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Volumn 2, Issue 3, 2012, Pages 1819-1852

Claudins and other tight junction proteins

Author keywords

[No Author keywords available]

Indexed keywords

CLAUDIN;

EID: 84861966218     PISSN: None     EISSN: 20404603     Source Type: Journal    
DOI: 10.1002/cphy.c110045     Document Type: Article
Times cited : (307)

References (295)
  • 3
    • 32544432516 scopus 로고    scopus 로고
    • Tight junctions: molecular architecture and function
    • Aijaz S, Balda MS, Matter K. Tight junctions: molecular architecture and function. Int Rev Cytol 248: 261-298, 2006.
    • (2006) Int Rev Cytol , vol.248 , pp. 261-298
    • Aijaz, S.1    Balda, M.S.2    Matter, K.3
  • 6
    • 70350648021 scopus 로고    scopus 로고
    • Regulation of mucosal structure and barrier function in rat colon exposed to tumor necrosis factor alpha and interferon gamma in vitro: A novel model for studying the pathomechanisms of inflammatory bowel disease cytokines
    • Amasheh M, Grotjohann I, Amasheh S, Fromm A, Söderholm JD, Zeitz M, Fromm M, Schulzke JD. Regulation of mucosal structure and barrier function in rat colon exposed to tumor necrosis factor alpha and interferon gamma in vitro: A novel model for studying the pathomechanisms of inflammatory bowel disease cytokines. Scand J Gastroent 44: 1226-1235. 2009.
    • (2009) Scand J Gastroent , vol.44 , pp. 1226-1235
    • Amasheh, M.1    Grotjohann, I.2    Amasheh, S.3    Fromm, A.4    Söderholm, J.D.5    Zeitz, M.6    Fromm, M.7    Schulzke, J.D.8
  • 7
    • 78649730159 scopus 로고    scopus 로고
    • TNFa-induced and berberine-antagonized tight junction barrier impairment via tyrosine kinase, pAkt, and NFkB signaling
    • Amasheh M, Fromm A, Krug SM, Amasheh S, Andres S, Zeitz M, Fromm M, Schulzke JD. TNFa-induced and berberine-antagonized tight junction barrier impairment via tyrosine kinase, pAkt, and NFkB signaling. J Cell Sci 123: 4145-4155, 2010
    • (2010) J Cell Sci , vol.123 , pp. 4145-4155
    • Amasheh, M.1    Fromm, A.2    Krug, S.M.3    Amasheh, S.4    Andres, S.5    Zeitz, M.6    Fromm, M.7    Schulzke, J.D.8
  • 8
    • 69849111327 scopus 로고    scopus 로고
    • Inflamed pouch mucosa possesses altered tight junctions indicating recurrence of inflammatory bowel disease
    • Amasheh S, Dullat S, Fromm M, Schulzke JD, Buhr HJ, Kroesen AJ. Inflamed pouch mucosa possesses altered tight junctions indicating recurrence of inflammatory bowel disease. Int J Colorectal Dis 24: 1149-1156, 2009.
    • (2009) Int J Colorectal Dis , vol.24 , pp. 1149-1156
    • Amasheh, S.1    Dullat, S.2    Fromm, M.3    Schulzke, J.D.4    Buhr, H.J.5    Kroesen, A.J.6
  • 9
    • 78650062278 scopus 로고    scopus 로고
    • Claudins of intestine and nephron - a correlation of molecular tight junction structure and barrier function
    • Amasheh S, Fromm M, Günzel D. Claudins of intestine and nephron - a correlation of molecular tight junction structure and barrier function. Acta Physiol 201: 133-140. 2011.
    • (2011) Acta Physiol , vol.201 , pp. 133-140
    • Amasheh, S.1    Fromm, M.2    Günzel, D.3
  • 13
  • 17
    • 33645843051 scopus 로고    scopus 로고
    • Claudin-8 modulates paracellular permeability to acidic and basic ions in MDCK II cells
    • Angelow S, Kim KJ, Yu AS. Claudin-8 modulates paracellular permeability to acidic and basic ions in MDCK II cells. J Physiol 571: 15-26, 2006.
    • (2006) J Physiol , vol.571 , pp. 15-26
    • Angelow, S.1    Kim, K.J.2    Yu, A.S.3
  • 18
    • 34547921509 scopus 로고    scopus 로고
    • Claudin-8 expression in renal epithelial cells augments the paracellular barrier by replacing endogenous claudin-2
    • Angelow S, Schneeberger EE, Yu AS. Claudin-8 expression in renal epithelial cells augments the paracellular barrier by replacing endogenous claudin-2. J Membr Biol 215: 147-159, 2007.
    • (2007) J Membr Biol , vol.215 , pp. 147-159
    • Angelow, S.1    Schneeberger, E.E.2    Yu, A.S.3
  • 19
    • 70350399482 scopus 로고    scopus 로고
    • Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis
    • Angelow S, Yu AS. Structure-function studies of claudin extracellular domains by cysteine-scanning mutagenesis. J Biol Chem 284: 29205-29017, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 29205-29017
    • Angelow, S.1    Yu, A.S.2
  • 20
    • 54149114711 scopus 로고    scopus 로고
    • Phosphorylation of claudin-4 is required for tight junction formation in a human keratinocyte cell line
    • Aono S, Hirai Y. Phosphorylation of claudin-4 is required for tight junction formation in a human keratinocyte cell line. Exp Cell Res 314: 3326-3339, 2008.
    • (2008) Exp Cell Res , vol.314 , pp. 3326-3339
    • Aono, S.1    Hirai, Y.2
  • 21
    • 33746483878 scopus 로고    scopus 로고
    • Role of the Cldn6 cytoplasmic tail domain in membrane targeting and epidermal differentiation in vivo
    • Arabzadeh A, Troy TC, Turksen K. Role of the Cldn6 cytoplasmic tail domain in membrane targeting and epidermal differentiation in vivo. Mol Cell Biol 26: 5876-5887, 2006.
    • (2006) Mol Cell Biol , vol.26 , pp. 5876-5887
    • Arabzadeh, A.1    Troy, T.C.2    Turksen, K.3
  • 22
    • 28044437976 scopus 로고    scopus 로고
    • Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells
    • Bagnoli F, Buti L, Tompkins L, Covacci A, Amieva MR. Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells. Proc Natl Acad Sci U S A 102: 16339-16344, 2005.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16339-16344
    • Bagnoli, F.1    Buti, L.2    Tompkins, L.3    Covacci, A.4    Amieva, M.R.5
  • 23
    • 59549100692 scopus 로고    scopus 로고
    • Tight junctions at a glance
    • Balda MS, Matter K. Tight junctions at a glance. J Cell Sci 121: 3677-3682, 2008.
    • (2008) J Cell Sci , vol.121 , pp. 3677-3682
    • Balda, M.S.1    Matter, K.2
  • 27
    • 38349075415 scopus 로고    scopus 로고
    • Developmental changes in proximal tubule NaCl transport
    • Baum M. Developmental changes in proximal tubule NaCl transport. Pediatr Nephrol 23: 185-194, 2008.
    • (2008) Pediatr Nephrol , vol.23 , pp. 185-194
    • Baum, M.1
  • 34
    • 67349276621 scopus 로고    scopus 로고
    • Tight junctions and tight junction proteins in mammalian epidermis
    • Brandner JM. Tight junctions and tight junction proteins in mammalian epidermis. Eur J Pharm Biopharm 72: 289-294, 2009.
    • (2009) Eur J Pharm Biopharm , vol.72 , pp. 289-294
    • Brandner, J.M.1
  • 35
    • 0141863221 scopus 로고    scopus 로고
    • Expression and localization of tight junction-associated proteins in human hair follicles
    • Brandner JM, McIntyre M, Kief S, Wladykowski E, Moll I. Expression and localization of tight junction-associated proteins in human hair follicles. Arch Dermatol Res 295: 211-221, 2003.
    • (2003) Arch Dermatol Res , vol.295 , pp. 211-221
    • Brandner, J.M.1    McIntyre, M.2    Kief, S.3    Wladykowski, E.4    Moll, I.5
  • 37
    • 70349320390 scopus 로고    scopus 로고
    • Arcobacter butzleri induces barrier dysfunction in intestinal epithelial cells
    • Bücker R, Troeger H, Kleer J, Fromm M, Schulzke JD. Arcobacter butzleri induces barrier dysfunction in intestinal epithelial cells. J Infect Dis 200: 756-764, 2009.
    • (2009) J Infect Dis , vol.200 , pp. 756-764
    • Bücker, R.1    Troeger, H.2    Kleer, J.3    Fromm, M.4    Schulzke, J.D.5
  • 40
    • 38949172779 scopus 로고    scopus 로고
    • Splice-site mutations in the TRIC gene underlie autosomal recessive nonsyndromic hearing impairment in Pakistani families
    • Chishti MS, Bhatti A, Tamim S, Lee K, McDonald ML, Leal SM, Ahmad W. Splice-site mutations in the TRIC gene underlie autosomal recessive nonsyndromic hearing impairment in Pakistani families. J Hum Genet 53: 101-105, 2008.
    • (2008) J Hum Genet , vol.53 , pp. 101-105
    • Chishti, M.S.1    Bhatti, A.2    Tamim, S.3    Lee, K.4    McDonald, M.L.5    Leal, S.M.6    Ahmad, W.7
  • 42
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: a model for the resistance of the zonula occludens
    • Claude P. Morphological factors influencing transepithelial permeability: a model for the resistance of the zonula occludens. J Membr Biol 39: 219-232, 1978.
    • (1978) J Membr Biol , vol.39 , pp. 219-232
    • Claude, P.1
  • 43
    • 0015837872 scopus 로고
    • Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia
    • Claude P, Goodenough DA. Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia. J Cell Biol 58: 390-400, 1973.
    • (1973) J Cell Biol , vol.58 , pp. 390-400
    • Claude, P.1    Goodenough, D.A.2
  • 44
    • 0014050624 scopus 로고
    • The transport of salt and water across isolated rat ileum. Evidence for at least two distinct pathways
    • Clarkson TW. The transport of salt and water across isolated rat ileum. Evidence for at least two distinct pathways. J Gen Physiol 50: 695-727, 1967.
    • (1967) J Gen Physiol , vol.50 , pp. 695-727
    • Clarkson, T.W.1
  • 47
  • 48
    • 16844382964 scopus 로고    scopus 로고
    • CAR: a virus receptor within the tight junction
    • Coyne CB, Bergelson JM. CAR: a virus receptor within the tight junction. Adv Drug Deliv Rev 57: 869-882, 2005.
    • (2005) Adv Drug Deliv Rev , vol.57 , pp. 869-882
    • Coyne, C.B.1    Bergelson, J.M.2
  • 51
    • 0035914113 scopus 로고    scopus 로고
    • Cingulin interacts with F-actin in vitro
    • D'Atri F, Citi S. Cingulin interacts with F-actin in vitro. FEBS Lett 507: 21-24, 2001.
    • (2001) FEBS Lett , vol.507 , pp. 21-24
    • D'Atri, F.1    Citi, S.2
  • 52
    • 0037008741 scopus 로고    scopus 로고
    • Evidence for a functional interaction between cingulin and ZO-1 in cultured cells
    • D'Atri F, Nadalutti F, Citi S. Evidence for a functional interaction between cingulin and ZO-1 in cultured cells. J Biol Chem 277: 27757-27764, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 27757-27764
    • D'Atri, F.1    Nadalutti, F.2    Citi, S.3
  • 55
    • 17044406611 scopus 로고    scopus 로고
    • The dynamics and energetics of water permeation and proton exclusion in aquaporins
    • de Groot BL, Grubmüller H. The dynamics and energetics of water permeation and proton exclusion in aquaporins. Curr Opin Struct Biol 15: 176-183, 2005.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 176-183
    • de Groot, B.L.1    Grubmüller, H.2
  • 57
    • 0028220576 scopus 로고
    • Renal magnesium handling and its hormonal control
    • de Rouffignac C, Quamme G. Renal magnesium handling and its hormonal control. Physiol Rev 74: 305-322, 1994
    • (1994) Physiol Rev , vol.74 , pp. 305-322
    • de Rouffignac, C.1    Quamme, G.2
  • 59
    • 0017459472 scopus 로고
    • Twenty-first Bowditch lecture. The epithelial junction: bridge, gate, and fence
    • Diamond JM. Twenty-first Bowditch lecture. The epithelial junction: bridge, gate, and fence. Physiologist 20: 10-18, 1977
    • (1977) Physiologist , vol.20 , pp. 10-18
    • Diamond, J.M.1
  • 60
    • 0014439655 scopus 로고
    • Biological membranes: the physical basis of ion and nonelectrolyte selectivity
    • Diamond JM, Wright EM. Biological membranes: the physical basis of ion and nonelectrolyte selectivity. Annu Rev Physiol 31: 581-646, 1969.
    • (1969) Annu Rev Physiol , vol.31 , pp. 581-646
    • Diamond, J.M.1    Wright, E.M.2
  • 61
    • 67249111377 scopus 로고    scopus 로고
    • Differential phosphorylation of occludin and tricellulin by CK2 and CK1
    • Dörfel MJ, Westphal JK, Huber O. Differential phosphorylation of occludin and tricellulin by CK2 and CK1. Ann NY Acad Sci 1165: 69-73, 2009.
    • (2009) Ann NY Acad Sci , vol.1165 , pp. 69-73
    • Dörfel, M.J.1    Westphal, J.K.2    Huber, O.3
  • 62
    • 22544434673 scopus 로고    scopus 로고
    • Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells
    • D'Souza T, Agarwal R, Morin PJ. Phosphorylation of claudin-3 at threonine 192 by cAMP-dependent protein kinase regulates tight junction barrier function in ovarian cancer cells. J Biol Chem280: 26233-26240, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 26233-26240
    • D'Souza, T.1    Agarwal, R.2    Morin, P.J.3
  • 63
    • 0020505406 scopus 로고
    • Structural integrity of hepatocyte tight junctions
    • Easter DW, Wade JB, Boyer JL. Structural integrity of hepatocyte tight junctions. J Cell Biol 96: 745-749, 1983.
    • (1983) J Cell Biol , vol.96 , pp. 745-749
    • Easter, D.W.1    Wade, J.B.2    Boyer, J.L.3
  • 64
    • 40949099049 scopus 로고    scopus 로고
    • Organization of multiprotein complexes at cell-cell junctions
    • Ebnet K. Organization of multiprotein complexes at cell-cell junctions. Histochem Cell Biol 130: 1-20, 2008.
    • (2008) Histochem Cell Biol , vol.130 , pp. 1-20
    • Ebnet, K.1
  • 65
    • 73049154846 scopus 로고
    • Cation selective glass electrodes and their mode of operation
    • Eisenman G. Cation selective glass electrodes and their mode of operation. Biophys J 2: 259-323, 1962.
    • (1962) Biophys J , vol.2 , pp. 259-323
    • Eisenman, G.1
  • 66
    • 59449086585 scopus 로고    scopus 로고
    • Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions
    • Elias BC, Suzuki T, Seth A, Giorgianni F, Kale G, Shen L, Turner JR, Naren A, Desiderio DM, Rao R. Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions. J Biol Chem 284: 1559-1569, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 1559-1569
    • Elias, B.C.1    Suzuki, T.2    Seth, A.3    Giorgianni, F.4    Kale, G.5    Shen, L.6    Turner, J.R.7    Naren, A.8    Desiderio, D.M.9    Rao, R.10
  • 67
    • 49749124586 scopus 로고    scopus 로고
    • Double gene deletion reveals lack of cooperation between claudin 11 and claudin 14 tight junction proteins
    • Elkouby-Naor L, Abassi Z, Lagziel A, Gow A, Ben-Yosef T. Double gene deletion reveals lack of cooperation between claudin 11 and claudin 14 tight junction proteins. Cell Tissue Res 333: 427-438, 2008.
    • (2008) Cell Tissue Res , vol.333 , pp. 427-438
    • Elkouby-Naor, L.1    Abassi, Z.2    Lagziel, A.3    Gow, A.4    Ben-Yosef, T.5
  • 70
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273: 29745-29753, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 71
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar MG, Palade GE. Junctional complexes in various epithelia. J Cell Biol 17: 375-412, 1963.
    • (1963) J Cell Biol , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 72
    • 33749516287 scopus 로고    scopus 로고
    • Limited contribution of claudin-5-dependent tight junction strands to endothelial barrier function
    • Fontijn RD, Rohlena J, van Marle J, Pannekoek H, Horrevoets AJ. Limited contribution of claudin-5-dependent tight junction strands to endothelial barrier function. Eur J Cell Biol 85: 1131-1144, 2006.
    • (2006) Eur J Cell Biol , vol.85 , pp. 1131-1144
    • Fontijn, R.D.1    Rohlena, J.2    van Marle, J.3    Pannekoek, H.4    Horrevoets, A.J.5
  • 74
    • 0015494421 scopus 로고
    • Route of passive ion permeation in epithelia
    • Frömter E, Diamond J. Route of passive ion permeation in epithelia. Nat New Biol 235: 9-13, 1972.
    • (1972) Nat New Biol , vol.235 , pp. 9-13
    • Frömter, E.1    Diamond, J.2
  • 75
    • 1642543216 scopus 로고    scopus 로고
    • Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions
    • Fujibe M, Chiba H, Kojima T, Soma T, Wada T, Yamashita T, Sawada N. Thr203 of claudin-1, a putative phosphorylation site for MAP kinase, is required to promote the barrier function of tight junctions. Exp Cell Res 295: 36-47, 2004.
    • (2004) Exp Cell Res , vol.295 , pp. 36-47
    • Fujibe, M.1    Chiba, H.2    Kojima, T.3    Soma, T.4    Wada, T.5    Yamashita, T.6    Sawada, N.7
  • 78
    • 0034617463 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein
    • Fujita K, Katahira J, Horiguchi Y, Sonoda N, Furuse M, Tsukita S. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS Lett 476: 258-261, 2000.
    • (2000) FEBS Lett , vol.476 , pp. 258-261
    • Fujita, K.1    Katahira, J.2    Horiguchi, Y.3    Sonoda, N.4    Furuse, M.5    Tsukita, S.6
  • 79
    • 0035897412 scopus 로고    scopus 로고
    • Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells
    • Furuse M, Furuse K, Sasaki H, Tsukita S. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol 153: 236-272, 2001.
    • (2001) J Cell Biol , vol.153 , pp. 236-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 80
    • 0037128938 scopus 로고    scopus 로고
    • Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice
    • Furuse M, Hata M, Furuse K, Yoshida Y, Haratake A, Sugitani Y, Noda T, Kubo A, Tsukita S. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J Cell Biol 156: 1099-1111, 2002
    • (2002) J Cell Biol , vol.156 , pp. 1099-1111
    • Furuse, M.1    Hata, M.2    Furuse, K.3    Yoshida, Y.4    Haratake, A.5    Sugitani, Y.6    Noda, T.7    Kubo, A.8    Tsukita, S.9
  • 82
    • 0032577975 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse M, Sasaki H, Fujimoto K, Tsukita S. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol 141: 1539-1550, 1998.
    • (1998) J Cell Biol , vol.141 , pp. 1539-1550
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 83
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse M, Sasaki H, Tsukita S. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J Cell Biol 147: 891-903, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 84
    • 72949113004 scopus 로고    scopus 로고
    • Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry
    • Gao F, Duan X, Lu X, Liu Y, Zheng L, Ding Z, Li J. Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry. Biochem Biophys Res Commun 391: 952-957, 2010.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 952-957
    • Gao, F.1    Duan, X.2    Lu, X.3    Liu, Y.4    Zheng, L.5    Ding, Z.6    Li, J.7
  • 85
    • 84856321555 scopus 로고    scopus 로고
    • Sequential biphasic changes in claudin1 and claudin4 expression are correlated to colorectal cancer progression and liver metastasis
    • Georges R, Bergmann F, Hamdi H, Zepp M, Eyol E, Hielscher T, Berger MR, Adwan H. Sequential biphasic changes in claudin1 and claudin4 expression are correlated to colorectal cancer progression and liver metastasis. J Cell Mol Med 16: 142-151, 2011.
    • (2011) J Cell Mol Med , vol.16 , pp. 142-151
    • Georges, R.1    Bergmann, F.2    Hamdi, H.3    Zepp, M.4    Eyol, E.5    Hielscher, T.6    Berger, M.R.7    Adwan, H.8
  • 86
    • 0033818743 scopus 로고    scopus 로고
    • Leaks in the epithelial barrier caused by spontaneous and TNFa-induced single-cell apoptosis
    • Gitter AH, Bendfeldt K, Schulzke JD, Fromm M. Leaks in the epithelial barrier caused by spontaneous and TNFa-induced single-cell apoptosis. FASEB J 14: 1749-1753, 2000.
    • (2000) FASEB J , vol.14 , pp. 1749-1753
    • Gitter, A.H.1    Bendfeldt, K.2    Schulzke, J.D.3    Fromm, M.4
  • 88
    • 77954644289 scopus 로고    scopus 로고
    • Regulation of claudins by posttranslational modifications and cell-signaling cascades
    • González-Mariscal L, Garay E, Quirós M. Regulation of claudins by posttranslational modifications and cell-signaling cascades. Curr Top Membr 65: 113-150, 2010
    • (2010) Curr Top Membr , vol.65 , pp. 113-150
    • González-Mariscal, L.1    Garay, E.2    Quirós, M.3
  • 89
  • 94
    • 64149132666 scopus 로고    scopus 로고
    • Function and regulation of claudins in the thick ascending limb of Henle
    • Günzel D, Yu ASL. Function and regulation of claudins in the thick ascending limb of Henle. Pflügers Arch. 458: 77-88, 2009.
    • (2009) Pflügers Arch. , vol.458 , pp. 77-88
    • Günzel, D.1    Yu, A.S.L.2
  • 95
    • 39849103311 scopus 로고    scopus 로고
    • The cytoplasmic plaque of tight junctions: A scaffolding and signalling center
    • Guillemot L, Paschoud S, Pulimeno P, Foglia A, Citi S. The cytoplasmic plaque of tight junctions: A scaffolding and signalling center. Biochim Biophys Acta 1778: 601-613, 2008.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 601-613
    • Guillemot, L.1    Paschoud, S.2    Pulimeno, P.3    Foglia, A.4    Citi, S.5
  • 96
    • 0004061828 scopus 로고
    • Critical permeation size of dextran molecules
    • Haller W. Critical permeation size of dextran molecules. Macromolecules 10: 83-86, 1977.
    • (1977) Macromolecules , vol.10 , pp. 83-86
    • Haller, W.1
  • 98
    • 77949686964 scopus 로고    scopus 로고
    • Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis
    • Han G, Ye M, Liu H, Song C, Sun D, Wu Y, Jiang X, Chen R, Wang C, Wang L, Zou H. Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis. Electrophoresis 31: 1080-1089, 2010.
    • (2010) Electrophoresis , vol.31 , pp. 1080-1089
    • Han, G.1    Ye, M.2    Liu, H.3    Song, C.4    Sun, D.5    Wu, Y.6    Jiang, X.7    Chen, R.8    Wang, C.9    Wang, L.10    Zou, H.11
  • 99
    • 74349087513 scopus 로고    scopus 로고
    • Ascorbate protects endothelial barrier function during septic insult: role of protein phosphatase type 2A
    • Han M, Pendem S, Teh SL, Sukumaran DK, Wu F, Wilson JX. Ascorbate protects endothelial barrier function during septic insult: role of protein phosphatase type 2A. Free Radic Biol Med 48: 128-135, 2010.
    • (2010) Free Radic Biol Med , vol.48 , pp. 128-135
    • Han, M.1    Pendem, S.2    Teh, S.L.3    Sukumaran, D.K.4    Wu, F.5    Wilson, J.X.6
  • 100
    • 44649142476 scopus 로고    scopus 로고
    • SnapShot: Tight and adherens junction signaling
    • Harder JL, Margolis B. SnapShot: Tight and adherens junction signaling. Cell 133: 1118.e1-2, 2008.
    • (2008) Cell , vol.133
    • Harder, J.L.1    Margolis, B.2
  • 101
    • 39849100440 scopus 로고    scopus 로고
    • Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
    • Hartsock A, Nelson WJ. Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton. Biochim Biophys Acta 1778: 660-669, 2008.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 660-669
    • Hartsock, A.1    Nelson, W.J.2
  • 103
    • 54349114505 scopus 로고    scopus 로고
    • Epithelial apoptosis is a prominent feature of the epithelial barrier disturbance in intestinal inflammation: Effect of pro-inflammatory interleukin-13 on epithelial cell function
    • Heller F, Fromm A, Gitter AH, Mankertz J, Schulzke JD. Epithelial apoptosis is a prominent feature of the epithelial barrier disturbance in intestinal inflammation: Effect of pro-inflammatory interleukin-13 on epithelial cell function. Mucosal Immunol 1(Suppl 1): S58-S61, 2008.
    • (2008) Mucosal Immunol , vol.1 , Issue.SUPPL. 1
    • Heller, F.1    Fromm, A.2    Gitter, A.H.3    Mankertz, J.4    Schulzke, J.D.5
  • 104
    • 79955504880 scopus 로고    scopus 로고
    • Transforming growth factor ß, a whey protein component, strengthens the intestinal barrier by upregulating claudin-4 in HT-29/B6 cells
    • Hering NA, Andres S, Fromm A, van Tol EA, Amasheh M, Mankertz J, Fromm M, Schulzke JD. Transforming growth factor ß, a whey protein component, strengthens the intestinal barrier by upregulating claudin-4 in HT-29/B6 cells. J Nutr 141: 783-789, 2011.
    • (2011) J Nutr , vol.141 , pp. 783-789
    • Hering, N.A.1    Andres, S.2    Fromm, A.3    van Tol, E.A.4    Amasheh, M.5    Mankertz, J.6    Fromm, M.7    Schulzke, J.D.8
  • 106
    • 33847127375 scopus 로고    scopus 로고
    • The claudin gene family: Expression in normal and neoplastic tissues
    • Hewitt KJ, Agarwal R, Morin PJ. The claudin gene family: Expression in normal and neoplastic tissues. BMC Cancer 6: 186, 2006.
    • (2006) BMC Cancer , vol.6 , pp. 186
    • Hewitt, K.J.1    Agarwal, R.2    Morin, P.J.3
  • 107
    • 33646792959 scopus 로고    scopus 로고
    • Claudin profiling in the mouse during postnatal intestinal development and along the gastrointestinal tract reveals complex expression patterns
    • Holmes JL, Van Itallie CM, Rasmussen JE, Anderson JM. Claudin profiling in the mouse during postnatal intestinal development and along the gastrointestinal tract reveals complex expression patterns. Gene Expr Patterns 6: 581-588, 2006.
    • (2006) Gene Expr Patterns , vol.6 , pp. 581-588
    • Holmes, J.L.1    Van Itallie, C.M.2    Rasmussen, J.E.3    Anderson, J.M.4
  • 108
    • 56349169898 scopus 로고    scopus 로고
    • Molecular mechanism of intestinal permeability: Interaction at tight junctions
    • Hossain Z, Hirata T. Molecular mechanism of intestinal permeability: Interaction at tight junctions. Mol Biosyst 4: 1181-1185, 2008.
    • (2008) Mol Biosyst , vol.4 , pp. 1181-1185
    • Hossain, Z.1    Hirata, T.2
  • 109
    • 27944501678 scopus 로고    scopus 로고
    • Paracellin-1 and the modulation of ion selectivity of tight junctions
    • Hou J, Paul DL, Goodenough DA. Paracellin-1 and the modulation of ion selectivity of tight junctions. J Cell Sci 118: 5109-5118, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 5109-5118
    • Hou, J.1    Paul, D.L.2    Goodenough, D.A.3
  • 110
  • 111
    • 70349326768 scopus 로고    scopus 로고
    • Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium
    • Hou J, Renigunta A, Gomes AS, Hou M, Paul DL, Waldegger S, Goodenough DA. Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium. Proc Natl Acad Sci U S A 106: 15350-15355, 2009.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 15350-15355
    • Hou, J.1    Renigunta, A.2    Gomes, A.S.3    Hou, M.4    Paul, D.L.5    Waldegger, S.6    Goodenough, D.A.7
  • 113
    • 78149272646 scopus 로고    scopus 로고
    • Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization
    • Hou J, Renigunta A, Yang J, Waldegger S. Claudin-4 forms paracellular chloride channel in the kidney and requires claudin-8 for tight junction localization. Proc Natl Acad Sci U S A 107: 18010-18015, 2010.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18010-18015
    • Hou, J.1    Renigunta, A.2    Yang, J.3    Waldegger, S.4
  • 115
    • 11144243665 scopus 로고    scopus 로고
    • Association of paracellin-1 with ZO-1 augments the reabsorption of divalent cations in renal epithelial cells
    • Ikari A, Hirai N, Shiroma M, Harada H, Sakai H, Hayashi H, Suzuki Y, Degawa M, Takagi K. Association of paracellin-1 with ZO-1 augments the reabsorption of divalent cations in renal epithelial cells. J Biol Chem 279: 54826-54832, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 54826-54832
    • Ikari, A.1    Hirai, N.2    Shiroma, M.3    Harada, H.4    Sakai, H.5    Hayashi, H.6    Suzuki, Y.7    Degawa, M.8    Takagi, K.9
  • 117
    • 33744544786 scopus 로고    scopus 로고
    • Phosphorylation of paracellin-1 at Ser217 by protein kinase A is essential for localization in tight junctions
    • Ikari A, Matsumoto S, Harada H, Takagi K, Hayashi H, Suzuki Y, Degawa M, Miwa M. Phosphorylation of paracellin-1 at Ser217 by protein kinase A is essential for localization in tight junctions. J Cell Sci 119: 1781-1789, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 1781-1789
    • Ikari, A.1    Matsumoto, S.2    Harada, H.3    Takagi, K.4    Hayashi, H.5    Suzuki, Y.6    Degawa, M.7    Miwa, M.8
  • 119
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S, Tsukita S. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J Cell Biol 171: 939-945, 2005.
    • (2005) J Cell Biol , vol.171 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Tsukita, S.6
  • 120
  • 121
    • 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 78: 849-855, 1999.
    • (1999) Eur J Cell Biol , vol.78 , pp. 849-855
    • Inai, T.1    Kobayashi, J.2    Shibata, Y.3
  • 122
    • 77952011552 scopus 로고    scopus 로고
    • The protoplasmic or exoplasmic face association of tight junction particles cannot predict paracellular permeability or heterotypic claudin compatibility
    • Inai T, Kamimura T, Hirose E, Iida H, Shibata Y. The protoplasmic or exoplasmic face association of tight junction particles cannot predict paracellular permeability or heterotypic claudin compatibility. Eur J Cell Biol 89: 547-556, 2010.
    • (2010) Eur J Cell Biol , vol.89 , pp. 547-556
    • Inai, T.1    Kamimura, T.2    Hirose, E.3    Iida, H.4    Shibata, Y.5
  • 123
    • 33645119393 scopus 로고    scopus 로고
    • Heterogeneity in expression and subcellular localization of tight junction proteins, claudin-10 and -15, examined by RT-PCR and immunofluorescence microscopy
    • Inai T, Sengoku A, Guan X, Hirose E, Iida H, Shibata Y. Heterogeneity in expression and subcellular localization of tight junction proteins, claudin-10 and -15, examined by RT-PCR and immunofluorescence microscopy. Arch Histol Cytol 68: 349-360, 2005.
    • (2005) Arch Histol Cytol , vol.68 , pp. 349-360
    • Inai, T.1    Sengoku, A.2    Guan, X.3    Hirose, E.4    Iida, H.5    Shibata, Y.6
  • 124
    • 39149138174 scopus 로고    scopus 로고
    • Comparative characterization of mouse rectum CMT93-I and -II cells by expression of claudin isoforms and tight junction morphology and function
    • Inai T, Sengoku A, Hirose E, Iida H, Shibata Y. Comparative characterization of mouse rectum CMT93-I and -II cells by expression of claudin isoforms and tight junction morphology and function. Histochem Cell Biol 129: 223-232, 2008.
    • (2008) Histochem Cell Biol , vol.129 , pp. 223-232
    • Inai, T.1    Sengoku, A.2    Hirose, E.3    Iida, H.4    Shibata, Y.5
  • 125
    • 0142026252 scopus 로고    scopus 로고
    • Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways
    • Ishizaki T, Chiba H, Kojima T, Fujibe M, Soma T, Miyajima H, Nagasawa K, Wada I, Sawada N. Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways. Exp Cell Res 290: 275-288, 2003.
    • (2003) Exp Cell Res , vol.290 , pp. 275-288
    • Ishizaki, T.1    Chiba, H.2    Kojima, T.3    Fujibe, M.4    Soma, T.5    Miyajima, H.6    Nagasawa, K.7    Wada, I.8    Sawada, N.9
  • 126
  • 128
    • 38649090109 scopus 로고    scopus 로고
    • Bradykinin does not induce gap formation between human endothelial cells
    • Jungmann P, Wilhelmi M, Oberleithner H, Riethmüller C. Bradykinin does not induce gap formation between human endothelial cells. Pflügers Arch 455: 1007-1016, 2008.
    • (2008) Pflügers Arch , vol.455 , pp. 1007-1016
    • Jungmann, P.1    Wilhelmi, M.2    Oberleithner, H.3    Riethmüller, C.4
  • 129
    • 0030846016 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin
    • Katahira J, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N. Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin. J Cell Biol 136: 1239-1247, 1997.
    • (1997) J Cell Biol , vol.136 , pp. 1239-1247
    • Katahira, J.1    Inoue, N.2    Horiguchi, Y.3    Matsuda, M.4    Sugimoto, N.5
  • 131
    • 48249090849 scopus 로고    scopus 로고
    • Identification of a novel intracellular interaction domain essential for Bves function
    • Kawaguchi M, Hager HA, Wada A, Koyama T, Chang MS, Bader DM. Identification of a novel intracellular interaction domain essential for Bves function. PLoS One 3: e2261, 2008.
    • (2008) PLoS One , vol.3
    • Kawaguchi, M.1    Hager, H.A.2    Wada, A.3    Koyama, T.4    Chang, M.S.5    Bader, D.M.6
  • 132
  • 133
    • 0036208599 scopus 로고    scopus 로고
    • Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments
    • Kiuchi-Saishin Y, Gotoh S, Furuse M, Takasuga A, Tano Y, Tsukita S. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J Am Soc Nephrol 13: 875-886, 2002.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 875-886
    • Kiuchi-Saishin, Y.1    Gotoh, S.2    Furuse, M.3    Takasuga, A.4    Tano, Y.5    Tsukita, S.6
  • 134
    • 0041355489 scopus 로고    scopus 로고
    • Membrane topology of Bves/Pop1A, a cell adhesion molecule that displays dynamic changes in cellular distribution during development
    • Knight RF, Bader DM, Backstrom JR. Membrane topology of Bves/Pop1A, a cell adhesion molecule that displays dynamic changes in cellular distribution during development. J Biol Chem278: 32872-3289, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 32872-3289
    • Knight, R.F.1    Bader, D.M.2    Backstrom, J.R.3
  • 135
    • 23144449383 scopus 로고    scopus 로고
    • Tight junction: A co-ordinator of cell signalling and membrane trafficking
    • Köhler K, Zahraoui A. Tight junction: A co-ordinator of cell signalling and membrane trafficking. Biol Cell 97: 659-665, 2005.
    • (2005) Biol Cell , vol.97 , pp. 659-665
    • Köhler, K.1    Zahraoui, A.2
  • 138
    • 34247842900 scopus 로고    scopus 로고
    • Hypoxia disrupts the barrier function of neural blood vessels through changes in the expression of claudin-5 in endothelial cells
    • Koto T, Takubo K, Ishida S, Shinoda H, Inoue M, Tsubota K, Okada Y, Ikeda E. Hypoxia disrupts the barrier function of neural blood vessels through changes in the expression of claudin-5 in endothelial cells. Am J Pathol 170: 1389-1397, 2007.
    • (2007) Am J Pathol , vol.170 , pp. 1389-1397
    • Koto, T.1    Takubo, K.2    Ishida, S.3    Shinoda, H.4    Inoue, M.5    Tsubota, K.6    Okada, Y.7    Ikeda, E.8
  • 139
    • 40949123971 scopus 로고    scopus 로고
    • Transforming growth factor-beta induces epithelial to mesenchymal transition by down-regulation of claudin-1 expression and the fence function in adult rat hepatocytes
    • Kojima T, Takano K, Yamamoto T, Murata M, Son S, Imamura M, Yamaguchi H, Osanai M, Chiba H, Himi T, Sawada N. Transforming growth factor-beta induces epithelial to mesenchymal transition by down-regulation of claudin-1 expression and the fence function in adult rat hepatocytes. Liver Int 28: 534-545, 2008.
    • (2008) Liver Int , vol.28 , pp. 534-545
    • Kojima, T.1    Takano, K.2    Yamamoto, T.3    Murata, M.4    Son, S.5    Imamura, M.6    Yamaguchi, H.7    Osanai, M.8    Chiba, H.9    Himi, T.10    Sawada, N.11
  • 142
    • 70449107587 scopus 로고    scopus 로고
    • Two-path impedance spectroscopy for measurement of paracellular and transcellular epithelial resistance
    • Krug SM, Fromm M, Günzel D. Two-path impedance spectroscopy for measurement of paracellular and transcellular epithelial resistance. Biophys J 97: 2202-2211, 2009b.
    • (2009) Biophys J , vol.97 , pp. 2202-2211
    • Krug, S.M.1    Fromm, M.2    Günzel, D.3
  • 148
    • 49049111072 scopus 로고    scopus 로고
    • Probing effects of pH change on dynamic response of Claudin-2 mediated adhesion using single molecule force spectroscopy
    • Lim TS, Vedula SR, Hui S, Kausalya PJ, Hunziker W, Lim CT. Probing effects of pH change on dynamic response of Claudin-2 mediated adhesion using single molecule force spectroscopy. Exp Cell Res 314: 2643-2651, 2008.
    • (2008) Exp Cell Res , vol.314 , pp. 2643-2651
    • Lim, T.S.1    Vedula, S.R.2    Hui, S.3    Kausalya, P.J.4    Hunziker, W.5    Lim, C.T.6
  • 149
    • 48049122836 scopus 로고    scopus 로고
    • Kinetics of adhesion mediated by extracellular loops of claudin-2 as revealed by single-molecule force spectroscopy
    • Lim TS, Vedula SR, Hunziker W, Lim CT. Kinetics of adhesion mediated by extracellular loops of claudin-2 as revealed by single-molecule force spectroscopy. J Mol Biol 381: 681-691, 2008.
    • (2008) J Mol Biol , vol.381 , pp. 681-691
    • Lim, T.S.1    Vedula, S.R.2    Hunziker, W.3    Lim, C.T.4
  • 150
    • 3543049587 scopus 로고    scopus 로고
    • Extensive expansion of the claudin gene family in the teleost fish, Fugu rubripes
    • Loh YH, Christoffels A, Brenner S, Hunziker W, Venkatesh B. Extensive expansion of the claudin gene family in the teleost fish, Fugu rubripes. Genome Res 14: 1248-1257, 2004.
    • (2004) Genome Res , vol.14 , pp. 1248-1257
    • Loh, Y.H.1    Christoffels, A.2    Brenner, S.3    Hunziker, W.4    Venkatesh, B.5
  • 154
    • 0015108839 scopus 로고
    • Localization of permeability barriers in the frog skin epithelium
    • Martinez-Palomo A, Erlij D, Bracho H. Localization of permeability barriers in the frog skin epithelium. J Cell Biol 50: 277-287, 1971.
    • (1971) J Cell Biol , vol.50 , pp. 277-287
    • Martinez-Palomo, A.1    Erlij, D.2    Bracho, H.3
  • 156
    • 1842426940 scopus 로고    scopus 로고
    • A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells
    • Supplemental movies
    • Matsuda M, Kubo A, Furuse M, Tsukita S. A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells. J Cell Sci 117: 1247-1257, 2004. Supplemental movies: http://jcs.biologists.org/content/117/7/1247/suppl/DC1.
    • (2004) J Cell Sci , vol.117 , pp. 1247-1257
    • Matsuda, M.1    Kubo, A.2    Furuse, M.3    Tsukita, S.4
  • 158
    • 24644496823 scopus 로고    scopus 로고
    • Mammalian tight junctions in the regulation of epithelial differentiation and proliferation
    • Matter K, Aijaz S, Tsapara A, Balda MS. Mammalian tight junctions in the regulation of epithelial differentiation and proliferation. Curr Opin Cell Biol 17: 453-458, 2005.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 453-458
    • Matter, K.1    Aijaz, S.2    Tsapara, A.3    Balda, M.S.4
  • 162
    • 61549107578 scopus 로고    scopus 로고
    • Expression of tight and adherens junction proteins in ulcerative colitis associated colorectal carcinoma: Upregulation of claudin-1, claudin-3, claudin-4, and beta-catenin
    • Mees ST, Mennigen R, Spieker T, Rijcken E, Senninger N, Haier J, Bruewer M. Expression of tight and adherens junction proteins in ulcerative colitis associated colorectal carcinoma: Upregulation of claudin-1, claudin-3, claudin-4, and beta-catenin. Int J Colorect Dis 24: 361-368. 2009.
    • (2009) Int J Colorect Dis , vol.24 , pp. 361-368
    • Mees, S.T.1    Mennigen, R.2    Spieker, T.3    Rijcken, E.4    Senninger, N.5    Haier, J.6    Bruewer, M.7
  • 163
    • 66149090738 scopus 로고    scopus 로고
    • Probiotic mixture VSL#3 protects the epithelial barrier by maintaining tight junction protein expression and preventing apoptosis in a murine model of colitis
    • Mennigen R, Nolte K, Rijcken E, Utech M, Loeffler B, Senninger N, Bruewer M. Probiotic mixture VSL#3 protects the epithelial barrier by maintaining tight junction protein expression and preventing apoptosis in a murine model of colitis. Am J Physiol Gastrointest Liver Physiol 296: G1140-G1149, 2009.
    • (2009) Am J Physiol Gastrointest Liver Physiol , vol.296
    • Mennigen, R.1    Nolte, K.2    Rijcken, E.3    Utech, M.4    Loeffler, B.5    Senninger, N.6    Bruewer, M.7
  • 164
    • 26244441572 scopus 로고    scopus 로고
    • PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells
    • Michel D, Arsanto JP, Massey-Harroche D, Béclin C, Wijnholds J, Le Bivic A. PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells. J Cell Sci 118: 4049-4057, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 4049-4057
    • Michel, D.1    Arsanto, J.P.2    Massey-Harroche, D.3    Béclin, C.4    Wijnholds, J.5    Le Bivic, A.6
  • 166
    • 34249297638 scopus 로고    scopus 로고
    • Claudin-based permeability barriers in taste buds
    • Michlig S, Damak S, Le Coutre J. Claudin-based permeability barriers in taste buds. J Comp Neurol 502: 1003-1011, 2007
    • (2007) J Comp Neurol , vol.502 , pp. 1003-1011
    • Michlig, S.1    Damak, S.2    Le Coutre, J.3
  • 169
    • 0037304386 scopus 로고    scopus 로고
    • Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4
    • Mitic LL, Unger VM, Anderson JM. Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Protein Sci 12: 218-227, 2003.
    • (2003) Protein Sci , vol.12 , pp. 218-227
    • Mitic, L.L.1    Unger, V.M.2    Anderson, J.M.3
  • 171
    • 16844365885 scopus 로고    scopus 로고
    • Molecular perspective on tight-junction assembly and epithelial polarity
    • Miyoshi J, Takai Y. Molecular perspective on tight-junction assembly and epithelial polarity. Adv Drug Deliv Rev 57: 815-855, 2005.
    • (2005) Adv Drug Deliv Rev , vol.57 , pp. 815-855
    • Miyoshi, J.1    Takai, Y.2
  • 172
    • 27544448588 scopus 로고    scopus 로고
    • Claudin proteins in human cancer: Promising new targets for diagnosis and therapy
    • Morin PJ. Claudin proteins in human cancer: Promising new targets for diagnosis and therapy. Cancer Res 65: 9603-9606, 2005.
    • (2005) Cancer Res , vol.65 , pp. 9603-9606
    • Morin, P.J.1
  • 173
    • 36549025937 scopus 로고    scopus 로고
    • Claudin proteins in ovarian cancer
    • Morin PJ. Claudin proteins in ovarian cancer. Dis Markers 23: 453-457, 2007.
    • (2007) Dis Markers , vol.23 , pp. 453-457
    • Morin, P.J.1
  • 174
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita K, Furuse M, Fujimoto K, Tsukita S. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci U S A 96: 511-516, 1999.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 175
    • 0036280768 scopus 로고    scopus 로고
    • Molecular architecture of tight junctions of periderm differs from that of the maculae occludentes of epidermis
    • Morita K, Furuse M, Yoshida Y, Itoh M, Sasaki H, Tsukita S, Miyachi Y. Molecular architecture of tight junctions of periderm differs from that of the maculae occludentes of epidermis. J Invest Dermatol 118: 1073-1079, 2002.
    • (2002) J Invest Dermatol , vol.118 , pp. 1073-1079
    • Morita, K.1    Furuse, M.2    Yoshida, Y.3    Itoh, M.4    Sasaki, H.5    Tsukita, S.6    Miyachi, Y.7
  • 176
    • 13544260880 scopus 로고    scopus 로고
    • The tight junction protein occludin and the adherens junction protein a-catenin share a common interaction mechanism with ZO-1
    • Müller SL, Portwich M, Schmidt A, Utepbergenov DI, Huber O, Blasig IE, Krause G. The tight junction protein occludin and the adherens junction protein a-catenin share a common interaction mechanism with ZO-1. J Biol Chem 280: 3747-3756, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 3747-3756
    • Müller, S.L.1    Portwich, M.2    Schmidt, A.3    Utepbergenov, D.I.4    Huber, O.5    Blasig, I.E.6    Krause, G.7
  • 177
    • 1542380399 scopus 로고    scopus 로고
    • Epithelial barriers, compartmentation, and cancer
    • Mullin JM. Epithelial barriers, compartmentation, and cancer. Science STKE 2004: pe2, 2004.
    • (2004) Science STKE , vol.2004
    • Mullin, J.M.1
  • 178
    • 68949129005 scopus 로고    scopus 로고
    • Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeability
    • Murakami T, Felinski EA, Antonetti DA. Occludin phosphorylation and ubiquitination regulate tight junction trafficking and vascular endothelial growth factor-induced permeability. J Biol Chem 284: 21036-21046, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 21036-21046
    • Murakami, T.1    Felinski, E.A.2    Antonetti, D.A.3
  • 180
    • 10944228240 scopus 로고    scopus 로고
    • The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells
    • Nava P, López S, Arias CF, Islas S, González-Mariscal L. The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells. J Cell Sci 117: 5509-5519, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 5509-5519
    • Nava, P.1    López, S.2    Arias, C.F.3    Islas, S.4    González-Mariscal, L.5
  • 181
    • 0034787457 scopus 로고    scopus 로고
    • Claudin-18, a novel downstream target gene for the T/EBP/NKX2.1 homeodomain transcription factor, encodes lung- and stomach-specific isoforms through alternative splicing
    • Niimi T, Nagashima K, Ward JM, Minoo P, Zimonjic DB, Popescu NC, Kimura S. Claudin-18, a novel downstream target gene for the T/EBP/NKX2.1 homeodomain transcription factor, encodes lung- and stomach-specific isoforms through alternative splicing. Mol Cell Biol 21: 7380-7390, 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 7380-7390
    • Niimi, T.1    Nagashima, K.2    Ward, J.M.3    Minoo, P.4    Zimonjic, D.B.5    Popescu, N.C.6    Kimura, S.7
  • 183
    • 0037009005 scopus 로고    scopus 로고
    • Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight jucntion complex
    • Nunbhakdi-Craig V, Machleidt T, Ogris E, Bellotto D, White CL, Sontag E. Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight jucntion complex. J Cell Biol 158: 967-978, 2002.
    • (2002) J Cell Biol , vol.158 , pp. 967-978
    • Nunbhakdi-Craig, V.1    Machleidt, T.2    Ogris, E.3    Bellotto, D.4    White, C.L.5    Sontag, E.6
  • 184
    • 37249018598 scopus 로고    scopus 로고
    • mRNA expression levels of tight junction protein genes in mouse brain capillary endothelial cells highly purified by magnetic cell sorting
    • Ohtsuki S, Yamaguchi H, Katsukura Y, Asashima T, Terasaki T. mRNA expression levels of tight junction protein genes in mouse brain capillary endothelial cells highly purified by magnetic cell sorting. J Neurochem 104: 147-154, 2008.
    • (2008) J Neurochem , vol.104 , pp. 147-154
    • Ohtsuki, S.1    Yamaguchi, H.2    Katsukura, Y.3    Asashima, T.4    Terasaki, T.5
  • 185
    • 33846476587 scopus 로고    scopus 로고
    • Claudins: Multifunctional players in epithelial tight junctions and their role in cancer
    • Oliveira SS, Morgado-Díaz JA. Claudins: Multifunctional players in epithelial tight junctions and their role in cancer. Cell Mol Life Sci 64: 17-28, 2006.
    • (2006) Cell Mol Life Sci , vol.64 , pp. 17-28
    • Oliveira, S.S.1    Morgado-Díaz, J.A.2
  • 186
    • 57449095650 scopus 로고    scopus 로고
    • Changes in the expression of claudins in active ulcerative colitis
    • Oshima T, Miwa H, Takashi Joh T. Changes in the expression of claudins in active ulcerative colitis. J Gastroenterol Hepatol 23(Suppl. 2): S146-S150, 2008.
    • (2008) J Gastroenterol Hepatol , vol.23 , Issue.SUPPL. 2
    • Oshima, T.1    Miwa, H.2    Takashi Joh, T.3
  • 187
    • 33644879427 scopus 로고    scopus 로고
    • Bves, a member of the Popeye domaincontaining gene family
    • Osler ME, Smith TK, Bader DM. Bves, a member of the Popeye domaincontaining gene family. Dev Dyn 235: 586-593, 2006.
    • (2006) Dev Dyn , vol.235 , pp. 586-593
    • Osler, M.E.1    Smith, T.K.2    Bader, D.M.3
  • 188
    • 74749100893 scopus 로고    scopus 로고
    • Claudins in human cancer: A review
    • Ouban A, Ahmed AA. Claudins in human cancer: A review. Histol Histopathol 25: 83-90, 2010.
    • (2010) Histol Histopathol , vol.25 , pp. 83-90
    • Ouban, A.1    Ahmed, A.A.2
  • 189
    • 0032535154 scopus 로고    scopus 로고
    • Genes for the CPE receptor (CPETR1) and the human homolog of RVP1 (CPETR2) are localized within theWilliams-Beuren Syndrome deletion
    • Paperna T, Peoples R, Wang YK, Kaplan P, Francke U. Genes for the CPE receptor (CPETR1) and the human homolog of RVP1 (CPETR2) are localized within theWilliams-Beuren Syndrome deletion. Genomics 54: 453-459, 1998.
    • (1998) Genomics , vol.54 , pp. 453-459
    • Paperna, T.1    Peoples, R.2    Wang, Y.K.3    Kaplan, P.4    Francke, U.5
  • 190
    • 79955931428 scopus 로고    scopus 로고
    • Claudin-19 and the barrier properties of the human retinal pigment epithelium
    • Peng S, Rao VS, Adelman RA, Rizzolo LJ. Claudin-19 and the barrier properties of the human retinal pigment epithelium. Invest Ophthalmol Vis Sci 52: 1392-1403, 2011.
    • (2011) Invest Ophthalmol Vis Sci , vol.52 , pp. 1392-1403
    • Peng, S.1    Rao, V.S.2    Adelman, R.A.3    Rizzolo, L.J.4
  • 192
    • 77953021608 scopus 로고    scopus 로고
    • Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules
    • Piehl C, Piontek J, Cording J, Wolburg H, Blasig IE. Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules. Cell Mol Life Sci 67: 2131-2140, 2010.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2131-2140
    • Piehl, C.1    Piontek, J.2    Cording, J.3    Wolburg, H.4    Blasig, I.E.5
  • 196
    • 77950663681 scopus 로고    scopus 로고
    • Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functions
    • Raleigh DR, Marchiando AM, Zhang Y, Shen L, Sasaki H, Wang Y, Long M, Turner JR. Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functions. Mol Biol Cell 21: 1200-1213, 2010.
    • (2010) Mol Biol Cell , vol.21 , pp. 1200-1213
    • Raleigh, D.R.1    Marchiando, A.M.2    Zhang, Y.3    Shen, L.4    Sasaki, H.5    Wang, Y.6    Long, M.7    Turner, J.R.8
  • 197
    • 16444374786 scopus 로고    scopus 로고
    • Claudin-1 is a strong prognostic indicator in stage II colonic cancer: a tissue microarray study
    • Resnick MB, Konkin T, Routhier J, Sabo E, Pricolo VE. Claudin-1 is a strong prognostic indicator in stage II colonic cancer: a tissue microarray study. Mod Pathol 18: 511-518. 2004.
    • (2004) Mod Pathol , vol.18 , pp. 511-518
    • Resnick, M.B.1    Konkin, T.2    Routhier, J.3    Sabo, E.4    Pricolo, V.E.5
  • 199
    • 34547287033 scopus 로고    scopus 로고
    • Analysis of the RPE transcriptome reveals dynamic changes during the development of the outer blood-retinal barrier
    • Rizzolo LJ, Chen X, Weitzman M, Sun R, Zhang H. Analysis of the RPE transcriptome reveals dynamic changes during the development of the outer blood-retinal barrier. Mol Vis 13: 1259-1273, 2007.
    • (2007) Mol Vis , vol.13 , pp. 1259-1273
    • Rizzolo, L.J.1    Chen, X.2    Weitzman, M.3    Sun, R.4    Zhang, H.5
  • 201
    • 77955124560 scopus 로고    scopus 로고
    • Enterohemorrhagic E. coli alters murine intestinal epithelial tight junction protein expression and barrier function in Shiga toxin independent manner
    • Roxas JL, Koutsouris A, Bellmeyer A, Tesfay S, Royan S, Falzari K, Harris A, Cheng H, Rhee KJ, Hecht G. Enterohemorrhagic E. coli alters murine intestinal epithelial tight junction protein expression and barrier function in Shiga toxin independent manner. Lab Invest 90: 1152-1168, 2010.
    • (2010) Lab Invest , vol.90 , pp. 1152-1168
    • Roxas, J.L.1    Koutsouris, A.2    Bellmeyer, A.3    Tesfay, S.4    Royan, S.5    Falzari, K.6    Harris, A.7    Cheng, H.8    Rhee, K.J.9    Hecht, G.10
  • 202
    • 0026607192 scopus 로고
    • Iontophoretic permeability of polyethylene glycols through hairless rat skin: application of hydrodynamic theory for hindered transport through liquid filled pores
    • Ruddy SB, Hadzija BW. Iontophoretic permeability of polyethylene glycols through hairless rat skin: application of hydrodynamic theory for hindered transport through liquid filled pores. Drug Des Discov 8: 207-224. 1992.
    • (1992) Drug Des Discov , vol.8 , pp. 207-224
    • Ruddy, S.B.1    Hadzija, B.W.2
  • 205
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou M, Fujimoto K, Doi Y, Itoh M, Fujimoto T, Furuse M, Takano H, Noda T, Tsukita S. Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J Cell Biol 141: 397-408, 1998
    • (1998) J Cell Biol , vol.141 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3    Itoh, M.4    Fujimoto, T.5    Furuse, M.6    Takano, H.7    Noda, T.8    Tsukita, S.9
  • 207
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara A, Furuse M, Saitou M, Ando-Akatsuka Y, Tsukita S. Possible involvement of phosphorylation of occludin in tight junction formation. J Cell Biol 137: 1393-1401. 1997.
    • (1997) J Cell Biol , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 208
    • 67649344470 scopus 로고    scopus 로고
    • Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells
    • Sallee JL, Burridge K. Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J Biol Chem 284: 14997-15006, 2009
    • (2009) J Biol Chem , vol.284 , pp. 14997-15006
    • Sallee, J.L.1    Burridge, K.2
  • 209
    • 24044493977 scopus 로고    scopus 로고
    • Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins
    • Sander GR, Cummins AG, Powell BC. Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins. FEBS Letters 579: 4851-4855, 2005.
    • (2005) FEBS Letters , vol.579 , pp. 4851-4855
    • Sander, G.R.1    Cummins, A.G.2    Powell, B.C.3
  • 210
    • 15444373200 scopus 로고    scopus 로고
    • Pathogenesis of diarrhea in ulcerative colitis: new views on an old problem
    • Sandle GI. Pathogenesis of diarrhea in ulcerative colitis: new views on an old problem. J Clin Gastroenterol 39: S49-S52, 2005.
    • (2005) J Clin Gastroenterol , vol.39
    • Sandle, G.I.1
  • 211
    • 57349141890 scopus 로고    scopus 로고
    • Effect of claudins 6 and 9 on paracellular permeability in MDCK II cells
    • Sas D, Hu M, Moe OW, Baum M. Effect of claudins 6 and 9 on paracellular permeability in MDCK II cells. Am J Physiol Regul Integr Comp Physiol 295: 1713-1719, 2008.
    • (2008) Am J Physiol Regul Integr Comp Physiol , vol.295 , pp. 1713-1719
    • Sas, D.1    Hu, M.2    Moe, O.W.3    Baum, M.4
  • 213
    • 0015353525 scopus 로고
    • Electrical potential differences and electromotive forces in epithelial tissues
    • Schultz SG. Electrical potential differences and electromotive forces in epithelial tissues. J Gen Physiol 59: 794-798, 1972.
    • (1972) J Gen Physiol , vol.59 , pp. 794-798
    • Schultz, S.G.1
  • 217
    • 67249109157 scopus 로고    scopus 로고
    • Mechanisms of outside-in signaling at the tight junction by junctional adhesion molecule A
    • Severson EA, Parkos CA. Mechanisms of outside-in signaling at the tight junction by junctional adhesion molecule A. Ann N Y Acad Sci 1165: 10-18, 2009.
    • (2009) Ann N Y Acad Sci , vol.1165 , pp. 10-18
    • Severson, E.A.1    Parkos, C.A.2
  • 219
    • 44149105668 scopus 로고    scopus 로고
    • The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state
    • Shen L, Weber CR, Turner JR. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J Cell Biol 181: 683-695, 2008.
    • (2008) J Cell Biol , vol.181 , pp. 683-695
    • Shen, L.1    Weber, C.R.2    Turner, J.R.3
  • 220
    • 34249668828 scopus 로고    scopus 로고
    • Protein phosphatase 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer
    • Seth A, Sheth P, Elias BC, Rao R. Protein phosphatase 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer. J Biol Chem 282: 11487-11498, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 11487-11498
    • Seth, A.1    Sheth, P.2    Elias, B.C.3    Rao, R.4
  • 221
    • 34547096543 scopus 로고    scopus 로고
    • Lipopolysaccharide disrupts tight junctions in cholangiocyte monolayers by a c-Src-, TLR4-, and LBP-dependent mechanism
    • Sheth P, Delos Santos N, Seth A, LaRusso NF, Rao RK. Lipopolysaccharide disrupts tight junctions in cholangiocyte monolayers by a c-Src-, TLR4-, and LBP-dependent mechanism. Am J Physiol Gastrointest Liver Physiol 293: 308-318, 2007.
    • (2007) Am J Physiol Gastrointest Liver Physiol , vol.293 , pp. 308-318
    • Sheth, P.1    Delos Santos, N.2    Seth, A.3    LaRusso, N.F.4    Rao, R.K.5
  • 222
    • 67650306418 scopus 로고    scopus 로고
    • Protein phosphatase 2A plays a role in hydrogen peroxide-induced disruption of tight junctions in Caco-2 cell monolayers
    • Sheth P, Samak G, Shull JA, Seth A, Rao R. Protein phosphatase 2A plays a role in hydrogen peroxide-induced disruption of tight junctions in Caco-2 cell monolayers. Biochem J 421: 59-70, 2009.
    • (2009) Biochem J , vol.421 , pp. 59-70
    • Sheth, P.1    Samak, G.2    Shull, J.A.3    Seth, A.4    Rao, R.5
  • 226
    • 77955349312 scopus 로고    scopus 로고
    • Claudin family of proteins and cancer: An overview
    • Singh AB, Sharma A, Dhawan P. Claudin family of proteins and cancer: An overview. J Oncol 2010: 541957, 2010.
    • (2010) J Oncol , vol.2010 , pp. 541957
    • Singh, A.B.1    Sharma, A.2    Dhawan, P.3
  • 227
    • 4644271738 scopus 로고    scopus 로고
    • Thr207 of claudin-5 is involved in size-selective loosening of the endothelial barrier by cyclic AMP
    • Soma T, Chiba H, Kato-Mori Y, Wada T, Yamashita T, Kojima T, Sawada N. Thr207 of claudin-5 is involved in size-selective loosening of the endothelial barrier by cyclic AMP. Exp Cell Res 300: 202-212, 2004.
    • (2004) Exp Cell Res , vol.300 , pp. 202-212
    • Soma, T.1    Chiba, H.2    Kato-Mori, Y.3    Wada, T.4    Yamashita, T.5    Kojima, T.6    Sawada, N.7
  • 228
    • 0033523773 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier
    • Sonoda N, Furuse M, Sasaki H, Yonemura S, Katahira J, Horiguchi Y, Tsukita S. Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier. J Cell Biol 147: 195-204, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 195-204
    • Sonoda, N.1    Furuse, M.2    Sasaki, H.3    Yonemura, S.4    Katahira, J.5    Horiguchi, Y.6    Tsukita, S.7
  • 229
    • 0015846194 scopus 로고
    • Further observations of the fine structure of freezecleaved tight junctions
    • Staehelin LA. Further observations of the fine structure of freezecleaved tight junctions. J Cell Sci 13: 763-786, 1973.
    • (1973) J Cell Sci , vol.13 , pp. 763-786
    • Staehelin, L.A.1
  • 230
    • 0014456576 scopus 로고
    • Freeze-etch appearance of tight junctions in the epithelium of small and large intestine of mice
    • Staehelin LA, Mukherjee TM, Williams AW. Freeze-etch appearance of tight junctions in the epithelium of small and large intestine of mice. Protoplasma 67: 165-184, 1969.
    • (1969) Protoplasma , vol.67 , pp. 165-184
    • Staehelin, L.A.1    Mukherjee, T.M.2    Williams, A.W.3
  • 231
    • 74549219792 scopus 로고    scopus 로고
    • Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family
    • Steed E, Rodrigues NT, Balda MS, Matter K. Identification of MarvelD3 as a tight junction-associated transmembrane protein of the occludin family. BMC Cell Biol 10: 95, 2009.
    • (2009) BMC Cell Biol , vol.10 , pp. 95
    • Steed, E.1    Rodrigues, N.T.2    Balda, M.S.3    Matter, K.4
  • 232
    • 0024211161 scopus 로고
    • Tight junction structure and ZO-1 content are identical in two strains of Madin- Darby canine kidney cells which differ in transepithelial resistance
    • Stevenson BR, Anderson JM, Goodenough DA, Mooseker MS. Tight junction structure and ZO-1 content are identical in two strains of Madin- Darby canine kidney cells which differ in transepithelial resistance. J Cell Biol 107: 2401-2408, 1988.
    • (1988) J Cell Biol , vol.107 , pp. 2401-2408
    • Stevenson, B.R.1    Anderson, J.M.2    Goodenough, D.A.3    Mooseker, M.S.4
  • 234
    • 0032406513 scopus 로고    scopus 로고
    • The mechanism of diarrhea in HIV is based on an impaired epithelial barrier function that could be induced by a specific cytokine pattern
    • Stockmann M, Schmitz H, Fromm M, Schmidt W, Rokos K, Pauli G, Scholz P, Riecken EO, Schulzke JD. The mechanism of diarrhea in HIV is based on an impaired epithelial barrier function that could be induced by a specific cytokine pattern. Ann N Y Acad Sci 859: 267-270, 1998.
    • (1998) Ann N Y Acad Sci , vol.859 , pp. 267-270
    • Stockmann, M.1    Schmitz, H.2    Fromm, M.3    Schmidt, W.4    Rokos, K.5    Pauli, G.6    Scholz, P.7    Riecken, E.O.8    Schulzke, J.D.9
  • 239
    • 77949720519 scopus 로고    scopus 로고
    • Mucosal expression of claudins 2, 3 and 4 in proximal and distal part of duodenum in children with coeliac disease
    • Szakál DN, Gyorffy H, Arató A, Cseh A, Molnár K, Papp M, Dezsofi A, Veres G. Mucosal expression of claudins 2, 3 and 4 in proximal and distal part of duodenum in children with coeliac disease. Virchows Arch 456: 245-250, 2010.
    • (2010) Virchows Arch , vol.456 , pp. 245-250
    • Szakál, D.N.1    Gyorffy, H.2    Arató, A.3    Cseh, A.4    Molnár, K.5    Papp, M.6    Dezsofi, A.7    Veres, G.8
  • 240
    • 3343021140 scopus 로고    scopus 로고
    • IL8 release, tight junction and cytoskeleton dynamic reorganization conducive to permeability increase are induced by dengue virus infection of microvascular endothelial monolayers
    • Talavera D, Castillo AM, Dominguez MC, Gutierrez AE, Meza I. IL8 release, tight junction and cytoskeleton dynamic reorganization conducive to permeability increase are induced by dengue virus infection of microvascular endothelial monolayers. J Gen Virol 85: 1801-1813, 2004.
    • (2004) J Gen Virol , vol.85 , pp. 1801-1813
    • Talavera, D.1    Castillo, A.M.2    Dominguez, M.C.3    Gutierrez, A.E.4    Meza, I.5
  • 243
    • 29644437500 scopus 로고    scopus 로고
    • EphA2 phosphorylates the cytoplasmic tail of claudin-4 and mediates paracellular permeability
    • Tanaka M, Kamata R, Sakai R. EphA2 phosphorylates the cytoplasmic tail of claudin-4 and mediates paracellular permeability. J Biol Chem 280: 42375-42382, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 42375-42382
    • Tanaka, M.1    Kamata, R.2    Sakai, R.3
  • 244
    • 79951659100 scopus 로고    scopus 로고
    • Dysregulation of Claudin family genes in colorectal cancer in a Chinese population
    • Tang W, Dou T, Zhong M, Wu Z. Dysregulation of Claudin family genes in colorectal cancer in a Chinese population. Biofactors 37: 65-73. 2011.
    • (2011) Biofactors , vol.37 , pp. 65-73
    • Tang, W.1    Dou, T.2    Zhong, M.3    Wu, Z.4
  • 245
    • 34547112045 scopus 로고    scopus 로고
    • WNK4 phosphorylates ser(206) of claudin-7 and promotes paracellular Cl- permeability
    • Tatum R, Zhang Y, Lu Q, Kim K, Jeansonne BG, Chen YH. WNK4 phosphorylates ser(206) of claudin-7 and promotes paracellular Cl- permeability. FEBS Lett 581: 3887-3891, 2007
    • (2007) FEBS Lett , vol.581 , pp. 3887-3891
    • Tatum, R.1    Zhang, Y.2    Lu, Q.3    Kim, K.4    Jeansonne, B.G.5    Chen, Y.H.6
  • 248
    • 0035705881 scopus 로고    scopus 로고
    • Simulation approaches to ion channel structure-function relationships
    • Tieleman DP, Biggin PC, Smith GR, Sansom MS. Simulation approaches to ion channel structure-function relationships. Q Rev Biophys 34: 473-561, 2001.
    • (2001) Q Rev Biophys , vol.34 , pp. 473-561
    • Tieleman, D.P.1    Biggin, P.C.2    Smith, G.R.3    Sansom, M.S.4
  • 251
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight-junction strands: Leading or supporting players?
    • Tsukita S, Furuse M. Occludin and claudins in tight-junction strands: Leading or supporting players? Trends Cell Biol 9: 268-273, 1999.
    • (1999) Trends Cell Biol , vol.9 , pp. 268-273
    • Tsukita, S.1    Furuse, M.2
  • 253
    • 56749184887 scopus 로고    scopus 로고
    • Tight junctionbased epithelial microenvironment and cell proliferation
    • Tsukita S, Yamazaki Y, Katsuno T, Tamura A, Tsukita S. Tight junctionbased epithelial microenvironment and cell proliferation. Oncogene 27: 6930-6938, 2008.
    • (2008) Oncogene , vol.27 , pp. 6930-6938
    • Tsukita, S.1    Yamazaki, Y.2    Katsuno, T.3    Tamura, A.4    Tsukita, S.5
  • 254
    • 0036336486 scopus 로고    scopus 로고
    • Permeability barrier dysfunction in transgenic mice overexpressing claudin 6
    • Turksen K, Troy TC. Permeability barrier dysfunction in transgenic mice overexpressing claudin 6. Development 129: 1775-1784, 2002.
    • (2002) Development , vol.129 , pp. 1775-1784
    • Turksen, K.1    Troy, T.C.2
  • 255
    • 34248561456 scopus 로고    scopus 로고
    • Heterogeneous expression of claudin-4 in human colorectal cancer: Decreased claudin-4 expression at the invasive front correlates cancer invasion and metastasis
    • Ueda J, Semba S, Chiba H, Sawada N, Seo Y, Kasuga M, Yokozaki H. Heterogeneous expression of claudin-4 in human colorectal cancer: Decreased claudin-4 expression at the invasive front correlates cancer invasion and metastasis. Pathobiology 74: 32-41, 2007.
    • (2007) Pathobiology , vol.74 , pp. 32-41
    • Ueda, J.1    Semba, S.2    Chiba, H.3    Sawada, N.4    Seo, Y.5    Kasuga, M.6    Yokozaki, H.7
  • 256
    • 70350509805 scopus 로고    scopus 로고
    • Intestinal mucosal barrier function in health and disease
    • Turner JR. Intestinal mucosal barrier function in health and disease. Nat Rev Immunol 9: 799-809, 2009.
    • (2009) Nat Rev Immunol , vol.9 , pp. 799-809
    • Turner, J.R.1
  • 257
    • 77954643393 scopus 로고    scopus 로고
    • Claudins in cancer biology
    • Valle BL, Morin PJ. Claudins in cancer biology. Curr Top Membr 65: 293-333, 2010.
    • (2010) Curr Top Membr , vol.65 , pp. 293-333
    • Valle, B.L.1    Morin, P.J.2
  • 258
    • 0018425385 scopus 로고
    • Tight junctions in the choroid plexus epithelium. A freeze-fracture study including complementary replicas
    • Van Deurs B, Koehler JK. Tight junctions in the choroid plexus epithelium. A freeze-fracture study including complementary replicas. J Cell Biol 80: 662-673, 1979.
    • (1979) J Cell Biol , vol.80 , pp. 662-673
    • Van Deurs, B.1    Koehler, J.K.2
  • 259
    • 0035013499 scopus 로고    scopus 로고
    • Regulated expression of claudin- 4 decreases paracellular conductance through a selective decrease in sodium permeability
    • Van Itallie C, Rahner C, Anderson JM. Regulated expression of claudin- 4 decreases paracellular conductance through a selective decrease in sodium permeability. J Clin Invest 107: 1319-1327, 2001.
    • (2001) J Clin Invest , vol.107 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 260
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins
    • Van Itallie CM, Fanning AS, Anderson JM. Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am J Physiol Renal Physiol 285: F1078-F1084, 2003.
    • (2003) Am J Physiol Renal Physiol , vol.285
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 261
    • 77955992054 scopus 로고    scopus 로고
    • Occludin is required for cytokine-induced regulation of tight junction barriers
    • Van Itallie CM, Fanning AS, Holmes J, Anderson JM. Occludin is required for cytokine-induced regulation of tight junction barriers. J Cell Sci 123: 2844-2852, 2010.
    • (2010) J Cell Sci , vol.123 , pp. 2844-2852
    • Van Itallie, C.M.1    Fanning, A.S.2    Holmes, J.3    Anderson, J.M.4
  • 262
    • 17844408453 scopus 로고    scopus 로고
    • Palmitoylation of claudins is required for efficient tight-junction localization
    • Van Itallie CM, Gambling TM, Carson JL Anderson JM. Palmitoylation of claudins is required for efficient tight-junction localization. J Cell Sci 118: 1427-1436, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 1427-1436
    • Van Itallie, C.M.1    Gambling, T.M.2    Carson J.L Anderson, J.M.3
  • 264
    • 79952800345 scopus 로고    scopus 로고
    • Claudin-2 forms homodimers and is a component of a high molecular weight protein complex
    • Van Itallie CM, Mitic LL, Anderson JM. Claudin-2 forms homodimers and is a component of a high molecular weight protein complex. J Biol Chem 286: 3442-3450, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 3442-3450
    • Van Itallie, C.M.1    Mitic, L.L.2    Anderson, J.M.3
  • 266
    • 0034435587 scopus 로고    scopus 로고
    • Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution
    • van Raaij MJ, Chouin E, van der Zandt H, Bergelson JM, Cusack S. Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution. Structure 8: 1147-1155, 2000.
    • (2000) Structure , vol.8 , pp. 1147-1155
    • van Raaij, M.J.1    Chouin, E.2    van der Zandt, H.3    Bergelson, J.M.4    Cusack, S.5
  • 267
    • 73949154760 scopus 로고    scopus 로고
    • Reversal of West Nile virus-induced blood-brain barrier disruption and tight junction proteins degradation by matrix metalloproteinases inhibitor
    • Verma S, Kumar M, Gurjav U, Lum S, Nerurkar VR. Reversal of West Nile virus-induced blood-brain barrier disruption and tight junction proteins degradation by matrix metalloproteinases inhibitor. Virology 397: 130-138, 2010.
    • (2010) Virology , vol.397 , pp. 130-138
    • Verma, S.1    Kumar, M.2    Gurjav, U.3    Lum, S.4    Nerurkar, V.R.5
  • 269
    • 67249112673 scopus 로고    scopus 로고
    • The role of JAM-A in inflammatory bowel disease: Unrevealing the ties that bind
    • Vetrano S, Danese S. The role of JAM-A in inflammatory bowel disease: Unrevealing the ties that bind. Ann N Y Acad Sci 1165: 308-313, 2009.
    • (2009) Ann N Y Acad Sci , vol.1165 , pp. 308-313
    • Vetrano, S.1    Danese, S.2
  • 270
    • 26844532768 scopus 로고    scopus 로고
    • The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases
    • Vitari AC, Deak M, Morrice NA, Alessi DR. The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases. Biochem J 391: 17-24, 2005.
    • (2005) Biochem J , vol.391 , pp. 17-24
    • Vitari, A.C.1    Deak, M.2    Morrice, N.A.3    Alessi, D.R.4
  • 271
    • 0021881877 scopus 로고
    • A re-assessment of the tricellular region of epithelial cell tight junctions in trachea of guinea pig
    • Walker DC, MacKenzie A, Hulbert WC, Hogg JC. A re-assessment of the tricellular region of epithelial cell tight junctions in trachea of guinea pig. Acta Anat (Basel) 122: 35-38, 1985.
    • (1985) Acta Anat (Basel) , vol.122 , pp. 35-38
    • Walker, D.C.1    MacKenzie, A.2    Hulbert, W.C.3    Hogg, J.C.4
  • 273
    • 0034891627 scopus 로고    scopus 로고
    • Functional modeling of tight junctions in intestinal cell monolayers using polyethylene glycol oligomers
    • Watson CJ, Rowland M, Warhurst G. Functional modeling of tight junctions in intestinal cell monolayers using polyethylene glycol oligomers. Am J Physiol Cell Physiol 281: C388-C397, 2001.
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Watson, C.J.1    Rowland, M.2    Warhurst, G.3
  • 274
    • 4544311402 scopus 로고    scopus 로고
    • Selective decrease in paracellular conductance of tight junctions: Role of the first extracellular domain of claudin-5
    • Wen H, Watry DD, Marcondes MC, Fox HS. Selective decrease in paracellular conductance of tight junctions: Role of the first extracellular domain of claudin-5. Mol Cell Biol 24: 8408-8417, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 8408-8417
    • Wen, H.1    Watry, D.D.2    Marcondes, M.C.3    Fox, H.S.4
  • 275
    • 70350342022 scopus 로고    scopus 로고
    • Transcriptional profiling of human cavernosal endothelial cells reveals distinctive cell adhesion phenotype and role for claudin 11 in vascular barrier function
    • Wessells H, Sullivan CJ, Tsubota Y, Engel KL, Kim B, Olson NE, Thorner D, Chitaley K. Transcriptional profiling of human cavernosal endothelial cells reveals distinctive cell adhesion phenotype and role for claudin 11 in vascular barrier function. Physiol Genomics 39: 100-108, 2009.
    • (2009) Physiol Genomics , vol.39 , pp. 100-108
    • Wessells, H.1    Sullivan, C.J.2    Tsubota, Y.3    Engel, K.L.4    Kim, B.5    Olson, N.E.6    Thorner, D.7    Chitaley, K.8
  • 278
    • 67650553423 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3
    • Winkler L, Gehring C, Wenzel A, Müller SL, Piehl C, Krause G, Blasig IE, Piontek J. Molecular determinants of the interaction between Clostridium perfringens enterotoxin fragments and claudin-3. J Biol Chem 284: 18863-18872, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 18863-18872
    • Winkler, L.1    Gehring, C.2    Wenzel, A.3    Müller, S.L.4    Piehl, C.5    Krause, G.6    Blasig, I.E.7    Piontek, J.8
  • 279
    • 0033521140 scopus 로고    scopus 로고
    • Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
    • Wittchen ES, Haskins J, Stevenson BR. Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. J Biol Chem 274: 35179-35185, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 280
    • 1642458089 scopus 로고    scopus 로고
    • Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control
    • Wu VM, Schulte J, Hirschi A, Tepass U, Beitel GJ. Sinuous is a Drosophila claudin required for septate junction organization and epithelial tube size control. J Cell Biol 164: 313-323, 2004.
    • (2004) J Cell Biol , vol.164 , pp. 313-323
    • Wu, V.M.1    Schulte, J.2    Hirschi, A.3    Tepass, U.4    Beitel, G.J.5
  • 283
    • 65549090565 scopus 로고    scopus 로고
    • Tight junction transmembrane protein claudin subtype expression and distribution in human corneal and conjunctival epithelium
    • Yoshida Y, Ban Y, Kinoshita S. Tight junction transmembrane protein claudin subtype expression and distribution in human corneal and conjunctival epithelium. Invest Ophthalmol Vis Sci 50: 2103-2108, 2009.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 2103-2108
    • Yoshida, Y.1    Ban, Y.2    Kinoshita, S.3
  • 284
    • 67249153151 scopus 로고    scopus 로고
    • Molecular basis for cation selectivity in claudin-2-based pores
    • Yu AS. Molecular basis for cation selectivity in claudin-2-based pores. Ann N Y Acad Sci 1165: 53-57, 2009.
    • (2009) Ann N Y Acad Sci , vol.1165 , pp. 53-57
    • Yu, A.S.1
  • 286
    • 60549090106 scopus 로고    scopus 로고
    • Molecular basis for cation selectivity in claudin-2-based paracellular pores: Identification of an electrostatic interaction site
    • Yu ASL, Cheng, MH, Angelow S, Günzel D, Kanzawa SA, Schneeberger EE, Fromm M, Coalson RD. Molecular basis for cation selectivity in claudin-2-based paracellular pores: Identification of an electrostatic interaction site. J Gen Physiol 133: 111-127, 2009.
    • (2009) J Gen Physiol , vol.133 , pp. 111-127
    • Yu, A.S.L.1    Cheng, M.H.2    Angelow, S.3    Günzel, D.4    Kanzawa, S.A.5    Schneeberger, E.E.6    Fromm, M.7    Coalson, R.D.8
  • 287
    • 0037930880 scopus 로고    scopus 로고
    • Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation
    • Yu ASL, Enck AH, Lencer WI, Schneeberger EE. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J Biol Chem 278: 17350-17359, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 17350-17359
    • Yu, A.S.L.1    Enck, A.H.2    Lencer, W.I.3    Schneeberger, E.E.4
  • 288
    • 33845995125 scopus 로고    scopus 로고
    • Changes in expression and distribution of claudin 2, 5 and 8 lead to discontinuous tight junctions and barrier dysfunction in active Crohn's disease
    • Zeissig S, Bürgel N, Günzel D, Richter JF, Mankertz J, Wahnschaffe U, Kroesen AJ, Zeitz M, Fromm M, Schulzke JD. Changes in expression and distribution of claudin 2, 5 and 8 lead to discontinuous tight junctions and barrier dysfunction in active Crohn's disease. Gut 56: 61-72, 2007.
    • (2007) Gut , vol.56 , pp. 61-72
    • Zeissig, S.1    Bürgel, N.2    Günzel, D.3    Richter, J.F.4    Mankertz, J.5    Wahnschaffe, U.6    Kroesen, A.J.7    Zeitz, M.8    Fromm, M.9    Schulzke, J.D.10
  • 289
    • 36048954580 scopus 로고    scopus 로고
    • Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C virus
    • Zheng A, Yuan F, Li Y, Zhu F, Hou P, Li J, Song X, Ding M, Deng H. Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C virus. J Virol 81: 12465-12471, 2007.
    • (2007) J Virol , vol.81 , pp. 12465-12471
    • Zheng, A.1    Yuan, F.2    Li, Y.3    Zhu, F.4    Hou, P.5    Li, J.6    Song, X.7    Ding, M.8    Deng, H.9
  • 291
    • 72549118951 scopus 로고    scopus 로고
    • Expression of tight-junction proteins in the inflamed and clinically uninvolved skin in patients with venous leg ulcers
    • Zorko MS, Veranic P, Leskovec NK, Pavlović MD, Lunder T. Expression of tight-junction proteins in the inflamed and clinically uninvolved skin in patients with venous leg ulcers. Clin Exp Dermatol 34: e949-e952, 2009.
    • (2009) Clin Exp Dermatol , vol.34
    • Zorko, M.S.1    Veranic, P.2    Leskovec, N.K.3    Pavlović, M.D.4    Lunder, T.5
  • 292
    • 77954644230 scopus 로고    scopus 로고
    • Biophysical methods to study tight junction permeability
    • Günzel D, Krug SM, Rosenthal R, Fromm M. Biophysical methods to study tight junction permeability. Curr Top Membr 65: 39-78, 2010.
    • (2010) Curr Top Membr , vol.65 , pp. 39-78
    • Günzel, D.1    Krug, S.M.2    Rosenthal, R.3    Fromm, M.4
  • 293
    • 84868094797 scopus 로고    scopus 로고
    • Claudins: Methods and protocols
    • (ed)
    • Turksen K (ed). Claudins: Methods and protocols. Methods in Molecular Biology 762: 1-461, 2011.
    • (2011) Methods in Molecular Biology , vol.762 , pp. 1-461
    • Turksen, K.1
  • 294
    • 84868120858 scopus 로고    scopus 로고
    • Molecular structure and function of the tight junction
    • (A follow-up volume will be published by the Ann NY Acad Sci in 2012.
    • Fromm M, Schulzke JD (eds). Molecular structure and function of the tight junction. Ann NY Acad Sci 1165: 1-346, 2009. (A follow-up volume will be published by the Ann NY Acad Sci in 2012.)
    • (2009) Ann NY Acad Sci , vol.1165 , pp. 1-346
    • Fromm, M.1    Schulzke, J.D.2
  • 295
    • 84868135003 scopus 로고    scopus 로고
    • Claudins
    • (ed).
    • Yu AS (ed). Claudins. Curr Top Membr 65: 1-341, 2010.
    • (2010) Curr Top Membr , vol.65 , pp. 1-341
    • Yu, A.S.1


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