메뉴 건너뛰기




Volumn 36, Issue , 2014, Pages 213-223

Tight junctions and the regulation of gene expression

Author keywords

Cingulin; Claudins; Gene expression; Tight junctions; ZO

Indexed keywords

CINGULIN; CLAUDIN; CLAUDIN 1; CLAUDIN 18; CLAUDIN 6; CLAUDIN 7; CLAUDIN 8; JUNCTIONAL ADHESION MOLECULE A; MAGI 1 PROTEIN; MARVELD3 PROTEIN; MEMBRANE ASSOCIATED GUANYLATE CYCLASE KINASE; METALLOPROTEINASE; OCCLUDIN; PARACINGULIN; PROTEIN ZO1; PROTEIN ZO2; RNA POLYMERASE II; SYMPLEKIN; TIGHT JUNCTION PROTEIN; UBINUCLEIN; UNCLASSIFIED DRUG;

EID: 85027920932     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2014.08.009     Document Type: Review
Times cited : (74)

References (88)
  • 1
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar M.G., Palade G.E. Junctional complexes in various epithelia. J Cell Biol 1963, 17:375-412.
    • (1963) J Cell Biol , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 3
    • 34248212466 scopus 로고    scopus 로고
    • TJ proteins that make round trips to the nucleus
    • Landes Bioscience/Springer Science/Business Media, Georgetown, TX/New York, NY, L. Gonzalez-Mariscal (Ed.)
    • Lopez-Bayghen E., Jaramillo B.E., Huerta M., Betanzos A., Gonzalez-Marical L. TJ proteins that make round trips to the nucleus. Tight junctions 2006, 76-100. Landes Bioscience/Springer Science/Business Media, Georgetown, TX/New York, NY. L. Gonzalez-Mariscal (Ed.).
    • (2006) Tight junctions , pp. 76-100
    • Lopez-Bayghen, E.1    Jaramillo, B.E.2    Huerta, M.3    Betanzos, A.4    Gonzalez-Marical, L.5
  • 4
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi C.J., Arpin M., Fanning A.S., Louvard D. The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc Natl Acad Sci U S A 1996, 93(20):10779-10784.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.20 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 5
    • 0037415643 scopus 로고    scopus 로고
    • The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density
    • Balda M.S., Garrett M.D., Matter K. The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J Cell Biol 2003, 160(3):423-432.
    • (2003) J Cell Biol , vol.160 , Issue.3 , pp. 423-432
    • Balda, M.S.1    Garrett, M.D.2    Matter, K.3
  • 6
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda M.S., Matter K. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J 2000, 19(9):2024-2033.
    • (2000) EMBO J , vol.19 , Issue.9 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 7
    • 13244260780 scopus 로고    scopus 로고
    • RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity
    • Frankel P., Aronheim A., Kavanagh E., Balda M.S., Matter K., Bunney T.D., et al. RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity. EMBO J 2005, 24(1):54-62.
    • (2005) EMBO J , vol.24 , Issue.1 , pp. 54-62
    • Frankel, P.1    Aronheim, A.2    Kavanagh, E.3    Balda, M.S.4    Matter, K.5    Bunney, T.D.6
  • 8
    • 33644773928 scopus 로고    scopus 로고
    • Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the ZO-1-regulated transcription factor ZONAB/DbpA
    • Sourisseau T., Georgiadis A., Tsapara A., Ali R.R., Pestell R., Matter K., et al. Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the ZO-1-regulated transcription factor ZONAB/DbpA. Mol Cell Biol 2006, 26(6):2387-2398.
    • (2006) Mol Cell Biol , vol.26 , Issue.6 , pp. 2387-2398
    • Sourisseau, T.1    Georgiadis, A.2    Tsapara, A.3    Ali, R.R.4    Pestell, R.5    Matter, K.6
  • 9
    • 70449699678 scopus 로고    scopus 로고
    • The Y-box factor ZONAB/DbpA associates with GEF-H1/Lfc and mediates Rho-stimulated transcription
    • Nie M., Aijaz S., Leefa Chong San I.V., Balda M.S., Matter K. The Y-box factor ZONAB/DbpA associates with GEF-H1/Lfc and mediates Rho-stimulated transcription. EMBO Rep 2009, 10(10):1125-1131.
    • (2009) EMBO Rep , vol.10 , Issue.10 , pp. 1125-1131
    • Nie, M.1    Aijaz, S.2    Leefa Chong San, I.V.3    Balda, M.S.4    Matter, K.5
  • 10
    • 33644861530 scopus 로고    scopus 로고
    • The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and regulates transcriptional activity of ZONAB
    • Tsapara A., Matter K., Balda M.S. The heat-shock protein Apg-2 binds to the tight junction protein ZO-1 and regulates transcriptional activity of ZONAB. Mol Biol Cell 2006, 17(3):1322-1330.
    • (2006) Mol Biol Cell , vol.17 , Issue.3 , pp. 1322-1330
    • Tsapara, A.1    Matter, K.2    Balda, M.S.3
  • 11
    • 84863577279 scopus 로고    scopus 로고
    • Stress- and Rho-activated ZO-1-associated nucleic acid binding protein binding to p21 mRNA mediates stabilization, translation, and cell survival
    • Nie M., Balda M.S., Matter K. Stress- and Rho-activated ZO-1-associated nucleic acid binding protein binding to p21 mRNA mediates stabilization, translation, and cell survival. Proc Natl Acad Sci U S A 2012, 109(27):10897-10902.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.27 , pp. 10897-10902
    • Nie, M.1    Balda, M.S.2    Matter, K.3
  • 12
    • 77949897625 scopus 로고    scopus 로고
    • ZONAB promotes proliferation and represses differentiation of proximal tubule epithelial cells
    • Lima W.R., Parreira K.S., Devuyst O., Caplanusi A., N'Kuli F., Marien B., et al. ZONAB promotes proliferation and represses differentiation of proximal tubule epithelial cells. J Am Soc Nephrol 2010, 21(3):478-488.
    • (2010) J Am Soc Nephrol , vol.21 , Issue.3 , pp. 478-488
    • Lima, W.R.1    Parreira, K.S.2    Devuyst, O.3    Caplanusi, A.4    N'Kuli, F.5    Marien, B.6
  • 13
    • 78651238212 scopus 로고    scopus 로고
    • The tight junction associated signalling proteins ZO-1 and ZONAB regulate retinal pigment epithelium homeostasis in mice
    • Georgiadis A., Tschernutter M., Bainbridge J.W., Balaggan K.S., Mowat F., West E.L., et al. The tight junction associated signalling proteins ZO-1 and ZONAB regulate retinal pigment epithelium homeostasis in mice. PLoS ONE 2010, 5(12):pe15730.
    • (2010) PLoS ONE , vol.5 , Issue.12 , pp. pe15730
    • Georgiadis, A.1    Tschernutter, M.2    Bainbridge, J.W.3    Balaggan, K.S.4    Mowat, F.5    West, E.L.6
  • 14
    • 33748679558 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 has several functional nuclear export signals
    • Gonzalez-Mariscal L., Ponce A., Alarcon L., Jaramillo B.E. The tight junction protein ZO-2 has several functional nuclear export signals. Exp Cell Res 2006, 312(17):3323-3335.
    • (2006) Exp Cell Res , vol.312 , Issue.17 , pp. 3323-3335
    • Gonzalez-Mariscal, L.1    Ponce, A.2    Alarcon, L.3    Jaramillo, B.E.4
  • 15
    • 84882790869 scopus 로고    scopus 로고
    • The intracellular fate of zonula occludens 2 is regulated by the phosphorylation of SR repeats and the phosphorylation/O-GlcNAcylation of S257
    • Quiros M., Alarcon L., Ponce A., Giannakouros T., Gonzalez-Mariscal L. The intracellular fate of zonula occludens 2 is regulated by the phosphorylation of SR repeats and the phosphorylation/O-GlcNAcylation of S257. Mol Biol Cell 2013, 24(16):2528-2543.
    • (2013) Mol Biol Cell , vol.24 , Issue.16 , pp. 2528-2543
    • Quiros, M.1    Alarcon, L.2    Ponce, A.3    Giannakouros, T.4    Gonzalez-Mariscal, L.5
  • 16
    • 70350221818 scopus 로고    scopus 로고
    • Phosphorylation of zona occludens-2 by protein kinase C epsilon regulates its nuclear exportation
    • Chamorro D., Alarcon L., Ponce A., Tapia R., Gonzalez-Aguilar H., Robles-Flores M., et al. Phosphorylation of zona occludens-2 by protein kinase C epsilon regulates its nuclear exportation. Mol Biol Cell 2009, 20(18):4120-4129.
    • (2009) Mol Biol Cell , vol.20 , Issue.18 , pp. 4120-4129
    • Chamorro, D.1    Alarcon, L.2    Ponce, A.3    Tapia, R.4    Gonzalez-Aguilar, H.5    Robles-Flores, M.6
  • 17
    • 64049116843 scopus 로고    scopus 로고
    • Zona occludens-2 inhibits cyclin D1 expression and cell proliferation and exhibits changes in localization along the cell cycle
    • Tapia R., Huerta M., Islas S., Avila-Flores A., Lopez-Bayghen E., Weiske J., et al. Zona occludens-2 inhibits cyclin D1 expression and cell proliferation and exhibits changes in localization along the cell cycle. Mol Biol Cell 2009, 20(3):1102-1117.
    • (2009) Mol Biol Cell , vol.20 , Issue.3 , pp. 1102-1117
    • Tapia, R.1    Huerta, M.2    Islas, S.3    Avila-Flores, A.4    Lopez-Bayghen, E.5    Weiske, J.6
  • 18
    • 0036343646 scopus 로고    scopus 로고
    • Nuclear localization of the tight junction protein ZO-2 in epithelial cells
    • Islas S., Vega J., Ponce L., Gonzalez-Mariscal L. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp Cell Res 2002, 274(1):138-148.
    • (2002) Exp Cell Res , vol.274 , Issue.1 , pp. 138-148
    • Islas, S.1    Vega, J.2    Ponce, L.3    Gonzalez-Mariscal, L.4
  • 20
    • 0037462794 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B
    • Traweger A., Fuchs R., Krizbai I.A., Weiger T.M., Bauer H.C., Bauer H. The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B. J Biol Chem 2003, 278(4):2692-2700.
    • (2003) J Biol Chem , vol.278 , Issue.4 , pp. 2692-2700
    • Traweger, A.1    Fuchs, R.2    Krizbai, I.A.3    Weiger, T.M.4    Bauer, H.C.5    Bauer, H.6
  • 21
    • 70849085965 scopus 로고    scopus 로고
    • The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain
    • Meerschaert K., Tun M.P., Remue E., De Ganck A., Boucherie C., Vanloo B., et al. The PDZ2 domain of zonula occludens-1 and -2 is a phosphoinositide binding domain. Cell Mol Life Sci 2009, 66(24):3951-3966.
    • (2009) Cell Mol Life Sci , vol.66 , Issue.24 , pp. 3951-3966
    • Meerschaert, K.1    Tun, M.P.2    Remue, E.3    De Ganck, A.4    Boucherie, C.5    Vanloo, B.6
  • 22
    • 0026058877 scopus 로고
    • Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing
    • Li H., Bingham P.M. Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing. Cell 1991, 67(2):335-342.
    • (1991) Cell , vol.67 , Issue.2 , pp. 335-342
    • Li, H.1    Bingham, P.M.2
  • 23
    • 2942601690 scopus 로고    scopus 로고
    • Characterization of the tight junction protein ZO-2 localized at the nucleus of epithelial cells
    • Jaramillo B.E., Ponce A., Moreno J., Betanzos A., Huerta M., Lopez-Bayghen E., et al. Characterization of the tight junction protein ZO-2 localized at the nucleus of epithelial cells. Exp Cell Res 2004, 297(1):247-258.
    • (2004) Exp Cell Res , vol.297 , Issue.1 , pp. 247-258
    • Jaramillo, B.E.1    Ponce, A.2    Moreno, J.3    Betanzos, A.4    Huerta, M.5    Lopez-Bayghen, E.6
  • 24
    • 0347986547 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 associates with Jun Fos and C/EBP transcription factors in epithelial cells
    • Betanzos A., Huerta M., Lopez-Bayghen E., Azuara E., Amerena J., Gonzalez-Mariscal L. The tight junction protein ZO-2 associates with Jun Fos and C/EBP transcription factors in epithelial cells. Exp Cell Res 2004, 292(1):51-66.
    • (2004) Exp Cell Res , vol.292 , Issue.1 , pp. 51-66
    • Betanzos, A.1    Huerta, M.2    Lopez-Bayghen, E.3    Azuara, E.4    Amerena, J.5    Gonzalez-Mariscal, L.6
  • 25
    • 37049037095 scopus 로고    scopus 로고
    • Cyclin D1 is transcriptionally down-regulated by ZO-2 via an E box and the transcription factor c-Myc
    • Huerta M., Munoz R., Tapia R., Soto-Reyes E., Ramirez L., Recillas-Targa F., et al. Cyclin D1 is transcriptionally down-regulated by ZO-2 via an E box and the transcription factor c-Myc. Mol Biol Cell 2007, 18(12):4826-4836.
    • (2007) Mol Biol Cell , vol.18 , Issue.12 , pp. 4826-4836
    • Huerta, M.1    Munoz, R.2    Tapia, R.3    Soto-Reyes, E.4    Ramirez, L.5    Recillas-Targa, F.6
  • 26
    • 18744372407 scopus 로고    scopus 로고
    • LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3
    • Huang H.Y., Li R., Sun Q., Wang J., Zhou P., Han H., et al. LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3. Yi Chuan Xue Bao 2002, 29(11):953-958.
    • (2002) Yi Chuan Xue Bao , vol.29 , Issue.11 , pp. 953-958
    • Huang, H.Y.1    Li, R.2    Sun, Q.3    Wang, J.4    Zhou, P.5    Han, H.6
  • 28
    • 38149086680 scopus 로고    scopus 로고
    • Nuclear Zonula occludens-2 alters gene expression and junctional stability in epithelial and endothelial cells
    • Traweger A., Lehner C., Farkas A., Krizbai I.A., Tempfer H., Klement E., et al. Nuclear Zonula occludens-2 alters gene expression and junctional stability in epithelial and endothelial cells. Differentiation 2008, 76(1):99-106.
    • (2008) Differentiation , vol.76 , Issue.1 , pp. 99-106
    • Traweger, A.1    Lehner, C.2    Farkas, A.3    Krizbai, I.A.4    Tempfer, H.5    Klement, E.6
  • 29
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • Mazurek S., Boschek C.B., Hugo F., Eigenbrodt E. Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin Cancer Biol 2005, 15(4):300-308.
    • (2005) Semin Cancer Biol , vol.15 , Issue.4 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 31
    • 0033516532 scopus 로고    scopus 로고
    • Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma
    • Chlenski A., Ketels K.V., Tsao M.S., Talamonti M.S., Anderson M.R., Oyasu R., et al. Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma. Int J Cancer 1999, 82(1):137-144.
    • (1999) Int J Cancer , vol.82 , Issue.1 , pp. 137-144
    • Chlenski, A.1    Ketels, K.V.2    Tsao, M.S.3    Talamonti, M.S.4    Anderson, M.R.5    Oyasu, R.6
  • 32
    • 84890439744 scopus 로고    scopus 로고
    • Regulation of membrane-type 1 matrix metalloproteinase expression by zonula occludens-2 in human lung cancer cells
    • Luczka E., Syne L., Nawrocki-Raby B., Kileztky C., Hunziker W., Birembaut P., et al. Regulation of membrane-type 1 matrix metalloproteinase expression by zonula occludens-2 in human lung cancer cells. Clin Exp Metastasis 2013, 30(7):833-843.
    • (2013) Clin Exp Metastasis , vol.30 , Issue.7 , pp. 833-843
    • Luczka, E.1    Syne, L.2    Nawrocki-Raby, B.3    Kileztky, C.4    Hunziker, W.5    Birembaut, P.6
  • 33
    • 65449154339 scopus 로고    scopus 로고
    • Nuclear localization and pro-apoptotic signaling of YAP2 require intact PDZ-binding motif
    • Oka T., Sudol M. Nuclear localization and pro-apoptotic signaling of YAP2 require intact PDZ-binding motif. Genes Cells 2009, 14(5):607-615.
    • (2009) Genes Cells , vol.14 , Issue.5 , pp. 607-615
    • Oka, T.1    Sudol, M.2
  • 34
    • 78649892579 scopus 로고    scopus 로고
    • Functional complexes between YAP2 and ZO-2 are PDZ domain-dependent, and regulate YAP2 nuclear localization and signalling
    • Oka T., Remue E., Meerschaert K., Vanloo B., Boucherie C., Gfeller D., et al. Functional complexes between YAP2 and ZO-2 are PDZ domain-dependent, and regulate YAP2 nuclear localization and signalling. Biochem J 2010, 432(3):461-472.
    • (2010) Biochem J , vol.432 , Issue.3 , pp. 461-472
    • Oka, T.1    Remue, E.2    Meerschaert, K.3    Vanloo, B.4    Boucherie, C.5    Gfeller, D.6
  • 35
    • 0034597533 scopus 로고    scopus 로고
    • Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins
    • Glaunsinger B.A., Lee S.S., Thomas M., Banks L., Javier R. Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins. Oncogene 2000, 19(46):5270-5280.
    • (2000) Oncogene , vol.19 , Issue.46 , pp. 5270-5280
    • Glaunsinger, B.A.1    Lee, S.S.2    Thomas, M.3    Banks, L.4    Javier, R.5
  • 36
    • 78651504041 scopus 로고    scopus 로고
    • Analysis of the PDZ binding specificities of Influenza A virus NS1 proteins
    • Thomas M., Kranjec C., Nagasaka K., Matlashewski G., Banks L. Analysis of the PDZ binding specificities of Influenza A virus NS1 proteins. Virol J 2011, 8:p25.
    • (2011) Virol J , vol.8 , pp. p25
    • Thomas, M.1    Kranjec, C.2    Nagasaka, K.3    Matlashewski, G.4    Banks, L.5
  • 37
    • 84864084443 scopus 로고    scopus 로고
    • Regulation of interferon-beta by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM
    • Kumar M., Liu H., Rice A.P. Regulation of interferon-beta by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM. PLOS ONE 2012, 7(7):pe41251.
    • (2012) PLOS ONE , vol.7 , Issue.7 , pp. pe41251
    • Kumar, M.1    Liu, H.2    Rice, A.P.3
  • 38
    • 0034689053 scopus 로고    scopus 로고
    • Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors
    • Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.F., Gruffat H., et al. Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors. J Cell Biol 2000, 148(6):1165-1176.
    • (2000) J Cell Biol , vol.148 , Issue.6 , pp. 1165-1176
    • Aho, S.1    Buisson, M.2    Pajunen, T.3    Ryoo, Y.W.4    Giot, J.F.5    Gruffat, H.6
  • 39
    • 84857040492 scopus 로고    scopus 로고
    • Identification of new interacting partners of the shuttling protein ubinuclein (Ubn-1)
    • Lupo J., Conti A., Sueur C., Coly P.A., Coute Y., Hunziker W., et al. Identification of new interacting partners of the shuttling protein ubinuclein (Ubn-1). Exp Cell Res 2012, 318(5):509-520.
    • (2012) Exp Cell Res , vol.318 , Issue.5 , pp. 509-520
    • Lupo, J.1    Conti, A.2    Sueur, C.3    Coly, P.A.4    Coute, Y.5    Hunziker, W.6
  • 40
    • 67449108023 scopus 로고    scopus 로고
    • Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos)
    • Aho S., Lupo J., Coly P.A., Sabine A., Castellazzi M., Morand P., et al. Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NACos). Biol Cell 2009, 101(6):319-334.
    • (2009) Biol Cell , vol.101 , Issue.6 , pp. 319-334
    • Aho, S.1    Lupo, J.2    Coly, P.A.3    Sabine, A.4    Castellazzi, M.5    Morand, P.6
  • 41
    • 84859185528 scopus 로고    scopus 로고
    • Identification of an ubinuclein 1 region required for stability and function of the human HIRA/UBN1/CABIN1/ASF1a histone H3.3 chaperone complex
    • Tang Y., Puri A., Ricketts M.D., Rai T.S., Hoffmann J., Hoi E., et al. Identification of an ubinuclein 1 region required for stability and function of the human HIRA/UBN1/CABIN1/ASF1a histone H3.3 chaperone complex. Biochemistry 2012, 51(12):2366-2377.
    • (2012) Biochemistry , vol.51 , Issue.12 , pp. 2366-2377
    • Tang, Y.1    Puri, A.2    Ricketts, M.D.3    Rai, T.S.4    Hoffmann, J.5    Hoi, E.6
  • 42
    • 0029840160 scopus 로고    scopus 로고
    • Symplekin, a novel type of tight junction plaque protein
    • Keon B.H., Schafer S., Kuhn C., Grund C., Franke W.W. Symplekin, a novel type of tight junction plaque protein. J Cell Biol 1996, 134(4):1003-1018.
    • (1996) J Cell Biol , vol.134 , Issue.4 , pp. 1003-1018
    • Keon, B.H.1    Schafer, S.2    Kuhn, C.3    Grund, C.4    Franke, W.W.5
  • 43
    • 33846136942 scopus 로고    scopus 로고
    • Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin
    • Kavanagh E., Buchert M., Tsapara A., Choquet A., Balda M.S., Hollande F., et al. Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin. J Cell Sci 2006, 119(Pt 24):5098-5105.
    • (2006) J Cell Sci , vol.119 , pp. 5098-5105
    • Kavanagh, E.1    Buchert, M.2    Tsapara, A.3    Choquet, A.4    Balda, M.S.5    Hollande, F.6
  • 44
    • 67649209016 scopus 로고    scopus 로고
    • The symplekin/ZONAB complex inhibits intestinal cell differentiation by the repression of AML1/Runx1
    • 164 e1-3
    • Buchert M., Darido C., Lagerqvist E., Sedello A., Cazevieille C., Buchholz F., et al. The symplekin/ZONAB complex inhibits intestinal cell differentiation by the repression of AML1/Runx1. Gastroenterology 2009, 137(1):156-164. 164 e1-3.
    • (2009) Gastroenterology , vol.137 , Issue.1 , pp. 156-164
    • Buchert, M.1    Darido, C.2    Lagerqvist, E.3    Sedello, A.4    Cazevieille, C.5    Buchholz, F.6
  • 46
    • 84884334464 scopus 로고    scopus 로고
    • Symplekin, a polyadenylation factor, prevents MOZ and MLL activity on HOXA9 in hematopoietic cells
    • Largeot A., Paggetti J., Broseus J., Aucagne R., Lagrange B., Martin R.Z., et al. Symplekin, a polyadenylation factor, prevents MOZ and MLL activity on HOXA9 in hematopoietic cells. Biochim Biophys Acta 2013, 1833(12):3054-3063.
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.12 , pp. 3054-3063
    • Largeot, A.1    Paggetti, J.2    Broseus, J.3    Aucagne, R.4    Lagrange, B.5    Martin, R.Z.6
  • 47
    • 0033611142 scopus 로고    scopus 로고
    • Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2 ZO-3, and myosin
    • Cordenonsi M., D'Atri F., Hammar E., Parry D.A., Kendrick-Jones J., Shore D., et al. Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2 ZO-3, and myosin. J Cell Biol 1999, 147(7):1569-1582.
    • (1999) J Cell Biol , vol.147 , Issue.7 , pp. 1569-1582
    • Cordenonsi, M.1    D'Atri, F.2    Hammar, E.3    Parry, D.A.4    Kendrick-Jones, J.5    Shore, D.6
  • 48
    • 8544277305 scopus 로고    scopus 로고
    • JACOP, a novel plaque protein localizing at the apical junctional complex with sequence similarity to cingulin
    • Ohnishi H., Nakahara T., Furuse K., Sasaki H., Tsukita S., Furuse M. JACOP, a novel plaque protein localizing at the apical junctional complex with sequence similarity to cingulin. J Biol Chem 2004, 279(44):46014-46022.
    • (2004) J Biol Chem , vol.279 , Issue.44 , pp. 46014-46022
    • Ohnishi, H.1    Nakahara, T.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Furuse, M.6
  • 49
    • 84890243481 scopus 로고    scopus 로고
    • The association of microtubules with tight junctions is promoted by cingulin phosphorylation by AMPK
    • Yano T., Matsui T., Tamura A., Uji M., Tsukita S. The association of microtubules with tight junctions is promoted by cingulin phosphorylation by AMPK. J Cell Biol 2013, 203(4):605-614.
    • (2013) J Cell Biol , vol.203 , Issue.4 , pp. 605-614
    • Yano, T.1    Matsui, T.2    Tamura, A.3    Uji, M.4    Tsukita, S.5
  • 50
    • 79955775739 scopus 로고    scopus 로고
    • A role for ZO-1 and PLEKHA7 in recruiting paracingulin to tight and adherens junctions of epithelial cells
    • Pulimeno P., Paschoud S., Citi S. A role for ZO-1 and PLEKHA7 in recruiting paracingulin to tight and adherens junctions of epithelial cells. J Biol Chem 2011, 286(19):16743-16750.
    • (2011) J Biol Chem , vol.286 , Issue.19 , pp. 16743-16750
    • Pulimeno, P.1    Paschoud, S.2    Citi, S.3
  • 51
    • 79551612886 scopus 로고    scopus 로고
    • Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis
    • Terry S.J., Zihni C., Elbediwy A., Vitiello E., Leefa Chong San I.V., Balda M.S., et al. Spatially restricted activation of RhoA signalling at epithelial junctions by p114RhoGEF drives junction formation and morphogenesis. Nat Cell Biol 2011, 13(2):159-166.
    • (2011) Nat Cell Biol , vol.13 , Issue.2 , pp. 159-166
    • Terry, S.J.1    Zihni, C.2    Elbediwy, A.3    Vitiello, E.4    Leefa Chong San, I.V.5    Balda, M.S.6
  • 52
    • 34548491399 scopus 로고    scopus 로고
    • Rho/Rho-associated kinase-II signaling mediates disassembly of epithelial apical junctions
    • Samarin S.N., Ivanov A.I., Flatau G., Parkos C.A., Nusrat A. Rho/Rho-associated kinase-II signaling mediates disassembly of epithelial apical junctions. Mol Biol Cell 2007, 18(9):3429-3439.
    • (2007) Mol Biol Cell , vol.18 , Issue.9 , pp. 3429-3439
    • Samarin, S.N.1    Ivanov, A.I.2    Flatau, G.3    Parkos, C.A.4    Nusrat, A.5
  • 53
    • 17844402719 scopus 로고    scopus 로고
    • Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition
    • Aijaz S., D'Atri F., Citi S., Balda M.S., Matter K. Binding of GEF-H1 to the tight junction-associated adaptor cingulin results in inhibition of Rho signaling and G1/S phase transition. Dev Cell 2005, 8(5):777-786.
    • (2005) Dev Cell , vol.8 , Issue.5 , pp. 777-786
    • Aijaz, S.1    D'Atri, F.2    Citi, S.3    Balda, M.S.4    Matter, K.5
  • 54
    • 57349127359 scopus 로고    scopus 로고
    • Paracingulin regulates the activity of Rac1 and RhoA GTPases by recruiting Tiam1 and GEF-H1 to epithelial junctions
    • Guillemot L., Paschoud S., Jond L., Foglia A., Citi S. Paracingulin regulates the activity of Rac1 and RhoA GTPases by recruiting Tiam1 and GEF-H1 to epithelial junctions. Mol Biol Cell 2008, 19(10):4442-4453.
    • (2008) Mol Biol Cell , vol.19 , Issue.10 , pp. 4442-4453
    • Guillemot, L.1    Paschoud, S.2    Jond, L.3    Foglia, A.4    Citi, S.5
  • 55
    • 9444239778 scopus 로고    scopus 로고
    • Disruption of the cingulin gene does not prevent tight junction formation but alters gene expression
    • Guillemot L., Hammar E., Kaister C., Ritz J., Caille D., Jond L., et al. Disruption of the cingulin gene does not prevent tight junction formation but alters gene expression. J Cell Sci 2004, 117(Pt 22):5245-5256.
    • (2004) J Cell Sci , vol.117 , pp. 5245-5256
    • Guillemot, L.1    Hammar, E.2    Kaister, C.3    Ritz, J.4    Caille, D.5    Jond, L.6
  • 56
    • 84872227438 scopus 로고    scopus 로고
    • Cingulin is dispensable for epithelial barrier function and tight junction structure, and plays a role in the control of claudin-2 expression and response to duodenal mucosa injury
    • Guillemot L., Schneider Y., Brun P., Castagliuolo I., Pizzuti D., Martines D., et al. Cingulin is dispensable for epithelial barrier function and tight junction structure, and plays a role in the control of claudin-2 expression and response to duodenal mucosa injury. J Cell Sci 2012, 125(Pt 21):5005-5014.
    • (2012) J Cell Sci , vol.125 , pp. 5005-5014
    • Guillemot, L.1    Schneider, Y.2    Brun, P.3    Castagliuolo, I.4    Pizzuti, D.5    Martines, D.6
  • 57
    • 33746637520 scopus 로고    scopus 로고
    • Cingulin regulates claudin-2 expression and cell proliferation through the small GTPase RhoA
    • Guillemot L., Citi S. Cingulin regulates claudin-2 expression and cell proliferation through the small GTPase RhoA. Mol Biol Cell 2006, 17(8):3569-3577.
    • (2006) Mol Biol Cell , vol.17 , Issue.8 , pp. 3569-3577
    • Guillemot, L.1    Citi, S.2
  • 58
    • 77956779433 scopus 로고    scopus 로고
    • The molecular basis for the structure, function and regulation of tight junctions
    • JAI Press Inc., Greenwich, A.J. North, D.R. Garrod, M.A.J. Chidgey (Eds.)
    • Citi S., Cordenonsi M. The molecular basis for the structure, function and regulation of tight junctions. Adhesive interactions of cells 1999, 203-233. JAI Press Inc., Greenwich. A.J. North, D.R. Garrod, M.A.J. Chidgey (Eds.).
    • (1999) Adhesive interactions of cells , pp. 203-233
    • Citi, S.1    Cordenonsi, M.2
  • 59
    • 12944262412 scopus 로고    scopus 로고
    • HuASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions
    • Nakamura T., Blechman J., Tada S., Rozovskaia T., Itoyama T., Bullrich F., et al. huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions. Proc Natl Acad Sci U S A 2000, 97(13):7284-7289.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , Issue.13 , pp. 7284-7289
    • Nakamura, T.1    Blechman, J.2    Tada, S.3    Rozovskaia, T.4    Itoyama, T.5    Bullrich, F.6
  • 60
    • 84873599355 scopus 로고    scopus 로고
    • The junctional proteins cingulin and paracingulin modulate the expression of tight junction protein genes through GATA-4
    • Guillemot L., Spadaro D., Citi S. The junctional proteins cingulin and paracingulin modulate the expression of tight junction protein genes through GATA-4. PLOS ONE 2013, 8(2):pe55873.
    • (2013) PLOS ONE , vol.8 , Issue.2 , pp. pe55873
    • Guillemot, L.1    Spadaro, D.2    Citi, S.3
  • 62
    • 84878506887 scopus 로고    scopus 로고
    • Claudins and the modulation of tight junction permeability
    • Gunzel D., Yu A.S. Claudins and the modulation of tight junction permeability. Physiol Rev 2013, 93(2):525-569.
    • (2013) Physiol Rev , vol.93 , Issue.2 , pp. 525-569
    • Gunzel, D.1    Yu, A.S.2
  • 66
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda M.S., Whitney J.A., Flores C., Gonzalez S., Cereijido M., Matter K. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J Cell Biol 1996, 134(4):1031-1049.
    • (1996) J Cell Biol , vol.134 , Issue.4 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 67
    • 0032922584 scopus 로고    scopus 로고
    • Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing
    • Lacaz-Vieira F., Jaeger M.M., Farshori P., Kachar B. Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing. J Membr Biol 1999, 168(3):289-297.
    • (1999) J Membr Biol , vol.168 , Issue.3 , pp. 289-297
    • Lacaz-Vieira, F.1    Jaeger, M.M.2    Farshori, P.3    Kachar, B.4
  • 68
    • 80051709700 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and -9 secreted by leukemic cells increase the permeability of blood-brain barrier by disrupting tight junction proteins
    • Feng S., Cen J., Huang Y., Shen H., Yao L., Wang Y., et al. Matrix metalloproteinase-2 and -9 secreted by leukemic cells increase the permeability of blood-brain barrier by disrupting tight junction proteins. PLoS ONE 2011, 6(8):pe20599.
    • (2011) PLoS ONE , vol.6 , Issue.8 , pp. pe20599
    • Feng, S.1    Cen, J.2    Huang, Y.3    Shen, H.4    Yao, L.5    Wang, Y.6
  • 69
    • 0033635344 scopus 로고    scopus 로고
    • Complex phenotype of mice lacking occludin, a component of tight junction strands
    • Saitou M., Furuse M., Sasaki H., Schulzke J.D., Fromm M., Takano H., et al. Complex phenotype of mice lacking occludin, a component of tight junction strands. Mol Biol Cell 2000, 11(12):4131-4142.
    • (2000) Mol Biol Cell , vol.11 , Issue.12 , pp. 4131-4142
    • Saitou, M.1    Furuse, M.2    Sasaki, H.3    Schulzke, J.D.4    Fromm, M.5    Takano, H.6
  • 70
    • 33749484749 scopus 로고    scopus 로고
    • Epigenetic silencing of occludin promotes tumorigenic and metastatic properties of cancer cells via modulations of unique sets of apoptosis-associated genes
    • Osanai M., Murata M., Nishikiori N., Chiba H., Kojima T., Sawada N. Epigenetic silencing of occludin promotes tumorigenic and metastatic properties of cancer cells via modulations of unique sets of apoptosis-associated genes. Cancer Res 2006, 66(18):9125-9133.
    • (2006) Cancer Res , vol.66 , Issue.18 , pp. 9125-9133
    • Osanai, M.1    Murata, M.2    Nishikiori, N.3    Chiba, H.4    Kojima, T.5    Sawada, N.6
  • 71
    • 0035038783 scopus 로고    scopus 로고
    • Perturbation of the tight junction permeability barrier by occludin loop peptides activates beta-catenin/TCF/LEF-mediated transcription
    • Vietor I., Bader T., Paiha K., Huber L.A. Perturbation of the tight junction permeability barrier by occludin loop peptides activates beta-catenin/TCF/LEF-mediated transcription. EMBO Rep 2001, 2(4):306-312.
    • (2001) EMBO Rep , vol.2 , Issue.4 , pp. 306-312
    • Vietor, I.1    Bader, T.2    Paiha, K.3    Huber, L.A.4
  • 72
    • 34249882821 scopus 로고    scopus 로고
    • Occludin-mediated premature senescence is a fail-safe mechanism against tumorigenesis in breast carcinoma cells
    • Osanai M., Murata M., Nishikiori N., Chiba H., Kojima T., Sawada N. Occludin-mediated premature senescence is a fail-safe mechanism against tumorigenesis in breast carcinoma cells. Cancer Sci 2007, 98(7):1027-1034.
    • (2007) Cancer Sci , vol.98 , Issue.7 , pp. 1027-1034
    • Osanai, M.1    Murata, M.2    Nishikiori, N.3    Chiba, H.4    Kojima, T.5    Sawada, N.6
  • 73
    • 74549219792 scopus 로고    scopus 로고
    • Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family
    • Steed E., Rodrigues N.T., Balda M.S., Matter K. Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family. BMC Cell Biol 2009, 10:95.
    • (2009) BMC Cell Biol , vol.10 , pp. 95
    • Steed, E.1    Rodrigues, N.T.2    Balda, M.S.3    Matter, K.4
  • 74
    • 84895737640 scopus 로고    scopus 로고
    • MarvelD3 couples tight junctions to the MEKK1-JNK pathway to regulate cell behavior and survival
    • Steed E., Elbediwy A., Vacca B., Dupasquier S., Hemkemeyer S.A., Suddason T., et al. MarvelD3 couples tight junctions to the MEKK1-JNK pathway to regulate cell behavior and survival. J Cell Biol 2014, 204(5):821-838.
    • (2014) J Cell Biol , vol.204 , Issue.5 , pp. 821-838
    • Steed, E.1    Elbediwy, A.2    Vacca, B.3    Dupasquier, S.4    Hemkemeyer, S.A.5    Suddason, T.6
  • 75
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions
    • Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S. Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. J Cell Biol 2001, 154(3):491-497.
    • (2001) J Cell Biol , vol.154 , Issue.3 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 76
    • 39849084922 scopus 로고    scopus 로고
    • Tight junction biogenesis during early development
    • Eckert J.J., Fleming T.P. Tight junction biogenesis during early development. Biochim Biophys Acta 2008, 1778(3):717-728.
    • (2008) Biochim Biophys Acta , vol.1778 , Issue.3 , pp. 717-728
    • Eckert, J.J.1    Fleming, T.P.2
  • 77
    • 37549038994 scopus 로고    scopus 로고
    • JAM-A regulates permeability and inflammation in the intestine in vivo
    • Laukoetter M.G., Nava P., Lee W.Y., Severson E.A., Capaldo C.T., Babbin B.A., et al. JAM-A regulates permeability and inflammation in the intestine in vivo. J Exp Med 2007, 204(13):3067-3076.
    • (2007) J Exp Med , vol.204 , Issue.13 , pp. 3067-3076
    • Laukoetter, M.G.1    Nava, P.2    Lee, W.Y.3    Severson, E.A.4    Capaldo, C.T.5    Babbin, B.A.6
  • 78
    • 81855228088 scopus 로고    scopus 로고
    • Claudin-1 up-regulates the repressor ZEB-1 to inhibit E-cadherin expression in colon cancer cells
    • Singh A.B., Sharma A., Smith J.J., Krishnan M., Chen X., Eschrich S., et al. Claudin-1 up-regulates the repressor ZEB-1 to inhibit E-cadherin expression in colon cancer cells. Gastroenterology 2011, 141(6):2140-2153.
    • (2011) Gastroenterology , vol.141 , Issue.6 , pp. 2140-2153
    • Singh, A.B.1    Sharma, A.2    Smith, J.J.3    Krishnan, M.4    Chen, X.5    Eschrich, S.6
  • 79
    • 0033376599 scopus 로고    scopus 로고
    • Claudin-1 contributes to the epithelial barrier function in MDCK cells
    • Inai T., Kobayashi J., Shibata Y. Claudin-1 contributes to the epithelial barrier function in MDCK cells. Eur J Cell Biol 1999, 78(12):849-855.
    • (1999) Eur J Cell Biol , vol.78 , Issue.12 , pp. 849-855
    • Inai, T.1    Kobayashi, J.2    Shibata, Y.3
  • 80
    • 79952708738 scopus 로고    scopus 로고
    • Claudin-2 knockdown decreases matrix metalloproteinase-9 activity and cell migration via suppression of nuclear Sp1 in A549 cells
    • Ikari A., Sato T., Takiguchi A., Atomi K., Yamazaki Y., Sugatani J. Claudin-2 knockdown decreases matrix metalloproteinase-9 activity and cell migration via suppression of nuclear Sp1 in A549 cells. Life Sci 2011, 88(13-14):628-633.
    • (2011) Life Sci , vol.88 , Issue.13-14 , pp. 628-633
    • Ikari, A.1    Sato, T.2    Takiguchi, A.3    Atomi, K.4    Yamazaki, Y.5    Sugatani, J.6
  • 81
    • 79952714520 scopus 로고    scopus 로고
    • Decrease in claudin-2 expression enhances cell migration in renal epithelial Madin-Darby canine kidney cells
    • Ikari A., Takiguchi A., Atomi K., Sato T., Sugatani J. Decrease in claudin-2 expression enhances cell migration in renal epithelial Madin-Darby canine kidney cells. J Cell Physiol 2011, 226(6):1471-1478.
    • (2011) J Cell Physiol , vol.226 , Issue.6 , pp. 1471-1478
    • Ikari, A.1    Takiguchi, A.2    Atomi, K.3    Sato, T.4    Sugatani, J.5
  • 82
    • 84879499448 scopus 로고    scopus 로고
    • Claudin-2 regulates colorectal inflammation via myosin light chain kinase-dependent signaling
    • Nishida M., Yoshida M., Nishiumi S., Furuse M., Azuma T. Claudin-2 regulates colorectal inflammation via myosin light chain kinase-dependent signaling. Dig Dis Sci 2013, 58(6):1546-1559.
    • (2013) Dig Dis Sci , vol.58 , Issue.6 , pp. 1546-1559
    • Nishida, M.1    Yoshida, M.2    Nishiumi, S.3    Furuse, M.4    Azuma, T.5
  • 83
    • 84885145558 scopus 로고    scopus 로고
    • Gene silencing of claudin6 enhances cell proliferation and migration accompanied with increased MMP2 activity via p38 MAPK signaling pathway in human breast epithelium cell line HBL100
    • Ren Y., Wu Q., Liu Y., Xu X., Quan C. Gene silencing of claudin6 enhances cell proliferation and migration accompanied with increased MMP2 activity via p38 MAPK signaling pathway in human breast epithelium cell line HBL100. Mol Med Rep 2013, 8(5):1505-1510.
    • (2013) Mol Med Rep , vol.8 , Issue.5 , pp. 1505-1510
    • Ren, Y.1    Wu, Q.2    Liu, Y.3    Xu, X.4    Quan, C.5
  • 84
    • 84856210973 scopus 로고    scopus 로고
    • Inflammation and disruption of the mucosal architecture in claudin-7-deficient mice
    • Ding L., Lu Z., Foreman O., Tatum R., Lu Q., Renegar R., et al. Inflammation and disruption of the mucosal architecture in claudin-7-deficient mice. Gastroenterology 2012, 142(2):305-315.
    • (2012) Gastroenterology , vol.142 , Issue.2 , pp. 305-315
    • Ding, L.1    Lu, Z.2    Foreman, O.3    Tatum, R.4    Lu, Q.5    Renegar, R.6
  • 85
    • 33947547489 scopus 로고    scopus 로고
    • Dysregulation of claudin-7 leads to loss of E-cadherin expression and the increased invasion of esophageal squamous cell carcinoma cells
    • Lioni M., Brafford P., Andl C., Rustgi A., El-Deiry W., Herlyn M., et al. Dysregulation of claudin-7 leads to loss of E-cadherin expression and the increased invasion of esophageal squamous cell carcinoma cells. Am J Pathol 2007, 170(2):709-721.
    • (2007) Am J Pathol , vol.170 , Issue.2 , pp. 709-721
    • Lioni, M.1    Brafford, P.2    Andl, C.3    Rustgi, A.4    El-Deiry, W.5    Herlyn, M.6
  • 86
    • 0037930880 scopus 로고    scopus 로고
    • Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation
    • Yu A.S., Enck A.H., Lencer W.I., Schneeberger E.E. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J Biol Chem 2003, 278(19):17350-17359.
    • (2003) J Biol Chem , vol.278 , Issue.19 , pp. 17350-17359
    • Yu, A.S.1    Enck, A.H.2    Lencer, W.I.3    Schneeberger, E.E.4
  • 87
    • 36749050385 scopus 로고    scopus 로고
    • Inhibition of hepatocellular carcinoma invasion by suppression of claudin-10 in HLE cells
    • Ip Y.C., Cheung S.T., Lee Y.T., Ho J.C., Fan S.T. Inhibition of hepatocellular carcinoma invasion by suppression of claudin-10 in HLE cells. Mol Cancer Ther 2007, 6(11):2858-2867.
    • (2007) Mol Cancer Ther , vol.6 , Issue.11 , pp. 2858-2867
    • Ip, Y.C.1    Cheung, S.T.2    Lee, Y.T.3    Ho, J.C.4    Fan, S.T.5
  • 88
    • 84905456192 scopus 로고    scopus 로고
    • Knockout mice reveal key roles for claudin 18 in alveolar barrier properties and fluid homeostasis
    • Li G., Flodby P., Luo J., Kage H., Sipos A., Gao D., et al. Knockout mice reveal key roles for claudin 18 in alveolar barrier properties and fluid homeostasis. Am J Respir Cell Mol Biol 2014, 51:210-222.
    • (2014) Am J Respir Cell Mol Biol , vol.51 , pp. 210-222
    • Li, G.1    Flodby, P.2    Luo, J.3    Kage, H.4    Sipos, A.5    Gao, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.