메뉴 건너뛰기




Volumn 124, Issue 1, 2015, Pages

Do lamin A and lamin C have unique roles?

Author keywords

Alternative splicing; Isoforms; Lamin A and lamin C; Laminopathies and distinct functions; Nuclear lamina

Indexed keywords

ISOPROTEIN; LAMIN A; LMNA PROTEIN, HUMAN; LMNA PROTEIN, MOUSE;

EID: 85027939794     PISSN: 00095915     EISSN: 14320886     Source Type: Journal    
DOI: 10.1007/s00412-014-0484-7     Document Type: Review
Times cited : (20)

References (98)
  • 2
    • 26444442065 scopus 로고    scopus 로고
    • Different splicing defects lead to differential effects downstream of the lipid and protein phosphatase activities of PTEN
    • COI: 1:CAS:528:DC%2BD2MXpsFams7c%3D, PID: 16014636
    • Agrawal S, Pilarski R, Eng C (2005) Different splicing defects lead to differential effects downstream of the lipid and protein phosphatase activities of PTEN. Hum Mol Genet 14(16):2459–2468. doi:10.1093/hmg/ddi246
    • (2005) Hum Mol Genet , vol.14 , Issue.16 , pp. 2459-2468
    • Agrawal, S.1    Pilarski, R.2    Eng, C.3
  • 3
    • 84886589170 scopus 로고    scopus 로고
    • The LMNA mutation p.Arg321Ter associated with dilated cardiomyopathy leads to reduced expression and a skewed ratio of lamin A and lamin C proteins
    • PID: 24001739
    • Al-Saaidi R, Rasmussen TB, Palmfeldt J, Nissen PH, Beqqali A, Hansen J, Bross P (2013) The LMNA mutation p.Arg321Ter associated with dilated cardiomyopathy leads to reduced expression and a skewed ratio of lamin A and lamin C proteins. Exp Cell Res. doi:10.1016/j.yexcr.2013.08.024
    • (2013) Exp Cell Res
    • Al-Saaidi, R.1    Rasmussen, T.B.2    Palmfeldt, J.3    Nissen, P.H.4    Beqqali, A.5    Hansen, J.6    Bross, P.7
  • 4
    • 19944426537 scopus 로고    scopus 로고
    • Mouse model carrying H222P-Lmna mutation develops muscular dystrophy and dilated cardiomyopathy similar to human striated muscle laminopathies
    • COI: 1:CAS:528:DC%2BD2MXitFGlsQ%3D%3D, PID: 15548545
    • Arimura T, Helbling-Leclerc A, Massart C, Varnous S, Niel F, Lacene E, Bonne G (2005) Mouse model carrying H222P-Lmna mutation develops muscular dystrophy and dilated cardiomyopathy similar to human striated muscle laminopathies. Hum Mol Genet 14(1):155–169. doi:10.1093/hmg/ddi017
    • (2005) Hum Mol Genet , vol.14 , Issue.1 , pp. 155-169
    • Arimura, T.1    Helbling-Leclerc, A.2    Massart, C.3    Varnous, S.4    Niel, F.5    Lacene, E.6    Bonne, G.7
  • 5
    • 0025362748 scopus 로고
    • Isoprenylation is required for the processing of the lamin A precursor
    • COI: 1:CAS:528:DyaK3cXhvFGkt7g%3D, PID: 2335559
    • Beck LA, Hosick TJ, Sinensky M (1990) Isoprenylation is required for the processing of the lamin A precursor. J Cell Biol 110(5):1489–1499
    • (1990) J Cell Biol , vol.110 , Issue.5 , pp. 1489-1499
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 6
    • 60849130395 scopus 로고    scopus 로고
    • The supramolecular organization of the C. elegans nuclear lamin filament
    • COI: 1:CAS:528:DC%2BD1MXisFamsL4%3D, PID: 19109977
    • Ben-Harush K, Wiesel N, Frenkiel-Krispin D, Moeller D, Soreq E, Aebi U, Medalia O (2009) The supramolecular organization of the C. elegans nuclear lamin filament. J Mol Biol 386(5):1392–1402. doi:10.1016/j.jmb.2008.12.024
    • (2009) J Mol Biol , vol.386 , Issue.5 , pp. 1392-1402
    • Ben-Harush, K.1    Wiesel, N.2    Frenkiel-Krispin, D.3    Moeller, D.4    Soreq, E.5    Aebi, U.6    Medalia, O.7
  • 7
    • 14644442325 scopus 로고    scopus 로고
    • Both lamin A and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization
    • COI: 1:CAS:528:DC%2BD2MXhvVCkt7k%3D, PID: 15748902
    • Broers JL, Kuijpers HJ, Ostlund C, Worman HJ, Endert J, Ramaekers FC (2005) Both lamin A and lamin C mutations cause lamina instability as well as loss of internal nuclear lamin organization. Exp Cell Res 304(2):582–592. doi:10.1016/j.yexcr.2004.11.020
    • (2005) Exp Cell Res , vol.304 , Issue.2 , pp. 582-592
    • Broers, J.L.1    Kuijpers, H.J.2    Ostlund, C.3    Worman, H.J.4    Endert, J.5    Ramaekers, F.C.6
  • 8
    • 33750379023 scopus 로고    scopus 로고
    • The laminopathies: the functional architecture of the nucleus and its contribution to disease
    • COI: 1:CAS:528:DC%2BD28Xht1Wgsr3E, PID: 16824021
    • Burke B, Stewart CL (2006) The laminopathies: the functional architecture of the nucleus and its contribution to disease. Annu Rev Genomics Hum Genet 7:369–405. doi:10.1146/annurev.genom.7.080505.115732
    • (2006) Annu Rev Genomics Hum Genet , vol.7 , pp. 369-405
    • Burke, B.1    Stewart, C.L.2
  • 9
    • 43449107982 scopus 로고    scopus 로고
    • Perturbation of wild-type lamin A metabolism results in a progeroid phenotype
    • COI: 1:CAS:528:DC%2BD1cXntFWntro%3D, PID: 18363904
    • Candelario J, Sudhakar S, Navarro S, Reddy S, Comai L (2008) Perturbation of wild-type lamin A metabolism results in a progeroid phenotype. Aging Cell 7(3):355–367. doi:10.1111/j.1474-9726.2008.00393.x
    • (2008) Aging Cell , vol.7 , Issue.3 , pp. 355-367
    • Candelario, J.1    Sudhakar, S.2    Navarro, S.3    Reddy, S.4    Comai, L.5
  • 10
    • 56249094179 scopus 로고    scopus 로고
    • Prelamin A is involved in early steps of muscle differentiation
    • COI: 1:CAS:528:DC%2BD1cXhsVWrtrrP, PID: 18951892
    • Capanni C, Del Coco R, Squarzoni S, Columbaro M, Mattioli E, Camozzi D, Lattanzi G (2008) Prelamin A is involved in early steps of muscle differentiation. Exp Cell Res 314(20):3628–3637. doi:10.1016/j.yexcr.2008.09.026
    • (2008) Exp Cell Res , vol.314 , Issue.20 , pp. 3628-3637
    • Capanni, C.1    Del Coco, R.2    Squarzoni, S.3    Columbaro, M.4    Mattioli, E.5    Camozzi, D.6    Lattanzi, G.7
  • 11
    • 20144368040 scopus 로고    scopus 로고
    • Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy
    • COI: 1:CAS:528:DC%2BD2MXjtVersbg%3D, PID: 15744034
    • Cenni V, Sabatelli P, Mattioli E, Marmiroli S, Capanni C, Ognibene A, Lattanzi G (2005) Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy. J Med Genet 42(3):214–220. doi:10.1136/jmg.2004.026112
    • (2005) J Med Genet , vol.42 , Issue.3 , pp. 214-220
    • Cenni, V.1    Sabatelli, P.2    Mattioli, E.3    Marmiroli, S.4    Capanni, C.5    Ognibene, A.6    Lattanzi, G.7
  • 12
    • 77954234017 scopus 로고    scopus 로고
    • Direct synthesis of lamin A, bypassing prelamin A processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice
    • COI: 1:CAS:528:DC%2BC3cXnvFSitLY%3D, PID: 20439468
    • Coffinier C, Jung HJ, Li Z, Nobumori C, Yun UJ, Farber EA, Young SG (2010) Direct synthesis of lamin A, bypassing prelamin A processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice. J Biol Chem 285(27):20818–20826. doi:10.1074/jbc.M110.128835
    • (2010) J Biol Chem , vol.285 , Issue.27 , pp. 20818-20826
    • Coffinier, C.1    Jung, H.J.2    Li, Z.3    Nobumori, C.4    Yun, U.J.5    Farber, E.A.6    Young, S.G.7
  • 13
    • 0024992429 scopus 로고
    • Differential transport and integration into the nuclear lamina for lamins A, B, and C
    • COI: 1:CAS:528:DyaK3cXkvFGhsbY%3D, PID: 2205247
    • Dagenais A, LeMyre A, Bibor-Hardy V (1990) Differential transport and integration into the nuclear lamina for lamins A, B, and C. Biochem Cell Biol 68(5):827–831
    • (1990) Biochem Cell Biol , vol.68 , Issue.5 , pp. 827-831
    • Dagenais, A.1    LeMyre, A.2    Bibor-Hardy, V.3
  • 15
    • 0032541346 scopus 로고    scopus 로고
    • Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics
    • COI: 1:CAS:528:DyaK1cXlslyiurY%3D, PID: 9707448
    • Dechat T, Gotzmann J, Stockinger A, Harris CA, Talle MA, Siekierka JJ, Foisner R (1998) Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics. EMBO J 17(16):4887–4902. doi:10.1093/emboj/17.16.4887
    • (1998) EMBO J , vol.17 , Issue.16 , pp. 4887-4902
    • Dechat, T.1    Gotzmann, J.2    Stockinger, A.3    Harris, C.A.4    Talle, M.A.5    Siekierka, J.J.6    Foisner, R.7
  • 16
    • 0037124053 scopus 로고    scopus 로고
    • Structure of the globular tail of nuclear lamin
    • COI: 1:CAS:528:DC%2BD38XktVCgsb0%3D, PID: 11901143
    • Dhe-Paganon S, Werner ED, Chi YI, Shoelson SE (2002) Structure of the globular tail of nuclear lamin. J Biol Chem 277(20):17381–17384. doi:10.1074/jbc.C200038200
    • (2002) J Biol Chem , vol.277 , Issue.20 , pp. 17381-17384
    • Dhe-Paganon, S.1    Werner, E.D.2    Chi, Y.I.3    Shoelson, S.E.4
  • 17
    • 79957654428 scopus 로고    scopus 로고
    • The lamin protein family
    • COI: 1:CAS:528:DC%2BC3MXotVWnsrs%3D, PID: 21639948
    • Dittmer TA, Misteli T (2011) The lamin protein family. Genome Biol 12(5):222. doi:10.1186/gb-2011-12-5-222
    • (2011) Genome Biol , vol.12 , Issue.5 , pp. 222
    • Dittmer, T.A.1    Misteli, T.2
  • 18
    • 33344458002 scopus 로고    scopus 로고
    • Age-related changes in lamin A/C expression in the osteoarticular system: laminopathies as a potential new aging mechanism
    • COI: 1:CAS:528:DC%2BD28XitValtLs%3D, PID: 16445967
    • Duque G, Rivas D (2006) Age-related changes in lamin A/C expression in the osteoarticular system: laminopathies as a potential new aging mechanism. Mech Ageing Dev 127(4):378–383. doi:10.1016/j.mad.2005.12.007
    • (2006) Mech Ageing Dev , vol.127 , Issue.4 , pp. 378-383
    • Duque, G.1    Rivas, D.2
  • 19
    • 84873531288 scopus 로고    scopus 로고
    • Lamin A/C is expressed in pluripotent mouse embryonic stem cells
    • PID: 23324457
    • Eckersley-Maslin MA, Bergmann JH, Lazar Z, Spector DL (2013) Lamin A/C is expressed in pluripotent mouse embryonic stem cells. Nucleus 4(1):53–60. doi:10.4161/nucl.23384
    • (2013) Nucleus , vol.4 , Issue.1 , pp. 53-60
    • Eckersley-Maslin, M.A.1    Bergmann, J.H.2    Lazar, Z.3    Spector, D.L.4
  • 20
    • 0032801145 scopus 로고    scopus 로고
    • Characterization of the hydra lamin and its gene: a molecular phylogeny of metazoan lamins
    • COI: 1:CAS:528:DyaK1MXltFSrtb0%3D, PID: 10441677
    • Erber A, Riemer D, Hofemeister H, Bovenschulte M, Stick R, Panopoulou G, Weber K (1999) Characterization of the hydra lamin and its gene: a molecular phylogeny of metazoan lamins. J Mol Evol 49(2):260–271
    • (1999) J Mol Evol , vol.49 , Issue.2 , pp. 260-271
    • Erber, A.1    Riemer, D.2    Hofemeister, H.3    Bovenschulte, M.4    Stick, R.5    Panopoulou, G.6    Weber, K.7
  • 21
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome
    • COI: 1:CAS:528:DC%2BD3sXjs1ynurY%3D, PID: 12714972
    • Eriksson M, Brown WT, Gordon LB, Glynn MW, Singer J, Scott L, Collins FS (2003) Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 423(6937):293–298. doi:10.1038/nature01629
    • (2003) Nature , vol.423 , Issue.6937 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3    Glynn, M.W.4    Singer, J.5    Scott, L.6    Collins, F.S.7
  • 22
    • 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
    • COI: 1:CAS:528:DC%2BD3cXjtVOh, PID: 10580070
    • Fatkin D, MacRae C, Sasaki T, Wolff MR, Porcu M, Frenneaux M, McDonough B (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(23):1715–1724. doi:10.1056/NEJM199912023412302
    • (1999) N Engl J Med , vol.341 , Issue.23 , pp. 1715-1724
    • Fatkin, D.1    MacRae, C.2    Sasaki, T.3    Wolff, M.R.4    Porcu, M.5    Frenneaux, M.6    McDonough, B.7
  • 23
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins
    • COI: 1:CAS:528:DyaL28XlvVGjtbs%3D, PID: 3462705
    • Fisher DZ, Chaudhary N, Blobel G (1986) cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc Natl Acad Sci U S A 83(17):6450–6454
    • (1986) Proc Natl Acad Sci U S A , vol.83 , Issue.17 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 24
    • 33644651157 scopus 로고    scopus 로고
    • Prelamin A and lamin A appear to be dispensable in the nuclear lamina
    • COI: 1:CAS:528:DC%2BD28XitlGktb8%3D, PID: 16511604
    • Fong LG, Ng JK, Lammerding J, Vickers TA, Meta M, Cote N, Young SG (2006) Prelamin A and lamin A appear to be dispensable in the nuclear lamina. J Clin Invest 116(3):743–752. doi:10.1172/JCI27125
    • (2006) J Clin Invest , vol.116 , Issue.3 , pp. 743-752
    • Fong, L.G.1    Ng, J.K.2    Lammerding, J.3    Vickers, T.A.4    Meta, M.5    Cote, N.6    Young, S.G.7
  • 25
    • 33847668294 scopus 로고    scopus 로고
    • Lamins A and C are present in the nuclei of early porcine embryos, with lamin A being distributed in large intranuclear foci
    • COI: 1:CAS:528:DC%2BD2sXisVaqt7s%3D
    • Foster HA, Stokes P, Forsey K, Leese HJ, Bridger JM (2007) Lamins A and C are present in the nuclei of early porcine embryos, with lamin A being distributed in large intranuclear foci. Chromosom Res 15(2):163–174. doi:10.1007/s10577-006-1088-8
    • (2007) Chromosom Res , vol.15 , Issue.2 , pp. 163-174
    • Foster, H.A.1    Stokes, P.2    Forsey, K.3    Leese, H.J.4    Bridger, J.M.5
  • 26
    • 0028342511 scopus 로고
    • Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice
    • COI: 1:CAS:528:DyaK2cXlsFSju78%3D, PID: 8187835
    • Furukawa K, Inagaki H, Hotta Y (1994) Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice. Exp Cell Res 212(2):426–430. doi:10.1006/excr.1994.1164
    • (1994) Exp Cell Res , vol.212 , Issue.2 , pp. 426-430
    • Furukawa, K.1    Inagaki, H.2    Hotta, Y.3
  • 27
    • 84855830585 scopus 로고    scopus 로고
    • Nuclear lamina at the crossroads of the cytoplasm and nucleus
    • COI: 1:CAS:528:DC%2BC38Xos1aqtA%3D%3D, PID: 22126840
    • Gerace L, Huber MD (2012) Nuclear lamina at the crossroads of the cytoplasm and nucleus. J Struct Biol 177(1):24–31. doi:10.1016/j.jsb.2011.11.007
    • (2012) J Struct Biol , vol.177 , Issue.1 , pp. 24-31
    • Gerace, L.1    Huber, M.D.2
  • 28
    • 0021702708 scopus 로고
    • Organization and modulation of nuclear lamina structure
    • COI: 1:CAS:528:DyaL2MXitFyqur0%3D, PID: 6597817
    • Gerace L, Comeau C, Benson M (1984) Organization and modulation of nuclear lamina structure. J Cell Sci Suppl 1:137–160
    • (1984) J Cell Sci Suppl , vol.1 , pp. 137-160
    • Gerace, L.1    Comeau, C.2    Benson, M.3
  • 29
    • 55549134278 scopus 로고    scopus 로고
    • Tethering by lamin A stabilizes and targets the ING1 tumour suppressor
    • COI: 1:CAS:528:DC%2BD1cXhtlais7vL, PID: 18836436
    • Han X, Feng X, Rattner JB, Smith H, Bose P, Suzuki K, Riabowol K (2008) Tethering by lamin A stabilizes and targets the ING1 tumour suppressor. Nat Cell Biol 10(11):1333–1340. doi:10.1038/ncb1792
    • (2008) Nat Cell Biol , vol.10 , Issue.11 , pp. 1333-1340
    • Han, X.1    Feng, X.2    Rattner, J.B.3    Smith, H.4    Bose, P.5    Suzuki, K.6    Riabowol, K.7
  • 30
    • 33646555082 scopus 로고    scopus 로고
    • SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton
    • COI: 1:CAS:528:DC%2BD28XkslCltrg%3D, PID: 16648470
    • Haque F, Lloyd DJ, Smallwood DT, Dent CL, Shanahan CM, Fry AM, Shackleton S (2006) SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to provide a physical connection between the nuclear lamina and the cytoskeleton. Mol Cell Biol 26(10):3738–3751. doi:10.1128/MCB.26.10.3738-3751.2006
    • (2006) Mol Cell Biol , vol.26 , Issue.10 , pp. 3738-3751
    • Haque, F.1    Lloyd, D.J.2    Smallwood, D.T.3    Dent, C.L.4    Shanahan, C.M.5    Fry, A.M.6    Shackleton, S.7
  • 31
    • 0033636843 scopus 로고    scopus 로고
    • Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells
    • COI: 1:CAS:528:DC%2BD3cXovFansbk%3D, PID: 11102526
    • Izumi M, Vaughan OA, Hutchison CJ, Gilbert DM (2000) Head and/or CaaX domain deletions of lamin proteins disrupt preformed lamin A and C but not lamin B structure in mammalian cells. Mol Biol Cell 11(12):4323–4337
    • (2000) Mol Biol Cell , vol.11 , Issue.12 , pp. 4323-4337
    • Izumi, M.1    Vaughan, O.A.2    Hutchison, C.J.3    Gilbert, D.M.4
  • 32
    • 3042829496 scopus 로고    scopus 로고
    • A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation
    • COI: 1:CAS:528:DC%2BD2cXlvVahsbc%3D, PID: 15210943
    • Johnson BR, Nitta RT, Frock RL, Mounkes L, Barbie DA, Stewart CL, Kennedy BK (2004) A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation. Proc Natl Acad Sci U S A 101(26):9677–9682. doi:10.1073/pnas.0403250101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.26 , pp. 9677-9682
    • Johnson, B.R.1    Nitta, R.T.2    Frock, R.L.3    Mounkes, L.4    Barbie, D.A.5    Stewart, C.L.6    Kennedy, B.K.7
  • 33
    • 84863115487 scopus 로고    scopus 로고
    • Regulation of prelamin A but not lamin C by miR-9, a brain-specific microRNA
    • COI: 1:CAS:528:DC%2BC38XivVOjtLg%3D, PID: 22308344
    • Jung HJ, Coffinier C, Choe Y, Beigneux AP, Davies BS, Yang SH, Fong LG (2012) Regulation of prelamin A but not lamin C by miR-9, a brain-specific microRNA. Proc Natl Acad Sci U S A 109(7):E423–E431. doi:10.1073/pnas.1111780109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.7 , pp. E423-E431
    • Jung, H.J.1    Coffinier, C.2    Choe, Y.3    Beigneux, A.P.4    Davies, B.S.5    Yang, S.H.6    Fong, L.G.7
  • 34
    • 84901640474 scopus 로고    scopus 로고
    • Emerin in health and disease
    • Koch AJ, Holaska JM (2014) Emerin in health and disease. Semin Cell Dev Biol 29C:95–106. doi:10.1016/j.semcdb.2013.12.008
    • (2014) Semin Cell Dev Biol , vol.29C , pp. 95-106
    • Koch, A.J.1    Holaska, J.M.2
  • 35
    • 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
    • PID: 22033280
    • Kolb T, Maass 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(5):425–433. doi:10.4161/nucl.2.5.17765
    • (2011) Nucleus , vol.2 , Issue.5 , pp. 425-433
    • Kolb, T.1    Maass, K.2    Hergt, M.3    Aebi, U.4    Herrmann, H.5
  • 36
    • 18444382032 scopus 로고    scopus 로고
    • The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy
    • COI: 1:CAS:528:DC%2BD38XksFOisrw%3D, PID: 12057196
    • Krimm I, Ostlund C, Gilquin B, Couprie J, Hossenlopp P, Mornon JP, Zinn-Justin S (2002) The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy. Structure 10(6):811–823
    • (2002) Structure , vol.10 , Issue.6 , pp. 811-823
    • Krimm, I.1    Ostlund, C.2    Gilquin, B.3    Couprie, J.4    Hossenlopp, P.5    Mornon, J.P.6    Zinn-Justin, S.7
  • 37
    • 33748744269 scopus 로고    scopus 로고
    • Lamins A and C but not lamin B1 regulate nuclear mechanics
    • COI: 1:CAS:528:DC%2BD28XoslKltLo%3D, PID: 16825190
    • Lammerding J, Fong LG, Ji JY, Reue K, Stewart CL, Young SG, Lee RT (2006) Lamins A and C but not lamin B1 regulate nuclear mechanics. J Biol Chem 281(35):25768–25780. doi:10.1074/jbc.M513511200
    • (2006) J Biol Chem , vol.281 , Issue.35 , pp. 25768-25780
    • Lammerding, J.1    Fong, L.G.2    Ji, J.Y.3    Reue, K.4    Stewart, C.L.5    Young, S.G.6    Lee, R.T.7
  • 38
    • 79957838252 scopus 로고    scopus 로고
    • Subcellular localization of SUN2 is regulated by lamin A and Rab5
    • COI: 1:CAS:528:DC%2BC3MXnt1Gqsrc%3D, PID: 21655223
    • Liang Y, Chiu PH, Yip KY, Chan SY (2011) Subcellular localization of SUN2 is regulated by lamin A and Rab5. PLoS One 6(5):e20507. doi:10.1371/journal.pone.0020507
    • (2011) PLoS One , vol.6 , Issue.5 , pp. e20507
    • Liang, Y.1    Chiu, P.H.2    Yip, K.Y.3    Chan, S.Y.4
  • 39
    • 21844432667 scopus 로고    scopus 로고
    • Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope
    • COI: 1:CAS:528:DC%2BD2MXlvVWhtrs%3D, PID: 15843432
    • Libotte T, Zaim H, Abraham S, Padmakumar VC, Schneider M, Lu W, Karakesisoglou I (2005) Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope. Mol Biol Cell 16(7):3411–3424. doi:10.1091/mbc.E04-11-1009
    • (2005) Mol Biol Cell , vol.16 , Issue.7 , pp. 3411-3424
    • Libotte, T.1    Zaim, H.2    Abraham, S.3    Padmakumar, V.C.4    Schneider, M.5    Lu, W.6    Karakesisoglou, I.7
  • 40
    • 0027257461 scopus 로고
    • Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C
    • COI: 1:CAS:528:DyaK3sXlsFeiu7g%3D, PID: 8344919
    • Lin F, Worman HJ (1993) Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J Biol Chem 268(22):16321–16326
    • (1993) J Biol Chem , vol.268 , Issue.22 , pp. 16321-16326
    • Lin, F.1    Worman, H.J.2
  • 41
    • 84870506099 scopus 로고    scopus 로고
    • Resveratrol rescues SIRT1-dependent adult stem cell decline and alleviates progeroid features in laminopathy-based progeria
    • COI: 1:CAS:528:DC%2BC38XhslyntbnN, PID: 23217256
    • Liu B, Ghosh S, Yang X, Zheng H, Liu X, Wang Z, Zhou Z (2012a) Resveratrol rescues SIRT1-dependent adult stem cell decline and alleviates progeroid features in laminopathy-based progeria. Cell Metab 16(6):738–750. doi:10.1016/j.cmet.2012.11.007
    • (2012) Cell Metab , vol.16 , Issue.6 , pp. 738-750
    • Liu, B.1    Ghosh, S.2    Yang, X.3    Zheng, H.4    Liu, X.5    Wang, Z.6    Zhou, Z.7
  • 42
    • 84866001590 scopus 로고    scopus 로고
    • Intracellular VEGF regulates the balance between osteoblast and adipocyte differentiation
    • COI: 1:CAS:528:DC%2BC38XhtlChsbrF, PID: 22886301
    • Liu Y, Berendsen AD, Jia S, Lotinun S, Baron R, Ferrara N, Olsen BR (2012b) Intracellular VEGF regulates the balance between osteoblast and adipocyte differentiation. J Clin Invest 122(9):3101–3113. doi:10.1172/JCI61209
    • (2012) J Clin Invest , vol.122 , Issue.9 , pp. 3101-3113
    • Liu, Y.1    Berendsen, A.D.2    Jia, S.3    Lotinun, S.4    Baron, R.5    Ferrara, N.6    Olsen, B.R.7
  • 43
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies
    • COI: 1:CAS:528:DC%2BD38Xjt1Grsbo%3D, PID: 11929849
    • Lloyd DJ, Trembath RC, Shackleton S (2002) A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum Mol Genet 11(7):769–777
    • (2002) Hum Mol Genet , vol.11 , Issue.7 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 44
    • 84899891410 scopus 로고    scopus 로고
    • Antagonistic functions of LMNA isoforms in energy expenditure and lifespan
    • COI: 1:CAS:528:DC%2BC2cXhtVyms77O, PID: 24639560
    • Lopez-Mejia IC, de Toledo M, Chavey C, Lapasset L, Cavelier P, Lopez-Herrera C, Tazi J (2014) Antagonistic functions of LMNA isoforms in energy expenditure and lifespan. EMBO Rep 15(5):529–539. doi:10.1002/embr.201338126
    • (2014) EMBO Rep , vol.15 , Issue.5 , pp. 529-539
    • Lopez-Mejia, I.C.1    de Toledo, M.2    Chavey, C.3    Lapasset, L.4    Cavelier, P.5    Lopez-Herrera, C.6    Tazi, J.7
  • 45
    • 84885438139 scopus 로고    scopus 로고
    • Investigation of splicing changes and post-translational processing of LMNA in sporadic inclusion body myositis
    • PID: 24040437
    • Luo YB, Mitrpant C, Johnsen R, Fabian V, Needham M, Fletcher S, Mastaglia FL (2013a) Investigation of splicing changes and post-translational processing of LMNA in sporadic inclusion body myositis. Int J Clin Exp Pathol 6(9):1723–1733
    • (2013) Int J Clin Exp Pathol , vol.6 , Issue.9 , pp. 1723-1733
    • Luo, Y.B.1    Mitrpant, C.2    Johnsen, R.3    Fabian, V.4    Needham, M.5    Fletcher, S.6    Mastaglia, F.L.7
  • 48
    • 0036966367 scopus 로고    scopus 로고
    • Increased solubility of lamins and redistribution of lamin C in X-linked Emery-Dreifuss muscular dystrophy fibroblasts
    • COI: 1:CAS:528:DC%2BD38XpsFyhs7k%3D, PID: 12490172
    • Markiewicz E, Venables R, Mauricio Alvarez R, Quinlan R, Dorobek M, Hausmanowa-Petrusewicz I, Hutchison C (2002) Increased solubility of lamins and redistribution of lamin C in X-linked Emery-Dreifuss muscular dystrophy fibroblasts. J Struct Biol 140(1–3):241–253
    • (2002) J Struct Biol , vol.140 , Issue.1-3 , pp. 241-253
    • Markiewicz, E.1    Venables, R.2    Mauricio Alvarez, R.3    Quinlan, R.4    Dorobek, M.5    Hausmanowa-Petrusewicz, I.6    Hutchison, C.7
  • 49
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • COI: 1:CAS:528:DyaL28XhsVejs7c%3D, PID: 3453101
    • McKeon FD, Kirschner MW, Caput D (1986) Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319(6053):463–468. doi:10.1038/319463a0
    • (1986) Nature , vol.319 , Issue.6053 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 50
    • 34249782557 scopus 로고    scopus 로고
    • Invertebrate lamins
    • COI: 1:CAS:528:DC%2BD2sXmtFOit7g%3D, PID: 17451683
    • Melcer S, Gruenbaum Y, Krohne G (2007) Invertebrate lamins. Exp Cell Res 313(10):2157–2166. doi:10.1016/j.yexcr.2007.03.004
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2157-2166
    • Melcer, S.1    Gruenbaum, Y.2    Krohne, G.3
  • 51
    • 36049034261 scopus 로고    scopus 로고
    • LMNA messenger RNA expression in highly active antiretroviral therapy-treated HIV-positive patients
    • COI: 1:CAS:528:DC%2BD2sXht1yms73O, PID: 18077842
    • Miranda M, Chacon MR, Vidal F, Megia A, Richart C, Veloso S, Vendrell J (2007) LMNA messenger RNA expression in highly active antiretroviral therapy-treated HIV-positive patients. J Acquir Immune Defic Syndr 46(4):384–389
    • (2007) J Acquir Immune Defic Syndr , vol.46 , Issue.4 , pp. 384-389
    • Miranda, M.1    Chacon, M.R.2    Vidal, F.3    Megia, A.4    Richart, C.5    Veloso, S.6    Vendrell, J.7
  • 53
    • 0037077382 scopus 로고    scopus 로고
    • Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro
    • COI: 1:CAS:528:DC%2BD38XmtVamtr4%3D, PID: 12163176
    • Mislow JM, Holaska JM, Kim MS, Lee KK, Segura-Totten M, Wilson KL, McNally EM (2002) Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro. FEBS Lett 525(1–3):135–140
    • (2002) FEBS Lett , vol.525 , Issue.1-3 , pp. 135-140
    • Mislow, J.M.1    Holaska, J.M.2    Kim, M.S.3    Lee, K.K.4    Segura-Totten, M.5    Wilson, K.L.6    McNally, E.M.7
  • 54
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells
    • COI: 1:CAS:528:DC%2BD3cXovFant7k%3D, PID: 11121432
    • 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(6):1155–1168
    • (2000) J Cell Biol , vol.151 , Issue.6 , pp. 1155-1168
    • Moir, R.D.1    Yoon, M.2    Khuon, S.3    Goldman, R.D.4
  • 55
    • 84865765996 scopus 로고    scopus 로고
    • Phenotypic diversity in patients with lipodystrophy associated with LMNA mutations
    • COI: 1:CAS:528:DC%2BC38XhsVWltLbF, PID: 22700598
    • Mory PB, Crispim F, Freire MB, Salles JE, Valerio CM, Godoy-Matos AF, Moises RS (2012) Phenotypic diversity in patients with lipodystrophy associated with LMNA mutations. Eur J Endocrinol 167(3):423–431. doi:10.1530/EJE-12-0268
    • (2012) Eur J Endocrinol , vol.167 , Issue.3 , pp. 423-431
    • Mory, P.B.1    Crispim, F.2    Freire, M.B.3    Salles, J.E.4    Valerio, C.M.5    Godoy-Matos, A.F.6    Moises, R.S.7
  • 56
    • 23944437599 scopus 로고    scopus 로고
    • Lamins A and C are differentially dysfunctional in autosomal dominant Emery-Dreifuss muscular dystrophy
    • COI: 1:CAS:528:DC%2BD2MXhtFGktb3N, PID: 16218190
    • Motsch I, Kaluarachchi M, Emerson LJ, Brown CA, Brown SC, Dabauvalle MC, Ellis JA (2005) Lamins A and C are differentially dysfunctional in autosomal dominant Emery-Dreifuss muscular dystrophy. Eur J Cell Biol 84(9):765–781. doi:10.1016/j.ejcb.2005.04.004
    • (2005) Eur J Cell Biol , vol.84 , Issue.9 , pp. 765-781
    • Motsch, I.1    Kaluarachchi, M.2    Emerson, L.J.3    Brown, C.A.4    Brown, S.C.5    Dabauvalle, M.C.6    Ellis, J.A.7
  • 57
    • 26444595257 scopus 로고    scopus 로고
    • Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice
    • COI: 1:CAS:528:DC%2BD2MXmt1ersbg%3D, PID: 15972724
    • Mounkes LC, Kozlov SV, Rottman JN, Stewart CL (2005) Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice. Hum Mol Genet 14(15):2167–2180. doi:10.1093/hmg/ddi221
    • (2005) Hum Mol Genet , vol.14 , Issue.15 , pp. 2167-2180
    • Mounkes, L.C.1    Kozlov, S.V.2    Rottman, J.N.3    Stewart, C.L.4
  • 58
    • 0346216789 scopus 로고    scopus 로고
    • Expression of emerin and lamins in muscle of patients with different forms of Emery-Dreifuss muscular dystrophy
    • COI: 1:CAS:528:DC%2BD2cXhsVSns7k%3D, PID: 14959564
    • Niebroj-Dobosz I, Fidzianska A, Hausmanowa-Petrusewicz I (2003) Expression of emerin and lamins in muscle of patients with different forms of Emery-Dreifuss muscular dystrophy. Acta Myol 22(2):52–57
    • (2003) Acta Myol , vol.22 , Issue.2 , pp. 52-57
    • Niebroj-Dobosz, I.1    Fidzianska, A.2    Hausmanowa-Petrusewicz, I.3
  • 59
    • 84864317150 scopus 로고    scopus 로고
    • Unique preservation of neural cells in Hutchinson-Gilford progeria syndrome is due to the expression of the neural-specific miR-9 microRNA
    • COI: 1:CAS:528:DC%2BC38XhtF2iur%2FL, PID: 22840390
    • Nissan X, Blondel S, Navarro C, Maury Y, Denis C, Girard M, Peschanski M (2012) Unique preservation of neural cells in Hutchinson-Gilford progeria syndrome is due to the expression of the neural-specific miR-9 microRNA. Cell Rep 2(1):1–9. doi:10.1016/j.celrep.2012.05.015
    • (2012) Cell Rep , vol.2 , Issue.1 , pp. 1-9
    • Nissan, X.1    Blondel, S.2    Navarro, C.3    Maury, Y.4    Denis, C.5    Girard, M.6    Peschanski, M.7
  • 60
    • 78349290448 scopus 로고    scopus 로고
    • Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice
    • COI: 1:CAS:528:DC%2BC3cXht1Oju7nE, PID: 20726853
    • Oh YS, Kim DG, Kim G, Choi EC, Kennedy BK, Suh Y, Kim S (2010) Downregulation of lamin A by tumor suppressor AIMP3/p18 leads to a progeroid phenotype in mice. Aging Cell 9(5):810–822. doi:10.1111/j.1474-9726.2010.00614.x
    • (2010) Aging Cell , vol.9 , Issue.5 , pp. 810-822
    • Oh, Y.S.1    Kim, D.G.2    Kim, G.3    Choi, E.C.4    Kennedy, B.K.5    Suh, Y.6    Kim, S.7
  • 61
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • PID: 20068231
    • Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Mann M (2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal 3(104):ra3. doi:10.1126/scisignal.2000475
    • (2010) Sci Signal , vol.3 , Issue.104 , pp. ra3
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3    Kumar, C.4    Miller, M.L.5    Jensen, L.J.6    Mann, M.7
  • 62
    • 81155124411 scopus 로고    scopus 로고
    • Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation
    • COI: 1:CAS:528:DC%2BC3MXhs1Sqt7vK, PID: 21951640
    • Pekovic V, Gibbs-Seymour I, Markiewicz E, Alzoghaibi F, Benham AM, Edwards R, Hutchison CJ (2011) Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation. Aging Cell 10(6):1067–1079. doi:10.1111/j.1474-9726.2011.00750.x
    • (2011) Aging Cell , vol.10 , Issue.6 , pp. 1067-1079
    • Pekovic, V.1    Gibbs-Seymour, I.2    Markiewicz, E.3    Alzoghaibi, F.4    Benham, A.M.5    Edwards, R.6    Hutchison, C.J.7
  • 63
    • 84860138137 scopus 로고    scopus 로고
    • Evolution of the lamin protein family: what introns can tell
    • PID: 22156746
    • Peter A, Reimer S (2012) Evolution of the lamin protein family: what introns can tell. Nucleus 3(1):44–59
    • (2012) Nucleus , vol.3 , Issue.1 , pp. 44-59
    • Peter, A.1    Reimer, S.2
  • 64
    • 12344326099 scopus 로고    scopus 로고
    • The lamin CxxM motif promotes nuclear membrane growth
    • PID: 15546914
    • Prufert K, Vogel A, Krohne G (2004) The lamin CxxM motif promotes nuclear membrane growth. J Cell Sci 117(Pt 25):6105–6116. doi:10.1242/jcs.01532
    • (2004) J Cell Sci , vol.117 , pp. 6105-6116
    • Prufert, K.1    Vogel, A.2    Krohne, G.3
  • 65
    • 0001071336 scopus 로고    scopus 로고
    • Distinct nuclear assembly pathways for lamins A and C lead to their increase during quiescence in Swiss 3 T3 cells
    • COI: 1:CAS:528:DyaK2sXnt1GiurY%3D, PID: 9410886
    • Pugh GE, Coates PJ, Lane EB, Raymond Y, Quinlan RA (1997) Distinct nuclear assembly pathways for lamins A and C lead to their increase during quiescence in Swiss 3 T3 cells. J Cell Sci 110(Pt 19):2483–2493
    • (1997) J Cell Sci , vol.110 , pp. 2483-2493
    • Pugh, G.E.1    Coates, P.J.2    Lane, E.B.3    Raymond, Y.4    Quinlan, R.A.5
  • 66
    • 0035696932 scopus 로고    scopus 로고
    • Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy
    • COI: 1:CAS:528:DC%2BD38XnvFKlsQ%3D%3D, PID: 11792810
    • Raharjo WH, Enarson P, Sullivan T, Stewart CL, Burke B (2001) Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy. J Cell Sci 114(Pt 24):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
  • 67
    • 84865273590 scopus 로고    scopus 로고
    • Neonatal progeria: increased ratio of progerin to lamin A leads to progeria of the newborn
    • COI: 1:CAS:528:DC%2BC38Xht1ahsrzO, PID: 22419169
    • Reunert J, Wentzell R, Walter M, Jakubiczka S, Zenker M, Brune T, Marquardt T (2012) Neonatal progeria: increased ratio of progerin to lamin A leads to progeria of the newborn. Eur J Hum Genet 20(9):933–937. doi:10.1038/ejhg.2012.36
    • (2012) Eur J Hum Genet , vol.20 , Issue.9 , pp. 933-937
    • Reunert, J.1    Wentzell, R.2    Walter, M.3    Jakubiczka, S.4    Zenker, M.5    Brune, T.6    Marquardt, T.7
  • 68
    • 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
    • COI: 1:STN:280:DyaK3c%2Fjt1CjtA%3D%3D, PID: 2680424
    • Rober RA, Weber K, Osborn M (1989) 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(2):365–378
    • (1989) Development , vol.105 , Issue.2 , pp. 365-378
    • Rober, R.A.1    Weber, K.2    Osborn, M.3
  • 70
    • 33845536580 scopus 로고    scopus 로고
    • Expression of nuclear and mitochondrial thyroid hormone receptors in postnatal rat tongue muscle
    • COI: 1:CAS:528:DC%2BD28Xht1yktbnP, PID: 17159345
    • Sato I, Miyado M, Miwa Y, Sunohara M (2006) Expression of nuclear and mitochondrial thyroid hormone receptors in postnatal rat tongue muscle. Cells Tissues Organs 183(4):195–205. doi:10.1159/000096510
    • (2006) Cells Tissues Organs , vol.183 , Issue.4 , pp. 195-205
    • Sato, I.1    Miyado, M.2    Miwa, Y.3    Sunohara, M.4
  • 71
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: many faces, many functions
    • COI: 1:CAS:528:DC%2BD2sXmtFOit7k%3D, PID: 17451680
    • Schirmer EC, Foisner R (2007) Proteins that associate with lamins: many faces, many functions. Exp Cell Res 313(10):2167–2179. doi:10.1016/j.yexcr.2007.03.012
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 72
    • 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
    • COI: 1:CAS:528:DC%2BD2cXotVOgsbk%3D, PID: 15284226
    • 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(41):42811–42817. doi:10.1074/jbc.M407705200
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 42811-42817
    • Schirmer, E.C.1    Gerace, L.2
  • 73
    • 84874344819 scopus 로고    scopus 로고
    • Lamin A/C haploinsufficiency modulates the differentiation potential of mouse embryonic stem cells
    • COI: 1:CAS:528:DC%2BC3sXjslyktL0%3D, PID: 23451281
    • Sehgal P, Chaturvedi P, Kumaran RI, Kumar S, Parnaik VK (2013) Lamin A/C haploinsufficiency modulates the differentiation potential of mouse embryonic stem cells. PLoS One 8(2):e57891. doi:10.1371/journal.pone.0057891
    • (2013) PLoS One , vol.8 , Issue.2 , pp. e57891
    • Sehgal, P.1    Chaturvedi, P.2    Kumaran, R.I.3    Kumar, S.4    Parnaik, V.K.5
  • 74
    • 58049195492 scopus 로고    scopus 로고
    • The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription
    • COI: 1:CAS:528:DC%2BD1MXjtFKhsw%3D%3D, PID: 19141474
    • Shimi T, Pfleghaar K, Kojima S, Pack CG, Solovei I, Goldman AE, Goldman RD (2008) The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription. Genes Dev 22(24):3409–3421. doi:10.1101/gad.1735208
    • (2008) Genes Dev , vol.22 , Issue.24 , pp. 3409-3421
    • Shimi, T.1    Pfleghaar, K.2    Kojima, S.3    Pack, C.G.4    Solovei, I.5    Goldman, A.E.6    Goldman, R.D.7
  • 75
    • 84876499240 scopus 로고    scopus 로고
    • Partners and post-translational modifications of nuclear lamins
    • COI: 1:CAS:528:DC%2BC3sXltV2ntLo%3D, PID: 23475188
    • Simon DN, Wilson KL (2013) Partners and post-translational modifications of nuclear lamins. Chromosoma 122(1–2):13–31. doi:10.1007/s00412-013-0399-8
    • (2013) Chromosoma , vol.122 , Issue.1-2 , pp. 13-31
    • Simon, D.N.1    Wilson, K.L.2
  • 76
    • 77956588049 scopus 로고    scopus 로고
    • Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail
    • PID: 21327074
    • Simon DN, Zastrow MS, Wilson KL (2010) Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail. Nucleus 1(3):264–272. doi:10.4161/nucl.1.3.11799
    • (2010) Nucleus , vol.1 , Issue.3 , pp. 264-272
    • Simon, D.N.1    Zastrow, M.S.2    Wilson, K.L.3
  • 77
    • 79951538944 scopus 로고    scopus 로고
    • Proteomics profiling of microdissected low- and high-grade prostate tumors identifies Lamin A as a discriminatory biomarker
    • COI: 1:CAS:528:DC%2BC3cXhsVahtLnP, PID: 20977276
    • Skvortsov S, Schafer G, Stasyk T, Fuchsberger C, Bonn GK, Bartsch G, Huber LA (2011) Proteomics profiling of microdissected low- and high-grade prostate tumors identifies Lamin A as a discriminatory biomarker. J Proteome Res 10(1):259–268. doi:10.1021/pr100921j
    • (2011) J Proteome Res , vol.10 , Issue.1 , pp. 259-268
    • Skvortsov, S.1    Schafer, G.2    Stasyk, T.3    Fuchsberger, C.4    Bonn, G.K.5    Bartsch, G.6    Huber, L.A.7
  • 78
    • 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
    • COI: 1:CAS:528:DC%2BD3cXntV2isrw%3D, PID: 10739751
    • Speckman RA, Garg A, Du F, Bennett L, Veile R, Arioglu E, Bowcock AM (2000) 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(4):1192–1198. doi:10.1086/302836
    • (2000) Am J Hum Genet , vol.66 , Issue.4 , pp. 1192-1198
    • Speckman, R.A.1    Garg, A.2    Du, F.3    Bennett, L.4    Veile, R.5    Arioglu, E.6    Bowcock, A.M.7
  • 79
    • 12344250822 scopus 로고    scopus 로고
    • Function of alternative splicing
    • COI: 1:CAS:528:DC%2BD2MXkvVSgtQ%3D%3D, PID: 15656968
    • Stamm S, Ben-Ari S, Rafalska I, Tang Y, Zhang Z, Toiber D, Soreq H (2005) Function of alternative splicing. Gene 344:1–20. doi:10.1016/j.gene.2004.10.022
    • (2005) Gene , vol.344 , pp. 1-20
    • Stamm, S.1    Ben-Ari, S.2    Rafalska, I.3    Tang, Y.4    Zhang, Z.5    Toiber, D.6    Soreq, H.7
  • 80
    • 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
    • COI: 1:CAS:528:DyaK3sXltFSit74%3D, PID: 1521501
    • Stick R (1992) 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(9):566–574
    • (1992) Chromosoma , vol.101 , Issue.9 , pp. 566-574
    • Stick, R.1
  • 81
    • 5144220584 scopus 로고    scopus 로고
    • Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins
    • COI: 1:CAS:528:DC%2BD2cXotlClurc%3D, PID: 15476822
    • Strelkov SV, Schumacher J, Burkhard P, Aebi U, Herrmann H (2004) Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J Mol Biol 343(4):1067–1080. doi:10.1016/j.jmb.2004.08.093
    • (2004) J Mol Biol , vol.343 , Issue.4 , pp. 1067-1080
    • Strelkov, S.V.1    Schumacher, J.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 82
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: their structure, assembly, and interactions
    • COI: 1:CAS:528:DyaK1cXmtVSlt70%3D, PID: 9724605
    • Stuurman N, Heins S, Aebi U (1998) Nuclear lamins: their structure, assembly, and interactions. J Struct Biol 122(1–2):42–66. doi:10.1006/jsbi.1998.3987
    • (1998) J Struct Biol , vol.122 , Issue.1-2 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 83
    • 84895763410 scopus 로고    scopus 로고
    • Label-free mass spectrometry exploits dozens of detected peptides to quantify lamins in wildtype and knockdown cells
    • PID: 24448480
    • Swift J, Harada T, Buxboim A, Shin JW, Tang HY, Speicher DW, Discher DE (2013a) Label-free mass spectrometry exploits dozens of detected peptides to quantify lamins in wildtype and knockdown cells. Nucleus 4(6):450–459. doi:10.4161/nucl.27413
    • (2013) Nucleus , vol.4 , Issue.6 , pp. 450-459
    • Swift, J.1    Harada, T.2    Buxboim, A.3    Shin, J.W.4    Tang, H.Y.5    Speicher, D.W.6    Discher, D.E.7
  • 84
    • 84883059455 scopus 로고    scopus 로고
    • Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation
    • PID: 23990565
    • Swift J, Ivanovska IL, Buxboim A, Harada T, Dingal PC, Pinter J, Discher DE (2013b) Nuclear lamin-A scales with tissue stiffness and enhances matrix-directed differentiation. Science 341(6149):1240104. doi:10.1126/science.1240104
    • (2013) Science , vol.341 , Issue.6149 , pp. 1240104
    • Swift, J.1    Ivanovska, I.L.2    Buxboim, A.3    Harada, T.4    Dingal, P.C.5    Pinter, J.6    Discher, D.E.7
  • 85
    • 47349128641 scopus 로고    scopus 로고
    • Specific contribution of lamin A and lamin C in the development of laminopathies
    • COI: 1:CAS:528:DC%2BD1cXptVekur4%3D, PID: 18538321
    • Sylvius N, Hathaway A, Boudreau E, Gupta P, Labib S, Bolongo PM, Tesson F (2008) Specific contribution of lamin A and lamin C in the development of laminopathies. Exp Cell Res 314(13):2362–2375. doi:10.1016/j.yexcr.2008.04.017
    • (2008) Exp Cell Res , vol.314 , Issue.13 , pp. 2362-2375
    • Sylvius, N.1    Hathaway, A.2    Boudreau, E.3    Gupta, P.4    Labib, S.5    Bolongo, P.M.6    Tesson, F.7
  • 86
    • 57849150788 scopus 로고    scopus 로고
    • Alternative splicing and disease
    • COI: 1:CAS:528:DC%2BD1cXhsFClsrbP, PID: 18992329
    • Tazi J, Bakkour N, Stamm S (2009) Alternative splicing and disease. Biochim Biophys Acta 1792(1):14–26. doi:10.1016/j.bbadis.2008.09.017
    • (2009) Biochim Biophys Acta , vol.1792 , Issue.1 , pp. 14-26
    • Tazi, J.1    Bakkour, N.2    Stamm, S.3
  • 87
    • 26444609690 scopus 로고    scopus 로고
    • A-type lamins are essential for TGF-beta1 induced PP2A to dephosphorylate transcription factors
    • PID: 16115815
    • Van Berlo JH, Voncken JW, Kubben N, Broers JL, Duisters R, van Leeuwen RE, Pinto YM (2005) A-type lamins are essential for TGF-beta1 induced PP2A to dephosphorylate transcription factors. Hum Mol Genet 14(19):2839–2849. doi:10.1093/hmg/ddi316
    • (2005) Hum Mol Genet , vol.14 , Issue.19 , pp. 2839-2849
    • Van Berlo, J.H.1    Voncken, J.W.2    Kubben, N.3    Broers, J.L.4    Duisters, R.5    van Leeuwen, R.E.6    Pinto, Y.M.7
  • 89
    • 33645833000 scopus 로고    scopus 로고
    • Unbalanced alternative splicing and its significance in cancer
    • COI: 1:CAS:528:DC%2BD28XktVGrs7g%3D, PID: 16547952
    • Venables JP (2006) Unbalanced alternative splicing and its significance in cancer. Bioessays 28(4):378–386. doi:10.1002/bies.20390
    • (2006) Bioessays , vol.28 , Issue.4 , pp. 378-386
    • Venables, J.P.1
  • 90
    • 80755129115 scopus 로고    scopus 로고
    • Nuclear lamins are differentially expressed in retinal neurons of the adult rat retina
    • COI: 1:CAS:528:DC%2BC3MXhtFyjt7fE, PID: 21842415
    • Wakabayashi T, Mori T, Hirahara Y, Koike T, Kubota Y, Takamori Y, Yamada H (2011) Nuclear lamins are differentially expressed in retinal neurons of the adult rat retina. Histochem Cell Biol 136(4):427–436. doi:10.1007/s00418-011-0853-8
    • (2011) Histochem Cell Biol , vol.136 , Issue.4 , pp. 427-436
    • Wakabayashi, T.1    Mori, T.2    Hirahara, Y.3    Koike, T.4    Kubota, Y.5    Takamori, Y.6    Yamada, H.7
  • 91
    • 77951651658 scopus 로고    scopus 로고
    • Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis
    • PID: 20068230
    • Wang Z, Udeshi ND, Slawson C, Compton PD, Sakabe K, Cheung WD, Hart GW (2010) Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis. Sci Signal 3(104):ra2. doi:10.1126/scisignal.2000526
    • (2010) Sci Signal , vol.3 , Issue.104 , pp. ra2
    • Wang, Z.1    Udeshi, N.D.2    Slawson, C.3    Compton, P.D.4    Sakabe, K.5    Cheung, W.D.6    Hart, G.W.7
  • 92
    • 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
    • COI: 1:CAS:528:DyaK3cXltVOhtQ%3D%3D, PID: 2583287
    • Weber K, Plessmann U, Traub P (1989) 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(2):411–414
    • (1989) FEBS Lett , vol.257 , Issue.2 , pp. 411-414
    • Weber, K.1    Plessmann, U.2    Traub, P.3
  • 93
    • 77955412244 scopus 로고    scopus 로고
    • LMNA rs4641 and the muscle lamin A and C isoforms in twins—metabolic implications and transcriptional regulation
    • COI: 1:CAS:528:DC%2BC3cXhtVGktrfN, PID: 20501691
    • Wegner L, Anthonsen S, Bork-Jensen J, Dalgaard L, Hansen T, Pedersen O, Vaag A (2010) LMNA rs4641 and the muscle lamin A and C isoforms in twins—metabolic implications and transcriptional regulation. J Clin Endocrinol Metab 95(8):3884–3892. doi:10.1210/jc.2009-2675
    • (2010) J Clin Endocrinol Metab , vol.95 , Issue.8 , pp. 3884-3892
    • Wegner, L.1    Anthonsen, S.2    Bork-Jensen, J.3    Dalgaard, L.4    Hansen, T.5    Pedersen, O.6    Vaag, A.7
  • 95
    • 34249788998 scopus 로고    scopus 로고
    • Laminopathies”: a wide spectrum of human diseases
    • COI: 1:CAS:528:DC%2BD2sXmtFOit70%3D, PID: 17467691
    • Worman HJ, Bonne G (2007) “Laminopathies”: a wide spectrum of human diseases. Exp Cell Res 313(10):2121–2133. doi:10.1016/j.yexcr.2007.03.028
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2121-2133
    • Worman, H.J.1    Bonne, G.2
  • 96
    • 79958806259 scopus 로고    scopus 로고
    • Biology of the Mi-2/NuRD complex in SLAC (stemness, longevity/ageing, and cancer)
    • PID: 21523247
    • Zhang Y (2011) Biology of the Mi-2/NuRD complex in SLAC (stemness, longevity/ageing, and cancer). Gene Regul Syst Bio 5:1–26. doi:10.4137/GRSB.S6510
    • (2011) Gene Regul Syst Bio , vol.5 , pp. 1-26
    • Zhang, Y.1
  • 97
    • 47549109045 scopus 로고    scopus 로고
    • Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies
    • COI: 1:CAS:528:DC%2BD1cXoslymurg%3D, PID: 18606848
    • Zhang YQ, Sarge KD (2008) Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. J Cell Biol 182(1):35–39. doi:10.1083/jcb.200712124
    • (2008) J Cell Biol , vol.182 , Issue.1 , pp. 35-39
    • Zhang, Y.Q.1    Sarge, K.D.2
  • 98
    • 84964898748 scopus 로고    scopus 로고
    • Influences of lamin A levels on induction of pluripotent stem cells
    • COI: 1:CAS:528:DC%2BC3sXhsFajtrc%3D, PID: 23213392
    • Zuo B, Yang J, Wang F, Wang L, Yin Y, Dan J, Liu L (2012) Influences of lamin A levels on induction of pluripotent stem cells. Biol Open 1(11):1118–1127. doi:10.1242/bio.20121586
    • (2012) Biol Open , vol.1 , Issue.11 , pp. 1118-1127
    • Zuo, B.1    Yang, J.2    Wang, F.3    Wang, L.4    Yin, Y.5    Dan, J.6    Liu, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.