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Volumn 17, Issue 7, 2011, Pages 2566-2593

Xin proteins and intercalated disc maturation, signaling and diseases

Author keywords

Cardiomyopathy with conduction defects; Intercalated disc formation; Postnatal lethality; Review; Severe growth retardation; Xin repeats

Indexed keywords

MAMMALIA; MUS;

EID: 84860284298     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/4072     Document Type: Article
Times cited : (38)

References (213)
  • 1
    • 0022410203 scopus 로고
    • Intercalated discs of mammalian heart: A review of structure and function
    • DOI 10.1016/0040-8166(85)90001-1
    • M.S. Forbes and N. Sperelakis: Intercalated discs of mammalian heart: a review of structure and function. Tissue Cell, 17, 605-48 (1985) (Pubitemid 16243839)
    • (1985) Tissue and Cell , vol.17 , Issue.5 , pp. 605-648
    • Forbes, M.S.1    Sperelakis, N.2
  • 2
    • 0025159130 scopus 로고
    • The cardiac gap junction and intercalated disc
    • DOI 10.1016/0167-5273(90)90030-9
    • N.J. Severs: The cardiac gap junction and intercalated disc. Int J Cardiol, 26, 137-73 (1990) (Pubitemid 20035665)
    • (1990) International Journal of Cardiology , vol.26 , Issue.2 , pp. 137-173
    • Severs, N.J.1
  • 3
    • 0037237653 scopus 로고    scopus 로고
    • Dilated cardiomyopathy: A disease of the intercalated disc?
    • DOI 10.1016/S1050-1738(02)00209-8, PII S1050173802002098
    • J.C. Perriard, A. Hirschy and E. Ehler: Dilated cardiomyopathy: a disease of the intercalated disc? Trends Cardiovasc Med, 13, 30-8 (2003) (Pubitemid 36120547)
    • (2003) Trends in Cardiovascular Medicine , vol.13 , Issue.1 , pp. 30-38
    • Perriard, J.-C.1    Hirschy, A.2    Ehler, E.3
  • 4
  • 5
    • 33745848407 scopus 로고    scopus 로고
    • Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy
    • DOI 10.1172/JCI27751
    • E. Garcia-Gras, R. Lombardi, M.J. Giocondo, J.T. Willerson, M.D. Schneider, D.S. Khoury and A.J. Marian: Suppression of canonical Wnt/beta-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy. J Clin Invest, 116, 2012-21 (2006) (Pubitemid 44033325)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.7 , pp. 2012-2021
    • Garcia-Gras, E.1    Lombardi, R.2    Giocondo, M.J.3    Willerson, J.T.4    Schneider, M.D.5    Khoury, D.S.6    Marian, A.J.7
  • 6
    • 33646107862 scopus 로고    scopus 로고
    • Dysregulation of cell adhesion proteins and cardiac arrhythmogenesis
    • J. Li, V.V. Patel and G.L. Radice: Dysregulation of cell adhesion proteins and cardiac arrhythmogenesis. Clin Med Res, 4, 42-52 (2006)
    • (2006) Clin Med Res , vol.4 , pp. 42-52
    • Li, J.1    Patel, V.V.2    Radice, G.L.3
  • 8
    • 34848821656 scopus 로고    scopus 로고
    • Molecular crosstalk between mechanical and electrical junctions at the intercalated disc
    • DOI 10.1161/CIRCRESAHA.107.161901, PII 0000301220070928000001
    • S. Rohr: Molecular crosstalk between mechanical and electrical junctions at the intercalated disc. Circ Res, 101, 637-9 (2007) (Pubitemid 47494090)
    • (2007) Circulation Research , vol.101 , Issue.7 , pp. 637-639
    • Rohr, S.1
  • 9
    • 77649100539 scopus 로고    scopus 로고
    • Cell-cell connection to cardiac disease
    • F. Sheikh, R.S. Ross and J. Chen: Cell-cell connection to cardiac disease. Trends Cardiovasc Med, 19, 182-90 (2009)
    • (2009) Trends Cardiovasc Med , vol.19 , pp. 182-190
    • Sheikh, F.1    Ross, R.S.2    Chen, J.3
  • 10
    • 51749110724 scopus 로고    scopus 로고
    • Remodelling of gap junctions and connexin expression in diseased myocardium
    • N.J. Severs, A.F. Bruce, E. Dupont and S. Rothery: Remodelling of gap junctions and connexin expression in diseased myocardium. Cardiovasc Res, 80, 9-19 (2008)
    • (2008) Cardiovasc Res , vol.80 , pp. 9-19
    • Severs, N.J.1    Bruce, A.F.2    Dupont, E.3    Rothery, S.4
  • 11
    • 84862755022 scopus 로고    scopus 로고
    • A new perspective on intercalated disc organization: Implications for heart disease
    • J. Li and G.L. Radice: A new perspective on intercalated disc organization: implications for heart disease. Dermatol Res Pract, 2010, 207835 (2010)
    • (2010) Dermatol Res Pract , vol.2010 , pp. 207835
    • Li, J.1    Radice, G.L.2
  • 13
    • 33745425651 scopus 로고    scopus 로고
    • The transitional junction: A new functional subcellular domain at the intercalated disc
    • DOI 10.1091/mbc.E05-12-1109
    • P.M. Bennett, A.M. Maggs, A.J. Baines and J.C. Pinder: The transitional junction: a new functional subcellular domain at the intercalated disc. Mol Biol Cell, 17, 2091-100 (2006) (Pubitemid 44011621)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 2091-2100
    • Bennett, P.M.1    Maggs, A.M.2    Baines, A.J.3    Pinder, J.C.4
  • 14
    • 0004998252 scopus 로고    scopus 로고
    • Differential displaying of mRNAs from the atrioventricular region of developing chicken hearts at stages 15 and 21
    • D.Z. Wang, X. Hu, J.L. Lin, G.T. Kitten, M. Solursh and J.J. Lin: Differential displaying of mRNAs from the atrioventricular region of developing chicken hearts at stages 15 and 21. Front Biosci, 1, a1-15 (1996)
    • (1996) Front Biosci , vol.1
    • Wang, D.Z.1    Hu, X.2    Lin, J.L.3    Kitten, G.T.4    Solursh, M.5    Lin, J.J.6
  • 16
    • 51349101183 scopus 로고    scopus 로고
    • Emergence of Xin demarcates a key innovation in heart evolution
    • S.E. Grosskurth, D. Bhattacharya, Q. Wang and J.J. Lin: Emergence of Xin demarcates a key innovation in heart evolution. PLoS ONE, 3, e2857 (2008)
    • (2008) PLoS ONE , vol.3
    • Grosskurth, S.E.1    Bhattacharya, D.2    Wang, Q.3    Lin, J.J.4
  • 19
    • 31344461886 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. I. Molecular definition in intercalated disks of cardiomyocytes by immunoelectron microscopy of desmosomal proteins
    • DOI 10.1016/j.ejcb.2005.11.003, PII S0171933505001962
    • W.W. Franke, C.M. Borrmann, C. Grund and S. Pieperhoff: The area composita of adhering junctions connecting heart muscle cells of vertebrates. I. Molecular definition in intercalated disks of cardiomyocytes by immunoelectron microscopy of desmosomal proteins. Eur J Cell Biol, 85, 69-82 (2006) (Pubitemid 43137112)
    • (2006) European Journal of Cell Biology , vol.85 , Issue.2 , pp. 69-82
    • Franke, W.W.1    Borrmann, C.M.2    Grund, C.3    Pieperhoff, S.4
  • 20
    • 33646555794 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. II. Colocalizations of desmosomal and fascia adhaerens molecules in the intercalated disk
    • C.M. Borrmann, C. Grund, C. Kuhn, I. Hofmann, S. Pieperhoff and W.W. Franke: The area composita of adhering junctions connecting heart muscle cells of vertebrates. II. Colocalizations of desmosomal and fascia adhaerens molecules in the intercalated disk. Eur J Cell Biol, 85, 469-85 (2006)
    • (2006) Eur J Cell Biol , vol.85 , pp. 469-485
    • Borrmann, C.M.1    Grund, C.2    Kuhn, C.3    Hofmann, I.4    Pieperhoff, S.5    Franke, W.W.6
  • 21
    • 34250811969 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates - IV: Coalescence and amalgamation of desmosomal and adhaerens junction components - Late processes in mammalian heart development
    • DOI 10.1016/j.ejcb.2007.04.001, PII S017193350700057X
    • S. Pieperhoff and W.W. Franke: The area composita of adhering junctions connecting heart muscle cells of vertebrates -IV: coalescence and amalgamation of desmosomal and adhaerens junction components -late processes in mammalian heart development. Eur J Cell Biol, 86, 377-91 (2007) (Pubitemid 46971921)
    • (2007) European Journal of Cell Biology , vol.86 , Issue.7 , pp. 377-391
    • Pieperhoff, S.1    Franke, W.W.2
  • 22
    • 47049103046 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. VI. Different precursor structures in nonmammalian species
    • S. Pieperhoff and W.W. Franke: The area composita of adhering junctions connecting heart muscle cells of vertebrates. VI. Different precursor structures in nonmammalian species. Eur J Cell Biol, 87, 413-30 (2008)
    • (2008) Eur J Cell Biol , vol.87 , pp. 413-430
    • Pieperhoff, S.1    Franke, W.W.2
  • 23
    • 68349128540 scopus 로고    scopus 로고
    • The junctions that don't fit the scheme: Special symmetrical cell-cell junctions of their own kind
    • W.W. Franke, S. Rickelt, M. Barth and S. Pieperhoff: The junctions that don't fit the scheme: special symmetrical cell-cell junctions of their own kind. Cell Tissue Res, 338, 1-17 (2009)
    • (2009) Cell Tissue Res , vol.338 , pp. 1-17
    • Franke, W.W.1    Rickelt, S.2    Barth, M.3    Pieperhoff, S.4
  • 27
    • 33748486911 scopus 로고    scopus 로고
    • α-E-catenin inactivation disrupts the cardiomyocyte adherens junction, resulting in cardiomyopathy and susceptibility to wall rupture
    • DOI 10.1161/CIRCULATIONAHA.106.634469, PII 0000301720060905000011
    • F. Sheikh, Y. Chen, X. Liang, A. Hirschy, A.E. Stenbit, Y. Gu, N.D. Dalton, T. Yajima, Y. Lu, K.U. Knowlton, K.L. Peterson, J.C. Perriard and J. Chen: alpha-E-catenin inactivation disrupts the cardiomyocyte adherens junction, resulting in cardiomyopathy and susceptibility to wall rupture. Circulation, 114, 1046-55 (2006) (Pubitemid 44358881)
    • (2006) Circulation , vol.114 , Issue.10 , pp. 1046-1055
    • Sheikh, F.1    Chen, Y.2    Liang, X.3    Hirschy, A.4    Stenbit, A.E.5    Gu, Y.6    Dalton, N.D.7    Yajima, T.8    Lu, Y.9    Knowlton, K.U.10    Peterson, K.L.11    Perriard, J.-C.12    Chen, J.13
  • 29
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • DOI 10.1016/j.yexcr.2007.03.039, PII S0014482707001097
    • A. Sonnenberg and R.K. Liem: Plakins in development and disease. Exp Cell Res, 313, 2189-203 (2007) (Pubitemid 46842974)
    • (2007) Experimental Cell Research , vol.313 , Issue.10 , pp. 2189-2203
    • Sonnenberg, A.1    Liem, R.K.H.2
  • 30
    • 20644437528 scopus 로고    scopus 로고
    • Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage
    • DOI 10.1083/jcb.143.7.2009
    • G.I. Gallicano, P. Kouklis, C. Bauer, M. Yin, V. Vasioukhin, L. Degenstein and E. Fuchs: Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage. J Cell Biol, 143, 2009-22 (1998) (Pubitemid 29022620)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 2009-2022
    • Ian Gallicano, G.1    Kouklis, P.2    Bauer, C.3    Yin, M.4    Vasioukhin, V.5    Degenstein, L.6    Fuchs, E.7
  • 32
    • 77957267604 scopus 로고    scopus 로고
    • The cardiac desmosome and arrhythmogenic cardiomyopathies: From gene to disease
    • M. Delmar and W.J. McKenna: The cardiac desmosome and arrhythmogenic cardiomyopathies: from gene to disease. Circ Res, 107, 700-14 (2010)
    • (2010) Circ Res , vol.107 , pp. 700-714
    • Delmar, M.1    McKenna, W.J.2
  • 36
    • 77449145091 scopus 로고    scopus 로고
    • Abnormal connexin43 in arrhythmogenic right ventricular cardiomyopathy caused by plakophilin-2 mutations
    • L.M. Fidler, G.J. Wilson, F. Liu, X. Cui, S.W. Scherer, G.P. Taylor and R.M. Hamilton: Abnormal connexin43 in arrhythmogenic right ventricular cardiomyopathy caused by plakophilin-2 mutations. J Cell Mol Med, 13, 4219-28 (2009)
    • (2009) J Cell Mol Med , vol.13 , pp. 4219-4228
    • Fidler, L.M.1    Wilson, G.J.2    Liu, F.3    Cui, X.4    Scherer, S.W.5    Taylor, G.P.6    Hamilton, R.M.7
  • 37
    • 39749165131 scopus 로고    scopus 로고
    • Gap junction remodelling in human heart failure is associated with increased interaction of connexin43 with ZO-1
    • DOI 10.1093/cvr/cvm083
    • A.F. Bruce, S. Rothery, E. Dupont and N.J. Severs: Gap junction remodelling in human heart failure is associated with increased interaction of connexin43 with ZO-1. Cardiovasc Res, 77, 757-65 (2008) (Pubitemid 351301863)
    • (2008) Cardiovascular Research , vol.77 , Issue.4 , pp. 757-765
    • Bruce, A.F.1    Rothery, S.2    Dupont, E.3    Severs, N.J.4
  • 39
    • 0025941699 scopus 로고
    • Altered patterns of gap junction distribution in ischemic heart disease. An immunohistochemical study of human myocardium using laser scanning confocal microscopy
    • J.H. Smith, C.R. Green, N.S. Peters, S. Rothery and N.J. Severs: Altered patterns of gap junction distribution in ischemic heart disease. An immunohistochemical study of human myocardium using laser scanning confocal microscopy. Am J Pathol, 139, 801-21 (1991)
    • (1991) Am J Pathol , vol.139 , pp. 801-821
    • Smith, J.H.1    Green, C.R.2    Peters, N.S.3    Rothery, S.4    Severs, N.J.5
  • 42
    • 1942534677 scopus 로고    scopus 로고
    • Connexin 43 expression and distribution in compensated and decompensated cardiac hypertrophy in patients with aortic stenosis
    • DOI 10.1016/j.cardiores.2003.12.010, PII S0008636303007788
    • S. Kostin, S. Dammer, S. Hein, W.P. Klovekorn, E.P. Bauer and J. Schaper: Connexin 43 expression and distribution in compensated and decompensated cardiac hypertrophy in patients with aortic stenosis. Cardiovasc Res, 62, 426-36 (2004) (Pubitemid 38496555)
    • (2004) Cardiovascular Research , vol.62 , Issue.2 , pp. 426-436
    • Kostin, S.1    Dammer, S.2    Hein, S.3    Klovekorn, W.P.4    Bauer, E.P.5    Schaper, J.6
  • 45
    • 0022993985 scopus 로고
    • Plakoglobin: A protein common to different kinds of intercellular adhering junctions
    • P. Cowin, H.P. Kapprell, W.W. Franke, J. Tamkun and R.O. Hynes: Plakoglobin: a protein common to different kinds of intercellular adhering junctions. Cell, 46, 1063-73 (1986) (Pubitemid 17182730)
    • (1986) Cell , vol.46 , Issue.7 , pp. 1063-1073
    • Cowin, P.1    Kapprell, H.-P.2    Franke, W.W.3
  • 46
    • 0030589631 scopus 로고    scopus 로고
    • Embryonic heart and skin defects in mice lacking plakoglobin
    • DOI 10.1006/dbio.1996.0346
    • C. Bierkamp, K.J. McLaughlin, H. Schwarz, O. Huber and R. Kemler: Embryonic heart and skin defects in mice lacking plakoglobin. Dev Biol, 180, 780-5 (1996) (Pubitemid 27037381)
    • (1996) Developmental Biology , vol.180 , Issue.2 , pp. 780-785
    • Bierkamp, C.1    McLaughlin, K.J.2    Schwarz, H.3    Huber, O.4    Kemler, R.5
  • 49
    • 0033788835 scopus 로고    scopus 로고
    • Plakoglobin and beta-catenin: Protein interactions, regulation and biological roles
    • J. Zhurinsky, M. Shtutman and A. Ben-Ze'ev: Plakoglobin and beta-catenin: protein interactions, regulation and biological roles. J Cell Sci, 113 ( Pt 18), 3127-39 (2000)
    • (2000) J Cell Sci , vol.113 , Issue.PART 18 , pp. 3127-3139
    • Zhurinsky, J.1    Shtutman, M.2    Ben-Ze'ev, A.3
  • 50
    • 0034036739 scopus 로고    scopus 로고
    • Differential mechanisms of LEF/TCF family-dependent transcriptional activation by β-catenin and plakoglobin
    • DOI 10.1128/MCB.20.12.4238-4252.2000
    • J. Zhurinsky, M. Shtutman and A. Ben-Ze'ev: Differential mechanisms of LEF/TCF family-dependent transcriptional activation by beta-catenin and plakoglobin. Mol Cell Biol, 20, 4238-52 (2000) (Pubitemid 30346619)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.12 , pp. 4238-4252
    • Zhurinsky, J.1    Shtutman, M.2    Ben-Ze'ev, A.3
  • 52
    • 79952268278 scopus 로고    scopus 로고
    • Cardiac-restricted deletion of plakoglobin results in progressive cardiomyopathy and activation of {beta}-catenin signaling
    • J. Li, D. Swope, N. Raess, L. Cheng, E.J. Muller and G.L. Radice: Cardiac-restricted deletion of plakoglobin results in progressive cardiomyopathy and activation of {beta}-catenin signaling. Mol Cell Biol, 31, 1134-44 (2011)
    • (2011) Mol Cell Biol , vol.31 , pp. 1134-1144
    • Li, J.1    Swope, D.2    Raess, N.3    Cheng, L.4    Muller, E.J.5    Radice, G.L.6
  • 53
    • 66149101609 scopus 로고    scopus 로고
    • Genetic fate mapping identifies second heart field progenitor cells as a source of adipocytes in arrhythmogenic right ventricular cardiomyopathy
    • R. Lombardi, J. Dong, G. Rodriguez, A. Bell, T.K. Leung, R.J. Schwartz, J.T. Willerson, R. Brugada and A.J. Marian: Genetic fate mapping identifies second heart field progenitor cells as a source of adipocytes in arrhythmogenic right ventricular cardiomyopathy. Circ Res, 104, 1076-84 (2009)
    • (2009) Circ Res , vol.104 , pp. 1076-1084
    • Lombardi, R.1    Dong, J.2    Rodriguez, G.3    Bell, A.4    Leung, T.K.5    Schwartz, R.J.6    Willerson, J.T.7    Brugada, R.8    Marian, A.J.9
  • 54
    • 0034679297 scopus 로고    scopus 로고
    • Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease)
    • G. McKoy, N. Protonotarios, A. Crosby, A. Tsatsopoulou, A. Anastasakis, A. Coonar, M. Norman, C. Baboonian, S. Jeffery and W.J. McKenna: Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet, 355, 2119-24 (2000) (Pubitemid 30364661)
    • (2000) Lancet , vol.355 , Issue.9221 , pp. 2119-2124
    • McKoy, G.1    Protonotarios, N.2    Crosby, A.3    Tsatsopoulou, A.4    Anastasakis, A.5    Coonar, A.6    Norman, M.7    Baboonian, C.8    Jeffery, S.9    McKenna, W.J.10
  • 58
    • 44449156929 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates. V. The importance of plakophilin-2 demonstrated by small interference RNAmediated knockdown in cultured rat cardiomyocytes
    • S. Pieperhoff, H. Schumacher and W.W. Franke: The area composita of adhering junctions connecting heart muscle cells of vertebrates. V. The importance of plakophilin-2 demonstrated by small interference RNAmediated knockdown in cultured rat cardiomyocytes. Eur J Cell Biol, 87, 399-411 (2008)
    • (2008) Eur J Cell Biol , vol.87 , pp. 399-411
    • Pieperhoff, S.1    Schumacher, H.2    Franke, W.W.3
  • 59
    • 34848820956 scopus 로고    scopus 로고
    • Connexin43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells
    • DOI 10.1161/CIRCRESAHA.107.154252, PII 0000301220070928000012
    • E.M. Oxford, H. Musa, K. Maass, W. Coombs, S.M. Taffet and M. Delmar: Connexin43 remodeling caused by inhibition of plakophilin-2 expression in cardiac cells. Circ Res, 101, 703-11 (2007) (Pubitemid 47494101)
    • (2007) Circulation Research , vol.101 , Issue.7 , pp. 703-711
    • Oxford, E.M.1    Musa, H.2    Maass, K.3    Coombs, W.4    Taffet, S.M.5    Delmar, M.6
  • 60
    • 0029825414 scopus 로고    scopus 로고
    • Plakophilins 2a and 2b: Constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
    • C. Mertens, C. Kuhn and W.W. Franke: Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. J Cell Biol, 135, 1009-25 (1996) (Pubitemid 26403775)
    • (1996) Journal of Cell Biology , vol.135 , Issue.4 , pp. 1009-1025
    • Mertens, C.1    Kuhn, C.2    Franke, W.W.3
  • 61
    • 0037155877 scopus 로고    scopus 로고
    • Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and β-catenin signaling
    • DOI 10.1074/jbc.M108765200
    • X. Chen, S. Bonne, M. Hatzfeld, F. van Roy and K.J. Green: Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta -catenin signaling. J Biol Chem, 277, 10512-22 (2002) (Pubitemid 34968174)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10512-10522
    • Chen, X.1    Bonne, S.2    Hatzfeld, M.3    Van Roy, F.4    Green, K.J.5
  • 62
    • 34347364710 scopus 로고    scopus 로고
    • A unique and specific interaction between αT-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs
    • DOI 10.1242/jcs.004713
    • S. Goossens, B. Janssens, S. Bonne, R. De Rycke, F. Braet, J. van Hengel and F. van Roy: A unique and specific interaction between alphaT-catenin and plakophilin-2 in the area composita, the mixed-type junctional structure of cardiac intercalated discs. J Cell Sci, 120, 2126-36 (2007) (Pubitemid 47010007)
    • (2007) Journal of Cell Science , vol.120 , Issue.12 , pp. 2126-2136
    • Goossens, S.1    Janssens, B.2    Bonne, S.3    De Rycke, R.4    Braet, F.5    Van Hengel, J.6    Van Roy, F.7
  • 65
    • 0037385290 scopus 로고    scopus 로고
    • Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains
    • DOI 10.1242/jcs.00275
    • M. Hatzfeld, K.J. Green and H. Sauter: Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains. J Cell Sci, 116, 1219-33 (2003) (Pubitemid 36410661)
    • (2003) Journal of Cell Science , vol.116 , Issue.7 , pp. 1219-1233
    • Hatzfeld, M.1    Green, K.J.2    Sauter, H.3
  • 67
    • 0029859086 scopus 로고    scopus 로고
    • Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: Evidence for a subfamily of closely related proteins
    • M. Hatzfeld and C. Nachtsheim: Cloning and characterization of a new armadillo family member, p0071, associated with the junctional plaque: evidence for a subfamily of closely related proteins. J Cell Sci, 109 ( Pt 11), 2767-78 (1996) (Pubitemid 26388361)
    • (1996) Journal of Cell Science , vol.109 , Issue.11 , pp. 2767-2778
    • Hatzfeld, M.1    Nachtsheim, C.2
  • 68
    • 14844340468 scopus 로고    scopus 로고
    • The p120 family of cell adhesion molecules
    • DOI 10.1016/j.ejcb.2004.12.016, PII S017193350400072X
    • M. Hatzfeld: The p120 family of cell adhesion molecules. Eur J Cell Biol, 84, 205-14 (2005) (Pubitemid 40353062)
    • (2005) European Journal of Cell Biology , vol.84 , Issue.2-3 , pp. 205-214
    • Hatzfeld, M.1
  • 69
    • 33846897476 scopus 로고    scopus 로고
    • Beyond regulation of cell adhesion: Local control of RhoA at the cleavage furrow by the p0071 catenin
    • R. Keil, A. Wolf, S. Huttelmaier and M. Hatzfeld: Beyond regulation of cell adhesion: local control of RhoA at the cleavage furrow by the p0071 catenin. Cell Cycle, 6, 122-7 (2007) (Pubitemid 46232487)
    • (2007) Cell Cycle , vol.6 , Issue.2 , pp. 122-127
    • Keil, R.1    Wolf, A.2    Huttelmaier, S.3    Hatzfeld, M.4
  • 70
    • 45249088344 scopus 로고    scopus 로고
    • 2+ medium in DJM-1 cells
    • DOI 10.1111/j.1346-8138.2008.00480.x
    • M. Kanno, Y. Aoyama, Y. Isa, Y. Yamamoto and Y. Kitajima: P120 catenin is associated with desmogleins when desmosomes are assembled in high-Ca2+ medium but not when disassembled in low-Ca2+ medium in DJM-1 cells. J Dermatol, 35, 317-24 (2008) (Pubitemid 351840233)
    • (2008) Journal of Dermatology , vol.35 , Issue.6 , pp. 317-324
    • Kanno, M.1    Aoyama, Y.2    Isa, Y.3    Yamamoto, Y.4    Kitajima, Y.5
  • 71
    • 42549173683 scopus 로고    scopus 로고
    • P120-catenin is a novel desmoglein 3 interacting partner: Identification of the p120-catenin association site of desmoglein 3
    • M. Kanno, Y. Isa, Y. Aoyama, Y. Yamamoto, M. Nagai, M. Ozawa and Y. Kitajima: P120-catenin is a novel desmoglein 3 interacting partner: identification of the p120-catenin association site of desmoglein 3. Exp Cell Res, 314, 1683-92 (2008)
    • (2008) Exp Cell Res , vol.314 , pp. 1683-1692
    • Kanno, M.1    Isa, Y.2    Aoyama, Y.3    Yamamoto, Y.4    Nagai, M.5    Ozawa, M.6    Kitajima, Y.7
  • 73
    • 0034618050 scopus 로고    scopus 로고
    • P120 catenin regulates the actin cytoskeleton via Rho family GTPases
    • N.K. Noren, B.P. Liu, K. Burridge and B. Kreft: p120 catenin regulates the actin cytoskeleton via Rho family GTPases. J Cell Biol, 150, 567-80 (2000)
    • (2000) J Cell Biol , vol.150 , pp. 567-580
    • Noren, N.K.1    Liu, B.P.2    Burridge, K.3    Kreft, B.4
  • 75
    • 56349123945 scopus 로고    scopus 로고
    • Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts
    • W. Meng, Y. Mushika, T. Ichii and M. Takeichi: Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts. Cell, 135, 948-59 (2008)
    • (2008) Cell , vol.135 , pp. 948-959
    • Meng, W.1    Mushika, Y.2    Ichii, T.3    Takeichi, M.4
  • 76
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (Zonula Occludens) in a variety of epithelia
    • DOI 10.1083/jcb.103.3.755
    • B.R. Stevenson, J.D. Siliciano, M.S. Mooseker and D.A. Goodenough: Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J Cell Biol, 103, 755-66 (1986) (Pubitemid 17177325)
    • (1986) Journal of Cell Biology , vol.103 , Issue.3 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3
  • 77
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • DOI 10.1161/hh0302.104471
    • R.J. Barker, R.L. Price and R.G. Gourdie: Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions. Circ Res, 90, 317-24 (2002) (Pubitemid 34638847)
    • (2002) Circulation Research , vol.90 , Issue.3 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 78
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • DOI 10.1074/jbc.273.21.12725
    • T. Toyofuku, M. Yabuki, K. Otsu, T. Kuzuya, M. Hori and M. Tada: Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J Biol Chem, 273, 12725-31 (1998) (Pubitemid 28246824)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.21 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Hori, M.5    Tada, M.6
  • 79
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to α catenin and actin filaments
    • DOI 10.1083/jcb.138.1.181
    • M. Itoh, A. Nagafuchi, S. Moroi and S. Tsukita: Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments. J Cell Biol, 138, 181-92 (1997) (Pubitemid 27337462)
    • (1997) Journal of Cell Biology , vol.138 , Issue.1 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 80
    • 1942503184 scopus 로고    scopus 로고
    • Gap junctions and connexin-interacting proteins
    • DOI 10.1016/j.cardiores.2003.12.009, PII S0008636303007776
    • B.N. Giepmans: Gap junctions and connexin-interacting proteins. Cardiovasc Res, 62, 233-45 (2004) (Pubitemid 38496537)
    • (2004) Cardiovascular Research , vol.62 , Issue.2 , pp. 233-245
    • Giepmans, B.N.G.1
  • 81
    • 13144252170 scopus 로고    scopus 로고
    • The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein
    • B.N. Giepmans and W.H. Moolenaar: The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein. Curr Biol, 8, 931-4 (1998) (Pubitemid 28371760)
    • (1998) Current Biology , vol.8 , Issue.16 , pp. 931-934
    • Giepmans, B.N.G.1    Moolenaar, W.H.2
  • 82
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule Plus-End-Tracking Proteins Target Gap Junctions Directly from the Cell Interior to Adherens Junctions
    • DOI 10.1016/j.cell.2006.12.037, PII S009286740700061X
    • R.M. Shaw, A.J. Fay, M.A. Puthenveedu, M. von Zastrow, Y.N. Jan and L.Y. Jan: Microtubule plus-endtracking proteins target gap junctions directly from the cell interior to adherens junctions. Cell, 128, 547-60 (2007) (Pubitemid 46198893)
    • (2007) Cell , vol.128 , Issue.3 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3    Von Zastrow, M.4    Jan, Y.-N.5    Jan, L.Y.6
  • 83
    • 21244490447 scopus 로고    scopus 로고
    • Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells
    • DOI 10.1074/jbc.M412921200
    • C.J. Wei, R. Francis, X. Xu and C.W. Lo: Connexin43 associated with an N-cadherin-containing multiprotein complex is required for gap junction formation in NIH3T3 cells. J Biol Chem, 280, 19925-36 (2005) (Pubitemid 41379521)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.20 , pp. 19925-19936
    • Wei, C.-J.1    Francis, R.2    Xu, X.3    Lo, C.W.4
  • 84
    • 0037371343 scopus 로고    scopus 로고
    • Role of catenins in the development of gap junctions in rat cardiomyocytes
    • J.C. Wu, R.Y. Tsai and T.H. Chung: Role of catenins in the development of gap junctions in rat cardiomyocytes. J Cell Biochem, 88, 823-35 (2003)
    • (2003) J Cell Biochem , vol.88 , pp. 823-835
    • Wu, J.C.1    Tsai, R.Y.2    Chung, T.H.3
  • 86
    • 28644434657 scopus 로고    scopus 로고
    • Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion
    • DOI 10.1091/mbc.E05-08-0737
    • A.W. Hunter, R.J. Barker, C. Zhu and R.G. Gourdie: Zonula occludens-1 alters connexin43 gap junction size and organization by influencing channel accretion. Mol Biol Cell, 16, 5686-98 (2005) (Pubitemid 41752218)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5686-5698
    • Hunter, A.W.1    Barker, R.J.2    Zhu, C.3    Gourdie, R.G.4
  • 87
    • 79955501784 scopus 로고    scopus 로고
    • Connexin 43 connexon to gap junction transition is regulated by zonula occludens-1
    • J.M. Rhett, J. Jourdan and R.G. Gourdie: Connexin 43 connexon to gap junction transition is regulated by zonula occludens-1. Mol Biol Cell, 22, 1516-28 (2011)
    • (2011) Mol Biol Cell , vol.22 , pp. 1516-1528
    • Rhett, J.M.1    Jourdan, J.2    Gourdie, R.G.3
  • 88
    • 37349087184 scopus 로고    scopus 로고
    • C-terminal truncation of connexin43 changes number, size, and localization of cardiac gap junction plaques
    • DOI 10.1161/CIRCRESAHA.107.162818, PII 0000301220071207000011
    • K. Maass, J. Shibayama, S.E. Chase, K. Willecke and M. Delmar: C-terminal truncation of connexin43 changes number, size, and localization of cardiac gap junction plaques. Circ Res, 101, 1283-91 (2007) (Pubitemid 350294645)
    • (2007) Circulation Research , vol.101 , Issue.12 , pp. 1283-1291
    • Maass, K.1    Shibayama, J.2    Chase, S.E.3    Willecke, K.4    Delmar, M.5
  • 89
  • 90
  • 91
    • 66149149492 scopus 로고    scopus 로고
    • Myofibril assembly visualized by imaging N-RAP, alpha-actinin, and actin in living cardiomyocytes
    • S.M. Manisastry, K.J. Zaal and R. Horowits: Myofibril assembly visualized by imaging N-RAP, alpha-actinin, and actin in living cardiomyocytes. Exp Cell Res, 315, 2126-39 (2009)
    • (2009) Exp Cell Res , vol.315 , pp. 2126-2139
    • Manisastry, S.M.1    Zaal, K.J.2    Horowits, R.3
  • 92
    • 0035846582 scopus 로고    scopus 로고
    • Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart
    • DOI 10.1021/bi0107445
    • J.Q. Zhang, B. Elzey, G. Williams, S. Lu, D.J. Law and R. Horowits: Ultrastructural and biochemical localization of NRAP at the interface between myofibrils and intercalated disks in the mouse heart. Biochemistry, 40, 14898-906 (2001) (Pubitemid 33136111)
    • (2001) Biochemistry , vol.40 , Issue.49 , pp. 14898-14906
    • Zhang, J.Q.1    Elzey, B.2    Williams, G.3    Lu, S.4    Law, D.J.5    Horowits, R.6
  • 94
    • 70349333829 scopus 로고    scopus 로고
    • Plakophilins: Multifunctional scaffolds for adhesion and signaling
    • A.E. Bass-Zubek, L.M. Godsel, M. Delmar and K.J. Green: Plakophilins: multifunctional scaffolds for adhesion and signaling. Curr Opin Cell Biol, 21, 708-16 (2009)
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 708-716
    • Bass-Zubek, A.E.1    Godsel, L.M.2    Delmar, M.3    Green, K.J.4
  • 95
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, β-Catenin, and Cadherin pathways
    • DOI 10.1126/science.1094291
    • W.J. Nelson and R. Nusse: Convergence of Wnt, β-catenin, and cadherin pathways. Science, 303, 1483-87 (2004) (Pubitemid 38314410)
    • (2004) Science , vol.303 , Issue.5663 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 96
    • 33750459738 scopus 로고    scopus 로고
    • Catenins: Keeping cells from getting their signals crossed
    • DOI 10.1016/j.devcel.2006.10.010, PII S153458070600462X
    • M. Perez-Moreno and E. Fuchs: Catenins: keeping cells from getting their signals crossed. Dev Cell, 11, 601-12 (2006) (Pubitemid 44644972)
    • (2006) Developmental Cell , vol.11 , Issue.5 , pp. 601-612
    • Perez-Moreno, M.1    Fuchs, E.2
  • 97
    • 35548943631 scopus 로고    scopus 로고
    • Catenins: playing both sides of the synapse
    • DOI 10.1016/j.ceb.2007.08.005, PII S0955067407001226, Cell to Cell Contact and Extracellular Matrix
    • A.V. Kwiatkowski, W.I. Weis and W.J. Nelson: Catenins: playing both sides of the synapse. Curr Opin Cell Biol, 19, 551-6 (2007) (Pubitemid 350016851)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 551-556
    • Kwiatkowski, A.V.1    Weis, W.I.2    Nelson, W.J.3
  • 98
    • 77950683362 scopus 로고    scopus 로고
    • Interplay of cadherinmediated cell adhesion and canonical Wnt signaling
    • J. Heuberger and W. Birchmeier: Interplay of cadherinmediated cell adhesion and canonical Wnt signaling. Cold Spring Harb Perspect Biol, 2, a002915 (2010)
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Heuberger, J.1    Birchmeier, W.2
  • 101
    • 0037089088 scopus 로고    scopus 로고
    • Remodeling the intercalated disc leads to cardiomyopathy in mice misexpressing cadherins in the heart
    • M.C. Ferreira-Cornwell, Y. Luo, N. Narula, J.M. Lenox, M. Lieberman and G.L. Radice: Remodeling the intercalated disc leads to cardiomyopathy in mice misexpressing cadherins in the heart. Journal of Cell Science, 115, 1623-34 (2002) (Pubitemid 34520592)
    • (2002) Journal of Cell Science , vol.115 , Issue.8 , pp. 1623-1634
    • Ferreira-Cornwell, M.C.1    Luo, Y.2    Narula, N.3    Lenox, J.M.4    Lieberman, M.5    Radice, G.L.6
  • 102
    • 14044256554 scopus 로고    scopus 로고
    • Induced deletion of the N-cadherin gene in the heart leads to dissolution of the intercalated disc structure
    • DOI 10.1161/01.RES.0000156274.72390.2c
    • I. Kostetskii, J. Li, Y. Xiong, R. Zhou, V.A. Ferrari, V.V. Patel, J.D. Molkentin and G.L. Radice: Induced deletion of the N-cadherin gene in the heart leads to dissolution of the intercalated disc structure. Circ Res, 96, 346-54 (2005) (Pubitemid 40279909)
    • (2005) Circulation Research , vol.96 , Issue.3 , pp. 346-354
    • Kostetskii, I.1    Li, J.2    Xiong, Y.3    Zhou, R.4    Ferrari, V.A.5    Patel, V.V.6    Molkentin, J.D.7    Radice, G.L.8
  • 104
    • 40649116404 scopus 로고    scopus 로고
    • N-cadherin haploinsufficiency affects cardiac gap junctions and arrhythmic susceptibility
    • J. Li, M.D. Levin, Y. Xiong, N. Petrenko, V.V. Patel and G.L. Radice: N-cadherin haploinsufficiency affects cardiac gap junctions and arrhythmic susceptibility. J Mol Cell Cardiol, 44, 597-606 (2008)
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 597-606
    • Li, J.1    Levin, M.D.2    Xiong, Y.3    Petrenko, N.4    Patel, V.V.5    Radice, G.L.6
  • 107
    • 77954333340 scopus 로고    scopus 로고
    • Cadherinmediated intercellular adhesion and signaling cascades involving small GTPases
    • T. Watanabe, K. Sato and K. Kaibuchi: Cadherinmediated intercellular adhesion and signaling cascades involving small GTPases. Cold Spring Harb Perspect Biol, 1, a003020 (2009)
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Watanabe, T.1    Sato, K.2    Kaibuchi, K.3
  • 108
    • 77953123743 scopus 로고    scopus 로고
    • Alpha-Catenin as a tension transducer that induces adherens junction development
    • S. Yonemura, Y. Wada, T. Watanabe, A. Nagafuchi and M. Shibata: alpha-Catenin as a tension transducer that induces adherens junction development. Nat Cell Biol, 12, 533-42 (2010)
    • (2010) Nat Cell Biol , vol.12 , pp. 533-542
    • Yonemura, S.1    Wada, Y.2    Watanabe, T.3    Nagafuchi, A.4    Shibata, M.5
  • 109
    • 77954410997 scopus 로고    scopus 로고
    • Vinculin potentiates Ecadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner
    • Q. le Duc, Q. Shi, I. Blonk, A. Sonnenberg, N. Wang, D. Leckband and J. de Rooij: Vinculin potentiates Ecadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J Cell Biol, 189, 1107-15 (2010)
    • (2010) J Cell Biol , vol.189 , pp. 1107-1115
    • Le Duc, Q.1    Shi, Q.2    Blonk, I.3    Sonnenberg, A.4    Wang, N.5    Leckband, D.6    De Rooij, J.7
  • 110
    • 77954414080 scopus 로고    scopus 로고
    • Neighborly relations: Cadherins and mechanotransduction
    • M. Smutny and A.S. Yap: Neighborly relations: cadherins and mechanotransduction. J Cell Biol, 189, 1075-7 (2010)
    • (2010) J Cell Biol , vol.189 , pp. 1075-1077
    • Smutny, M.1    Yap, A.S.2
  • 113
    • 0035252357 scopus 로고    scopus 로고
    • Inhibition of Wnt activity induces heart formation from posterior mesoderm
    • DOI 10.1101/gad.855501
    • M.J. Marvin, G. di Rocco, A. Gardiner, S.M. Bush and A.B. Lassar: Inhibition of Wnt activity induces heart formation from posterior mesoderm. Genes & Dev, 15, 316-27 (2001) (Pubitemid 32155147)
    • (2001) Genes and Development , vol.15 , Issue.3 , pp. 316-327
    • Marvin, M.J.1    Di Rocco, G.2    Gardiner, A.3    Bush, S.M.4    Lassar, A.B.5
  • 114
    • 0035252105 scopus 로고    scopus 로고
    • Wnt signals from the neural tube block ectopic cardiogenesis
    • DOI 10.1101/gad.871501
    • E. Tzahor and A.B. Lassar: Wnt signals from the neural tube block ectopic cardiogenesis. Genes & Dev, 15, 255-60 (2001) (Pubitemid 32155141)
    • (2001) Genes and Development , vol.15 , Issue.3 , pp. 255-260
    • Tzahor, E.1    Lassar, A.B.2
  • 116
    • 34447130140 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling promotes expansion of Isl-1-positive cardiac progenitor cells through regulation of FGF signaling
    • DOI 10.1172/JCI31731
    • E.D. Cohen, Z. Wang, J.J. Lepore, M.M. Lu, M.M. Taketo, D.J. Epstein and E.E. Morrisey: Wnt/beta-catenin signaling promotes expansion of Isl-1-positive cardiac progenitor cells through regulation of FGF signaling. J Clin Invest, 117, 1794-804 (2007) (Pubitemid 47036313)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.7 , pp. 1794-1804
    • Cohen, E.D.1    Wang, Z.2    Lepore, J.J.3    Min, M.L.4    Taketo, M.M.5    Epstein, D.J.6    Morrisey, E.E.7
  • 118
    • 33644680809 scopus 로고    scopus 로고
    • Building the mammalian heart from two sources of myocardial cells
    • M. Buckingham, S. Meilhac and S. Zaffran: Building the mammalian heart from two sources of myocardial cells. Nat Rev Genet, 6, 826-35 (2005)
    • (2005) Nat Rev Genet , vol.6 , pp. 826-835
    • Buckingham, M.1    Meilhac, S.2    Zaffran, S.3
  • 119
    • 33748621746 scopus 로고    scopus 로고
    • Making or breaking the heart: From lineage determination to morphogenesis
    • DOI 10.1016/j.cell.2006.09.003, PII S0092867406011500
    • D. Srivastava: Making or breaking the heart: from lineage determination to morphogenesis. Cell, 126, 1037-48 (2006) (Pubitemid 44380303)
    • (2006) Cell , vol.126 , Issue.6 , pp. 1037-1048
    • Srivastava, D.1
  • 121
    • 34548422439 scopus 로고    scopus 로고
    • Molecular scaffolds regulate bidirectional crosstalk between Wnt and classical seven-transmembrane-domain receptor signaling pathways
    • T. Force, K. Woulfe, W.J. Koch and R. Kerkela: Molecular scaffolds regulate bidirectional crosstalk between Wnt and classical seven-transmembrane- domain receptor signaling pathways. Sci STKE, 2007, pe41 (2007)
    • (2007) Sci STKE , vol.2007
    • Force, T.1    Woulfe, K.2    Koch, W.J.3    Kerkela, R.4
  • 122
    • 34548180135 scopus 로고    scopus 로고
    • Cardiac-specific haploinsufficiency of β-catenin attenuates cardiac hypertrophy but enhances fetal gene expression in response to aortic constriction
    • DOI 10.1016/j.yjmcc.2007.06.006, PII S0022282807010759
    • J. Qu, J. Zhou, X.P. Yi, B. Dong, H. Zheng, L.M. Miller, X. Wang, M.D. Schneider and F. Li: Cardiacspecific haploinsufficiency of beta-catenin attenuates cardiac hypertrophy but enhances fetal gene expression in response to aortic constriction. J Mol Cell Cardiol, 43, 319-26 (2007) (Pubitemid 47304446)
    • (2007) Journal of Molecular and Cellular Cardiology , vol.43 , Issue.3 , pp. 319-326
    • Qu, J.1    Zhou, J.2    Ping Yi, X.3    Dong, B.4    Zheng, H.5    Miller, L.M.6    Wang, X.7    Schneider, M.D.8    Li, F.9
  • 128
  • 129
    • 0037064055 scopus 로고    scopus 로고
    • Wnt signaling protects 3T3-L1 preadipocytes from apoptosis through induction of insulin-like growth factors
    • DOI 10.1074/jbc.M206402200
    • K.A. Longo, J.A. Kennell, M.J. Ochocinska, S.E. Ross, W.S. Wright and O.A. MacDougald: Wnt signaling protects 3T3-L1 preadipocytes from apoptosis through induction of insulin-like growth factors. J Biol Chem, 277, 38239-44 (2002) (Pubitemid 35154678)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38239-38244
    • Longo, K.A.1    Kennell, J.A.2    Ochocinska, M.J.3    Ross, S.E.4    Wright, W.S.5    MacDougald, O.A.6
  • 132
    • 0036945719 scopus 로고    scopus 로고
    • Localization of sodium channels in intercalated disks modulates cardiac conduction
    • DOI 10.1161/01.RES.0000046237.54156.0A
    • J.P. Kucera, S. Rohr and Y. Rudy: Localization of sodium channels in intercalated disks modulates cardiac conduction. Circ Res, 91, 1176-82 (2002) (Pubitemid 36076367)
    • (2002) Circulation Research , vol.91 , Issue.12 , pp. 1176-1182
    • Kucera, J.P.1    Rohr, S.2    Rudy, Y.3
  • 133
    • 1642370591 scopus 로고    scopus 로고
    • Distinct Subcellular Localization of Different Sodium Channel α and β Subunits in Single Ventricular Myocytes from Mouse Heart
    • DOI 10.1161/01.CIR.0000121421.61896.24
    • S.K. Maier, R.E. Westenbroek, K.A. McCormick, R. Curtis, T. Scheuer and W.A. Catterall: Distinct subcellular localization of different sodium channel alpha and beta subunits in single ventricular myocytes from mouse heart. Circulation, 109, 1421-7 (2004) (Pubitemid 38387830)
    • (2004) Circulation , vol.109 , Issue.11 , pp. 1421-1427
    • Maier, S.K.G.1    Westenbroek, R.E.2    McCormick, K.A.3    Curtis, R.4    Scheuer, T.5    Catterall, W.A.6
  • 136
    • 0030466763 scopus 로고    scopus 로고
    • Immunocytochemical localization of rh1 sodium channel in adult rat heart atria and ventricle: Presence in terminal intercalated disks
    • S.A. Cohen: Immunocytochemical localization of rH1 sodium channel in adult rat heart atria and ventricle. Presence in terminal intercalated disks. Circulation, 94, 3083-6 (1996) (Pubitemid 26427470)
    • (1996) Circulation , vol.94 , Issue.12 , pp. 3083-3086
    • Cohen, S.A.1
  • 137
    • 4644348991 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated and nonphosphorylated sodium channel β1 subunits are differentially localized in cardiac myocytes
    • DOI 10.1074/jbc.M407243200
    • J.D. Malhotra, V. Thyagarajan, C. Chen and L.L. Isom: Tyrosine-phosphorylated and nonphosphorylated sodium channel beta1 subunits are differentially localized in cardiac myocytes. J Biol Chem, 279, 40748-54 (2004) (Pubitemid 39287670)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40748-40754
    • Malhotra, J.D.1    Thyagarajan, V.2    Chen, C.3    Isom, L.L.4
  • 138
    • 22544486622 scopus 로고    scopus 로고
    • Sodium channels as macromolecular complexes: Implications for inherited arrhythmia syndromes
    • DOI 10.1016/j.cardiores.2005.04.003, PII S0008636305001781
    • L.S. Meadows and L.L. Isom: Sodium channels as macromolecular complexes: implications for inherited arrhythmia syndromes. Cardiovasc Res, 67, 448-58 (2005) (Pubitemid 41019552)
    • (2005) Cardiovascular Research , vol.67 , Issue.3 , pp. 448-458
    • Meadows, L.S.1    Isom, L.L.2
  • 139
    • 70349242035 scopus 로고    scopus 로고
    • Loss of plakophilin-2 expression leads to decreased sodium current and slower conduction velocity in cultured cardiac myocytes
    • P.Y. Sato, H. Musa, W. Coombs, G. Guerrero-Serna, G.A. Patino, S.M. Taffet, L.L. Isom and M. Delmar: Loss of plakophilin-2 expression leads to decreased sodium current and slower conduction velocity in cultured cardiac myocytes. Circ Res, 105, 523-6 (2009)
    • (2009) Circ Res , vol.105 , pp. 523-526
    • Sato, P.Y.1    Musa, H.2    Coombs, W.3    Guerrero-Serna, G.4    Patino, G.A.5    Taffet, S.M.6    Isom, L.L.7    Delmar, M.8
  • 142
    • 0029061401 scopus 로고
    • Molecular regulation of atrioventricular valvuloseptal morphogenesis
    • L.M. Eisenberg and R.R. Markwald: Molecular regulation of atrioventricular valvuloseptal morphogenesis. Circ Res, 77, 1-6 (1995)
    • (1995) Circ Res , vol.77 , pp. 1-6
    • Eisenberg, L.M.1    Markwald, R.R.2
  • 143
    • 77649129153 scopus 로고    scopus 로고
    • Developmental basis of adult cardiovascular diseases: Valvular heart diseases
    • R.R. Markwald, R.A. Norris, R. Moreno-Rodriguez and R.A. Levine: Developmental basis of adult cardiovascular diseases: valvular heart diseases. Ann N Y Acad Sci, 1188, 177-83 (2010)
    • (2010) Ann N y Acad Sci , vol.1188 , pp. 177-183
    • Markwald, R.R.1    Norris, R.A.2    Moreno-Rodriguez, R.3    Levine, R.A.4
  • 147
    • 33846017683 scopus 로고    scopus 로고
    • Myomaxin Is a novel transcriptional target of MEF2A that encodes a Xin-related α-actinin-interacting protein
    • DOI 10.1074/jbc.M603244200
    • H.T. Huang, O.M. Brand, M. Mathew, C. Ignatiou, E.P. Ewen, S.A. McCalmon and F.J. Naya: Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-related alpha-actinin-interacting protein. J Biol Chem, 281, 39370-9 (2006) (Pubitemid 46041896)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39370-39379
    • Huang, H.-T.1    Brand, O.M.2    Mathew, M.3    Ignatiou, C.4    Ewen, E.P.5    McCalmon, S.A.6    Naya, F.J.7
  • 148
    • 0036729618 scopus 로고    scopus 로고
    • Localization of the novel Xin protein to the adherens junction complex in cardiac and skeletal muscle during development
    • DOI 10.1002/dvdy.10131
    • H.W. Sinn, J. Balsamo, J. Lilien and J.J. Lin: Localization of the novel Xin protein to the adherens junction complex in cardiac and skeletal muscle during development. Dev Dyn, 225, 1-13 (2002) (Pubitemid 34983143)
    • (2002) Developmental Dynamics , vol.225 , Issue.1 , pp. 1-13
    • Sinn, H.W.1    Balsamo, J.2    Lilien, J.3    Lin, J.J.-C.4
  • 149
    • 33744941082 scopus 로고    scopus 로고
    • Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP
    • DOI 10.1016/j.yexcr.2006.03.015, PII S0014482706001108
    • P.F.M. van der Ven, E. Ehler, P. Vakeel, S. Eulitz, J.A. Schenk, H. Milting, B. Micheel and D.O. Furst: Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mens/VASP. Exp Cell Res, 312, 2154-67 (2006) (Pubitemid 43850938)
    • (2006) Experimental Cell Research , vol.312 , Issue.11 , pp. 2154-2167
    • Van Der Ven, P.F.M.1    Ehler, E.2    Vakeel, P.3    Eulitz, S.4    Schenk, J.A.5    Milting, H.6    Micheel, B.7    Furst, D.O.8
  • 150
    • 0028279115 scopus 로고
    • Mef2 gene expression marks the cardiac and skeletal muscle lineages during mouse embryogenesis
    • D.G. Edmondson, G.E. Lyons, J.F. Martin and E.N. Olson: Mef2 gene expression marks the cardiac and skeletal muscle lineages during mouse embryogenesis. Development, 120, 1251-63 (1994) (Pubitemid 24150050)
    • (1994) Development , vol.120 , Issue.5 , pp. 1251-1263
    • Edmondson, D.G.1    Lyons, G.E.2    Martin, J.F.3    Olson, E.N.4
  • 151
    • 0027700251 scopus 로고
    • Erratum: A novel murine homeobox gene expressed in early heart progenitor cells and their myogenic descendants (Development (1993) 119 (419-431))
    • T.J. Lints, L.M. Parsons, L. Hartley, I. Lyons and R.P. Harvey: Nkx-2.5: a novel murine homeobox gene expressed in early heart progenitor cells and their myogenic descendants. Development, 119, 969 (1993) (Pubitemid 23337435)
    • (1993) Development , vol.119 , Issue.3 , pp. 969
    • Lints, T.J.1    Parsons, L.M.2    Hartley, L.3    Lyons, I.4    Harvey, R.P.5
  • 152
    • 0029090829 scopus 로고
    • Myogenic and morphogenetic defects in the heart tubes of murine embryos lacking the homeo box gene Nkx2-5
    • I. Lyons, L.M. Parsons, L. Hartley, R. Li, J.E. Andrews, L. Robb and R.P. Harvey: Myogenic and morphogenetic defects in the heart tubes of murine embryos lacking the homeo box gene Nkx2-5. Genes Dev, 9, 1654-66 (1995)
    • (1995) Genes Dev , vol.9 , pp. 1654-1666
    • Lyons, I.1    Parsons, L.M.2    Hartley, L.3    Li, R.4    Andrews, J.E.5    Robb, L.6    Harvey, R.P.7
  • 153
    • 0030911475 scopus 로고    scopus 로고
    • Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C
    • DOI 10.1126/science.276.5317.1404
    • Q. Lin, J. Schwarz, C. Bucana and E.N. Olson: Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C. Science, 276, 1404-7 (1997) (Pubitemid 27235406)
    • (1997) Science , vol.276 , Issue.5317 , pp. 1404-1407
    • Lin, Q.1    Schwarz, J.2    Bucana, C.3    Olson, E.N.4
  • 155
    • 77952421832 scopus 로고
    • Ontogenetic implication of the myocardial ultrastructure in the development of mammalian heart
    • R. van Praagh and A. Takao (eds.), Futura Publishing Co., Mount Kisco, NY
    • R. Hirakow and T. Gotoh: Ontogenetic implication of the myocardial ultrastructure in the development of mammalian heart. In R. van Praagh and A. Takao (eds.), Etiology and morphogenesis of congenital heart disease, Futura Publishing Co., Mount Kisco, NY, (1980), pp. 99-108.
    • (1980) Etiology and Morphogenesis of Congenital Heart Disease , pp. 99-108
    • Hirakow, R.1    Gotoh, T.2
  • 157
    • 0034691296 scopus 로고    scopus 로고
    • Cardiac hypertrophy is not a required compensatory response to short- term pressure overload
    • J.A. Hill, M. Karimi, W. Kutschke, R.L. Davisson, K. Zimmerman, Z. Wang, R.E. Kerber and R.M. Weiss: Cardiac hypertrophy is not a required compensatory response to short-term pressure overload. Circulation, 101, 2863-9 (2000) (Pubitemid 30396019)
    • (2000) Circulation , vol.101 , Issue.24 , pp. 2863-2869
    • Hill, J.A.1    Karimi, M.2    Kutschke, W.3    Davisson, R.L.4    Zimmerman, K.5    Wang, Z.6    Kerber, R.E.7    Weiss, R.M.8
  • 160
    • 32944472418 scopus 로고    scopus 로고
    • A novel gene (Cmya3) induced in the heart by angiotensin II-dependent but not salt-dependent hypertension in mice
    • DOI 10.1016/j.amjhyper.2005.08.017, PII S0895706105011556
    • A. Duka, F. Schwartz, I. Duka, C. Johns, E. Melista, I. Gavras and H. Gavras: A novel gene (Cmya3) induced in the heart by angiotensin II-dependent but not saltdependent hypertension in mice. Am J Hypertens, 19, 275-81 (2006) (Pubitemid 43261508)
    • (2006) American Journal of Hypertension , vol.19 , Issue.3 , pp. 275-281
    • Duka, A.1    Schwartz, F.2    Duka, I.3    Johns, C.4    Melista, E.5    Gavras, I.6    Gavras, H.7
  • 161
    • 0003626442 scopus 로고
    • Version 1.D1, Department of Zoology, University of Oxford, Oxford, England
    • A. Rambaut. SE-AL sequence alignment program. Version 1.D1, Department of Zoology, University of Oxford, Oxford, England, 1995.
    • (1995) SE-AL Sequence Alignment Program
    • Rambaut, A.1
  • 162
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins and T.J. Gibson: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignments through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Research, 22, 4673-80 (1994) (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 163
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: Selection of best-fit models of protein evolution
    • DOI 10.1093/bioinformatics/bti263
    • F. Abascal, R. Zardoya and D. Posada: ProtTest: selection of best-fit models of protein evolution. Bioinformatics, 21, 2104-5 (2005) (Pubitemid 40668057)
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 164
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • DOI 10.1080/10635150390235520
    • S. Guindon and O. Gascuel: A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol, 52, 696-704 (2003) (Pubitemid 37365050)
    • (2003) Systematic Biology , vol.52 , Issue.5 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 165
    • 14644397888 scopus 로고    scopus 로고
    • RAxML-III: A fast program for maximum likelihood-based inference of large phylogenetic trees
    • DOI 10.1093/bioinformatics/bti191
    • A. Stamatakis, T. Ludwig and H. Meier: RAxML-III: a fast program for maximum likelihood-based inference of large phylogenetic trees. Bioinformatics, 21, 456-63 (2005) (Pubitemid 40310232)
    • (2005) Bioinformatics , vol.21 , Issue.4 , pp. 456-463
    • Stamatakis, A.1    Ludwig, T.2    Meier, H.3
  • 166
    • 0018344540 scopus 로고
    • Cellular mechanisms of normal growth in the mammalian heart. I. Qualitative and quantitative features of ventricular architecture in the dog from birth to five months of age
    • M.J. Legato: Cellular mechanisms of normal growth in the mammalian heart. I. Qualitative and quantitative features of ventricular architecture in the dog from birth to five months of age. Circ Res, 44, 250-62 (1979) (Pubitemid 9120521)
    • (1979) Circulation Research , vol.44 , Issue.2 , pp. 250-262
    • Legato, M.J.1
  • 167
    • 0031024666 scopus 로고    scopus 로고
    • Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium
    • B.D. Angst, L.U. Khan, N.J. Severs, K. Whitely, S. Rothery, R.P. Thompson, A.I. Magee and R.G. Gourdie: Dissociated spatial patterning of gap junctions and cell adhesion junctions during postnatal differentiation of ventricular myocardium. Circ Res, 80, 88-94 (1997) (Pubitemid 27030373)
    • (1997) Circulation Research , vol.80 , Issue.1 , pp. 88-94
    • Angst, B.D.1    Khan, L.U.R.2    Severs, N.J.3    Whitely, K.4    Rothery, S.5    Thompson, R.P.6    Magee, A.I.7    Gourdie, R.G.8
  • 168
    • 30044442758 scopus 로고    scopus 로고
    • Establishment of cardiac cytoarchitecture in the developing mouse heart
    • DOI 10.1016/j.ydbio.2005.10.046, PII S0012160605007839
    • A. Hirschy, F. Schatzmann, E. Ehler and J.C. Perriard: Establishment of cardiac cytoarchitecture in the developing mouse heart. Dev Biol, 289, 430-41 (2006) (Pubitemid 43049945)
    • (2006) Developmental Biology , vol.289 , Issue.2 , pp. 430-441
    • Hirschy, A.1    Schatzmann, F.2    Ehler, E.3    Perriard, J.-C.4
  • 169
    • 0028093157 scopus 로고
    • Spatiotemporal relation between gap junctions and fascia adherens junctions during postnatal development of human ventricular myocardium
    • N.S. Peters, N.J. Severs, S.M. Rothery, C. Lincoln, M.H. Yacoub and C.R. Green: Spatiotemporal relation between gap junctions and fascia adherens junctions during postnatal development of human ventricular myocardium. Circulation, 90, 713-25 (1994) (Pubitemid 24242737)
    • (1994) Circulation , vol.90 , Issue.2 , pp. 713-725
    • Peters, N.S.1    Severs, N.J.2    Rothery, S.M.3    Lincoln, C.4    Yacoub, M.H.5    Green, C.R.6
  • 170
    • 0032896831 scopus 로고    scopus 로고
    • In vitro reestablishment of cell-cell contacts in adult rat cardiomyocytes. Functional role of transmembrane components in the formation of new intercalated disk-like cell contacts
    • H.M. Eppenberger and C. Zuppinger: In vitro reestablishment of cell-cell contacts in adult rat cardiomyocytes. Functional role of transmembrane components in the formation of new intercalated disk-like cell contacts. Faseb J, 13 Suppl, S83-9 (1999)
    • (1999) Faseb J , vol.13 , Issue.SUPPL.
    • Eppenberger, H.M.1    Zuppinger, C.2
  • 171
    • 0030053566 scopus 로고    scopus 로고
    • N-cadherin in adult rat cardiomyocytes in culture II. Spatio-temporal appearance of proteins involved in cell-cell contact and communication. Formation of two distinct N-cadherin/catenin complexes
    • C.M. Hertig, S. Butz, S. Koch, M. Eppenberger-Eberhardt, R. Kemler and H.M. Eppenberger: N-cadherin in adult rat cardiomyocytes in culture. II. Spatio-temporal appearance of proteins involved in cell-cell contact and communication. Formation of two distinct Ncadherin/ catenin complexes. J Cell Sci, 109 ( Pt 1), 11-20 (1996) (Pubitemid 26037923)
    • (1996) Journal of Cell Science , vol.109 , Issue.1 , pp. 11-20
    • Hertig, C.M.1    Butz, S.2    Koch, S.3    Eppenberger-Eberhardt, M.4    Kemler, R.5    Eppenberger, H.M.6
  • 172
    • 0030029950 scopus 로고    scopus 로고
    • N-cadherin in adult rat cardiomyocytes in culture. I. Functional role of N-cadherin and impairment of cell-cell contact by a truncated N-cadherin mutant
    • C.M. Hertig, M. Eppenberger-Eberhardt, S. Koch and H.M. Eppenberger: N-cadherin in adult rat cardiomyocytes in culture. I. Functional role of N-cadherin and impairment of cell-cell contact by a truncated N-cadherin mutant. J Cell Sci, 109 ( Pt 1), 1-10 (1996) (Pubitemid 26037922)
    • (1996) Journal of Cell Science , vol.109 , Issue.1 , pp. 1-10
    • Hertig, C.M.1    Eppenberger-Eberhardt, M.2    Koch, S.3    Eppenberger, H.M.4
  • 173
    • 0032820709 scopus 로고    scopus 로고
    • Mobility and cytoskeletal interactions of cell adhesion receptors
    • DOI 10.1016/S0955-0674(99)00020-4
    • A. Kusumi, K. Suzuki and K. Koyasako: Mobility and cytoskeletal interactions of cell adhesion receptors. Curr Opin Cell Biol, 11, 582-90 (1999) (Pubitemid 29460399)
    • (1999) Current Opinion in Cell Biology , vol.11 , Issue.5 , pp. 582-590
    • Kusumi, A.1    Suzuki, K.2    Koyasako, K.3
  • 174
    • 0032482201 scopus 로고    scopus 로고
    • The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120(ctn)
    • DOI 10.1083/jcb.141.3.779
    • A.S. Yap, C.M. Niessen and B.M. Gumbiner: The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn. J Cell Biol, 141, 779-89 (1998) (Pubitemid 28217921)
    • (1998) Journal of Cell Biology , vol.141 , Issue.3 , pp. 779-789
    • Yap, A.S.1    Niessen, C.M.2    Gumbiner, B.M.3
  • 175
    • 77649263931 scopus 로고    scopus 로고
    • Spontaneous assembly and active disassembly balance adherens junction homeostasis
    • S. Hong, R.B. Troyanovsky and S.M. Troyanovsky: Spontaneous assembly and active disassembly balance adherens junction homeostasis. Proc Natl Acad Sci U S A, 107, 3528-33 (2010)
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3528-3533
    • Hong, S.1    Troyanovsky, R.B.2    Troyanovsky, S.M.3
  • 176
    • 35848939400 scopus 로고    scopus 로고
    • Stable and unstable cadherin dimers: Mechanisms of formation and roles in cell adhesion
    • DOI 10.1091/mbc.E07-01-0084
    • R.B. Troyanovsky, O. Laur and S.M. Troyanovsky: Stable and unstable cadherin dimers: mechanisms of formation and roles in cell adhesion. Mol Biol Cell, 18, 4343-52 (2007) (Pubitemid 350060163)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4343-4352
    • Troyanovsky, R.B.1    Laur, O.2    Troyanovsky, S.M.3
  • 177
    • 41949125038 scopus 로고    scopus 로고
    • Immediate-early signaling induced by E-cadherin engagement and adhesion
    • T.D. Perez, M. Tamada, M.P. Sheetz and W.J. Nelson: Immediate-early signaling induced by E-cadherin engagement and adhesion. J Biol Chem, 283, 5014-22 (2008)
    • (2008) J Biol Chem , vol.283 , pp. 5014-5022
    • Perez, T.D.1    Tamada, M.2    Sheetz, M.P.3    Nelson, W.J.4
  • 179
    • 66349095429 scopus 로고    scopus 로고
    • Endocytosis is required for E-cadherin redistribution at mature adherens junctions
    • S. de Beco, C. Gueudry, F. Amblard and S. Coscoy: Endocytosis is required for E-cadherin redistribution at mature adherens junctions. Proc Natl Acad Sci U S A, 106, 7010-5 (2009)
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7010-7015
    • De Beco, S.1    Gueudry, C.2    Amblard, F.3    Coscoy, S.4
  • 180
    • 28444457747 scopus 로고    scopus 로고
    • Hexagonal packing of Drosophila wing epithelial cells by the planar cell polarity pathway
    • DOI 10.1016/j.devcel.2005.10.016, PII S153458070500420X
    • A.K. Classen, K.I. Anderson, E. Marois and S. Eaton: Hexagonal packing of Drosophila wing epithelial cells by the planar cell polarity pathway. Dev Cell, 9, 805-17 (2005) (Pubitemid 41724108)
    • (2005) Developmental Cell , vol.9 , Issue.6 , pp. 805-817
    • Classen, A.-K.1    Anderson, K.I.2    Marois, E.3    Eaton, S.4
  • 181
    • 16344363943 scopus 로고    scopus 로고
    • Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin
    • DOI 10.1091/mbc.E04-10-0867
    • J.G. Lock and J.L. Stow: Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin. Mol Biol Cell, 16, 1744-55 (2005) (Pubitemid 40471945)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.4 , pp. 1744-1755
    • Lock, J.G.1    Stow, J.L.2
  • 183
    • 28344439885 scopus 로고    scopus 로고
    • α-catenin is a molecular switch that binds E-cadherin-β- catenin and regulates actin-filament assembly
    • DOI 10.1016/j.cell.2005.09.021, PII S009286740500975X
    • F. Drees, S. Pokutta, S. Yamada, W.J. Nelson and W.I. Weis: Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell, 123, 903-15 (2005) (Pubitemid 41721035)
    • (2005) Cell , vol.123 , Issue.5 , pp. 903-915
    • Drees, F.1    Pokutta, S.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 184
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • DOI 10.1016/j.cell.2005.09.020, PII S0092867405009748
    • S. Yamada, S. Pokutta, F. Drees, W.I. Weis and W.J. Nelson: Deconstructing the cadherin-catenin-actin complex. Cell, 123, 889-901 (2005) (Pubitemid 41721034)
    • (2005) Cell , vol.123 , Issue.5 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 185
    • 77952929975 scopus 로고    scopus 로고
    • Molecular bases of cell-cell junctions stability and dynamics
    • M. Cavey and T. Lecuit: Molecular bases of cell-cell junctions stability and dynamics. Cold Spring Harb Perspect Biol, 1, a002998 (2009)
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Cavey, M.1    Lecuit, T.2
  • 186
    • 44849115958 scopus 로고    scopus 로고
    • A two-tiered mechanism for stabilization and immobilization of E-cadherin
    • DOI 10.1038/nature06953, PII NATURE06953
    • M. Cavey, M. Rauzi, P.F. Lenne and T. Lecuit: A twotiered mechanism for stabilization and immobilization of Ecadherin. Nature, 453, 751-6 (2008) (Pubitemid 351793782)
    • (2008) Nature , vol.453 , Issue.7196 , pp. 751-756
    • Cavey, M.1    Rauzi, M.2    Lenne, P.-F.3    Lecuit, T.4
  • 187
    • 38349138921 scopus 로고    scopus 로고
    • EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt
    • K. Abe and M. Takeichi: EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt. Proc Natl Acad Sci U S A, 105, 13-9 (2008)
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 188
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • DOI 10.1083/jcb.200701058
    • S. Yamada and W.J. Nelson: Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J Cell Biol, 178, 517-27 (2007) (Pubitemid 47196158)
    • (2007) Journal of Cell Biology , vol.178 , Issue.3 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 189
    • 33846847701 scopus 로고    scopus 로고
    • Rap1: A key regulator in cell-cell junction formation
    • DOI 10.1242/jcs.03306
    • M.R. Kooistra, N. Dube and J.L. Bos: Rap1: a key regulator in cell-cell junction formation. J Cell Sci, 120, 17-22 (2007) (Pubitemid 46206645)
    • (2007) Journal of Cell Science , vol.120 , Issue.1 , pp. 17-22
    • Kooistra, M.R.H.1    Dube, N.2    Bos, J.L.3
  • 190
    • 63249115761 scopus 로고    scopus 로고
    • Cell-cell junction formation: The role of Rap1 and Rap1 guanine nucleotide exchange factors
    • W.J. Pannekoek, M.R. Kooistra, F.J. Zwartkruis and J.L. Bos: Cell-cell junction formation: the role of Rap1 and Rap1 guanine nucleotide exchange factors. Biochim Biophys Acta, 1788, 790-6 (2009)
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 790-796
    • Pannekoek, W.J.1    Kooistra, M.R.2    Zwartkruis, F.J.3    Bos, J.L.4
  • 191
    • 26244462666 scopus 로고    scopus 로고
    • Enhanced functional gap junction neoformation by protein kinase A-dependent and Epac-dependent signals downstream of cAMP in cardiac myocytes
    • DOI 10.1161/01.RES.0000183880.49270.f9
    • S. Somekawa, S. Fukuhara, Y. Nakaoka, H. Fujita, Y. Saito and N. Mochizuki: Enhanced functional gap junction neoformation by protein kinase A-dependent and Epacdependent signals downstream of cAMP in cardiac myocytes. Circ Res, 97, 655-62 (2005) (Pubitemid 41416334)
    • (2005) Circulation Research , vol.97 , Issue.7 , pp. 655-662
    • Somekawa, S.1    Fukuhara, S.2    Nakaoka, Y.3    Fujita, H.4    Saito, Y.5    Mochizuki, N.6
  • 192
    • 34547590898 scopus 로고    scopus 로고
    • Disruption of planar cell polarity signaling results in congenital heart defects and cardiomyopathy attributable to early cardiomyocyte disorganization
    • DOI 10.1161/CIRCRESAHA.106.142406, PII 0000301220070720000007
    • H.M. Phillips, H.J. Rhee, J.N. Murdoch, V. Hildreth, J.D. Peat, R.H. Anderson, A.J. Copp, B. Chaudhry and D.J. Henderson: Disruption of planar cell polarity signaling results in congenital heart defects and cardiomyopathy attributable to early cardiomyocyte disorganization. Circ Res, 101, 137-45 (2007) (Pubitemid 47196581)
    • (2007) Circulation Research , vol.101 , Issue.2 , pp. 137-145
    • Phillips, H.M.1    Rhee, H.J.2    Murdoch, J.N.3    Hildreth, V.4    Peat, J.D.5    Anderson, R.H.6    Copp, A.J.7    Chaudhry, B.8    Henderson, D.J.9
  • 193
    • 9644289331 scopus 로고    scopus 로고
    • N-cadherin-mediated cell adhesion determines the plasticity for cell alignment in response to mechanical stretch in cultured cardiomyocytes
    • DOI 10.1016/j.bbrc.2004.11.019, PII S0006291X04025628
    • T. Matsuda, K. Takahashi, T. Nariai, T. Ito, T. Takatani, Y. Fujio and J. Azuma: N-cadherin-mediated cell adhesion determines the plasticity for cell alignment in response to mechanical stretch in cultured cardiomyocytes. Biochem Biophys Res Commun, 326, 228-32 (2005) (Pubitemid 39573223)
    • (2004) Biochemical and Biophysical Research Communications , vol.326 , Issue.1 , pp. 228-232
    • Matsuda, T.1    Takahashi, K.2    Nariai, T.3    Ito, T.4    Takatani, T.5    Fujio, Y.6    Azuma, J.7
  • 196
    • 0038607961 scopus 로고    scopus 로고
    • N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane
    • DOI 10.1074/jbc.M211452200
    • J.K. Wahl, 3rd, Y.J. Kim, J.M. Cullen, K.R. Johnson and M.J. Wheelock: N-cadherin-catenin complexes form prior to cleavage of the proregion and transport to the plasma membrane. J Biol Chem, 278, 17269-76 (2003) (Pubitemid 36799609)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 17269-17276
    • Wahl III, J.K.1    Kim, Y.J.2    Cullen, J.M.3    Johnson, K.R.4    Wheelock, M.J.5
  • 199
    • 48549087054 scopus 로고    scopus 로고
    • On the mechanisms of arrhythmias in the myocardium of mXinalpha-deficient murine left atrialpulmonary veins
    • Y.J. Lai, E.Y. Huang, H.I. Yeh, Y.L. Chen, J.J. Lin and C.I. Lin: On the mechanisms of arrhythmias in the myocardium of mXinalpha-deficient murine left atrialpulmonary veins. Life Sci, 83, 272-83 (2008)
    • (2008) Life Sci , vol.83 , pp. 272-283
    • Lai, Y.J.1    Huang, E.Y.2    Yeh, H.I.3    Chen, Y.L.4    Lin, J.J.5    Lin, C.I.6
  • 201
    • 25444529765 scopus 로고    scopus 로고
    • Molecular physiology of cardiac repolarization
    • DOI 10.1152/physrev.00002.2005
    • J.M. Nerbonne and R.S. Kass: Molecular physiology of cardiac repolarization. Physiol Rev, 85, 1205-53 (2005) (Pubitemid 41362269)
    • (2005) Physiological Reviews , vol.85 , Issue.4 , pp. 1205-1253
    • Nerbonne, J.M.1    Kass, R.S.2
  • 205
    • 0028834748 scopus 로고
    • Disruption of cell-cell adhesion in an inbred strain of hereditary cardiomyopathic hamster (Bio 14.6)
    • Y. Fujio, F. Yamada-Honda, N. Sato, H. Funai, A. Wada, N. Awata and N. Shibata: Disruption of cell-cell adhesion in an inbred strain of hereditary cardiomyopathic hamster (Bio 14.6). Cardiovasc Res, 30, 899-904 (1995)
    • (1995) Cardiovasc Res , vol.30 , pp. 899-904
    • Fujio, Y.1    Yamada-Honda, F.2    Sato, N.3    Funai, H.4    Wada, A.5    Awata, N.6    Shibata, N.7
  • 206
    • 0036216492 scopus 로고    scopus 로고
    • Structural correlate of atrial fibrillation in human patients
    • DOI 10.1016/S0008-6363(02)00273-0, PII S0008636302002730
    • S. Kostin, G. Klein, Z. Szalay, S. Hein, E.P. Bauer and J. Schaper: Structural correlate of atrial fibrillation in human patients. Cardiovasc Res, 54, 361-79 (2002) (Pubitemid 34327915)
    • (2002) Cardiovascular Research , vol.54 , Issue.2 , pp. 361-379
    • Kostin, S.1    Klein, G.2    Szalay, Z.3    Hein, S.4    Bauer, E.P.5    Schaper, J.6
  • 207
    • 0033083390 scopus 로고    scopus 로고
    • Chronic pressure overload cardiac hypertrophy and failure in guinea pigs: III. Intercalated disc remodeling
    • DOI 10.1006/jmcc.1998.0886
    • X. Wang and A.M. Gerdes: Chronic pressure overload cardiac hypertrophy and failure in guinea pigs: III. intercalated disc remodeling. J Mol Cell Cardiol, 31, 333-43 (1999) (Pubitemid 29089882)
    • (1999) Journal of Molecular and Cellular Cardiology , vol.31 , Issue.2 , pp. 333-343
    • Wang, X.1    Gerdes, A.M.2
  • 208
    • 0030031004 scopus 로고    scopus 로고
    • Mapping a cardiomyopathy locus to chromosome 3p22-p25
    • T.M. Olson and M.T. Keating: Mapping a cardiomyopathy locus to chromosome 3p22-p25. J Clin Invest, 97, 528-32 (1996) (Pubitemid 26039420)
    • (1996) Journal of Clinical Investigation , vol.97 , Issue.2 , pp. 528-532
    • Olson, T.M.1    Keating, M.T.2
  • 212
    • 0030724006 scopus 로고    scopus 로고
    • ARVD4, a new locus for arrhythmogenic right ventricular cardiomyopathy, maps to chromosome 2 long arm
    • DOI 10.1006/geno.1997.4927
    • A. Rampazzo, A. Nava, M. Miorin, P. Fonderico, B. Pope, N. Tiso, B. Livolsi, R. Zimbello, G. Thiene and G.A. Danieli: ARVD4, a new locus for arrhythmogrnic right ventricular cardiomyopathy, maps to chromosome 2 long arm. Genomics, 45, 259-63 (1997) (Pubitemid 27467614)
    • (1997) Genomics , vol.45 , Issue.2 , pp. 259-263
    • Rampazzo, A.1    Nava, A.2    Miorin, M.3    Fonderico, P.4    Pope, B.5    Tiso, N.6    Livolsi, B.7    Zimbello, R.8    Thiene, G.9    Danieli, G.A.10
  • 213
    • 33750259884 scopus 로고    scopus 로고
    • Genome-wide scan for premature hypertension supports linkage to chromosome 2 in a large Kyrgyz family
    • DOI 10.1161/01.HYP.0000244107.13957.2b, PII 0000426820061100000025
    • B. Kalmyrzaev, A. Aldashev, M. Khalmatov, A. Polupanov, A. Jumagulova, L. Mamanova, M.R. Wilkins and M. Town: Genome-wide scan for premature hypertension supports linkage to chromosome 2 in a large Kyrgyz family. Hypertension, 48, 908-13 (2006) (Pubitemid 44611004)
    • (2006) Hypertension , vol.48 , Issue.5 , pp. 908-913
    • Kalmyrzaev, B.1    Aldashev, A.2    Khalmatov, M.3    Polupanov, A.4    Jumagulova, A.5    Mamanova, L.6    Wilkins, M.R.7    Town, M.8


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