Muskiewicz, K., Allen, P.D., Leboulch, P. and Gussoni, E. Role of bone marrow cell trafficking in replenishing skeletal muscle SP and MP cell populations. J. Cell Sci. 117 (2004) 1979-1988.
    • (2004) J. Cell Sci. , vol.117 , pp. 1979-1988
    • Rivier, F.1    Alkan, O.2    Flint, A.F.3    Muskiewicz, K.4    Allen, P.D.5    Leboulch, P.6    Gussoni, E.7
  • 145
    • 76749152709 scopus 로고    scopus 로고
    • Integrase-defective lentiviral vectors: Progress and applications
    • Banasik, M.B. and McCray, P.B.J. Integrase-defective lentiviral vectors: progress and applications. Gene Ther. 17 (2010) 150-157.
    • (2010) Gene Ther , vol.17 , pp. 150-157
    • Banasik, M.B.1    McCray, P.B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.