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Volumn 8, Issue 12, 2013, Pages

Viscoelastic behavior of human lamin A proteins in the context of dilated cardiomyopathy

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOMYOPATHY, DILATED; CELL LINE; ELASTICITY; GENE EXPRESSION; HUMANS; LAMIN TYPE A; MUTATION; PROTEIN FOLDING; SHEAR STRENGTH; VISCOSITY;

EID: 84893566167     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0083410     Document Type: Article
Times cited : (28)

References (67)
  • 1
    • 0013925189 scopus 로고
    • On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates
    • Fawcett DW (1966) On the occurrence of a fibrous lamina on the inner aspect of the nuclear envelope in certain cells of vertebrates. Am J Anat 119: 129-145.
    • (1966) Am J Anat , vol.119 , pp. 129-145
    • Fawcett, D.W.1
  • 3
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate Filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • DOI 10.1146/annurev.biochem.73.011303.073823
    • Herrmann H, Aebi U (2004) Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu Rev Biochem 73: 749-789. (Pubitemid 39050385)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 4
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L, Burke B (1988) Functional organization of the nuclear envelope. Annu Rev Cell Biol 4: 335-374. (Pubitemid 19139260)
    • (1988) Annual Review of Cell Biology , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 5
    • 0023085878 scopus 로고
    • The nucleus: Structure, function, and dynamics
    • Newport JW, Forbes DJ (1987) The nucleus: structure, function, and dynamics. Annu Rev Biochem 56: 535-565.
    • (1987) Annu Rev Biochem , vol.56 , pp. 535-565
    • Newport, J.W.1    Forbes, D.J.2
  • 8
    • 0028247078 scopus 로고
    • Dynamic properties of nuclear lamins: Lamin B is associated with sites of DNA replication
    • DOI 10.1083/jcb.125.6.1201
    • Moir RD, Montag-Lowy M, Goldman RD (1994) Dynamic properties of nuclear lamins: lamin B is associated with sites of DNA replication. J Cell Biol 125: 1201-1212. (Pubitemid 24189526)
    • (1994) Journal of Cell Biology , vol.125 , Issue.6 , pp. 1201-1212
    • Moir, R.D.1    Montag-Lowy, M.2    Goldman, R.D.3
  • 9
    • 0026733562 scopus 로고
    • Ligand-independent reduction of cAMP receptors in Dictyostelium discoideum cells over-expressing a mutated ras gene
    • Luderus ME, Kesbeke F, Knetsch ML, Van Driel R, Reymond CD, et al. (1992) Ligand-independent reduction of cAMP receptors in Dictyostelium discoideum cells over-expressing a mutated ras gene. Eur J Biochem 208: 235-240.
    • (1992) Eur J Biochem , vol.208 , pp. 235-240
    • Luderus, M.E.1    Kesbeke, F.2    Knetsch, M.L.3    Van Driel, R.4    Reymond, C.D.5
  • 10
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak P, Sasseville AM, Raymond Y, Cook PR (1995) Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J Cell Sci 108 (Pt 2): 635-644.
    • (1995) J Cell Sci , vol.108 , Issue.PART 2 , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 11
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins A and B1: Different pathways of assembly during nuclear envelope formation in living cells
    • Moir RD, Yoon M, Khuon S, Goldman RD (2000) Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells. J Cell Biol 151: 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
  • 12
    • 80054715001 scopus 로고    scopus 로고
    • Lamin A and lamin C form homodimers and coexist in higher complex forms both in the nucleoplasmic fraction and in the lamina of cultured human cells
    • Kolb T, Maab K, Hergt M, Aebi U, Herrmann H (2011) Lamin A and lamin C form homodimers and coexist in higher complex forms both in the nucleoplasmic fraction and in the lamina of cultured human cells. Nucleus 2: 425-433.
    • (2011) Nucleus , vol.2 , pp. 425-433
    • Kolb, T.1    Maab, K.2    Hergt, M.3    Aebi, U.4    Herrmann, H.5
  • 13
    • 38949154474 scopus 로고    scopus 로고
    • Filaments made from A- and B-type lamins differ in structure and organization
    • DOI 10.1242/jcs.022020
    • Goldberg MW, Huttenlauch I, Hutchison CJ, Stick R (2008) Filaments made from A-and B-type lamins differ in structure and organization. J Cell Sci 121: 215-225. (Pubitemid 351228454)
    • (2008) Journal of Cell Science , vol.121 , Issue.2 , pp. 215-225
    • Goldberg, M.W.1    Huttenlauch, I.2    Hutchison, C.J.3    Stick, R.4
  • 14
    • 58049195492 scopus 로고    scopus 로고
    • The A-and B-type nuclear lamin networks: Microdomains involved in chromatin organization and transcription
    • Shimi T, Pfleghaar K, Kojima S-i, Pack C-G, Solovei I, et al. (2008) The A-and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev 22: 3409-3421.
    • (2008) Genes Dev , vol.22 , pp. 3409-3421
    • Shimi, T.1    Pfleghaar, K.2    Kojima, S.-I.3    Pack, C.-G.4    Solovei, I.5
  • 15
    • 33645116709 scopus 로고    scopus 로고
    • The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers
    • Delbarre E, Tramier M, Coppey-Moisan M, Gaillard C, Courvalin JC, et al. (2006) The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers. Hum Mol Genet 15: 1113-1122.
    • (2006) Hum Mol Genet , vol.15 , pp. 1113-1122
    • Delbarre, E.1    Tramier, M.2    Coppey-Moisan, M.3    Gaillard, C.4    Courvalin, J.C.5
  • 16
    • 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
    • DOI 10.1074/jbc.M407705200
    • Schirmer EC, Gerace L (2004) The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths. J Biol Chem 279: 42811-42817. (Pubitemid 39372169)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 42811-42817
    • Schirmer, E.C.1    Gerace, L.2
  • 17
    • 0033518282 scopus 로고    scopus 로고
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease
    • Fatkin D, MacRae C, Sasaki T, Wolff MR, Porcu M, et al. (1999) Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N Engl J Med 341: 1715-1724.
    • (1999) N Engl J Med , vol.341 , pp. 1715-1724
    • Fatkin, D.1    MacRae, C.2    Sasaki, T.3    Wolff, M.R.4    Porcu, M.5
  • 18
    • 0028116218 scopus 로고
    • Idiopathic dilated cardiomyopathy
    • DOI 10.1056/NEJM199412083312307
    • Dec GW, Fuster V (1994) Idiopathic dilated cardiomyopathy. N Engl J Med 331: 1564-1575. (Pubitemid 24366905)
    • (1994) New England Journal of Medicine , vol.331 , Issue.23 , pp. 1564-1575
    • Dec, G.W.1    Fuster, V.2
  • 19
    • 14644442325 scopus 로고    scopus 로고
    • Both lamin A and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization
    • DOI 10.1016/j.yexcr.2004.11.020
    • Broers JL, Kuijpers HJ, Ostlund C, Worman HJ, Endert J, et al. (2005) Both lamin A and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization. Exp Cell Res 304: 582-592. (Pubitemid 40321134)
    • (2005) Experimental Cell Research , vol.304 , Issue.2 , pp. 582-592
    • Broers, J.L.V.1    Kuijpers, H.J.H.2    Ostlund, C.3    Worman, H.J.4    Endert, J.5    Ramaekers, F.C.S.6
  • 21
    • 6344282993 scopus 로고    scopus 로고
    • Nuclear envelope breakdown requires overcoming the mechanical integrity of the nuclear lamina
    • DOI 10.1074/jbc.M402474200
    • Panorchan P, Schafer BW, Wirtz D, Tseng Y (2004) Nuclear envelope breakdown requires overcoming the mechanical integrity of the nuclear lamina. J Biol Chem 279: 43462-43467. (Pubitemid 39390645)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 43462-43467
    • Panorchan, P.1    Schafer, B.W.2    Wirtz, D.3    Tseng, Y.4
  • 22
    • 16244388205 scopus 로고    scopus 로고
    • The nuclear membrane and mechanotransduction: Impaired nuclear mechanics and mechanotransduction in lamin A/C deficient cells
    • discussion 273-268
    • Lammerding J, Lee RT (2005) The nuclear membrane and mechanotransduction: impaired nuclear mechanics and mechanotransduction in lamin A/C deficient cells. Novartis Found Symp 264: 264-273; discussion 273-268.
    • (2005) Novartis Found Symp , vol.264 , pp. 264-273
    • Lammerding, J.1    Lee, R.T.2
  • 23
    • 34347241775 scopus 로고    scopus 로고
    • Studying the mechanics of cellular processes by atomic force microscopy
    • Radmacher M (2007) Studying the mechanics of cellular processes by atomic force microscopy. Methods Cell Biol 83: 347-372.
    • (2007) Methods Cell Biol , vol.83 , pp. 347-372
    • Radmacher, M.1
  • 25
    • 40349101951 scopus 로고    scopus 로고
    • Towards an integrated understanding of the structure and mechanics of the cell nucleus
    • DOI 10.1002/bies.20720
    • Rowat AC, Lammerding J, Herrmann H, Aebi U (2008) Towards an integrated understanding of the structure and mechanics of the cell nucleus. Bioessays 30: 226-236. (Pubitemid 351341127)
    • (2008) BioEssays , vol.30 , Issue.3 , pp. 226-236
    • Rowat, A.C.1    Lammerding, J.2    Herrmann, H.3    Aebi, U.4
  • 26
    • 25844513869 scopus 로고    scopus 로고
    • Power-law rheology of isolated nuclei with deformation mapping of nuclear substructures
    • DOI 10.1529/biophysj.105.062554
    • Dahl KN, Engler AJ, Pajerowski JD, Discher DE (2005) Power-law rheology of isolated nuclei with deformation mapping of nuclear substructures. Biophys J 89: 2855-2864. (Pubitemid 41401072)
    • (2005) Biophysical Journal , vol.89 , Issue.4 , pp. 2855-2864
    • Dahl, K.N.1    Engler, A.J.2    Pajerowski, J.D.3    Discher, D.E.4
  • 27
    • 4544228141 scopus 로고    scopus 로고
    • The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
    • DOI 10.1242/jcs.01357
    • Dahl KN, Kahn SM, Wilson KL, Discher DE (2004) The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. J Cell Sci 117: 4779-4786. (Pubitemid 39433444)
    • (2004) Journal of Cell Science , vol.117 , Issue.20 , pp. 4779-4786
    • Dahl, K.N.1    Kahn, S.M.2    Wilson, K.L.3    Discher, D.E.4
  • 28
    • 68049139442 scopus 로고    scopus 로고
    • Influence of lamin A on the mechanical properties of amphibian oocyte nuclei measured by atomic force microscopy
    • Schäpe J, Prausse S, Radmacher M, Stick R (2009) Influence of lamin A on the mechanical properties of amphibian oocyte nuclei measured by atomic force microscopy. Biophy J 96: 4319-4325.
    • (2009) Biophy J , vol.96 , pp. 4319-4325
    • Schäpe, J.1    Prausse, S.2    Radmacher, M.3    Stick, R.4
  • 29
    • 84883059455 scopus 로고    scopus 로고
    • Nuclear Lamin-A Scales with Tissue Stiffness and Enhances Matrix-Directed Differentiation
    • Swift J, Ivanovska IL, Buxboim A, Harada T, Dingal PDP, et al. (2013) Nuclear Lamin-A Scales with Tissue Stiffness and Enhances Matrix-Directed Differentiation. Science 341: 1240104.
    • (2013) Science , vol.341 , pp. 1240104
    • Swift, J.1    Ivanovska, I.L.2    Buxboim, A.3    Harada, T.4    Dingal, P.D.P.5
  • 30
  • 31
    • 57949113000 scopus 로고    scopus 로고
    • Identification of mutational hot spots in LMNA encoding lamin A/C in patients with familial dilated cardiomyopathy
    • Perrot A, Hussein S, Ruppert V, Schmidt HH, Wehnert MS, et al. (2009) Identification of mutational hot spots in LMNA encoding lamin A/C in patients with familial dilated cardiomyopathy. Basic Res Cardiol 104: 90-99.
    • (2009) Basic Res Cardiol , vol.104 , pp. 90-99
    • Perrot, A.1    Hussein, S.2    Ruppert, V.3    Schmidt, H.H.4    Wehnert, M.S.5
  • 33
    • 79960214825 scopus 로고    scopus 로고
    • Gene expression, chromosome position and lamin A/C mutations
    • Puckelwartz MJ, Depreux FF, McNally EM (2011) Gene expression, chromosome position and lamin A/C mutations. Nucleus 2: 162-167.
    • (2011) Nucleus , vol.2 , pp. 162-167
    • Puckelwartz, M.J.1    Depreux, F.F.2    McNally, E.M.3
  • 34
    • 52949111684 scopus 로고    scopus 로고
    • Long-term outcome and risk stratification in dilated cardiolaminopathies
    • Pasotti M, Klersy C, Pilotto A, Marziliano N, Rapezzi C, et al. (2008) Long-term outcome and risk stratification in dilated cardiolaminopathies. J Am Coll Cardiol 52: 1250-1260.
    • (2008) J Am Coll Cardiol , vol.52 , pp. 1250-1260
    • Pasotti, M.1    Klersy, C.2    Pilotto, A.3    Marziliano, N.4    Rapezzi, C.5
  • 36
    • 0025876766 scopus 로고
    • Expression in Escherichia coli of human lamins A and C: Influence of head and tail domains on assembly properties and paracrystal formation
    • Moir RD, Donaldson AD, Stewart M (1991) Expression in Escherichia coli of human lamins A and C: influence of head and tail domains on assembly properties and paracrystal formation. J Cell Sci 99 (Pt 2): 363-372. (Pubitemid 21925024)
    • (1991) Journal of Cell Science , vol.99 , Issue.2 , pp. 363-372
    • Moir, R.D.1    Donaldson, A.D.2    Stewart, M.3
  • 38
    • 0043169526 scopus 로고    scopus 로고
    • The mechanical properties of simple epithelial keratins 8 and 18: Discriminating between interfacial and bulk elasticities
    • DOI 10.1016/S1047-8477(03)00101-1
    • Yamada S, Wirtz D, Coulombe PA (2003) The mechanical properties of simple epithelial keratins 8 and 18: discriminating between interfacial and bulk elasticities. J Struct Biol 143: 45-55. (Pubitemid 36918491)
    • (2003) Journal of Structural Biology , vol.143 , Issue.1 , pp. 45-55
    • Yamada, S.1    Wirtz, D.2    Coulombe, P.A.3
  • 40
    • 19744380331 scopus 로고    scopus 로고
    • Scaling of F-actin network rheology to probe single filament elasticity and dynamics
    • Gardel M, Shin J, MacKintosh F, Mahadevan L, Matsudaira P, et al. (2004) Scaling of F-actin network rheology to probe single filament elasticity and dynamics. Phys Rev Lett 93: 188102.
    • (2004) Phys Rev Lett , vol.93 , pp. 188102
    • Gardel, M.1    Shin, J.2    MacKintosh, F.3    Mahadevan, L.4    Matsudaira, P.5
  • 41
    • 0016633449 scopus 로고
    • Infinite-dilution viscoelastic properties of tobacco mosaic virus
    • Nemoto N, Schrag JL, Ferry JD, Fulton RW (1975) Infinite-dilution viscoelastic properties of tobacco mosaic virus. Biopolymers 14: 409-417.
    • (1975) Biopolymers , vol.14 , pp. 409-417
    • Nemoto, N.1    Schrag, J.L.2    Ferry, J.D.3    Fulton, R.W.4
  • 42
    • 0020203413 scopus 로고    scopus 로고
    • Lower frequency and higher frequency relaxations in dynamic electric birefringence of poly (γ-Benzyl L-Glutamate) in m-cresol
    • Mori Y, Ookubo N, Hayakawa R, Wada Y (2003) Lower frequency and higher frequency relaxations in dynamic electric birefringence of poly (γ-Benzyl L-Glutamate) in m-cresol. J Polym Sci: Pol Phys Edition 20: 2111-2124.
    • (2003) J Polym Sci: Pol Phys Edition , vol.20 , pp. 2111-2124
    • Mori, Y.1    Ookubo, N.2    Hayakawa, R.3    Wada, Y.4
  • 44
    • 0034680846 scopus 로고    scopus 로고
    • Strain Hardening of actin filament networks regulation by the dynamic cross-linking protein α- Actinin
    • Xu J, Tseng Y, Wirtz D (2000) Strain Hardening of actin filament networks regulation by the dynamic cross-linking protein α- actinin. J Biol Chem 275: 35886-35892.
    • (2000) J Biol Chem , vol.275 , pp. 35886-35892
    • Xu, J.1    Tseng, Y.2    Wirtz, D.3
  • 46
    • 46049117087 scopus 로고    scopus 로고
    • Probing nonlinear rheology with inertioelastic oscillations
    • Yao NY, Larsen RJ, Weitz DA (2008) Probing nonlinear rheology with inertioelastic oscillations. J Rheol 52: 1013.
    • (2008) J Rheol , vol.52 , pp. 1013
    • Yao, N.Y.1    Larsen, R.J.2    Weitz, D.A.3
  • 47
  • 48
    • 36949026410 scopus 로고    scopus 로고
    • The glassy wormlike chain
    • Kroy K, Glaser J (2007) The glassy wormlike chain. New J Phys 9: 416.
    • (2007) New J Phys , vol.9 , pp. 416
    • Kroy, K.1    Glaser, J.2
  • 49
    • 84883365377 scopus 로고    scopus 로고
    • Mechanics of intermediate filament networks assembled from keratins K8 and K18
    • Pawelzyk P, Herrmann H, Willenbacher N (2013) Mechanics of intermediate filament networks assembled from keratins K8 and K18. Soft Matter 9: 8871-8880.
    • (2013) Soft Matter , vol.9 , pp. 8871-8880
    • Pawelzyk, P.1    Herrmann, H.2    Willenbacher, N.3
  • 51
    • 0001051166 scopus 로고    scopus 로고
    • Scaling of the microrheology of semidilute F-actin solutions
    • Gisler T, Weitz DA (1999) Scaling of the microrheology of semidilute F-actin solutions. Phys Rev Lett 82: 1606-1609. (Pubitemid 129646685)
    • (1999) Physical Review Letters , vol.82 , Issue.7 , pp. 1606-1609
    • Gisler, T.1    Weitz, D.A.2
  • 52
    • 33846314328 scopus 로고    scopus 로고
    • Reversible stress softening of actin networks
    • DOI 10.1038/nature05459, PII NATURE05459
    • Chaudhuri O, Parekh SH, Fletcher DA (2007) Reversible stress softening of actin networks. Nature 445: 295-298. (Pubitemid 46122813)
    • (2007) Nature , vol.445 , Issue.7125 , pp. 295-298
    • Chaudhuri, O.1    Parekh, S.H.2    Fletcher, D.A.3
  • 54
    • 0025765110 scopus 로고
    • Viscoelastic properties of vimentin compared with other filamentous biopolymer networks
    • Janmey PA, Euteneuer U, Traub P, Schliwa M (1991) Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol 113: 155-160. (Pubitemid 21909682)
    • (1991) Journal of Cell Biology , vol.113 , Issue.1 , pp. 155-160
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 55
    • 63449103436 scopus 로고    scopus 로고
    • Desmin and vimentin intermediate filament networks: Their viscoelastic properties investigated by mechanical rheometry
    • Schopferer M, Bar H, Hochstein B, Sharma S, Mucke N, et al. (2009) Desmin and vimentin intermediate filament networks: their viscoelastic properties investigated by mechanical rheometry. J Mol Biol 388: 133-143.
    • (2009) J Mol Biol , vol.388 , pp. 133-143
    • Schopferer, M.1    Bar, H.2    Hochstein, B.3    Sharma, S.4    Mucke, N.5
  • 56
    • 0031045209 scopus 로고    scopus 로고
    • Heterotypic interactions and filament assembly of type I and type II cytokeratins in vitro: Viscometry and determinations of relative affinities
    • Hofmann I, Franke W (1997) Heterotypic interactions and filament assembly of type I and type II cytokeratins in vitro: viscometry and determinations of relative affinities. EurJ Cell Biol 72: 122.
    • (1997) EurJ Cell Biol , vol.72 , pp. 122
    • Hofmann, I.1    Franke, W.2
  • 57
    • 77749309961 scopus 로고    scopus 로고
    • Dynamics of the bacterial intermediate filament crescentin in vitro and in vivo
    • Esue O, Rupprecht L, Sun SX, Wirtz D (2010) Dynamics of the bacterial intermediate filament crescentin in vitro and in vivo. PLoS One 5: e8855.
    • (2010) PLoS One , vol.5
    • Esue, O.1    Rupprecht, L.2    Sun, S.X.3    Wirtz, D.4
  • 58
    • 0029814578 scopus 로고    scopus 로고
    • Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract
    • Zhang C, Jenkins H, Goldberg MW, Allen TD, Hutchison CJ (1996) Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract. J Cell Sci 109 (Pt 9): 2275-2286. (Pubitemid 26325490)
    • (1996) Journal of Cell Science , vol.109 , Issue.9 , pp. 2275-2286
    • Zhang, C.1    Jenkins, H.2    Goldberg, M.W.3    Allen, T.D.4    Hutchison, C.J.5
  • 59
    • 34249782557 scopus 로고    scopus 로고
    • Invertebrate lamins
    • DOI 10.1016/j.yexcr.2007.03.004, PII S0014482707001073
    • Melcer S, Gruenbaum Y, Krohne G (2007) Invertebrate lamins. Exp Cell Res 313: 2157-2166. (Pubitemid 46844822)
    • (2007) Experimental Cell Research , vol.313 , Issue.10 , pp. 2157-2166
    • Melcer, S.1    Gruenbaum, Y.2    Krohne, G.3
  • 60
    • 84455208122 scopus 로고    scopus 로고
    • Mouse B-Type Lamins Are Required for Proper Organogenesis But Not by Embryonic Stem Cells
    • Kim Y, Sharov AA, McDole K, Cheng M, Hao H, et al. (2011) Mouse B-Type Lamins Are Required for Proper Organogenesis But Not by Embryonic Stem Cells. Science 334: 1706-1710.
    • (2011) Science , vol.334 , pp. 1706-1710
    • Kim, Y.1    Sharov, A.A.2    McDole, K.3    Cheng, M.4    Hao, H.5
  • 61
    • 67650047792 scopus 로고    scopus 로고
    • Changing nuclear landscape and unique PML structures during early epigenetic transitions of human embryonic stem cells
    • Butler JT, Hall LL, Smith KP, Lawrence JB (2009) Changing nuclear landscape and unique PML structures during early epigenetic transitions of human embryonic stem cells. J Cel Biochem 107: 609-621.
    • (2009) J Cel Biochem , vol.107 , pp. 609-621
    • Butler, J.T.1    Hall, L.L.2    Smith, K.P.3    Lawrence, J.B.4
  • 63
    • 84862812868 scopus 로고    scopus 로고
    • Chromatin plasticity as a differentiation index during muscle differentiation of C2C12 myoblasts
    • Watanabe TM, Higuchi S, Kawauchi K, Tsukasaki Y, Ichimura T, et al. (2012) Chromatin plasticity as a differentiation index during muscle differentiation of C2C12 myoblasts. Biochem Biophys Res Commun 418: 742-747.
    • (2012) Biochem Biophys Res Commun , vol.418 , pp. 742-747
    • Watanabe, T.M.1    Higuchi, S.2    Kawauchi, K.3    Tsukasaki, Y.4    Ichimura, T.5
  • 64
    • 41349120957 scopus 로고    scopus 로고
    • Structure-function relationship of biological gels revealed by multiple-particle tracking and differential interference contrast microscopy: The case of human lamin networks
    • Panorchan P, Wirtz D, Tseng Y (2004) Structure-function relationship of biological gels revealed by multiple-particle tracking and differential interference contrast microscopy: the case of human lamin networks. Phys Rev E Stat Nonlin Soft Matter Phys 70: 041906.
    • (2004) Phys Rev E Stat Nonlin Soft Matter Phys , vol.70 , pp. 041906
    • Panorchan, P.1    Wirtz, D.2    Tseng, Y.3


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