메뉴 건너뛰기




Volumn 773, Issue , 2014, Pages 435-470

Nuclear mechanics in cancer

Author keywords

Cytoskeleton; LINC complex; Mechanical stability; Mechanotransduction; Nuclear lamina

Indexed keywords

EMERIN; KASH DOMAIN PROTEIN; LAMIN A; LAMIN B; LAMIN B1; LAMIN C; NESPRIN; NUCLEAR PROTEIN; NUCLEOPROTEIN; SUN DOMAIN PROTEIN; UNCLASSIFIED DRUG;

EID: 84934441880     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4899-8032-8_20     Document Type: Article
Times cited : (120)

References (244)
  • 1
    • 0004146420 scopus 로고
    • An Atlas of fi ne structure
    • 2nd edn. W. B Saunders Company, PA
    • Fawcett DW (1966) An Atlas of fi ne structure. The cell, 2nd edn. W. B. Saunders Company, PA
    • (1966) The Cell
    • Fawcett, D.W.1
  • 2
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • doi: 10.1016/j.cell.2011.02.013
    • Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144(5): 646-674. doi: 10.1016/j.cell.2011.02.013
    • (2011) Cell , vol.144 , Issue.5 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 3
    • 34249864531 scopus 로고    scopus 로고
    • Biomechanics and biophysics of cancer cells
    • doi: 10.1016/j.actbio.2007.04.002
    • Suresh S (2007) Biomechanics and biophysics of cancer cells. Acta Biomater 3(4):413-438. doi: 10.1016/j.actbio.2007.04.002
    • (2007) Acta Biomater , vol.3 , Issue.4 , pp. 413-438
    • Suresh, S.1
  • 5
    • 62449217983 scopus 로고    scopus 로고
    • Oral cancer diagnosis by mechanical phenotyping
    • doi: 10.1158/0008-5472.can-08-4073
    • Remmerbach TW, Wottawah F, Dietrich J, Lincoln B, Wittekind C, Guck J (2009) Oral cancer diagnosis by mechanical phenotyping. Cancer Res 69(5):1728-1732. doi: 10.1158/0008-5472.can-08-4073
    • (2009) Cancer Res , vol.69 , Issue.5 , pp. 1728-1732
    • Remmerbach, T.W.1    Wottawah, F.2    Dietrich, J.3    Lincoln, B.4    Wittekind, C.5    Guck, J.6
  • 7
    • 36849037967 scopus 로고    scopus 로고
    • Nanomechanical analysis of cells from cancer patients
    • doi: 10.1038/nnano.2007.388
    • Cross SE, Jin YS, Rao J, Gimzewski JK (2007) Nanomechanical analysis of cells from cancer patients. Nat Nanotechnol 2(12):780-783. doi: 10.1038/nnano.2007.388
    • (2007) Nat Nanotechnol , vol.2 , Issue.12 , pp. 780-783
    • Cross, S.E.1    Jin, Y.S.2    Rao, J.3    Gimzewski, J.K.4
  • 8
    • 84857566619 scopus 로고    scopus 로고
    • Cellular traction stresses increase with increasing metastatic potential
    • doi: 10.1371/journal. pone.0032572
    • Kraning-Rush CM, Califano JP, Reinhart-King CA (2012) Cellular traction stresses increase with increasing metastatic potential. PLoS One 7(2):e32572. doi: 10.1371/journal. pone.0032572
    • (2012) PLoS One , vol.7 , Issue.2
    • Kraning-Rush, C.M.1    Califano, J.P.2    Reinhart-King, C.A.3
  • 9
    • 77958451884 scopus 로고    scopus 로고
    • Cancer cell stiffness: Integrated roles of three-dimensional matrix stiffness and transforming potential
    • doi: 10.1016/j.bpj.2010.07.051
    • Baker EL, Lu J, Yu D, Bonnecaze RT, Zaman MH (2010) Cancer cell stiffness: integrated roles of three-dimensional matrix stiffness and transforming potential. Biophys J 99(7): 2048-2057. doi: 10.1016/j.bpj.2010.07. 051
    • (2010) Biophys J , vol.99 , Issue.7 , pp. 2048-2057
    • Baker, E.L.1    Lu, J.2    Yu, D.3    Bonnecaze, R.T.4    Zaman, M.H.5
  • 11
    • 4544237763 scopus 로고    scopus 로고
    • Nuclear structure in cancer cells
    • doi: 10.1038/nrc1430
    • Zink D, Fischer AH, Nickerson JA (2004) Nuclear structure in cancer cells. Nat Rev Cancer 4(9):677-687. doi: 10.1038/nrc1430
    • (2004) Nat Rev Cancer , vol.4 , Issue.9 , pp. 677-687
    • Zink, D.1    Fischer, A.H.2    Nickerson, J.A.3
  • 12
    • 84862882928 scopus 로고    scopus 로고
    • Lamins at a glance
    • doi: 10.1242/jcs.087288
    • Ho CY, Lammerding J (2012) Lamins at a glance. J Cell Sci 125(Pt 9):2087-2093. doi: 10.1242/jcs.087288
    • (2012) J Cell Sci , vol.125 , Issue.PART 9 , pp. 2087-2093
    • Ho, C.Y.1    Lammerding, J.2
  • 13
    • 84875604713 scopus 로고    scopus 로고
    • Cancer biology and the nuclear envelope: A convoluted relationship
    • doi: 10.1016/j.semcancer.2012.01.008
    • de Las Heras JI, Batrakou DG, Schirmer EC (2013) Cancer biology and the nuclear envelope: a convoluted relationship. Semin Cancer Biol 23(2):125-137. doi: 10.1016/j.semcancer.2012.01.008
    • (2013) Semin Cancer Biol , vol.23 , Issue.2 , pp. 125-137
    • De Las Heras, J.I.1    Batrakou, D.G.2    Schirmer, E.C.3
  • 15
    • 44949118668 scopus 로고    scopus 로고
    • Nuclear shape, mechanics, and mechanotransduction
    • doi: 10.1161/circresaha.108.173989
    • Dahl KN, Ribeiro AJ, Lammerding J (2008) Nuclear shape, mechanics, and mechanotransduction. Circ Res 102(11):1307-1318. doi: 10.1161/circresaha.108. 173989
    • (2008) Circ Res , vol.102 , Issue.11 , pp. 1307-1318
    • Dahl, K.N.1    Ribeiro, A.J.2    Lammerding, J.3
  • 16
    • 79960476819 scopus 로고    scopus 로고
    • Nuclear mechanics in disease
    • doi: 10.1146/annurev-bioeng-071910-124736
    • Zwerger M, Ho CY, Lammerding J (2011) Nuclear mechanics in disease. Annu Rev Biomed Eng 13:397-428. doi: 10.1146/annurev-bioeng-071910-124736
    • (2011) Annu Rev Biomed Eng , vol.13 , pp. 397-428
    • Zwerger, M.1    Ho, C.Y.2    Lammerding, J.3
  • 17
    • 84861910740 scopus 로고    scopus 로고
    • Mechanics of the nucleus
    • doi: 10.1002/cphy.c100038
    • Lammerding J (2011) Mechanics of the nucleus. Compr Physiol 1(2):783-807. doi: 10.1002/cphy.c100038
    • (2011) Compr Physiol , vol.1 , Issue.2 , pp. 783-807
    • Lammerding, J.1
  • 18
    • 58049211966 scopus 로고    scopus 로고
    • Mechanotransduction at a distance: Mechanically coupling the extracellular matrix with the nucleus
    • doi: 10.1038/nrm2594
    • Wang N, Tytell JD, Ingber DE (2009) Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus. Nat Rev Mol Cell Biol 10(1):75-82. doi: 10.1038/nrm2594
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.1 , pp. 75-82
    • Wang, N.1    Tytell, J.D.2    Ingber, D.E.3
  • 19
    • 84880028245 scopus 로고    scopus 로고
    • Physical limits of cell migration: Control by ECM space and nuclear deformation and tuning by proteolysis and traction force
    • doi: 10.1083/jcb.201210152
    • Wolf K, Te Lindert M, Krause M, Alexander S, Te Riet J, Willis AL, Hoffman RM, Figdor CG, Weiss SJ, Friedl P (2013) Physical limits of cell migration: control by ECM space and nuclear deformation and tuning by proteolysis and traction force. J Cell Biol 201(7): 1069-1084. doi: 10.1083/jcb.201210152
    • (2013) J Cell Biol , vol.201 , Issue.7 , pp. 1069-1084
    • Wolf, K.1    Te Lindert, M.2    Krause, M.3    Alexander, S.4    Te Riet, J.5    Willis, A.L.6    Hoffman, R.M.7    Figdor, C.G.8    Weiss, S.J.9    Friedl, P.10
  • 20
    • 79951553475 scopus 로고    scopus 로고
    • Nuclear mechanics during cell migration
    • doi: 10.1016/j.ceb.2010.10.015
    • Friedl P, Wolf K, Lammerding J (2011) Nuclear mechanics during cell migration. Curr Opin Cell Biol 23(1):55-64. doi: 10.1016/j.ceb.2010.10.015
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.1 , pp. 55-64
    • Friedl, P.1    Wolf, K.2    Lammerding, J.3
  • 21
    • 58149331216 scopus 로고    scopus 로고
    • Dysfunctional connections between the nucleus and the actin and microtubule networks in laminopathic models
    • doi: 10.1529/biophysj.108.139428
    • Hale CM, Shrestha AL, Khatau SB, Stewart-Hutchinson PJ, Hernandez L, Stewart CL, Hodzic D, Wirtz D (2008) Dysfunctional connections between the nucleus and the actin and microtubule networks in laminopathic models. Biophys J 95(11):5462-5475. doi: 10.1529/biophysj.108.139428
    • (2008) Biophys J , vol.95 , Issue.11 , pp. 5462-5475
    • Hale, C.M.1    Shrestha, A.L.2    Khatau, S.B.3    Stewart-Hutchinson, P.J.4    Hernandez, L.5    Stewart, C.L.6    Hodzic, D.7    Wirtz, D.8
  • 22
    • 77954333003 scopus 로고    scopus 로고
    • Actomyosin tension exerted on the nucleus through nesprin-1 connections infl uences endothelial cell adhesion, migration, and cyclic strain-induced reorientation
    • doi: 10.1016/j.bpj.2010.04.011
    • Chancellor TJ, Lee J, Thodeti CK, Lele T (2010) Actomyosin tension exerted on the nucleus through nesprin-1 connections infl uences endothelial cell adhesion, migration, and cyclic strain-induced reorientation. Biophys J 99(1):115-123. doi: 10.1016/j.bpj.2010.04.011
    • (2010) Biophys J , vol.99 , Issue.1 , pp. 115-123
    • Chancellor, T.J.1    Lee, J.2    Thodeti, C.K.3    Lele, T.4
  • 23
    • 79958769441 scopus 로고    scopus 로고
    • Molecular mechanisms of centrosome and cytoskeleton anchorage at the nuclear envelope
    • doi: 10.1007/s00018-010-0535-z
    • Schneider M, Lu W, Neumann S, Brachner A, Gotzmann J, Noegel AA, Karakesisoglou I (2011) Molecular mechanisms of centrosome and cytoskeleton anchorage at the nuclear envelope. Cell Mol Life Sci 68(9):1593-1610. doi: 10.1007/s00018-010-0535-z
    • (2011) Cell Mol Life Sci , vol.68 , Issue.9 , pp. 1593-1610
    • Schneider, M.1    Lu, W.2    Neumann, S.3    Brachner, A.4    Gotzmann, J.5    Noegel, A.A.6    Karakesisoglou, I.7
  • 24
    • 79960685238 scopus 로고    scopus 로고
    • The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton
    • doi: 10.1074/jbc.M111.233700
    • Lombardi ML, Jaalouk DE, Shanahan CM, Burke B, Roux KJ, Lammerding J (2011) The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton. J Biol Chem 286(30):26743-26753. doi: 10.1074/jbc.M111.233700
    • (2011) J Biol Chem , vol.286 , Issue.30 , pp. 26743-26753
    • Lombardi, M.L.1    De, J.2    Shanahan, C.M.3    Burke, B.4    Roux, K.J.5    Lammerding, J.6
  • 25
    • 84863334769 scopus 로고    scopus 로고
    • Histone modifi cations and lamin A regulate chromatin protein dynamics in early embryonic stem cell differentiation
    • doi: 10.1038/ncomms1915
    • Melcer S, Hezroni H, Rand E, Nissim-Rafi nia M, Skoultchi A, Stewart CL, Bustin M, Meshorer E (2012) Histone modifi cations and lamin A regulate chromatin protein dynamics in early embryonic stem cell differentiation. Nat Commun 3:910. doi: 10.1038/ncomms1915
    • (2012) Nat Commun , vol.3 , pp. 910
    • Melcer, S.1    Hezroni, H.2    Rand, E.3    Nissim-Rafinia, M.4    Skoultchi, A.5    Stewart, C.L.6    Bustin, M.7    Meshorer, E.8
  • 26
    • 30444437477 scopus 로고    scopus 로고
    • Subnuclear organelles: New insights into form and function
    • doi: 10.1016/j.tcb.2005.11.005
    • Handwerger KE, Gall JG (2006) Subnuclear organelles: new insights into form and function. Trends Cell Biol 16(1):19-26. doi: 10.1016/j.tcb.2005.11.005
    • (2006) Trends Cell Biol , vol.16 , Issue.1 , pp. 19-26
    • Handwerger, K.E.1    Gall, J.G.2
  • 27
    • 65349090225 scopus 로고    scopus 로고
    • Nuclear neighborhoods and gene expression
    • doi: 10.1016/j.gde.2009.02.007
    • Zhao R, Bodnar MS, Spector DL (2009) Nuclear neighborhoods and gene expression. Curr Opin Genet Dev 19(2):172-179. doi: 10.1016/j.gde.2009.02.007
    • (2009) Curr Opin Genet Dev , vol.19 , Issue.2 , pp. 172-179
    • Zhao, R.1    Bodnar, M.S.2    Spector, D.L.3
  • 28
    • 79952601700 scopus 로고    scopus 로고
    • Biogenesis of nuclear bodies
    • doi: 10.1101/cshperspect.a000711
    • Dundr M, Misteli T (2010) Biogenesis of nuclear bodies. Cold Spring Harb Perspect Biol 2(12):a000711. doi: 10.1101/cshperspect.a000711
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , Issue.12
    • Dundr, M.1    Misteli, T.2
  • 29
    • 0019842267 scopus 로고
    • The nuclear envelope and the architecture of the nuclear periphery
    • Franke WW, Scheer U, Krohne G, Jarasch ED (1981) The nuclear envelope and the architecture of the nuclear periphery. J Cell Biol 91(3 Pt 2):39s-50s
    • (1981) J Cell Biol , vol.91 , Issue.3 PART 2
    • Franke, W.W.1    Scheer, U.2    Krohne, G.3    Jarasch, E.D.4
  • 30
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: Many faces, many functions
    • doi: 10.1016/j.yexcr.2007.03.012
    • 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
  • 31
    • 0021830499 scopus 로고
    • Role of the nuclear envelope in synthesis, processing, and transport of membrane glycoproteins
    • Puddington L, Lively MO, Lyles DS (1985) Role of the nuclear envelope in synthesis, processing, and transport of membrane glycoproteins. J Biol Chem 260(9):5641-5647
    • (1985) J Biol Chem , vol.260 , Issue.9 , pp. 5641-5647
    • Puddington, L.1    Lively, M.O.2    Lyles, D.S.3
  • 32
    • 0037064176 scopus 로고    scopus 로고
    • Role of ANC-1 in tethering nuclei to the actin cytoskeleton
    • doi: 10.1126/science.1075119
    • Starr DA, Han M (2002) Role of ANC-1 in tethering nuclei to the actin cytoskeleton. Science 298(5592):406-409. doi: 10.1126/science.1075119
    • (2002) Science , vol.298 , Issue.5592 , pp. 406-409
    • Starr, D.A.1    Han, M.2
  • 33
    • 2342466617 scopus 로고    scopus 로고
    • Matefin, a Caenorhabditis elegans germ line-specifi c SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development
    • doi: 10.1073/pnas.0307880101
    • Fridkin A, Mills E, Margalit A, Neufeld E, Lee KK, Feinstein N, Cohen M, Wilson KL, Gruenbaum Y (2004) Matefi n, a Caenorhabditis elegans germ line-specifi c SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development. Proc Natl Acad Sci USA 101(18):6987-6992. doi: 10.1073/pnas.0307880101
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.18 , pp. 6987-6992
    • Fridkin, A.1    Mills, E.2    Margalit, A.3    Neufeld, E.4    Lee, K.K.5    Feinstein, N.6    Cohen, M.7    Wilson, K.L.8    Gruenbaum, Y.9
  • 34
    • 84863613755 scopus 로고    scopus 로고
    • Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specifi c intracellular scaffolds
    • doi: 10.1371/journal.pone.0040098
    • Rajgor D, Mellad JA, Autore F, Zhang Q, Shanahan CM (2012) Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specifi c intracellular scaffolds. PLoS One 7(7):e40098. doi: 10.1371/journal.pone.0040098
    • (2012) PLoS One , vol.7 , Issue.7
    • Rajgor, D.1    Mellad, J.A.2    Autore, F.3    Zhang, Q.4    Shanahan, C.M.5
  • 35
    • 1842850780 scopus 로고    scopus 로고
    • Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton
    • doi: 10.1016/j.yexcr.2004.01.014
    • Padmakumar VC, Abraham S, Braune S, Noegel AA, Tunggal B, Karakesisoglou I, Korenbaum E (2004) Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton. Exp Cell Res 295(2):330-339. doi: 10.1016/j.yexcr.2004.01.014
    • (2004) Exp Cell Res , vol.295 , Issue.2 , pp. 330-339
    • Padmakumar, V.C.1    Abraham, S.2    Braune, S.3    Noegel, A.A.4    Tunggal, B.5    Karakesisoglou, I.6    Korenbaum, E.7
  • 36
    • 28544437813 scopus 로고    scopus 로고
    • Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
    • doi: 10.1083/jcb.200506083
    • Wilhelmsen K, Litjens SH, Kuikman I, Tshimbalanga N, Janssen H, van den Bout I, Raymond K, Sonnenberg A (2005) Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J Cell Biol 171(5):799-810. doi: 10.1083/jcb.200506083
    • (2005) J Cell Biol , vol.171 , Issue.5 , pp. 799-810
    • Wilhelmsen, K.1    Litjens, S.H.2    Kuikman, I.3    Tshimbalanga, N.4    Janssen, H.5    Van Den Bout, I.6    Raymond, K.7    Sonnenberg, A.8
  • 38
    • 14944383270 scopus 로고    scopus 로고
    • Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle
    • doi: 10.1242/jcs.01642
    • Zhang Q, Ragnauth CD, Skepper JN, Worth NF, Warren DT, Roberts RG, Weissberg PL, Ellis JA, Shanahan CM (2005) Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle. J Cell Sci 118(Pt 4):673-687. doi: 10.1242/jcs.01642
    • (2005) J Cell Sci , vol.118 , Issue.PART 4 , pp. 673-687
    • Zhang, Q.1    Ragnauth, C.D.2    Skepper, J.N.3    Worth, N.F.4    Warren, D.T.5    Roberts, R.G.6    Weissberg, P.L.7    Ellis, J.A.8    Shanahan, C.M.9
  • 39
    • 12344291865 scopus 로고    scopus 로고
    • Bone morphogenetic proteins
    • doi:HHV6108EX6P056CA [pii] 10.1080/08977190412331279890
    • Chen D, Zhao M, Mundy G (2004) Bone morphogenetic proteins. Growth Factors 22(4): 233-241, doi:HHV6108EX6P056CA [pii] 10.1080/08977190412331279890
    • (2004) Growth Factors , vol.22 , Issue.4 , pp. 233-241
    • Chen, D.1    Zhao, M.2    Mundy, G.3
  • 40
    • 49749169414 scopus 로고
    • An electron microscope study of the nuclear envelope of amphibian oocytes
    • Wischnitzer S (1958) An electron microscope study of the nuclear envelope of amphibian oocytes. J Ultrastruct Res 1(3):201-222
    • (1958) J Ultrastruct Res , vol.1 , Issue.3 , pp. 201-222
    • Wischnitzer, S.1
  • 41
    • 0028294522 scopus 로고
    • Integral membrane proteins and dynamic organization of the nuclear envelope
    • Gerace L, Foisner R (1994) Integral membrane proteins and dynamic organization of the nuclear envelope. Trends Cell Biol 4(4):127-131
    • (1994) Trends Cell Biol , vol.4 , Issue.4 , pp. 127-131
    • Gerace, L.1    Foisner, R.2
  • 42
    • 84861384878 scopus 로고    scopus 로고
    • Functional architecture of the nuclear pore complex
    • doi: 10.1146/annurev-biophys-050511-102328
    • Grossman E, Medalia O, Zwerger M (2012) Functional architecture of the nuclear pore complex. Annu Rev Biophys 41:557-584. doi: 10.1146/annurev-biophys- 050511-102328
    • (2012) Annu Rev Biophys , vol.41 , pp. 557-584
    • Grossman, E.1    Medalia, O.2    Zwerger, M.3
  • 43
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny S, Dreyfuss G (1999) Transport of proteins and RNAs in and out of the nucleus. Cell 99(7):677-690
    • (1999) Cell , vol.99 , Issue.7 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 44
    • 33645962474 scopus 로고    scopus 로고
    • Nuclear pores form de novo from both sides of the nuclear envelope
    • doi: 10.1126/science.1124196
    • D'Angelo MA, Anderson DJ, Richard E, Hetzer MW (2006) Nuclear pores form de novo from both sides of the nuclear envelope. Science 312(5772):440-443. doi: 10.1126/science.1124196
    • (2006) Science , vol.312 , Issue.5772 , pp. 440-443
    • D'Angelo, M.A.1    Anderson, D.J.2    Richard, E.3    Hetzer, M.W.4
  • 45
    • 52949107958 scopus 로고    scopus 로고
    • Structure, dynamics and function of nuclear pore complexes
    • doi: 10.1016/j.tcb.2008.07.009
    • D'Angelo MA, Hetzer MW (2008) Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol 18(10):456-466. doi: 10.1016/j.tcb.2008.07.009
    • (2008) Trends Cell Biol , vol.18 , Issue.10 , pp. 456-466
    • D'Angelo, M.A.1    Hetzer, M.W.2
  • 46
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane
    • doi: 10.1073/pnas.211201898
    • Dreger M, Bengtsson L, Schöneberg T, Otto H, Hucho F (2001) Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc Natl Acad Sci USA 98(21):11943-11948. doi: 10.1073/pnas.211201898
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.21 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schöneberg, T.3    Otto, H.4    Hucho, F.5
  • 48
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • doi: 10.1126/science.1088176
    • Schirmer EC, Florens L, Guan T, Yates JR, Gerace L (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301(5638):1380-1382. doi: 10.1126/science.1088176
    • (2003) Science , vol.301 , Issue.5638 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates, J.R.4    Gerace, L.5
  • 51
    • 84875175486 scopus 로고    scopus 로고
    • When lamins go bad: Nuclear structure and disease
    • doi: 10.1016/j.cell.2013.02.015
    • Schreiber KH, Kennedy BK (2013) When lamins go bad: nuclear structure and disease. Cell 152(6):1365-1375. doi: 10.1016/j.cell.2013.02.015
    • (2013) Cell , vol.152 , Issue.6 , pp. 1365-1375
    • Schreiber, K.H.1    Kennedy, B.K.2
  • 52
    • 0025306949 scopus 로고
    • Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery
    • Paddy MR, Belmont AS, Saumweber H, Agard DA, Sedat JW (1990) Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery. Cell 62(1):89-106
    • (1990) Cell , vol.62 , Issue.1 , pp. 89-106
    • Paddy, M.R.1    Belmont, A.S.2    Saumweber, H.3    Agard, D.A.4    Sedat, J.W.5
  • 53
    • 0037335755 scopus 로고    scopus 로고
    • Molecular architecture of intermediate fi laments
    • doi: 10.1002/bies.10246
    • Strelkov S, Herrmann H, Aebi U (2003) Molecular architecture of intermediate fi laments. Bioessays 25(3):243-251. doi: 10.1002/bies.10246
    • (2003) Bioessays , vol.25 , Issue.3 , pp. 243-251
    • Strelkov, S.1    Herrmann, H.2    Aebi, U.3
  • 54
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediatetype fi laments
    • doi: 10.1038/323560a0
    • Aebi U, Cohn J, Buhle L, Gerace L (1986) The nuclear lamina is a meshwork of intermediatetype fi laments. Nature 323(6088):560-564. doi: 10.1038/323560a0
    • (1986) Nature , vol.323 , Issue.6088 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 55
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate fi laments: 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 fi laments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu Rev Biochem 73:749-789. doi: 10.1146/annurev.biochem.73.011303. 073823
    • (2004) Annu Rev Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 56
    • 84860138137 scopus 로고    scopus 로고
    • Evolution of the lamin protein family: What introns can tell
    • 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
  • 58
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • doi: 10.1006/jsbi.1998.3987
    • 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
  • 60
    • 0036500259 scopus 로고    scopus 로고
    • Nuclear lamins: Building blocks of nuclear architecture
    • doi: 10.1101/gad.960502
    • Goldman RD, Gruenbaum Y, Moir RD, Shumaker DK, Spann TP (2002) Nuclear lamins: building blocks of nuclear architecture. Genes Dev 16(5):533-547. doi: 10.1101/gad.960502
    • (2002) Genes Dev , vol.16 , Issue.5 , pp. 533-547
    • Goldman, R.D.1    Gruenbaum, Y.2    Moir, R.D.3    Shumaker, D.K.4    Spann, T.P.5
  • 61
    • 0025845750 scopus 로고
    • The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2
    • Kitten GT, Nigg EA (1991) The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2. J Cell Biol 113(1):13-23
    • (1991) J Cell Biol , vol.113 , Issue.1 , pp. 13-23
    • Kitten, G.T.1    Nigg, E.A.2
  • 62
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • doi: 10.1242/jcs.01102
    • Zastrow MS, Vlcek S, Wilson KL (2004) Proteins that bind A-type lamins: integrating isolated clues. J Cell Sci 117
    • (2004) J Cell Sci , vol.117 , Issue.PART 7 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 63
    • 80052417470 scopus 로고    scopus 로고
    • Lamina-independent lamins in the nuclear interior serve important functions
    • doi: 10.1101/sqb.2010.75.018
    • Dechat T, Gesson K, Foisner R (2010) Lamina-independent lamins in the nuclear interior serve important functions. Cold Spring Harb Symp Quant Biol 75:533-543. doi: 10.1101/sqb.2010.75.018
    • (2010) Cold Spring Harb Symp Quant Biol , vol.75 , pp. 533-543
    • Dechat, T.1    Gesson, K.2    Foisner, R.3
  • 64
    • 0024241247 scopus 로고
    • Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones
    • Höger TH, Krohne G, Franke WW (1988) Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones. Eur J Cell Biol 47(2):283-290
    • (1988) Eur J Cell Biol , vol.47 , Issue.2 , pp. 283-290
    • Höger, T.H.1    Krohne, G.2    Franke, W.W.3
  • 65
    • 0025165401 scopus 로고
    • Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin
    • Höger TH, Zatloukal K, Waizenegger I, Krohne G (1990) Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Chromosoma 99(6):379-390
    • (1990) Chromosoma , vol.99 , Issue.6 , pp. 379-390
    • Höger, T.H.1    Zatloukal, K.2    Waizenegger, I.3    Krohne, G.4
  • 66
    • 0027257461 scopus 로고
    • Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C
    • 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
  • 67
    • 0028980880 scopus 로고
    • Structural organization of the human gene (LMNB1) encoding nuclear lamin B1
    • doi: 10.1006/geno.1995.1036
    • Lin F, Worman HJ (1995) Structural organization of the human gene (LMNB1) encoding nuclear lamin B1. Genomics 27(2):230-236. doi: 10.1006/geno.1995.1036
    • (1995) Genomics , vol.27 , Issue.2 , pp. 230-236
    • Lin, F.1    Worman, H.J.2
  • 68
    • 0033939554 scopus 로고    scopus 로고
    • Review: The dynamics of the nuclear lamins during the cell cycle-relationship between structure and function
    • doi: 10.1006/jsbi.2000.4251
    • Moir RD, Spann TP, Lopez-Soler RI, Yoon M, Goldman AE, Khuon S, Goldman RD (2000) Review: the dynamics of the nuclear lamins during the cell cycle-relationship between structure and function. J Struct Biol 129(2-3):324-334. doi: 10.1006/jsbi.2000.4251
    • (2000) J Struct Biol , vol.129 , Issue.2-3 , pp. 324-334
    • Moir, R.D.1    Spann, T.P.2    Lopez-Soler, R.I.3    Yoon, M.4    Goldman, A.E.5    Khuon, S.6    Goldman, R.D.7
  • 69
    • 9444268739 scopus 로고    scopus 로고
    • The nucleolus and transcription of ribosomal genes
    • doi: 10.1016/j.biolcel.2004.04.015
    • Raska I, Koberna K, Malínský J, Fidlerová H, Masata M (2004) The nucleolus and transcription of ribosomal genes. Biol Cell 96(8):579-594. doi: 10.1016/j.biolcel.2004.04.015
    • (2004) Biol Cell , vol.96 , Issue.8 , pp. 579-594
    • Raska, I.1    Koberna, K.2    Malínský, J.3    Fidlerová, H.4    Masata, M.5
  • 70
    • 1542569574 scopus 로고    scopus 로고
    • Cajal bodies
    • Matera AG (2003) Cajal bodies. Curr Biol 13(13):R503
    • (2003) Curr Biol , vol.13 , Issue.13
    • Matera, A.G.1
  • 71
    • 0032231895 scopus 로고    scopus 로고
    • Coiled bodies and gems: Janus or gemini?
    • doi: 10.1086/301992
    • Matera AG, Frey MR (1998) Coiled bodies and gems: Janus or gemini? Am J Hum Genet 63(2):317-321. doi: 10.1086/301992
    • (1998) Am J Hum Genet , vol.63 , Issue.2 , pp. 317-321
    • Matera, A.G.1    Frey, M.R.2
  • 72
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • doi: 10.1002/bies.20089
    • Dellaire G, Bazett-Jones DP (2004) PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26(9):963-977. doi: 10.1002/bies.20089
    • (2004) Bioessays , vol.26 , Issue.9 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 74
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • Pederson T, Aebi U (2002) Actin in the nucleus: what form and what for? J Struct Biol 140(1-3):3-9
    • (2002) J Struct Biol , vol.140 , Issue.1-3 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 75
    • 59649083719 scopus 로고    scopus 로고
    • Cell and molecular biology of nuclear actin
    • doi: 10.1016/s1937-6448(08)01806-6
    • Hofmann WA (2009) Cell and molecular biology of nuclear actin. Int Rev Cell Mol Biol 273:219-263. doi: 10.1016/s1937-6448(08)01806-6
    • (2009) Int Rev Cell Mol Biol , vol.273 , pp. 219-263
    • Hofmann, W.A.1
  • 77
    • 80455168204 scopus 로고    scopus 로고
    • Nuclear actin and myosins: Life without fi laments
    • doi: 10.1038/ncb2364
    • de Lanerolle P, Serebryannyy L (2011) Nuclear actin and myosins: life without fi laments. Nat Cell Biol 13(11):1282-1288. doi: 10.1038/ncb2364
    • (2011) Nat Cell Biol , vol.13 , Issue.11 , pp. 1282-1288
    • De Lanerolle, P.1    Serebryannyy, L.2
  • 78
    • 14344265557 scopus 로고    scopus 로고
    • Spectrin repeat proteins in the nucleus
    • doi: 10.1002/bies.20177
    • Young KG, Kothary R (2005) Spectrin repeat proteins in the nucleus. Bioessays 27(2): 144-152. doi: 10.1002/bies.20177
    • (2005) Bioessays , vol.27 , Issue.2 , pp. 144-152
    • Young, K.G.1    Kothary, R.2
  • 79
    • 32244437071 scopus 로고    scopus 로고
    • Nuclear titin interacts with A-and B-type lamins in vitro and in vivo
    • doi: 10.1242/jcs.02728
    • Zastrow MS, Flaherty DB, Benian GM, Wilson KL (2006) Nuclear titin interacts with A-and B-type lamins in vitro and in vivo. J Cell Sci 119(Pt 2):239-249. doi: 10.1242/jcs.02728
    • (2006) J Cell Sci , vol.119 , Issue.PART 2 , pp. 239-249
    • Zastrow, M.S.1    Flaherty, D.B.2    Benian, G.M.3    Wilson, K.L.4
  • 80
    • 0034160165 scopus 로고    scopus 로고
    • Searching for a function for nuclear actin
    • Rando OJ, Zhao K, Crabtree GR (2000) Searching for a function for nuclear actin. Trends Cell Biol 10(3):92-97
    • (2000) Trends Cell Biol , vol.10 , Issue.3 , pp. 92-97
    • Rando, O.J.1    Zhao, K.2    Crabtree, G.R.3
  • 81
    • 32644451623 scopus 로고    scopus 로고
    • Nucleoplasmic betaactin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations
    • doi: 10.1083/jcb.200507101
    • McDonald D, Carrero G, Andrin C, de Vries G, Hendzel MJ (2006) Nucleoplasmic betaactin exists in a dynamic equilibrium between low-mobility polymeric species and rapidly diffusing populations. J Cell Biol 172(4):541-552. doi: 10.1083/jcb.200507101
    • (2006) J Cell Biol , vol.172 , Issue.4 , pp. 541-552
    • McDonald, D.1    Carrero, G.2    Andrin, C.3    De Vries, G.4    Hendzel, M.J.5
  • 82
    • 65249111020 scopus 로고    scopus 로고
    • Actin dynamics and functions in the interphase nucleus: Moving toward an understanding of nuclear polymeric actin
    • doi: 10.1139/o08-133
    • Gieni RS, Hendzel MJ (2009) Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin. Biochem Cell Biol 87(1):283-306. doi: 10.1139/o08-133
    • (2009) Biochem Cell Biol , vol.87 , Issue.1 , pp. 283-306
    • Gieni, R.S.1    Hendzel, M.J.2
  • 83
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • doi: 10.1093/emboj/17.6.1635
    • Wada A, Fukuda M, Mishima M, Nishida E (1998) Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J 17(6):1635-1641. doi: 10.1093/emboj/17.6.1635
    • (1998) EMBO J , vol.17 , Issue.6 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 84
    • 84875456639 scopus 로고    scopus 로고
    • Visualization of actin fi laments and monomers in somatic cell nuclei
    • doi: 10.1091/mbc.E12-09-0685
    • Belin BJ, Cimini BA, Blackburn EH, Mullins RD (2013) Visualization of actin fi laments and monomers in somatic cell nuclei. Mol Biol Cell 24(7):982-994. doi: 10.1091/mbc.E12-09-0685
    • (2013) Mol Biol Cell , vol.24 , Issue.7 , pp. 982-994
    • Belin, B.J.1    Cimini, B.A.2    Blackburn, E.H.3    Mullins, R.D.4
  • 85
    • 77956076208 scopus 로고    scopus 로고
    • Nuclear functions of actin
    • doi: 10.1101/cshperspect.a000620
    • Visa N, Percipalle P (2010) Nuclear functions of actin. Cold Spring Harb Perspect Biol 2(4):a000620. doi: 10.1101/cshperspect.a000620
    • (2010) Cold Spring Harb Perspect Biol , vol.2 , Issue.4
    • Visa, N.1    Percipalle, P.2
  • 86
    • 0017687532 scopus 로고
    • Nuclear matrix. Isolation and characterization of a framework structure from rat liver nuclei
    • Berezney R, Coffey DS (1977) Nuclear matrix. Isolation and characterization of a framework structure from rat liver nuclei. J Cell Biol 73(3):616-637
    • (1977) J Cell Biol , vol.73 , Issue.3 , pp. 616-637
    • Berezney, R.1    Coffey, D.S.2
  • 87
    • 58049198445 scopus 로고    scopus 로고
    • Mechanotransduction gone awry
    • doi: 10.1038/nrm2597
    • Jaalouk DE, Lammerding J (2009) Mechanotransduction gone awry. Nat Rev Mol Cell Biol 10(1):63-73. doi: 10.1038/nrm2597
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.1 , pp. 63-73
    • Jaalouk, D.E.1    Lammerding, J.2
  • 88
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: New insights into their functions from in vivo studies
    • doi: 10.1038/nrm2476
    • Heasman SJ, Ridley AJ (2008) Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 9(9):690-701. doi: 10.1038/nrm2476
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 89
    • 0031705402 scopus 로고    scopus 로고
    • Simulations of the erythrocyte cytoskeleton at large deformation. II. Micropipette aspiration
    • doi: 10.1016/s0006-3495(98)74076-7
    • Discher DE, Boal DH, Boey SK (1998) Simulations of the erythrocyte cytoskeleton at large deformation. II. Micropipette aspiration. Biophys J 75(3):1584-1597. doi: 10.1016/s0006-3495(98)74076-7
    • (1998) Biophys J , vol.75 , Issue.3 , pp. 1584-1597
    • Discher, D.E.1    Boal, D.H.2    Boey, S.K.3
  • 90
    • 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
    • (2004) J Cell Sci , vol.117 , Issue.PART 20 , pp. 4779-4786
    • Dahl, K.N.1    Kahn, S.M.2    Wilson, K.L.3    De, D.4
  • 91
    • 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(4):2855-2864. doi: 10.1529/biophysj.105.062554
    • (2005) Biophys J , vol.89 , Issue.4 , pp. 2855-2864
    • Dahl, K.N.1    Engler, A.J.2    Pajerowski, J.D.3    Discher, D.E.4
  • 92
    • 33845436306 scopus 로고    scopus 로고
    • Mechanical properties of the cell nucleus and the effect of emerin defi ciency
    • doi: 10.1529/biophysj.106.086454
    • Rowat AC, Lammerding J, Ipsen JH (2006) Mechanical properties of the cell nucleus and the effect of emerin defi ciency. Biophys J 91(12):4649-4664. doi: 10.1529/biophysj.106.086454
    • (2006) Biophys J , vol.91 , Issue.12 , pp. 4649-4664
    • Rowat, A.C.1    Lammerding, J.2    Ipsen, J.H.3
  • 93
    • 0034708375 scopus 로고    scopus 로고
    • Viscoelastic properties of the cell nucleus
    • doi: 10.1006/bbrc.2000.2360
    • Guilak F, Tedrow JR, Burgkart R (2000) Viscoelastic properties of the cell nucleus. Biochem Biophys Res Commun 269(3):781-786. doi: 10.1006/bbrc.2000.2360
    • (2000) Biochem Biophys Res Commun , vol.269 , Issue.3 , pp. 781-786
    • Guilak, F.1    Tedrow, J.R.2    Burgkart, R.3
  • 94
    • 0342656135 scopus 로고    scopus 로고
    • Atomic force microscopy of the cell nucleus
    • doi: 10.1006/jsbi.2000.4233
    • Jiménez-García LF, Fragoso-Soriano R (2000) Atomic force microscopy of the cell nucleus. J Struct Biol 129(2-3):218-222. doi: 10.1006/jsbi.2000.4233
    • (2000) J Struct Biol , vol.129 , Issue.2-3 , pp. 218-222
    • Jiménez-García, L.F.1    Fragoso-Soriano, R.2
  • 95
    • 68049139442 scopus 로고    scopus 로고
    • Infl uence of lamin A on the mechanical properties of amphibian oocyte nuclei measured by atomic force microscopy
    • doi: 10.1016/j.bpj.2009.02.048
    • Schäpe J, Prausse S, Radmacher M, Stick R (2009) Infl uence of lamin A on the mechanical properties of amphibian oocyte nuclei measured by atomic force microscopy. Biophys J 96(10):4319-4325. doi: 10.1016/j.bpj.2009.02.048
    • (2009) Biophys J , vol.96 , Issue.10 , pp. 4319-4325
    • Schäpe, J.1    Prausse, S.2    Radmacher, M.3    Stick, R.4
  • 96
    • 83455179417 scopus 로고    scopus 로고
    • Amphibian oocyte nuclei expressing lamin A with the progeria mutation E145K exhibit an increased elastic modulus
    • doi: 10.4161/nucl.2.4.16119
    • Kaufmann A, Heinemann F, Radmacher M, Stick R (2011) Amphibian oocyte nuclei expressing lamin A with the progeria mutation E145K exhibit an increased elastic modulus. Nucleus 2(4):310-319. doi: 10.4161/nucl.2.4.16119
    • (2011) Nucleus , vol.2 , Issue.4 , pp. 310-319
    • Kaufmann, A.1    Heinemann, F.2    Radmacher, M.3    Stick, R.4
  • 97
    • 24144481867 scopus 로고    scopus 로고
    • Abnormal nuclear shape and impaired mechanotransduction in emerin-defi cient cells
    • doi: 10.1083/jcb.200502148
    • Lammerding J, Hsiao J, Schulze PC, Kozlov S, Stewart CL, Lee RT (2005) Abnormal nuclear shape and impaired mechanotransduction in emerin-defi cient cells. J Cell Biol 170(5): 781-791. doi: 10.1083/jcb.200502148
    • (2005) J Cell Biol , vol.170 , Issue.5 , pp. 781-791
    • Lammerding, J.1    Hsiao, J.2    Schulze, P.C.3    Kozlov, S.4    Stewart, C.L.5    Lee, R.T.6
  • 98
    • 33748744269 scopus 로고    scopus 로고
    • Lamins A and C but not lamin B1 regulate nuclear mechanics
    • doi: 10.1074/jbc.M513511200
    • 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
  • 99
    • 0036137722 scopus 로고    scopus 로고
    • Contribution of the nucleus to the mechanical properties of endothelial cells
    • Caille N, Thoumine O, Tardy Y, Meister JJ (2002) Contribution of the nucleus to the mechanical properties of endothelial cells. J Biomech 35(2):177-187
    • (2002) J Biomech , vol.35 , Issue.2 , pp. 177-187
    • Caille, N.1    Thoumine, O.2    Tardy, Y.3    Meister, J.J.4
  • 100
    • 2942516225 scopus 로고    scopus 로고
    • Micro-organization and visco-elasticity of the interphase nucleus revealed by particle nanotracking
    • doi: 10.1242/jcs.01073
    • Tseng Y, Lee JS, Kole TP, Jiang I, Wirtz D (2004) Micro-organization and visco-elasticity of the interphase nucleus revealed by particle nanotracking. J Cell Sci 117
    • (2004) J Cell Sci , vol.117 , Issue.PART 10 , pp. 2159-2167
    • Tseng, Y.1    Lee, J.S.2    Kole, T.P.3    Jiang, I.4    Wirtz, D.5
  • 101
    • 84869406280 scopus 로고    scopus 로고
    • Chromatin decondensation and nuclear softening accompany Nanog downregulation in embryonic stem cells
    • doi: 10.1016/j. bpj.2012.10.015
    • Chalut KJ, Höpfl er M, Lautenschläger F, Boyde L, Chan CJ, Ekpenyong A, Martinez-Arias A, Guck J (2012) Chromatin decondensation and nuclear softening accompany Nanog downregulation in embryonic stem cells. Biophys J 103(10):2060-2070. doi: 10.1016/j. bpj.2012.10.015
    • (2012) Biophys J , vol.103 , Issue.10 , pp. 2060-2070
    • Chalut, K.J.1    Höpfler, M.2    Lautenschläger, F.3    Boyde, L.4    Chan, C.J.5    Ekpenyong, A.6    Martinez-Arias, A.7    Guck, J.8
  • 103
    • 84875466803 scopus 로고    scopus 로고
    • Nuclear envelope composition determines the ability of neutrophil-type cells to passage through micron-scale constrictions
    • doi: 10.1074/jbc.M112.441535
    • Rowat AC, Jaalouk DE, Zwerger M, Ung WL, Eydelnant IA, Olins DE, Olins AL, Herrmann H, Weitz DA, Lammerding J (2013) Nuclear envelope composition determines the ability of neutrophil-type cells to passage through micron-scale constrictions. J Biol Chem 288(12):8610-8618. doi: 10.1074/jbc.M112.441535
    • (2013) J Biol Chem , vol.288 , Issue.12 , pp. 8610-8618
    • Rowat, A.C.1    Jaalouk, D.E.2    Zwerger, M.3    Ung, W.L.4    Eydelnant, I.A.5    Olins, D.E.6    Olins, A.L.7    Herrmann, H.8    Weitz, D.A.9    Lammerding, J.10
  • 104
    • 4744344929 scopus 로고    scopus 로고
    • Stiffness properties for Nucleus standard straight and contour electrode arrays
    • doi: 10.1016/j. medengphy.2004.05.001
    • Kha HN, Chen BK, Clark GM, Jones R (2004) Stiffness properties for Nucleus standard straight and contour electrode arrays. Med Eng Phys 26(8):677-685. doi: 10.1016/j. medengphy.2004.05.001
    • (2004) Med Eng Phys , vol.26 , Issue.8 , pp. 677-685
    • Kha, H.N.1    Chen, B.K.2    Clark, G.M.3    Jones, R.4
  • 105
    • 34249734843 scopus 로고    scopus 로고
    • Mechanics and deformation of the nucleus in micropipette aspiration experiment
    • doi: 10.1016/j.jbiomech.2006.09.023
    • Vaziri A, Mofrad MR (2007) Mechanics and deformation of the nucleus in micropipette aspiration experiment. J Biomech 40(9):2053-2062. doi: 10.1016/j.jbiomech.2006.09.023
    • (2007) J Biomech , vol.40 , Issue.9 , pp. 2053-2062
    • Vaziri, A.1    Mofrad, M.R.2
  • 106
    • 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(3):226-236. doi: 10.1002/bies.20720
    • (2008) Bioessays , vol.30 , Issue.3 , pp. 226-236
    • Rowat, A.C.1    Lammerding, J.2    Herrmann, H.3    Aebi, U.4
  • 107
    • 35649028495 scopus 로고    scopus 로고
    • Physical plasticity of the nucleus in stem cell differentiation
    • doi: 10.1073/pnas.0702576104
    • Pajerowski JD, Dahl KN, Zhong FL, Sammak PJ, Discher DE (2007) Physical plasticity of the nucleus in stem cell differentiation. Proc Natl Acad Sci USA 104(40):15619-15624. doi: 10.1073/pnas.0702576104
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.40 , pp. 15619-15624
    • Pajerowski, J.D.1    Dahl, K.N.2    Zhong, F.L.3    Sammak, P.J.4    Discher, D.E.5
  • 109
    • 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
    • doi: 10.4161/nucl.2.5.17765
    • 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
  • 110
    • 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(Pt 2):215-225. doi: 10.1242/jcs.022020
    • (2008) J Cell Sci , vol.121 , Issue.PART 2 , pp. 215-225
    • Goldberg, M.W.1    Huttenlauch, I.2    Hutchison, C.J.3    Stick, R.4
  • 112
    • 79960214825 scopus 로고    scopus 로고
    • Gene expression, chromosome position and lamin A/C mutations
    • doi: 10.1083/jcb.201101046 , 10.4161/nucl.2.3.16003
    • Puckelwartz MJ, Depreux FF, McNally EM (2011) Gene expression, chromosome position and lamin A/C mutations. Nucleus 2(3):162-167. doi: 10.1083/jcb.201101046 , 10.4161/nucl.2.3.16003
    • (2011) Nucleus , vol.2 , Issue.3 , pp. 162-167
    • Puckelwartz, M.J.1    Depreux, F.F.2    McNally, E.M.3
  • 114
    • 33847342966 scopus 로고    scopus 로고
    • The nuclear lamina. Both a structural framework and a platform for genome organization
    • Bridger JM, Foeger N, Kill IR, Herrmann H (2007) The nuclear lamina. Both a structural framework and a platform for genome organization. FEBS J 274(6):1354-1361
    • (2007) FEBS J , vol.274 , Issue.6 , pp. 1354-1361
    • Bridger, J.M.1    Foeger, N.2    Kill, I.R.3    Herrmann, H.4
  • 115
    • 21644448611 scopus 로고    scopus 로고
    • Dynamics of nuclear lamina assembly and disassembly
    • Broers JL, Ramaekers FC (2004) Dynamics of nuclear lamina assembly and disassembly. Symp Soc Exp Biol 56:177-192
    • (2004) Symp Soc Exp Biol , vol.56 , pp. 177-192
    • Broers, J.L.1    Ramaekers, F.C.2
  • 117
    • 84876499240 scopus 로고    scopus 로고
    • Partners and post-translational modifi cations of nuclear lamins
    • doi: 10.1007/s00412-013-0399-8
    • Simon DN, Wilson KL (2013) Partners and post-translational modifi cations 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
  • 118
    • 77956198726 scopus 로고    scopus 로고
    • Beyond lamins other structural components of the nucleoskeleton
    • doi: 10.1016/s0091-679x(10)98005-9
    • Zhong Z, Wilson KL, Dahl KN (2010) Beyond lamins other structural components of the nucleoskeleton. Methods Cell Biol 98:97-119. doi: 10.1016/s0091-679x(10)98005-9
    • (2010) Methods Cell Biol , vol.98 , pp. 97-119
    • Zhong, Z.1    Wilson, K.L.2    Dahl, K.N.3
  • 119
    • 79952808491 scopus 로고    scopus 로고
    • Nucleoskeleton mechanics at a glance
    • doi: 10.1242/jcs.069096
    • Dahl KN, Kalinowski A (2011) Nucleoskeleton mechanics at a glance. J Cell Sci 124 (Pt 5):675-678. doi: 10.1242/jcs.069096
    • (2011) J Cell Sci , vol.124 , Issue.PART 5 , pp. 675-678
    • Dahl, K.N.1    Kalinowski, A.2
  • 120
    • 84875190548 scopus 로고    scopus 로고
    • Nuclear positioning
    • doi: 10.1016/j.cell.2013.02.031
    • Gundersen GG, Worman HJ (2013) Nuclear positioning. Cell 152(6):1376-1389. doi: 10.1016/j.cell.2013.02.031
    • (2013) Cell , vol.152 , Issue.6 , pp. 1376-1389
    • Gundersen, G.G.1    Worman, H.J.2
  • 121
    • 84885846858 scopus 로고    scopus 로고
    • The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin
    • doi: 10.1007/s00412-013-0417-x
    • Rothballer A, Kutay U (2013) The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin. Chromosoma. doi: 10.1007/s00412-013-0417-x
    • (2013) Chromosoma
    • Rothballer, A.1    Kutay, U.2
  • 122
    • 0032772929 scopus 로고    scopus 로고
    • UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. Elegans development
    • Malone CJ, Fixsen WD, Horvitz HR, Han M (1999) UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. Elegans development. Development 126(14):3171-3181
    • (1999) Development , vol.126 , Issue.14 , pp. 3171-3181
    • Malone, C.J.1    Fixsen, W.D.2    Horvitz, H.R.3    Han, M.4
  • 123
    • 0036193442 scopus 로고    scopus 로고
    • Lamindependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans
    • doi: 10.1091/mbc.01-06-0294
    • Lee KK, Starr D, Cohen M, Liu J, Han M, Wilson KL, Gruenbaum Y (2002) Lamindependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans. Mol Biol Cell 13(3):892-901. doi: 10.1091/mbc.01-06-0294
    • (2002) Mol Biol Cell , vol.13 , Issue.3 , pp. 892-901
    • Lee, K.K.1    Starr, D.2    Cohen, M.3    Liu, J.4    Han, M.5    Wilson, K.L.6    Gruenbaum, Y.7
  • 124
    • 0346094458 scopus 로고    scopus 로고
    • The C. Elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • Malone CJ, Misner L, Le Bot N, Tsai MC, Campbell JM, Ahringer J, White JG (2003) The C. Elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus. Cell 115(7):825-836
    • (2003) Cell , vol.115 , Issue.7 , pp. 825-836
    • Malone, C.J.1    Misner, L.2    Le Bot, N.3    Tsai, M.C.4    Campbell, J.M.5    Ahringer, J.6    White, J.G.7
  • 125
    • 0037439661 scopus 로고    scopus 로고
    • ANChors away: An actin based mechanism of nuclear positioning
    • Starr DA, Han M (2003) ANChors away: an actin based mechanism of nuclear positioning. J Cell Sci 116(Pt 2):211-216
    • (2003) J Cell Sci , vol.116 , Issue.PART 2 , pp. 211-216
    • Starr, D.A.1    Han, M.2
  • 127
    • 78049394356 scopus 로고    scopus 로고
    • Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges
    • doi: 10.1146/annurev-cellbio-100109-104037
    • Starr DA, Fridolfsson HN (2010) Interactions between nuclei and the cytoskeleton are mediated by SUN-KASH nuclear-envelope bridges. Annu Rev Cell Dev Biol 26:421-444. doi: 10.1146/annurev-cellbio-100109-104037
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 421-444
    • Starr, D.A.1    Fridolfsson, H.N.2
  • 128
    • 34249777825 scopus 로고    scopus 로고
    • LEM-Domain proteins: New insights into lamin-interacting proteins
    • doi: 10.1016/s0074-7696(07)61001-8
    • Wagner N, Krohne G (2007) LEM-Domain proteins: new insights into lamin-interacting proteins. Int Rev Cytol 261:1-46. doi: 10.1016/s0074-7696(07) 61001-8
    • (2007) Int Rev Cytol , vol.261 , pp. 1-46
    • Wagner, N.1    Krohne, G.2
  • 129
    • 77957678443 scopus 로고    scopus 로고
    • LINC complexes in health and disease
    • doi: 10.4161/nucl.1.1.10530
    • Méjat A, Misteli T (2010) LINC complexes in health and disease. Nucleus 1(1):40-52. doi: 10.4161/nucl.1.1.10530
    • (2010) Nucleus , vol.1 , Issue.1 , pp. 40-52
    • Méjat, A.1    Misteli, T.2
  • 130
    • 84861543038 scopus 로고    scopus 로고
    • LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins
    • doi: 10.1016/j.cell.2012.03.046
    • Sosa BA, Rothballer A, Kutay U, Schwartz TU (2012) LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Cell 149(5):1035-1047. doi: 10.1016/j.cell.2012.03.046
    • (2012) Cell , vol.149 , Issue.5 , pp. 1035-1047
    • Sosa, B.A.1    Rothballer, A.2    Kutay, U.3    Schwartz, T.U.4
  • 131
    • 56349160730 scopus 로고    scopus 로고
    • Torsin A binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton
    • doi: 10.1242/jcs.029454
    • Nery FC, Zeng J, Niland BP, Hewett J, Farley J, Irimia D, Li Y, Wiche G, Sonnenberg A, Breakefi eld XO (2008) TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. J Cell Sci 121(Pt 20):3476-3486. doi: 10.1242/jcs.029454
    • (2008) J Cell Sci , vol.121 , Issue.PART 20 , pp. 3476-3486
    • Nery, F.C.1    Zeng, J.2    Niland, B.P.3    Hewett, J.4    Farley, J.5    Irimia, D.6    Li, Y.7    Wiche, G.8    Sonnenberg, A.9    Breakefield, X.O.10
  • 132
    • 78651103909 scopus 로고    scopus 로고
    • Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
    • doi: 10.1073/pnas.1000824108
    • Folker ES, Ostlund C, Luxton GW, Worman HJ, Gundersen GG (2011) Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement. Proc Natl Acad Sci USA 108(1):131-136. doi: 10.1073/pnas.1000824108
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.1 , pp. 131-136
    • Folker, E.S.1    Ostlund, C.2    Luxton, G.W.3    Worman, H.J.4    Gundersen, G.G.5
  • 133
    • 81855212456 scopus 로고    scopus 로고
    • Keeping the LINC: The importance of nucleocytoskeletal coupling in intracellular force transmission and cellular function
    • doi: 10.1042/bst20110686
    • Lombardi ML, Lammerding J (2011) Keeping the LINC: the importance of nucleocytoskeletal coupling in intracellular force transmission and cellular function. Biochem Soc Trans 39(6):1729-1734. doi: 10.1042/bst20110686
    • (2011) Biochem Soc Trans , vol.39 , Issue.6 , pp. 1729-1734
    • Lombardi, M.L.1    Lammerding, J.2
  • 134
    • 0031017220 scopus 로고    scopus 로고
    • Demonstration of mechanical connections between integrins, cytoskeletal fi laments, and nucleoplasm that stabilize nuclear structure
    • Maniotis AJ, Chen CS, Ingber DE (1997) Demonstration of mechanical connections between integrins, cytoskeletal fi laments, and nucleoplasm that stabilize nuclear structure. Proc Natl Acad Sci USA 94(3):849-854
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.3 , pp. 849-854
    • Maniotis, A.J.1    Chen, C.S.2    De, I.3
  • 135
    • 0029029742 scopus 로고
    • The product of the spindle formation gene sad1+ associates with the fi ssion yeast spindle pole body and is essential for viability
    • Hagan I, Yanagida M (1995) The product of the spindle formation gene sad1+ associates with the fi ssion yeast spindle pole body and is essential for viability. J Cell Biol 129(4):1033-1047
    • (1995) J Cell Biol , vol.129 , Issue.4 , pp. 1033-1047
    • Hagan, I.1    Yanagida, M.2
  • 136
    • 84878585819 scopus 로고    scopus 로고
    • Structural insights into LINC complexes
    • doi: 10.1016/j.sbi.2013.03.005
    • Sosa BA, Kutay U, Schwartz TU (2013) Structural insights into LINC complexes. Curr Opin Struct Biol 23(2):285-291. doi: 10.1016/j.sbi.2013.03.005
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.2 , pp. 285-291
    • Sosa, B.A.1    Kutay, U.2    Schwartz, T.U.3
  • 137
    • 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
    • doi: 10.1128/mcb.26.10.3738-3751.2006
    • Haque F, Lloyd DJ, Smallwood DT, Dent CL, Shanahan CM, Fry AM, Trembath RC, 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    Trembath, R.C.7    Shackleton, S.8
  • 138
  • 139
    • 79953305444 scopus 로고    scopus 로고
    • The nucleoporin Nup88 is interacting with nuclear lamin A
    • doi: 10.1091/mbc.E10-05-0463
    • Lussi YC, Hügi I, Laurell E, Kutay U, Fahrenkrog B (2011) The nucleoporin Nup88 is interacting with nuclear lamin A. Mol Biol Cell 22(7):1080-1090. doi: 10.1091/mbc.E10-05-0463
    • (2011) Mol Biol Cell , vol.22 , Issue.7 , pp. 1080-1090
    • Lussi, Y.C.1    Hügi, I.2    Laurell, E.3    Kutay, U.4    Fahrenkrog, B.5
  • 140
    • 69449090753 scopus 로고    scopus 로고
    • Bringing KASH under the SUN: The many faces of nucleocytoskeletal connections
    • doi: 10.1083/jcb.200906068
    • Razafsky D, Hodzic D (2009) Bringing KASH under the SUN: the many faces of nucleocytoskeletal connections. J Cell Biol 186(4):461-472. doi: 10.1083/jcb.200906068
    • (2009) J Cell Biol , vol.186 , Issue.4 , pp. 461-472
    • Razafsky, D.1    Hodzic, D.2
  • 141
    • 0034644646 scopus 로고    scopus 로고
    • Syne-1, a dystrophin-and Klarsichtrelated protein associated with synaptic nuclei at the neuromuscular junction
    • doi: 10.1074/jbc.M004775200
    • Apel ED, Lewis RM, Grady RM, Sanes JR (2000) Syne-1, a dystrophin-and Klarsichtrelated protein associated with synaptic nuclei at the neuromuscular junction. J Biol Chem 275(41):31986-31995. doi: 10.1074/jbc.M004775200
    • (2000) J Biol Chem , vol.275 , Issue.41 , pp. 31986-31995
    • Apel, E.D.1    Lewis, R.M.2    Grady, R.M.3    Sanes, J.R.4
  • 142
    • 79951552495 scopus 로고    scopus 로고
    • Nesprins LINC the nucleus and cytoskeleton
    • doi: 10.1016/j.ceb.2010.11.006
    • Mellad JA, Warren DT, Shanahan CM (2011) Nesprins LINC the nucleus and cytoskeleton. Curr Opin Cell Biol 23(1):47-54. doi: 10.1016/j.ceb.2010.11.006
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.1 , pp. 47-54
    • Mellad, J.A.1    Warren, D.T.2    Shanahan, C.M.3
  • 143
    • 0036674866 scopus 로고    scopus 로고
    • NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
    • Zhen YY, Libotte T, Munck M, Noegel AA, Korenbaum E (2002) NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J Cell Sci 115(Pt 15):3207-3222
    • (2002) J Cell Sci , vol.115 , Issue.PART 15 , pp. 3207-3222
    • Zhen, Y.Y.1    Libotte, T.2    Munck, M.3    Noegel, A.A.4    Korenbaum, E.5
  • 144
    • 60549099949 scopus 로고    scopus 로고
    • Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization
    • doi: 10.1073/pnas.0808602106
    • Roux KJ, Crisp ML, Liu Q, Kim D, Kozlov S, Stewart CL, Burke B (2009) Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization. Proc Natl Acad Sci USA 106(7):2194-2199. doi: 10.1073/pnas.0808602106
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.7 , pp. 2194-2199
    • Roux, K.J.1    Crisp, M.L.2    Liu, Q.3    Kim, D.4    Kozlov, S.5    Stewart, C.L.6    Burke, B.7
  • 146
    • 0036155776 scopus 로고    scopus 로고
    • Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C
    • Mislow JM, Kim MS, Davis DB, McNally EM (2002) Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C. J Cell Sci 115(Pt 1):61-70
    • (2002) J Cell Sci , vol.115 , Issue.PART 1 , pp. 61-70
    • Mislow, J.M.1    Kim, M.S.2    Davis, D.B.3    McNally, E.M.4
  • 148
    • 84865018091 scopus 로고    scopus 로고
    • A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis
    • doi: 10.1083/jcb.201204085
    • Morimoto A, Shibuya H, Zhu X, Kim J, Ishiguro K, Han M, Watanabe Y (2012) A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis. J Cell Biol 198(2):165-172. doi: 10.1083/jcb.201204085
    • (2012) J Cell Biol , vol.198 , Issue.2 , pp. 165-172
    • Morimoto, A.1    Shibuya, H.2    Zhu, X.3    Kim, J.4    Ishiguro, K.5    Han, M.6    Watanabe, Y.7
  • 149
    • 34548818532 scopus 로고    scopus 로고
    • A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
    • doi: 10.1083/jcb.200702026
    • Salpingidou G, Smertenko A, Hausmanowa-Petrucewicz I, Hussey PJ, Hutchison CJ (2007) A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J Cell Biol 178(6):897-904. doi: 10.1083/jcb.200702026
    • (2007) J Cell Biol , vol.178 , Issue.6 , pp. 897-904
    • Salpingidou, G.1    Smertenko, A.2    Hausmanowa-Petrucewicz, I.3    Hussey, P.J.4    Hutchison, C.J.5
  • 150
    • 68949170696 scopus 로고    scopus 로고
    • An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells
    • doi: 10.1242/jcs.047373
    • Buch C, Lindberg R, Figueroa R, Gudise S, Onischenko E, Hallberg E (2009) An integral protein of the inner nuclear membrane localizes to the mitotic spindle in mammalian cells. J Cell Sci 122(Pt 12):2100-2107. doi: 10.1242/jcs.047373
    • (2009) J Cell Sci , vol.122 , Issue.PART 12 , pp. 2100-2107
    • Buch, C.1    Lindberg, R.2    Figueroa, R.3    Gudise, S.4    Onischenko, E.5    Hallberg, E.6
  • 151
    • 79958115156 scopus 로고    scopus 로고
    • Samp1 is functionally associated with the LINC complex and A-type lamina networks
    • doi: 10.1242/jcs.078923
    • Gudise S, Figueroa RA, Lindberg R, Larsson V, Hallberg E (2011) Samp1 is functionally associated with the LINC complex and A-type lamina networks. J Cell Sci 124(Pt 12):2077-2085. doi: 10.1242/jcs.078923
    • (2011) J Cell Sci , vol.124 , Issue.PART 12 , pp. 2077-2085
    • Gudise, S.1    Figueroa, R.A.2    Lindberg, R.3    Larsson, V.4    Hallberg, E.5
  • 153
    • 77955901384 scopus 로고    scopus 로고
    • Linear arrays of nuclear envelope proteins harness retrograde actin fl ow for nuclear movement
    • doi: 10.1126/science.1189072
    • Luxton GW, Gomes ER, Folker ES, Vintinner E, Gundersen GG (2010) Linear arrays of nuclear envelope proteins harness retrograde actin fl ow for nuclear movement. Science 329(5994):956-959. doi: 10.1126/science.1189072
    • (2010) Science , vol.329 , Issue.5994 , pp. 956-959
    • Luxton, G.W.1    Gomes, E.R.2    Folker, E.S.3    Vintinner, E.4    Gundersen, G.G.5
  • 154
    • 42649137624 scopus 로고    scopus 로고
    • Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness
    • doi: 10.1016/j.yexcr.2008.02.022
    • Stewart-Hutchinson PJ, Hale CM, Wirtz D, Hodzic D (2008) Structural requirements for the assembly of LINC complexes and their function in cellular mechanical stiffness. Exp Cell Res 314(8):1892-1905. doi: 10.1016/j.yexcr.2008. 02.022
    • (2008) Exp Cell Res , vol.314 , Issue.8 , pp. 1892-1905
    • Stewart-Hutchinson, P.J.1    Hale, C.M.2    Wirtz, D.3    Hodzic, D.4
  • 155
    • 0035431155 scopus 로고    scopus 로고
    • A bouquet makes ends meet
    • doi: 10.1038/35085086
    • Scherthan H (2001) A bouquet makes ends meet. Nat Rev Mol Cell Biol 2(8):621-627. doi: 10.1038/35085086
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.8 , pp. 621-627
    • Scherthan, H.1
  • 156
    • 1042265578 scopus 로고    scopus 로고
    • Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fi ssion yeast
    • doi: 10.1007/s00438-003-0938-8
    • Miki F, Kurabayashi A, Tange Y, Okazaki K, Shimanuki M, Niwa O (2004) Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fi ssion yeast. Mol Genet Genomics 270(6):449-461. doi: 10.1007/s00438-003-0938-8
    • (2004) Mol Genet Genomics , vol.270 , Issue.6 , pp. 449-461
    • Miki, F.1    Kurabayashi, A.2    Tange, Y.3    Okazaki, K.4    Shimanuki, M.5    Niwa, O.6
  • 157
    • 33645962805 scopus 로고    scopus 로고
    • Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet arrangement of chromosomes
    • doi: 10.1016/j.cell.2006.01.048
    • Chikashige Y, Tsutsumi C, Yamane M, Okamasa K, Haraguchi T, Hiraoka Y (2006) Meiotic proteins bqt1 and bqt2 tether telomeres to form the bouquet arrangement of chromosomes. Cell 125(1):59-69. doi: 10.1016/j.cell.2006.01.048
    • (2006) Cell , vol.125 , Issue.1 , pp. 59-69
    • Chikashige, Y.1    Tsutsumi, C.2    Yamane, M.3    Okamasa, K.4    Haraguchi, T.5    Hiraoka, Y.6
  • 158
    • 0030940408 scopus 로고    scopus 로고
    • A novel fi ssion yeast gene, kms1+, is required for the formation of meiotic prophase-specifi c nuclear architecture
    • Shimanuki M, Miki F, Ding DQ, Chikashige Y, Hiraoka Y, Horio T, Niwa O (1997) A novel fi ssion yeast gene, kms1+, is required for the formation of meiotic prophase-specifi c nuclear architecture. Mol Gen Genet 254(3):238-249
    • (1997) Mol Gen Genet , vol.254 , Issue.3 , pp. 238-249
    • Shimanuki, M.1    Miki, F.2    Ding, D.Q.3    Chikashige, Y.4    Hiraoka, Y.5    Horio, T.6    Niwa, O.7
  • 159
    • 34249281252 scopus 로고    scopus 로고
    • The nuclear envelope protein Matefi n/SUN-1 is required for homologous pairing in C. Elegans meiosis
    • doi: 10.1016/j.devcel.2007.05.004
    • Penkner A, Tang L, Novatchkova M, Ladurner M, Fridkin A, Gruenbaum Y, Schweizer D, Loidl J, Jantsch V (2007) The nuclear envelope protein Matefi n/SUN-1 is required for homologous pairing in C. Elegans meiosis. Dev Cell 12(6):873-885. doi: 10.1016/j.devcel.2007.05.004
    • (2007) Dev Cell , vol.12 , Issue.6 , pp. 873-885
    • Penkner, A.1    Tang, L.2    Novatchkova, M.3    Ladurner, M.4    Fridkin, A.5    Gruenbaum, Y.6    Schweizer, D.7    Loidl, J.8    Jantsch, V.9
  • 160
    • 70350034129 scopus 로고    scopus 로고
    • KDP-1 is a nuclear envelope KASH protein required for cell-cycle progression
    • doi: 10.1242/jcs.051607
    • McGee MD, Stagljar I, Starr DA (2009) KDP-1 is a nuclear envelope KASH protein required for cell-cycle progression. J Cell Sci 122(Pt 16):2895-2905. doi: 10.1242/jcs.051607
    • (2009) J Cell Sci , vol.122 , Issue.PART 16 , pp. 2895-2905
    • McGee, M.D.1    Stagljar, I.2    Starr, D.A.3
  • 162
    • 74849107200 scopus 로고    scopus 로고
    • Loss of A-type lamins and genomic instability
    • Gonzalez-Suarez I, Redwood AB, Gonzalo S (2009) Loss of A-type lamins and genomic instability. Cell Cycle 8(23):3860-3865
    • (2009) Cell Cycle , vol.8 , Issue.23 , pp. 3860-3865
    • Gonzalez-Suarez, I.1    Redwood, A.B.2    Gonzalo, S.3
  • 164
    • 84866424053 scopus 로고    scopus 로고
    • Dynamic force-induced direct dissociation of protein complexes in a nuclear body in living cells
    • doi: 10.1038/ncomms1873
    • Poh YC, Shevtsov SP, Chowdhury F, Wu DC, Na S, Dundr M, Wang N (2012) Dynamic force-induced direct dissociation of protein complexes in a nuclear body in living cells. Nat Commun 3:866. doi: 10.1038/ncomms1873
    • (2012) Nat Commun , vol.3 , pp. 866
    • Poh, Y.C.1    Shevtsov, S.P.2    Chowdhury, F.3    Wu, D.C.4    Na, S.5    Dundr, M.6    Wang, N.7
  • 165
    • 84871276691 scopus 로고    scopus 로고
    • Force-induced changes in subnuclear movement and rheology
    • doi: 10.1016/j.bpj.2012.10.039
    • Booth-Gauthier EA, Alcoser TA, Yang G, Dahl KN (2012) Force-induced changes in subnuclear movement and rheology. Biophys J 103(12):2423-2431. doi: 10.1016/j.bpj.2012.10.039
    • (2012) Biophys J , vol.103 , Issue.12 , pp. 2423-2431
    • Booth-Gauthier, E.A.1    Alcoser, T.A.2    Yang, G.3    Dahl, K.N.4
  • 166
    • 0030987115 scopus 로고    scopus 로고
    • Mechanical continuity and reversible chromosome disassembly within intact genomes removed from living cells
    • Maniotis AJ, Bojanowski K, Ingber DE (1997) Mechanical continuity and reversible chromosome disassembly within intact genomes removed from living cells. J Cell Biochem 65(1):114-130
    • (1997) J Cell Biochem , vol.65 , Issue.1 , pp. 114-130
    • Maniotis, A.J.1    Bojanowski, K.2    Ingber, D.E.3
  • 167
    • 0347477365 scopus 로고    scopus 로고
    • Mechanobiology and diseases of mechanotransduction
    • Ingber DE (2003) Mechanobiology and diseases of mechanotransduction. Ann Med 35(8):564-577
    • (2003) Ann Med , vol.35 , Issue.8 , pp. 564-577
    • Ingber, D.E.1
  • 168
    • 33744488545 scopus 로고    scopus 로고
    • Cellular mechanotransduction: Putting all the pieces together again
    • doi: 10.1096/fj.05-5424rev
    • Ingber DE (2006) Cellular mechanotransduction: putting all the pieces together again. FASEB J 20(7):811-827. doi: 10.1096/fj.05-5424rev
    • (2006) FASEB J , vol.20 , Issue.7 , pp. 811-827
    • Ingber, D.E.1
  • 169
    • 12344296398 scopus 로고    scopus 로고
    • Control of basement membrane remodeling and epithelial branching morphogenesis in embryonic lung by Rho and cytoskeletal tension
    • doi: 10.1002/dvdy.20237
    • Moore KA, Polte T, Huang S, Shi B, Alsberg E, Sunday ME, Ingber DE (2005) Control of basement membrane remodeling and epithelial branching morphogenesis in embryonic lung by Rho and cytoskeletal tension. Dev Dyn 232(2):268-281. doi: 10.1002/dvdy.20237
    • (2005) Dev Dyn , vol.232 , Issue.2 , pp. 268-281
    • Moore, K.A.1    Polte, T.2    Huang, S.3    Shi, B.4    Alsberg, E.5    Sunday, M.E.6    Ingber, D.E.7
  • 170
    • 16244388205 scopus 로고    scopus 로고
    • The nuclear membrane and mechanotransduction: Impaired nuclear mechanics and mechanotransduction in lamin A/C defi cient cells
    • discussion 273-268
    • Lammerding J, Lee RT (2005) The nuclear membrane and mechanotransduction: impaired nuclear mechanics and mechanotransduction in lamin A/C defi cient 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
  • 171
    • 77956187161 scopus 로고    scopus 로고
    • Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis
    • doi: 10.1016/j. biocel.2010.07.001
    • Brosig M, Ferralli J, Gelman L, Chiquet M, Chiquet-Ehrismann R (2010) Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis. Int J Biochem Cell Biol 42(10):1717-1728. doi: 10.1016/j. biocel.2010.07.001
    • (2010) Int J Biochem Cell Biol , vol.42 , Issue.10 , pp. 1717-1728
    • Brosig, M.1    Ferralli, J.2    Gelman, L.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 172
    • 84878116428 scopus 로고    scopus 로고
    • Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics
    • doi: 10.1038/nature12105
    • Ho CY, Jaalouk DE, Vartiainen MK, Lammerding J (2013) Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics. Nature 497(7450):507-511. doi: 10.1038/nature12105
    • (2013) Nature , vol.497 , Issue.7450 , pp. 507-511
    • Ho, C.Y.1    Jaalouk, D.E.2    Vartiainen, M.K.3    Lammerding, J.4
  • 173
    • 70350233499 scopus 로고    scopus 로고
    • Nuclear margin irregularity and cancer: A review
    • Dey P (2009) Nuclear margin irregularity and cancer: a review. Anal Quant Cytol Histol 31(5):345-352
    • (2009) Anal Quant Cytol Histol , vol.31 , Issue.5 , pp. 345-352
    • Dey, P.1
  • 174
    • 0035691915 scopus 로고    scopus 로고
    • Nuclear envelope disorganization in fi broblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene
    • Vigouroux C, Auclair M, Dubosclard E, Pouchelet M, Capeau J, Courvalin JC, Buendia B (2001) Nuclear envelope disorganization in fi broblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene. J Cell Sci 114(Pt 24):4459-4468
    • (2001) J Cell Sci , vol.114 , Issue.PART 24 , pp. 4459-4468
    • Vigouroux, C.1    Auclair, M.2    Dubosclard, E.3    Pouchelet, M.4    Capeau, J.5    Courvalin, J.C.6    Buendia, B.7
  • 176
    • 81855169565 scopus 로고    scopus 로고
    • Cancer invasion and the microenvironment: Plasticity and reciprocity
    • doi: 10.1016/j.cell.2011.11.016
    • Friedl P, Alexander S (2011) Cancer invasion and the microenvironment: plasticity and reciprocity. Cell 147(5):992-1009. doi: 10.1016/j.cell.2011.11. 016
    • (2011) Cell , vol.147 , Issue.5 , pp. 992-1009
    • Friedl, P.1    Alexander, S.2
  • 180
    • 0037244266 scopus 로고    scopus 로고
    • Lamin expression in normal human skin, actinic keratosis, squamous cell carcinoma and basal cell carcinoma
    • Tilli CM, Ramaekers FC, Broers JL, Hutchison CJ, Neumann HA (2003) Lamin expression in normal human skin, actinic keratosis, squamous cell carcinoma and basal cell carcinoma. Br J Dermatol 148(1):102-109
    • (2003) Br J Dermatol , vol.148 , Issue.1 , pp. 102-109
    • Tilli, C.M.1    Ramaekers, F.C.2    Broers, J.L.3    Hutchison, C.J.4    Neumann, H.A.5
  • 181
    • 36849039867 scopus 로고    scopus 로고
    • Identifi cation of differentially expressed proteins in ovarian cancer using high-density protein microarrays
    • doi: 10.1073/pnas.0708572104
    • Hudson ME, Pozdnyakova I, Haines K, Mor G, Snyder M (2007) Identifi cation of differentially expressed proteins in ovarian cancer using high-density protein microarrays. Proc Natl Acad Sci USA 104(44):17494-17499. doi: 10.1073/pnas.0708572104
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.44 , pp. 17494-17499
    • Hudson, M.E.1    Pozdnyakova, I.2    Haines, K.3    Mor, G.4    Snyder, M.5
  • 182
    • 59149092901 scopus 로고    scopus 로고
    • Lamin A: A putative colonic epithelial stem cell biomarker which identifi es colorectal tumours with a more aggressive phenotype
    • doi: 10.1042/bst0361350
    • Willis ND, Wilson RG, Hutchison CJ (2008) Lamin A: a putative colonic epithelial stem cell biomarker which identifi es colorectal tumours with a more aggressive phenotype. Biochem Soc Trans 36(Pt 6):1350-1353. doi: 10.1042/bst0361350
    • (2008) Biochem Soc Trans , vol.36 , Issue.PART 6 , pp. 1350-1353
    • Willis, N.D.1    Wilson, R.G.2    Hutchison, C.J.3
  • 184
    • 34547569807 scopus 로고    scopus 로고
    • Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion
    • doi: 10.1038/ncb1616
    • Wolf K, Wu YI, Liu Y, Geiger J, Tam E, Overall C, Stack MS, Friedl P (2007) Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 9(8):893-904. doi: 10.1038/ncb1616
    • (2007) Nat Cell Biol , vol.9 , Issue.8 , pp. 893-904
    • Wolf, K.1    Wu, Y.I.2    Liu, Y.3    Geiger, J.4    Tam, E.5    Overall, C.6    Stack, M.S.7    Friedl, P.8
  • 185
    • 79953100080 scopus 로고    scopus 로고
    • Nuclear envelope structural defects cause chromosomal numerical instability and aneuploidy in ovarian cancer
    • doi: 10.1186/1741-7015-9-28
    • Capo-chichi CD, Cai KQ, Simpkins F, Ganjei-Azar P, Godwin AK, Xu XX (2011) Nuclear envelope structural defects cause chromosomal numerical instability and aneuploidy in ovarian cancer. BMC Med 9:28. doi: 10.1186/1741-7015-9-28
    • (2011) BMC Med , vol.9 , pp. 28
    • Capo-Chichi, C.D.1    Cai, K.Q.2    Simpkins, F.3    Ganjei-Azar, P.4    Godwin, A.K.5    Xu, X.X.6
  • 186
    • 60149112087 scopus 로고    scopus 로고
    • Reduced expression of lamin A/C correlates with poor histological differentiation and prognosis in primary gastric carcinoma
    • doi: 10.1186/1756-9966-28-8
    • Wu Z, Wu L, Weng D, Xu D, Geng J, Zhao F (2009) Reduced expression of lamin A/C correlates with poor histological differentiation and prognosis in primary gastric carcinoma. J Exp Clin Cancer Res 28:8. doi: 10.1186/1756-9966- 28-8
    • (2009) J Exp Clin Cancer Res , vol.28 , pp. 8
    • Wu, Z.1    Wu, L.2    Weng, D.3    Xu, D.4    Geng, J.5    Zhao, F.6
  • 188
    • 80054706102 scopus 로고    scopus 로고
    • The role of Lamin A in cytoskeleton organization in colorectal cancer cells: A proteomic investigation
    • doi: 10.4161/nucl.2.5.17775
    • Foster CR, Robson JL, Simon WJ, Twigg J, Cruikshank D, Wilson RG, Hutchison CJ (2011) The role of Lamin A in cytoskeleton organization in colorectal cancer cells: a proteomic investigation. Nucleus 2(5):434-443. doi: 10.4161/nucl.2.5.17775
    • (2011) Nucleus , vol.2 , Issue.5 , pp. 434-443
    • Foster, C.R.1    Robson, J.L.2    Simon, W.J.3    Twigg, J.4    Cruikshank, D.5    Wilson, R.G.6    Hutchison, C.J.7
  • 192
    • 84863814698 scopus 로고    scopus 로고
    • The role of nuclear matrix proteins binding to matrix attachment regions (Mars) in prostate cancer cell differentiation
    • doi: 10.1371/journal.pone.0040617
    • Barboro P, Repaci E, D'Arrigo C, Balbi C (2012) The role of nuclear matrix proteins binding to matrix attachment regions (Mars) in prostate cancer cell differentiation. PLoS One 7(7):e40617. doi: 10.1371/journal.pone.0040617
    • (2012) PLoS One , vol.7 , Issue.7
    • Barboro, P.1    Repaci, E.2    D'Arrigo, C.3    Balbi, C.4
  • 195
    • 84875190221 scopus 로고    scopus 로고
    • Genome architecture: Domain organization of interphase chromosomes
    • doi: 10.1016/j.cell.2013.02.001
    • Bickmore WA, van Steensel B (2013) Genome architecture: domain organization of interphase chromosomes. Cell 152(6):1270-1284. doi: 10.1016/j.cell.2013.02.001
    • (2013) Cell , vol.152 , Issue.6 , pp. 1270-1284
    • Bickmore, W.A.1    Van Steensel, B.2
  • 196
    • 84871501642 scopus 로고    scopus 로고
    • The nuclear lamins: Fl exibility in function
    • doi: 10.1038/nrm3488
    • Burke B, Stewart CL (2013) The nuclear lamins: fl exibility in function. Nat Rev Mol Cell Biol 14(1):13-24. doi: 10.1038/nrm3488
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.1 , pp. 13-24
    • Burke, B.1    Stewart, C.L.2
  • 197
    • 80054686286 scopus 로고    scopus 로고
    • Tumor metastasis: Molecular insights and evolving paradigms
    • doi: 10.1016/j.cell.2011.09.024
    • Valastyan S, Weinberg RA (2011) Tumor metastasis: molecular insights and evolving paradigms. Cell 147(2):275-292. doi: 10.1016/j.cell.2011.09.024
    • (2011) Cell , vol.147 , Issue.2 , pp. 275-292
    • Valastyan, S.1    Weinberg, R.A.2
  • 198
    • 0036151201 scopus 로고    scopus 로고
    • A close-up view of migrating Langerhans cells in the skin
    • doi: 10.1046/j.0022-202x.2001.01631.x
    • Stoitzner P, Pfaller K, Stössel H, Romani N (2002) A close-up view of migrating Langerhans cells in the skin. J Invest Dermatol 118(1):117-125. doi: 10.1046/j.0022-202x.2001.01631.x
    • (2002) J Invest Dermatol , vol.118 , Issue.1 , pp. 117-125
    • Stoitzner, P.1    Pfaller, K.2    Stössel, H.3    Romani, N.4
  • 199
    • 84867884892 scopus 로고    scopus 로고
    • Intravital third harmonic generation microscopy of collective melanoma cell invasion. Principles of interface guidance and microvesicle dynamics
    • Weigelin B, Bakker G-J, Friedl P (2012) Intravital third harmonic generation microscopy of collective melanoma cell invasion. Principles of interface guidance and microvesicle dynamics. IntraVital 1(1):32-43
    • (2012) IntraVital , vol.1 , Issue.1 , pp. 32-43
    • Weigelin, B.1    Bakker, G.-J.2    Friedl, P.3
  • 200
    • 77951757643 scopus 로고    scopus 로고
    • Pseudopodial actin dynamics control epithelial-mesenchymal transition in metastatic cancer cells
    • doi: 10.1158/0008-5472.can-09-4439
    • Shankar J, Messenberg A, Chan J, Underhill TM, Foster LJ, Nabi IR (2010) Pseudopodial actin dynamics control epithelial-mesenchymal transition in metastatic cancer cells. Cancer Res 70(9):3780-3790. doi: 10.1158/0008-5472.can- 09-4439
    • (2010) Cancer Res , vol.70 , Issue.9 , pp. 3780-3790
    • Shankar, J.1    Messenberg, A.2    Chan, J.3    Underhill, T.M.4    Foster, L.J.5    Nabi, I.R.6
  • 201
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules, and vimentin intermediate fi laments cooperate for elongation of invadopodia
    • doi: 10.1083/jcb.200909113
    • Schoumacher M, Goldman RD, Louvard D, Vignjevic DM (2010) Actin, microtubules, and vimentin intermediate fi laments cooperate for elongation of invadopodia. J Cell Biol 189(3):541-556. doi: 10.1083/jcb.200909113
    • (2010) J Cell Biol , vol.189 , Issue.3 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 202
    • 84855926245 scopus 로고    scopus 로고
    • Chemotaxis of cell populations through confi ned spaces at single-cell resolution
    • doi: 10.1371/journal.pone.0029211
    • Tong Z, Balzer EM, Dallas MR, Hung WC, Stebe KJ, Konstantopoulos K (2012) Chemotaxis of cell populations through confi ned spaces at single-cell resolution. PLoS One 7(1):e29211. doi: 10.1371/journal.pone.0029211
    • (2012) PLoS One , vol.7 , Issue.1
    • Tong, Z.1    Balzer, E.M.2    Dallas, M.R.3    Hung, W.C.4    Stebe, K.J.5    Konstantopoulos, K.6
  • 203
    • 84874812062 scopus 로고    scopus 로고
    • Hutchinson-Gilford progeria syndrome alters nuclear shape and reduces cell motility in three dimensional model substrates
    • doi: 10.1039/c3ib20231c
    • Booth-Gauthier EA, Du V, Ghibaudo M, Rape AD, Dahl KN, Ladoux B (2013) Hutchinson-Gilford progeria syndrome alters nuclear shape and reduces cell motility in three dimensional model substrates. Integr Biol (Camb) 5(3):569-577. doi: 10.1039/c3ib20231c
    • (2013) Integr Biol (Camb) , vol.5 , Issue.3 , pp. 569-577
    • Booth-Gauthier, E.A.1    Du, V.2    Ghibaudo, M.3    Rape, A.D.4    Dahl, K.N.5    Ladoux, B.6
  • 204
    • 43449096922 scopus 로고    scopus 로고
    • Increased mechanosensitivity and nuclear stiffness in Hutchinson-Gilford progeria cells: Effects of farnesyltransferase inhibitors
    • doi: 10.1111/j.1474-9726.2008.00382.x
    • Verstraeten VL, Ji JY, Cummings KS, Lee RT, Lammerding J (2008) Increased mechanosensitivity and nuclear stiffness in Hutchinson-Gilford progeria cells: effects of farnesyltransferase inhibitors. Aging Cell 7(3):383-393. doi: 10.1111/j.1474-9726.2008.00382.x
    • (2008) Aging Cell , vol.7 , Issue.3 , pp. 383-393
    • Verstraeten, V.L.1    Ji, J.Y.2    Cummings, K.S.3    Lee, R.T.4    Lammerding, J.5
  • 205
    • 33745904741 scopus 로고    scopus 로고
    • Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome
    • doi: 10.1073/pnas.0601058103
    • Dahl KN, Scaffi di P, Islam MF, Yodh AG, Wilson KL, Misteli T (2006) Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci USA 103(27):10271-10276. doi: 10.1073/pnas.0601058103
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.27 , pp. 10271-10276
    • Dahl, K.N.1    Scaffi Di, P.2    Islam, M.F.3    Yodh, A.G.4    Wilson, K.L.5    Misteli, T.6
  • 206
    • 84859589311 scopus 로고    scopus 로고
    • Lamin A/C protein is overexpressed in tissue-invading prostate cancer and promotes prostate cancer cell growth, migration and invasion through the PI3K/AKT/PTEN pathway
    • doi: 10.1093/carcin/bgs022
    • Kong L, Schäfer G, Bu H, Zhang Y, Klocker H (2012) Lamin A/C protein is overexpressed in tissue-invading prostate cancer and promotes prostate cancer cell growth, migration and invasion through the PI3K/AKT/PTEN pathway. Carcinogenesis 33(4):751-759. doi: 10.1093/carcin/bgs022
    • (2012) Carcinogenesis , vol.33 , Issue.4 , pp. 751-759
    • Kong, L.1    Schäfer, G.2    Bu, H.3    Zhang, Y.4    Klocker, H.5
  • 207
    • 84875162180 scopus 로고    scopus 로고
    • Enclosing chromatin: Reassembly of the nucleus after open mitosis
    • doi: 10.1016/j.cell.2013.02.046
    • Wandke C, Kutay U (2013) Enclosing chromatin: reassembly of the nucleus after open mitosis. Cell 152(6):1222-1225. doi: 10.1016/j.cell.2013.02.046
    • (2013) Cell , vol.152 , Issue.6 , pp. 1222-1225
    • Wandke, C.1    Kutay, U.2
  • 208
    • 84860122715 scopus 로고    scopus 로고
    • Transient nuclear envelope rupturing during interphase in human cancer cells
    • doi: 10.4161/nucl.18954
    • Vargas JD, Hatch EM, Anderson DJ, Hetzer MW (2012) Transient nuclear envelope rupturing during interphase in human cancer cells. Nucleus 3(1):88-100. doi: 10.4161/nucl.18954
    • (2012) Nucleus , vol.3 , Issue.1 , pp. 88-100
    • Vargas, J.D.1    Hatch, E.M.2    Anderson, D.J.3    Hetzer, M.W.4
  • 210
    • 84873349707 scopus 로고    scopus 로고
    • Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome
    • doi: 10.1101/gr.138032.112
    • McCord RP, Nazario-Toole A, Zhang H, Chines PS, Zhan Y, Erdos MR, Collins FS, Dekker J, Cao K (2013) Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome. Genome Res 23(2):260-269. doi: 10.1101/gr.138032.112
    • (2013) Genome Res , vol.23 , Issue.2 , pp. 260-269
    • McCord, R.P.1    Nazario-Toole, A.2    Zhang, H.3    Chines, P.S.4    Zhan, Y.5    Erdos, M.R.6    Collins, F.S.7    Dekker, J.8    Cao, K.9
  • 212
    • 84881086323 scopus 로고    scopus 로고
    • Cancer as a dysregulated epigenome allowing cellular growth advantage at the expense of the host
    • doi: 10.1038/nrc3486
    • Timp W, Feinberg AP (2013) Cancer as a dysregulated epigenome allowing cellular growth advantage at the expense of the host. Nat Rev Cancer 13(7):497-510. doi: 10.1038/nrc3486
    • (2013) Nat Rev Cancer , vol.13 , Issue.7 , pp. 497-510
    • Timp, W.1    Feinberg, A.P.2
  • 213
    • 0034756597 scopus 로고    scopus 로고
    • Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1
    • doi: 10.1093/embo-reports/kve199
    • Polioudaki H, Kourmouli N, Drosou V, Bakou A, Theodoropoulos PA, Singh PB, Giannakouros T, Georgatos SD (2001) Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1. EMBO Rep 2(10):920-925. doi: 10.1093/embo-reports/kve199
    • (2001) EMBO Rep , vol.2 , Issue.10 , pp. 920-925
    • Polioudaki, H.1    Kourmouli, N.2    Drosou, V.3    Bakou, A.4    Theodoropoulos, P.A.5    Singh, P.B.6    Giannakouros, T.7    Georgatos, S.D.8
  • 215
    • 26444589253 scopus 로고    scopus 로고
    • The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
    • doi: 10.1242/jcs.02521
    • Somech R, Shaklai S, Geller O, Amariglio N, Simon AJ, Rechavi G, Gal-Yam EN (2005) The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J Cell Sci 118(Pt 17):4017-4025. doi: 10.1242/jcs.02521
    • (2005) J Cell Sci , vol.118 , Issue.PART 17 , pp. 4017-4025
    • Somech, R.1    Shaklai, S.2    Geller, O.3    Amariglio, N.4    Simon, A.J.5    Rechavi, G.6    Gal-Yam, E.N.7
  • 216
    • 1542284570 scopus 로고    scopus 로고
    • Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy
    • Haraguchi T, Holaska JM, Yamane M, Koujin T, Hashiguchi N, Mori C, Wilson KL, Hiraoka Y (2004) Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy. Eur J Biochem 271(5):1035-1045
    • (2004) Eur J Biochem , vol.271 , Issue.5 , pp. 1035-1045
    • Haraguchi, T.1    Holaska, J.M.2    Yamane, M.3    Koujin, T.4    Hashiguchi, N.5    Mori, C.6    Wilson, K.L.7    Hiraoka, Y.8
  • 218
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cellless (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • doi: 10.1074/jbc.M208811200
    • Holaska JM, Lee KK, Kowalski AK, Wilson KL (2003) Transcriptional repressor germ cellless (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J Biol Chem 278(9):6969-6975. doi: 10.1074/jbc.M208811200
    • (2003) J Biol Chem , vol.278 , Issue.9 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 219
    • 84555179609 scopus 로고    scopus 로고
    • Extracellular matrix degradation and remodeling in development and disease
    • doi: 10.1101/cshperspect.a005058
    • Lu P, Takai K, Weaver VM, Werb Z (2011) Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb Perspect Biol 3(12). doi: 10.1101/cshperspect. a005058
    • (2011) Cold Spring Harb Perspect Biol , vol.3 , Issue.12
    • Lu, P.1    Takai, K.2    Weaver, V.M.3    Werb, Z.4
  • 220
    • 84858406337 scopus 로고    scopus 로고
    • Introduction: Why analyze single cells?
    • doi: 10.1007/978-1-61779-567-1-1
    • Di Carlo D, Tse HT, Gossett DR (2012) Introduction: why analyze single cells? Methods Mol Biol 853:1-10. doi: 10.1007/978-1-61779-567-1-1
    • (2012) Methods Mol Biol , vol.853 , pp. 1-10
    • Di Carlo, D.1    Tse, H.T.2    Gossett, D.R.3
  • 222
    • 68849103042 scopus 로고    scopus 로고
    • Loss of GATA6 leads to nuclear deformation and aneuploidy in ovarian cancer
    • doi: 10.1128/mcb.00087-09
    • Capo-chichi CD, Cai KQ, Testa JR, Godwin AK, Xu XX (2009) Loss of GATA6 leads to nuclear deformation and aneuploidy in ovarian cancer. Mol Cell Biol 29(17):4766-4777. doi: 10.1128/mcb.00087-09
    • (2009) Mol Cell Biol , vol.29 , Issue.17 , pp. 4766-4777
    • Capo-Chichi, C.D.1    Cai, K.Q.2    Testa, J.R.3    Godwin, A.K.4    Xu, X.X.5
  • 223
    • 21244491570 scopus 로고    scopus 로고
    • Inactivation of the lamin A/C gene by CpG island promoter hypermethylation in hematologic malignancies, and its association with poor survival in nodal diffuse large B-cell lymphoma
    • doi: 10.1200/jco.2005.11.650
    • Agrelo R, Setien F, Espada J, Artiga MJ, Rodriguez M, Pérez-Rosado A, Sanchez-Aguilera A, Fraga MF, Piris MA, Esteller M (2005) Inactivation of the lamin A/C gene by CpG island promoter hypermethylation in hematologic malignancies, and its association with poor survival in nodal diffuse large B-cell lymphoma. J Clin Oncol 23(17):3940-3947. doi: 10.1200/jco.2005.11.650
    • (2005) J Clin Oncol , vol.23 , Issue.17 , pp. 3940-3947
    • Agrelo, R.1    Setien, F.2    Espada, J.3    Artiga, M.J.4    Rodriguez, M.5    Pérez-Rosado, A.6    Sanchez-Aguilera, A.7    Fraga, M.F.8    Piris, M.A.9    Esteller, M.10
  • 224
    • 65249098993 scopus 로고    scopus 로고
    • Differential protein mapping of ovarian serous adenocarcinomas: Identifi cation of potential markers for distinct tumor stage
    • doi: 10.1021/pr800820z
    • Wang Y, Wu R, Cho KR, Thomas DG, Gossner G, Liu JR, Giordano TJ, Shedden KA, Misek DE, Lubman DM (2009) Differential protein mapping of ovarian serous adenocarcinomas: identifi cation of potential markers for distinct tumor stage. J Proteome Res 8(3):1452-1463. doi: 10.1021/pr800820z
    • (2009) J Proteome Res , vol.8 , Issue.3 , pp. 1452-1463
    • Wang, Y.1    Wu, R.2    Cho, K.R.3    Thomas, D.G.4    Gossner, G.5    Liu, J.R.6    Giordano, T.J.7    Shedden, K.A.8    Misek, D.E.9    Lubman, D.M.10
  • 225
    • 79951538944 scopus 로고    scopus 로고
    • Proteomics profi ling of microdissected low-and high-grade prostate tumors identifi es Lamin A as a discriminatory biomarker
    • doi: 10.1021/pr100921j
    • Skvortsov S, Schäfer G, Stasyk T, Fuchsberger C, Bonn GK, Bartsch G, Klocker H, Huber LA (2011) Proteomics profi ling of microdissected low-and high-grade prostate tumors identifi es 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    Schäfer, G.2    Stasyk, T.3    Fuchsberger, C.4    Bonn, G.K.5    Bartsch, G.6    Klocker, H.7    Huber, L.A.8
  • 226
    • 55949104084 scopus 로고    scopus 로고
    • Proteome analysis of membrane fractions in colorectal carcinomas by using 2D-DIGE saturation labeling
    • doi: 10.1021/pr800152u
    • Alfonso P, Cañamero M, Fernández-Carbonié F, Núñez A, Casal JI (2008) Proteome analysis of membrane fractions in colorectal carcinomas by using 2D-DIGE saturation labeling. J Proteome Res 7(10):4247-4255. doi: 10.1021/pr800152u
    • (2008) J Proteome Res , vol.7 , Issue.10 , pp. 4247-4255
    • Alfonso, P.1    Cañamero, M.2    Fernández-Carbonié, F.3    Núñez, A.4    Casal, J.I.5
  • 229
    • 73649104101 scopus 로고    scopus 로고
    • Circulating Lamin B1 (LMNB1) biomarker detects early stages of liver cancer in patients
    • doi: 10.1021/pr9002118
    • Sun S, Xu MZ, Poon RT, Day PJ, Luk JM (2010) Circulating Lamin B1 (LMNB1) biomarker detects early stages of liver cancer in patients. J Proteome Res 9(1):70-78. doi: 10.1021/pr9002118
    • (2010) J Proteome Res , vol.9 , Issue.1 , pp. 70-78
    • Sun, S.1    Xu, M.Z.2    Poon, R.T.3    Day, P.J.4    Luk, J.M.5
  • 231
    • 84883480839 scopus 로고    scopus 로고
    • Lamin B1 is a novel therapeutic target of betulinic acid in pancreatic cancer
    • doi: 10.1158/1078-0432.ccr-12-3630
    • Li L, Du Y, Kong X, Li Z, Jia Z, Cui J, Gao J, Wang L, Xie K (2013) Lamin B1 is a novel therapeutic target of betulinic acid in pancreatic cancer. Clin Cancer Res. doi: 10.1158/1078-0432.ccr-12-3630
    • (2013) Clin Cancer Res
    • Li, L.1    Du, Y.2    Kong, X.3    Li, Z.4    Jia, Z.5    Cui, J.6    Gao, J.7    Wang, L.8    Xie, K.9
  • 232
    • 34247364137 scopus 로고    scopus 로고
    • Enhanced expression of the nuclear envelope LAP2 transcriptional repressors in normal and malignant activated lymphocytes
    • doi: 10.1007/s00277-007-0275-9
    • Somech R, Gal-Yam EN, Shaklai S, Geller O, Amariglio N, Rechavi G, Simon AJ (2007) Enhanced expression of the nuclear envelope LAP2 transcriptional repressors in normal and malignant activated lymphocytes. Ann Hematol 86(6):393-401. doi: 10.1007/s00277-007-0275-9
    • (2007) Ann Hematol , vol.86 , Issue.6 , pp. 393-401
    • Somech, R.1    Gal-Yam, E.N.2    Shaklai, S.3    Geller, O.4    Amariglio, N.5    Rechavi, G.6    Simon, A.J.7
  • 233
    • 0345580750 scopus 로고    scopus 로고
    • The nuclear pore complex protein Nup88 is overexpressed in tumor cells
    • Martínez N, Alonso A, Moragues MD, Pontón J, Schneider J (1999) The nuclear pore complex protein Nup88 is overexpressed in tumor cells. Cancer Res 59(21):5408-5411
    • (1999) Cancer Res , vol.59 , Issue.21 , pp. 5408-5411
    • Martínez, N.1    Alonso, A.2    Moragues, M.D.3    Pontón, J.4    Schneider, J.5
  • 235
    • 70249132113 scopus 로고    scopus 로고
    • Nucleoporin 88 expression in normal and neoplastic squamous epithelia of the uterine cervix
    • doi: 10.1016/j. anndiagpath.2009.05.005
    • Brustmann H, Hager M (2009) Nucleoporin 88 expression in normal and neoplastic squamous epithelia of the uterine cervix. Ann Diagn Pathol 13(5):303-307. doi: 10.1016/j. anndiagpath.2009.05.005
    • (2009) Ann Diagn Pathol , vol.13 , Issue.5 , pp. 303-307
    • Brustmann, H.1    Hager, M.2
  • 237
    • 0036301249 scopus 로고    scopus 로고
    • Nup88 (karyoporin) in human malignant neoplasms and dysplasias: Correlations of immunostaining of tissue sections, cytologic smears, and immunoblot analysis
    • Gould VE, Orucevic A, Zentgraf H, Gattuso P, Martinez N, Alonso A (2002) Nup88 (karyoporin) in human malignant neoplasms and dysplasias: correlations of immunostaining of tissue sections, cytologic smears, and immunoblot analysis. Hum Pathol 33(5):536-544
    • (2002) Hum Pathol , vol.33 , Issue.5 , pp. 536-544
    • Gould, V.E.1    Orucevic, A.2    Zentgraf, H.3    Gattuso, P.4    Martinez, N.5    Alonso, A.6
  • 239
    • 33847326741 scopus 로고    scopus 로고
    • Nup88 expression in normal mucosa, adenoma, primary adenocarcinoma and lymph node metastasis in the colorectum
    • doi: 10.1159/000099154
    • Zhang ZY, Zhao ZR, Jiang L, Li JC, Gao YM, Cui DS, Wang CJ, Schneider J, Wang MW, Sun XF (2007) Nup88 expression in normal mucosa, adenoma, primary adenocarcinoma and lymph node metastasis in the colorectum. Tumour Biol 28(2):93-99. doi: 10.1159/000099154
    • (2007) Tumour Biol , vol.28 , Issue.2 , pp. 93-99
    • Zhang, Z.Y.1    Zhao, Z.R.2    Jiang, L.3    Li, J.C.4    Gao, Y.M.5    Cui, D.S.6    Wang, C.J.7    Schneider, J.8    Wang, M.W.9    Sun, X.F.10
  • 240
    • 67649435612 scopus 로고    scopus 로고
    • Nuclear pore proteins and cancer
    • doi: 10.1016/j.semcdb.2009.03.003
    • Xu S, Powers MA (2009) Nuclear pore proteins and cancer. Semin Cell Dev Biol 20(5): 620-630. doi: 10.1016/j.semcdb.2009.03.003
    • (2009) Semin Cell Dev Biol , vol.20 , Issue.5 , pp. 620-630
    • Xu, S.1    Powers, M.A.2
  • 241
    • 0037067661 scopus 로고    scopus 로고
    • The oncoprotein Set/TAF-1beta, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing
    • doi: 10.1074/jbc.M202256200
    • Cervoni N, Detich N, Seo SB, Chakravarti D, Szyf M (2002) The oncoprotein Set/TAF-1beta, an inhibitor of histone acetyltransferase, inhibits active demethylation of DNA, integrating DNA methylation and transcriptional silencing. J Biol Chem 277(28):25026-25031. doi: 10.1074/jbc.M202256200
    • (2002) J Biol Chem , vol.277 , Issue.28 , pp. 25026-25031
    • Cervoni, N.1    Detich, N.2    Seo, S.B.3    Chakravarti, D.4    Szyf, M.5
  • 243
    • 79959304638 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity in breast cancer
    • Jun
    • Capo-chichi CD, Cai KQ, Smedberg J, Ganjei-Azar P, Godwin AK, Xu XX. Loss of A-type lamin expression compromises nuclear envelope integrity in breast cancer. Chin J Cancer. 2011 Jun;30(6):415-425. http://www.ncbi.nlm.nih.gov/ pubmed/21627864
    • (2011) Chin J Cancer , vol.30 , Issue.6 , pp. 415-415
    • Capo-Chichi, C.D.1    Cai, K.Q.2    Smedberg, J.3    Ganjei-Azar, P.4    Godwin, A.K.5    Xu, X.X.6
  • 244
    • 84891346537 scopus 로고    scopus 로고
    • The clinicopathological signifi cance of lamin A/C, lamin B1 and lamin B receptor mRNA expression in human breast cancer
    • Dec doi: 10.2478/s11658-013-0109-9. Epub 2013 Nov 30.
    • Wazir U, Ahmed MH, Bridger JM, Harvey A, Jiang WG, Sharma AK, Mokbel K. The clinicopathological signifi cance of lamin A/C, lamin B1 and lamin B receptor mRNA expression in human breast cancer. Cell Mol Biol Lett. 2013 Dec;18(4):595-611. doi: 10.2478/s11658-013-0109-9. Epub 2013 Nov 30. http://www.ncbi.nlm.nih.gov/pubmed/24293108
    • (2013) Cell Mol Biol Lett , vol.18 , Issue.4 , pp. 595-611
    • Wazir, U.1    Ahmed, M.H.2    Bridger, J.M.3    Harvey, A.4    Jiang, W.G.5    Sharma, A.K.6    Mokbel, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.