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Volumn 279, Issue C, 2010, Pages 1-32

Functions of claudin tight junction proteins and their complex interactions in various physiological systems

Author keywords

Claudin; Membrane proteins; Tight junction proteins; Tight junctions

Indexed keywords

CLAUDIN; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR; GREEN FLUORESCENT PROTEIN;

EID: 77957921618     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(10)79001-8     Document Type: Article
Times cited : (75)

References (110)
  • 4
    • 0037115724 scopus 로고    scopus 로고
    • Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
    • Amasheh, S., Meiri, N., Gitter, A.H., Schoneberg, T., Mankertz, J., Schulzke, J.D., et al., 2002. Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J. Cell Sci. 115 (Pt 24), 4969-4976.
    • (2002) J. Cell Sci. , vol.115 , Issue.PART 24 , pp. 4969-4976
    • Amasheh, S.1    Meiri, N.2    Gitter, A.H.3    Schoneberg, T.4    Mankertz, J.5    Schulzke, J.D.6
  • 5
    • 22144441209 scopus 로고    scopus 로고
    • Contribution of claudin-5 to barrier properties in tight junctions of epithelial cells
    • Amasheh, S., Schmidt, T., Mahn, M., Florian, P., Mankertz, J., Tavalali, S., et al., 2005. Contribution of claudin-5 to barrier properties in tight junctions of epithelial cells. Cell Tissue Res. 321 (1), 89-96.
    • (2005) Cell Tissue Res , vol.321 , Issue.1 , pp. 89-96
    • Amasheh, S.1    Schmidt, T.2    Mahn, M.3    Florian, P.4    Mankertz, J.5    Tavalali, S.6
  • 6
    • 0035354574 scopus 로고    scopus 로고
    • Molecular structure of tight junctions and their role in epithelial transport
    • Anderson, J.M., 2001. Molecular structure of tight junctions and their role in epithelial transport. News Physiol. Sci. 16, 126-130.
    • (2001) News Physiol. Sci. , vol.16 , pp. 126-130
    • Anderson, J.M.1
  • 9
    • 10744222330 scopus 로고    scopus 로고
    • Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration
    • Ben-Yosef, T., Belyantseva, I.A., Saunders, T.L., Hughes, E.D., Kawamoto, K., Van Itallie, C.M., et al., 2003. Claudin 14 knockout mice, a model for autosomal recessive deafness DFNB29, are deaf due to cochlear hair cell degeneration. Hum. Mol. Genet. 12, 2049-2061.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2049-2061
    • Ben-Yosef, T.1    Belyantseva, I.A.2    Saunders, T.L.3    Hughes, E.D.4    Kawamoto, K.5    Van Itallie, C.M.6
  • 10
    • 0036014853 scopus 로고    scopus 로고
    • Organization and formation of the tight junction system in human epidermis and cultured keratinocytes
    • Brandner, J.M., Kief, S., Grund, C., Rendl, M., Houdek, P., Kuhn, C., et al., 2002. Organization and formation of the tight junction system in human epidermis and cultured keratinocytes. Eur. J. Cell Biol. 81, 253-263.
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 253-263
    • Brandner, J.M.1    Kief, S.2    Grund, C.3    Rendl, M.4    Houdek, P.5    Kuhn, C.6
  • 11
    • 0031918158 scopus 로고    scopus 로고
    • Role of tight junctions in establishing and maintaining cell polarity
    • Cereijido, M., Valdes, J., Shoshani, L., Contreras, R.G., 1998. Role of tight junctions in establishing and maintaining cell polarity. Annu. Rev. Physiol. 60, 161-177.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 161-177
    • Cereijido, M.1    Valdes, J.2    Shoshani, L.3    Contreras, R.G.4
  • 12
    • 12444288064 scopus 로고    scopus 로고
    • The importance of calcium influx, calpain and calmodulin for the activation of CaCo-2 cell death pathways by Clostridium perfringens enterotoxin
    • Chakrabarti, G., McClane, B.A., 2005. The importance of calcium influx, calpain and calmodulin for the activation of CaCo-2 cell death pathways by Clostridium perfringens enterotoxin. Cell. Microbiol. 7, 129-146.
    • (2005) Cell. Microbiol. , vol.7 , pp. 129-146
    • Chakrabarti, G.1    McClane, B.A.2
  • 13
    • 0015837872 scopus 로고
    • Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia
    • Claude, P., Goodenough, D.A., 1973. Fracture faces of zonulae occludentes from "tight" and "leaky" epithelia. J. Cell Biol. 58, 390-400.
    • (1973) J. Cell Biol. , vol.58 , pp. 390-400
    • Claude, P.1    Goodenough, D.A.2
  • 16
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio, O.R., Van Itallie, C., Rahner, C., Anderson, J.M., 2003. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am. J. Physiol. Cell Physiol. 284, C1346-C1354.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Colegio, O.R.1    Van Itallie, C.2    Rahner, C.3    Anderson, J.M.4
  • 19
    • 0019806209 scopus 로고
    • Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane?
    • Dragsten, P.R., Blumenthal, R., Handler, J.S., 1981. Membrane asymmetry in epithelia: is the tight junction a barrier to diffusion in the plasma membrane? Nature 294, 718-722.
    • (1981) Nature , vol.294 , pp. 718-722
    • Dragsten, P.R.1    Blumenthal, R.2    Handler, J.S.3
  • 20
    • 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., 2008. Double gene deletion reveals lack of cooperation between claudin 11 and claudin 14 tight junction proteins. Cell Tissue Res. 333, 427-438.
    • (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
  • 21
    • 0035195390 scopus 로고    scopus 로고
    • Claudin-2 is selectively expressed in proximal nephron in mouse kidney
    • Enck, A.H., Berger, U.V., Yu, A.S., 2001. Claudin-2 is selectively expressed in proximal nephron in mouse kidney. Am. J. Physiol. Renal Physiol. 281, F966-F974.
    • (2001) Am. J. Physiol. Renal Physiol. , vol.281
    • Enck, A.H.1    Berger, U.V.2    Yu, A.S.3
  • 22
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar, M.G., Palade, G.E., 1963. Junctional complexes in various epithelia. J. Cell Biol. 17, 375-412.
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 25
    • 0015494421 scopus 로고
    • Route of passive ion permeation in epithelia
    • Fromter, E., Diamond, J., 1972. Route of passive ion permeation in epithelia. Nat. New Biol. 235, 9-13.
    • (1972) Nat. New Biol. , vol.235 , pp. 9-13
    • Fromter, E.1    Diamond, J.2
  • 26
    • 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., 2000. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS Lett. 476, 258-261.
    • (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
  • 27
    • 0027744129 scopus 로고
    • Occludin: a novel integral membrane protein localizing at tight junctions
    • Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., et al., 1993. Occludin: a novel integral membrane protein localizing at tight junctions. J. Cell Biol. 123, 1777-1788.
    • (1993) J. Cell Biol. , vol.123 , pp. 1777-1788
    • Furuse, M.1    Hirase, T.2    Itoh, M.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6
  • 28
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse, M., Fujita, K., Hiiragi, T., Fujimoto, K., Tsukita, S., 1998a. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J. Cell Biol. 141, 1539-1550.
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 29
    • 0032547833 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., 1998b. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143, 391-401.
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 30
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse, M., Sasaki, H., Tsukita, S., 1999. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J. Cell Biol. 147, 891-903.
    • (1999) J. Cell Biol. , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 31
    • 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., et al., 2002. 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) 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
  • 33
    • 0030013202 scopus 로고    scopus 로고
    • Connexins, connexons, and intercellular communication
    • Goodenough, D.A., Goliger, J.A., Paul, D.L., 1996. Connexins, connexons, and intercellular communication. Annu. Rev. Biochem. 65, 475-502.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 475-502
    • Goodenough, D.A.1    Goliger, J.A.2    Paul, D.L.3
  • 34
    • 0001636804 scopus 로고    scopus 로고
    • CNS myelin and sertoli cell tight junction strands are absent in Osp/claudin-11 null mice
    • Gow, A., Southwood, C.M., Li, J.S., Pariali, M., Riordan, G.P., Brodie, S.E., et al., 1999. CNS myelin and sertoli cell tight junction strands are absent in Osp/claudin-11 null mice. Cell 99, 649-659.
    • (1999) Cell , vol.99 , pp. 649-659
    • Gow, A.1    Southwood, C.M.2    Li, J.S.3    Pariali, M.4    Riordan, G.P.5    Brodie, S.E.6
  • 35
    • 4143135446 scopus 로고    scopus 로고
    • Deafness in Claudin 11-null mice reveals the critical contribution of basal cell tight junctions to stria vascularis function
    • Gow, A., Davies, C., Southwood, C.M., Frolenkov, G., Chrustowski, M., Ng, L., et al., 2004. Deafness in Claudin 11-null mice reveals the critical contribution of basal cell tight junctions to stria vascularis function. J. Neurosci. 24, 7051-7062.
    • (2004) J. Neurosci. , vol.24 , pp. 7051-7062
    • Gow, A.1    Davies, C.2    Southwood, C.M.3    Frolenkov, G.4    Chrustowski, M.5    Ng, L.6
  • 36
    • 7644230747 scopus 로고    scopus 로고
    • Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: a tight junction disease
    • Hadj-Rabia, S., Baala, L., Vabres, P., Hamel-Teillac, D., Jacquemin, E., Fabre, M., et al., 2004. Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: a tight junction disease. Gastroenterology 127, 1386-1390.
    • (2004) Gastroenterology , vol.127 , pp. 1386-1390
    • Hadj-Rabia, S.1    Baala, L.2    Vabres, P.3    Hamel-Teillac, D.4    Jacquemin, E.5    Fabre, M.6
  • 37
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • Hamazaki, Y., Itoh, M., Sasaki, H., Furuse, M., Tsukita, S., 2002. Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J. Biol. Chem. 277, 455-461.
    • (2002) J. Biol. Chem. , vol.277 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 38
    • 21844456631 scopus 로고    scopus 로고
    • The zebrafish gene claudinj is essential for normal ear function and important for the formation of the otoliths
    • Hardison, A.L., Lichten, L., Banerjee-Basu, S., Becker, T.S., Burgess, S.M., 2005. The zebrafish gene claudinj is essential for normal ear function and important for the formation of the otoliths. Mech. Dev. 122, 949-958.
    • (2005) Mech. Dev. , vol.122 , pp. 949-958
    • Hardison, A.L.1    Lichten, L.2    Banerjee-Basu, S.3    Becker, T.S.4    Burgess, S.M.5
  • 39
    • 0034068924 scopus 로고    scopus 로고
    • Null mutation of PCLN-1/Claudin-16 results in bovine chronic interstitial nephritis
    • Hirano, T., Kobayashi, N., Itoh, T., Takasuga, A., Nakamaru, T., Hirotsune, S., et al., 2000. Null mutation of PCLN-1/Claudin-16 results in bovine chronic interstitial nephritis. Genome Res. 10, 659-663.
    • (2000) Genome Res , vol.10 , pp. 659-663
    • Hirano, T.1    Kobayashi, N.2    Itoh, T.3    Takasuga, A.4    Nakamaru, T.5    Hirotsune, S.6
  • 40
    • 0036010110 scopus 로고    scopus 로고
    • A new deletion mutation in bovine Claudin-16 (CL-16) deficiency and diagnosis
    • Hirano, T., Hirotsune, S., Sasaki, S., Kikuchi, T., Sugimoto, Y., 2002. A new deletion mutation in bovine Claudin-16 (CL-16) deficiency and diagnosis. Anim. Genet. 33, 118-122.
    • (2002) Anim. Genet. , vol.33 , pp. 118-122
    • Hirano, T.1    Hirotsune, S.2    Sasaki, S.3    Kikuchi, T.4    Sugimoto, Y.5
  • 41
    • 0030751655 scopus 로고    scopus 로고
    • Occludin as a possible determinant of tight junction permeability in endothelial cells
    • Hirase, T., Staddon, J.M., Saitou, M., Ando-Akatsuka, Y., Itoh, M., Furuse, M., et al., 1997. Occludin as a possible determinant of tight junction permeability in endothelial cells. J. Cell Sci. 110 (Pt 14), 1603-1613.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 14 , pp. 1603-1613
    • Hirase, T.1    Staddon, J.M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Itoh, M.5    Furuse, M.6
  • 42
    • 27944501678 scopus 로고    scopus 로고
    • Paracellin-1 and the modulation of ion selectivity of tight junctions
    • Hou, J., Paul, D.L., Goodenough, D.A., 2005. Paracellin-1 and the modulation of ion selectivity of tight junctions. J. Cell Sci. 118 (Pt 21), 5109-5118.
    • (2005) J. Cell Sci. , vol.118 , Issue.PART 21 , pp. 5109-5118
    • Hou, J.1    Paul, D.L.2    Goodenough, D.A.3
  • 43
    • 33845991201 scopus 로고    scopus 로고
    • Study of claudin function by RNA interference
    • Hou, J., Gomes, A.S., Paul, D.L., Goodenough, D.A., 2006. Study of claudin function by RNA interference. J. Biol. Chem. 281 (47), 36117-36123.
    • (2006) J. Biol. Chem. , vol.281 , Issue.47 , pp. 36117-36123
    • Hou, J.1    Gomes, A.S.2    Paul, D.L.3    Goodenough, D.A.4
  • 44
    • 34447126892 scopus 로고    scopus 로고
    • Transgenic RNAi depletion of claudin-16 and the renal handling of magnesium
    • Hou, J., Shan, Q., Wang, T., Gomes, A.S., Yan, Q., Paul, D.L., et al., 2007. Transgenic RNAi depletion of claudin-16 and the renal handling of magnesium. J. Biol. Chem. 282, 17114-17122.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17114-17122
    • Hou, J.1    Shan, Q.2    Wang, T.3    Gomes, A.S.4    Yan, Q.5    Paul, D.L.6
  • 45
    • 38849149203 scopus 로고    scopus 로고
    • Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex
    • Hou, J., Renigunta, A., Konrad, M., Gomes, A.S., Schneeberger, E.E., Paul, D.L., et al., 2008. Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex. J. Clin. Invest. 118, 619-628.
    • (2008) J. Clin. Invest. , vol.118 , pp. 619-628
    • Hou, J.1    Renigunta, A.2    Konrad, M.3    Gomes, A.S.4    Schneeberger, E.E.5    Paul, D.L.6
  • 46
    • 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, A.S., Hou, M., Paul, D.L., Waldegger, S., et al., 2009. Claudin-16 and claudin-19 interaction is required for their assembly into tight junctions and for renal reabsorption of magnesium. Proc. Natl. Acad. Sci. USA 106, 15350-15355.
    • (2009) Proc. Natl. Acad. Sci. USA , 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
  • 47
    • 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., et al., 2004. Association of paracellin-1 with ZO-1 augments the reabsorption of divalent cations in renal epithelial cells. J. Biol. Chem. 279, 54826-54832.
    • (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
  • 48
    • 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., 2005. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J. Cell Biol. 171, 939-945.
    • (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
  • 49
    • 0033376599 scopus 로고    scopus 로고
    • Claudin-1 contributes to the epithelial barrier function in MDCK cells
    • Inai, T., Kobayashi, J., Shibata, Y., 1999. Claudin-1 contributes to the epithelial barrier function in MDCK cells. Eur. J. Cell Biol. 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
  • 50
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • Itoh, M., Furuse, M., Morita, K., Kubota, K., Saitou, M., Tsukita, S., 1999. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J. Cell Biol. 147, 1351-1363.
    • (1999) J. Cell Biol. , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 51
    • 1542778870 scopus 로고    scopus 로고
    • Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells
    • Jeansonne, B., Lu, Q., Goodenough, D.A., Chen, Y.H., 2003. Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells. Cell. Mol. Biol. (Noisy-le-grand) 49, 13-21.
    • (2003) Cell. Mol. Biol. (Noisy-le-grand) , vol.49 , pp. 13-21
    • Jeansonne, B.1    Lu, Q.2    Goodenough, D.A.3    Chen, Y.H.4
  • 52
    • 0030716491 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo
    • Katahira, J., Sugiyama, H., Inoue, N., Horiguchi, Y., Matsuda, M., Sugimoto, N., 1997. Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo. J. Biol. Chem. 272, 26652-26658.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26652-26658
    • Katahira, J.1    Sugiyama, H.2    Inoue, N.3    Horiguchi, Y.4    Matsuda, M.5    Sugimoto, N.6
  • 53
    • 8744310611 scopus 로고    scopus 로고
    • Compartmentalization established by claudin-11-based tight junctions in stria vascularis is required for hearing through generation of endocochlear potential
    • Kitajiri, S., Miyamoto, T., Mineharu, A., Sonoda, N., Furuse, K., Hata, M., et al., 2004a. Compartmentalization established by claudin-11-based tight junctions in stria vascularis is required for hearing through generation of endocochlear potential. J. Cell Sci. 117, 5087-5096.
    • (2004) J. Cell Sci. , vol.117 , pp. 5087-5096
    • Kitajiri, S.1    Miyamoto, T.2    Mineharu, A.3    Sonoda, N.4    Furuse, K.5    Hata, M.6
  • 54
    • 0347123651 scopus 로고    scopus 로고
    • Expression patterns of claudins, tight junction adhesion molecules, in the inner ear
    • Kitajiri, S.I., Furuse, M., Morita, K., Saishin-Kiuchi, Y., Kido, H., Ito, J., et al., 2004b. Expression patterns of claudins, tight junction adhesion molecules, in the inner ear. Hear. Res. 187, 25-34.
    • (2004) Hear. Res. , vol.187 , pp. 25-34
    • Kitajiri, S.I.1    Furuse, M.2    Morita, K.3    Saishin-Kiuchi, Y.4    Kido, H.5    Ito, J.6
  • 55
    • 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., 2002. Differential expression patterns of claudins, tight junction membrane proteins, in mouse nephron segments. J. Am. Soc. Nephrol. 13, 875-886.
    • (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
  • 56
    • 33751097262 scopus 로고    scopus 로고
    • Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement
    • Konrad, M., Schaller, A., Seelow, D., Pandey, A.V., Waldegger, S., Lesslauer, A., et al., 2006. Mutations in the tight-junction gene claudin 19 (CLDN19) are associated with renal magnesium wasting, renal failure, and severe ocular involvement. Am. J. Hum. Genet. 79, 949-957.
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 949-957
    • Konrad, M.1    Schaller, A.2    Seelow, D.3    Pandey, A.V.4    Waldegger, S.5    Lesslauer, A.6
  • 57
    • 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., 2007. Hypoxia disrupts the barrier function of neural blood vessels through changes in the expression of claudin-5 in endothelial cells. Am. Soc. Investig. Pathol. 170 (4), 1389-1397.
    • (2007) Am. Soc. Investig. Pathol. , vol.170 , Issue.4 , pp. 1389-1397
    • Koto, T.1    Takubo, K.2    Ishida, S.3    Shinoda, H.4    Inoue, M.5    Tsubota, K.6
  • 58
    • 36749037222 scopus 로고    scopus 로고
    • A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9
    • Kovalenko, O.V., Yang, X.H., Hemler, M.E., 2007. A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9. Mol. Cell. Proteomics 6, 1855-1867.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1855-1867
    • Kovalenko, O.V.1    Yang, X.H.2    Hemler, M.E.3
  • 59
    • 0031656747 scopus 로고    scopus 로고
    • Desmosomes: intercellular adhesive junctions specialized for attachment of intermediate filaments
    • Kowalczyk, A.P., Bornslaeger, E.A., Norvell, S.M., Palka, H.L., Green, K.J., 1999. Desmosomes: intercellular adhesive junctions specialized for attachment of intermediate filaments. Int. Rev. Cytol. 185, 237-302.
    • (1999) Int. Rev. Cytol. , vol.185 , pp. 237-302
    • Kowalczyk, A.P.1    Bornslaeger, E.A.2    Norvell, S.M.3    Palka, H.L.4    Green, K.J.5
  • 60
    • 2442689137 scopus 로고    scopus 로고
    • Expression of claudin-7 and -8 along the mouse nephron
    • Li, W.Y., Huey, C.L., Yu, A.S., 2004. Expression of claudin-7 and -8 along the mouse nephron. Am. J. Physiol. Renal Physiol. 286, F1063-F1071.
    • (2004) Am. J. Physiol. Renal Physiol. , vol.286
    • Li, W.Y.1    Huey, C.L.2    Yu, A.S.3
  • 61
    • 48049122836 scopus 로고    scopus 로고
    • Kinetics of adhesion mediated by extracellular loops of claudin-2 as revealed by single-molecule force spectroscopy
    • Lim, T.S., Vedula, S.R., Hunziker, W., Lim, C.T., 2008. Kinetics of adhesion mediated by extracellular loops of claudin-2 as revealed by single-molecule force spectroscopy. J. Mol. Biol. 381, 681-691.
    • (2008) J. Mol. Biol. , vol.381 , pp. 681-691
    • Lim, T.S.1    Vedula, S.R.2    Hunziker, W.3    Lim, C.T.4
  • 62
    • 0031943571 scopus 로고    scopus 로고
    • Regulation of the movement of solutes across tight junctions
    • Madara, J.L., 1998. Regulation of the movement of solutes across tight junctions. Annu. Rev. Physiol. 60, 143-159.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 143-159
    • Madara, J.L.1
  • 64
    • 0033851771 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions I Tight junction structure and function: lessons from mutant animals and proteins
    • Mitic, L.L., Van Itallie, C.M., Anderson, J.M., 2000. Molecular physiology and pathophysiology of tight junctions I. Tight junction structure and function: lessons from mutant animals and proteins. Am. J. Physiol. Gastrointest. Liver Physiol. 279, G250-G254.
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279
    • Mitic, L.L.1    Van Itallie, C.M.2    Anderson, J.M.3
  • 65
    • 21044437802 scopus 로고    scopus 로고
    • Tight junctions in Schwann cells of peripheral myelinated axons: a lesson from claudin-19-deficient mice
    • Miyamoto, T., Morita, K., Takemoto, D., Takeuchi, K., Kitano, Y., Miyakawa, T., et al., 2005. Tight junctions in Schwann cells of peripheral myelinated axons: a lesson from claudin-19-deficient mice. J. Cell Biol. 169, 527-538.
    • (2005) J. Cell Biol. , vol.169 , pp. 527-538
    • Miyamoto, T.1    Morita, K.2    Takemoto, D.3    Takeuchi, K.4    Kitano, Y.5    Miyakawa, T.6
  • 66
    • 27544448588 scopus 로고    scopus 로고
    • Claudin proteins in human cancer: promising new targets for diagnosis and therapy
    • Morin, P.J., 2005. Claudin proteins in human cancer: promising new targets for diagnosis and therapy. Cancer Res. 65, 9603-9606.
    • (2005) Cancer Res , vol.65 , pp. 9603-9606
    • Morin, P.J.1
  • 67
    • 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., 1999. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc. Natl. Acad. Sci. USA 96, 511-516.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 68
    • 0031798631 scopus 로고    scopus 로고
    • Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes
    • Moroi, S., Saitou, M., Fujimoto, K., Sakakibara, A., Furuse, M., Yoshida, O., et al., 1998. Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes. Am. J. Physiol. 274, C1708-C1717.
    • (1998) Am. J. Physiol. , vol.274
    • Moroi, S.1    Saitou, M.2    Fujimoto, K.3    Sakakibara, A.4    Furuse, M.5    Yoshida, O.6
  • 69
    • 17544399838 scopus 로고    scopus 로고
    • A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting
    • Muller, D., Kausalya, P.J., Claverie-Martin, F., Meij, I.C., Eggert, P., Garcia-Nieto, V., et al., 2003. A novel claudin 16 mutation associated with childhood hypercalciuria abolishes binding to ZO-1 and results in lysosomal mistargeting. Am. J. Hum. Genet. 73, 1293-1301.
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 1293-1301
    • Muller, D.1    Kausalya, P.J.2    Claverie-Martin, F.3    Meij, I.C.4    Eggert, P.5    Garcia-Nieto, V.6
  • 71
    • 0035479827 scopus 로고    scopus 로고
    • Molecular architecture of adherens junctions
    • Nagafuchi, A., 2001. Molecular architecture of adherens junctions. Curr. Opin. Cell Biol. 13, 600-603.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 600-603
    • Nagafuchi, A.1
  • 73
    • 0037648580 scopus 로고    scopus 로고
    • Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice
    • Nitta, T., Hata, M., Gotoh, S., Seo, Y., Sasaki, H., Hashimoto, N., et al., 2003. Size-selective loosening of the blood-brain barrier in claudin-5-deficient mice. J. Cell Biol. 161, 653-660.
    • (2003) J. Cell Biol. , vol.161 , pp. 653-660
    • Nitta, T.1    Hata, M.2    Gotoh, S.3    Seo, Y.4    Sasaki, H.5    Hashimoto, N.6
  • 74
    • 33845900444 scopus 로고    scopus 로고
    • Distinct subdomain organization and molecular composition of a tight junction with adherens junction features
    • Nunes, F.D., Lopez, L.N., Lin, H.W., Davies, C., Azevedo, R.B., Gow, A., et al., 2006. Distinct subdomain organization and molecular composition of a tight junction with adherens junction features. J. Cell Sci. 119, 4819-4827.
    • (2006) J. Cell Sci. , vol.119 , pp. 4819-4827
    • Nunes, F.D.1    Lopez, L.N.2    Lin, H.W.3    Davies, C.4    Azevedo, R.B.5    Gow, A.6
  • 75
    • 20144388728 scopus 로고    scopus 로고
    • Abnormal development of nephrons in claudin-16-defective Japanese black cattle
    • Okada, K., Ishikawa, N., Fujimori, K., Goryo, M., Ikeda, M., Sasaki, J., et al., 2005. Abnormal development of nephrons in claudin-16-defective Japanese black cattle. J. Vet. Med. Sci. 67, 171-178.
    • (2005) J. Vet. Med. Sci. , vol.67 , pp. 171-178
    • Okada, K.1    Ishikawa, N.2    Fujimori, K.3    Goryo, M.4    Ikeda, M.5    Sasaki, J.6
  • 76
    • 0032535154 scopus 로고    scopus 로고
    • Genes for the CPE receptor (CPETR1) and the human homolog of RVP1 (CPETR2) are localized within the Williams-Beuren syndrome deletion
    • Paperna, T., Peoples, R., Wang, Y.K., Kaplan, P., Francke, U., 1998. Genes for the CPE receptor (CPETR1) and the human homolog of RVP1 (CPETR2) are localized within the Williams-Beuren syndrome deletion. Genomics 54, 453-459.
    • (1998) Genomics , vol.54 , pp. 453-459
    • Paperna, T.1    Peoples, R.2    Wang, Y.K.3    Kaplan, P.4    Francke, U.5
  • 77
    • 38049166110 scopus 로고    scopus 로고
    • Formation of tight junction: determinants of homophilic interaction between classic claudins
    • Piontek, J., Winkler, L., Wolburg, H., Muller, S.L., Zuleger, N., Piehl, C., et al., 2008. Formation of tight junction: determinants of homophilic interaction between classic claudins. FASEB J. 22, 146-158.
    • (2008) FASEB J , vol.22 , pp. 146-158
    • Piontek, J.1    Winkler, L.2    Wolburg, H.3    Muller, S.L.4    Zuleger, N.5    Piehl, C.6
  • 78
    • 0037191066 scopus 로고    scopus 로고
    • Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells
    • Poliak, S., Matlis, S., Ullmer, C., Scherer, S.S., Peles, E., 2002. Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells. J. Cell Biol. 159, 361-372.
    • (2002) J. Cell Biol. , vol.159 , pp. 361-372
    • Poliak, S.1    Matlis, S.2    Ullmer, C.3    Scherer, S.S.4    Peles, E.5
  • 80
    • 3543024486 scopus 로고    scopus 로고
    • The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions
    • Ruffer, C., Gerke, V., 2004. The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions. Eur. J. Cell Biol. 83, 135-144.
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 135-144
    • Ruffer, C.1    Gerke, V.2
  • 81
    • 0032550221 scopus 로고    scopus 로고
    • Occludindeficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou, M., Fujimoto, K., Doi, Y., Itoh, M., Fujimoto, T., Furuse, M., 1998. Occludindeficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J. Cell Biol. 141, 397-408.
    • (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
  • 85
    • 0034674563 scopus 로고    scopus 로고
    • CaCo- 2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin
    • Singh, U., Van Itallie, C.M., Mitic, L.L., Anderson, J.M., McClane, B.A., 2000. CaCo- 2 cells treated with Clostridium perfringens enterotoxin form multiple large complex species, one of which contains the tight junction protein occludin. J. Biol. Chem. 275, 18407-18417.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18407-18417
    • Singh, U.1    Van Itallie, C.M.2    Mitic, L.L.3    Anderson, J.M.4    McClane, B.A.5
  • 86
    • 0031172452 scopus 로고    scopus 로고
    • Identification, characterization, and precise mapping of a human gene encoding a novel membrane-spanning protein from the 22q11 region deleted in velo-cardio-facial syndrome
    • Sirotkin, H., Morrow, B., Saint-Jore, B., Puech, A., Das Gupta, R., Patanjali, S.R., et al., 1997. Identification, characterization, and precise mapping of a human gene encoding a novel membrane-spanning protein from the 22q11 region deleted in velo-cardio-facial syndrome. Genomics 42, 245-251.
    • (1997) Genomics , vol.42 , pp. 245-251
    • Sirotkin, H.1    Morrow, B.2    Saint-Jore, B.3    Puech, A.4    Das Gupta, R.5    Patanjali, S.R.6
  • 87
    • 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., et al., 1999. 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) 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
  • 88
  • 90
    • 27744479065 scopus 로고    scopus 로고
    • Phosphorylation of ephrin-B1 via the interaction with claudin following cell-cell contact formation
    • Tanaka, M., Kamata, R., Sakai, R., 2005. Phosphorylation of ephrin-B1 via the interaction with claudin following cell-cell contact formation. EMBO J. 24, 3700-3711.
    • (2005) EMBO J , vol.24 , pp. 3700-3711
    • Tanaka, M.1    Kamata, R.2    Sakai, R.3
  • 92
    • 0035897413 scopus 로고    scopus 로고
    • OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes
    • Tiwari-Woodruff, S.K., Buznikov, A.G., Vu, T.Q., Micevych, P.E., Chen, K., Kornblum, H.I., et al., 2001. OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes. J. Cell Biol. 153, 295-305.
    • (2001) J. Cell Biol. , vol.153 , pp. 295-305
    • Tiwari-Woodruff, S.K.1    Buznikov, A.G.2    Vu, T.Q.3    Micevych, P.E.4    Chen, K.5    Kornblum, H.I.6
  • 94
    • 20444416411 scopus 로고    scopus 로고
    • Delayed epidermal permeability barrier formation and hair follicle aberrations in Inv-Cldn6 mice
    • Troy, T.C., Rahbar, R., Arabzadeh, A., Cheung, R.M., Turksen, K., 2005. Delayed epidermal permeability barrier formation and hair follicle aberrations in Inv-Cldn6 mice. Mech. Dev. 122, 805-819.
    • (2005) Mech. Dev. , vol.122 , pp. 805-819
    • Troy, T.C.1    Rahbar, R.2    Arabzadeh, A.3    Cheung, R.M.4    Turksen, K.5
  • 95
    • 0034599992 scopus 로고    scopus 로고
    • Pores in the wall: claudins constitute tight junction strands containing aqueous pores
    • Tsukita, S., Furuse, M., 2000. Pores in the wall: claudins constitute tight junction strands containing aqueous pores. J. Cell Biol. 149, 13-16.
    • (2000) J. Cell Biol. , vol.149 , pp. 13-16
    • Tsukita, S.1    Furuse, M.2
  • 97
    • 0036336486 scopus 로고    scopus 로고
    • Permeability barrier dysfunction in transgenic mice overexpressing claudin 6
    • Turksen, K., Troy, T.C., 2002. Permeability barrier dysfunction in transgenic mice overexpressing claudin 6. Development 129, 1775-1784.
    • (2002) Development , vol.129 , pp. 1775-1784
    • Turksen, K.1    Troy, T.C.2
  • 98
    • 0034504947 scopus 로고    scopus 로고
    • Putting the squeeze' on the tight junction: understanding cytoskeletal regulation
    • Turner, J.R., 2000. 'Putting the squeeze' on the tight junction: understanding cytoskeletal regulation. Semin. Cell Dev. Biol. 11, 301-308.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 301-308
    • Turner, J.R.1
  • 99
    • 10444264499 scopus 로고    scopus 로고
    • The molecular physiology of tight junction pores
    • Van Itallie, C.M., Anderson, J.M., 2004. The molecular physiology of tight junction pores. Physiology (Bethesda) 19, 331-338.
    • (2004) Physiology (Bethesda) , vol.19 , pp. 331-338
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 100
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie, C.M., Anderson, J.M., 2006. Claudins and epithelial paracellular transport. Annu. Rev. Physiol. 68, 403-429.
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 101
    • 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, J.M., 2001. Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J. Clin. Invest. 107, 1319-1327.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 102
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins
    • Van Itallie, C.M., Fanning, A.S., Anderson, J.M., 2003. Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am. J. Physiol. Renal Physiol. 285 (6), F1078-F1084.
    • (2003) Am. J. Physiol. Renal Physiol. , vol.285 , Issue.6
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 104
    • 0022748005 scopus 로고
    • The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells
    • van Meer, G., Simons, K., 1986. The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells. EMBO J. 5, 1455-1464.
    • (1986) EMBO J , vol.5 , pp. 1455-1464
    • van Meer, G.1    Simons, K.2
  • 105
    • 0022516245 scopus 로고
    • The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next
    • van Meer, G., Gumbiner, B., Simons, K., 1986. The tight junction does not allow lipid molecules to diffuse from one epithelial cell to the next. Nature 322, 639-641.
    • (1986) Nature , vol.322 , pp. 639-641
    • van Meer, G.1    Gumbiner, B.2    Simons, K.3
  • 106
    • 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, D.D., Marcondes, M.C., Fox, H.S., 2004. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell. Biol. 24 (19), 8408-8417.
    • (2004) Mol. Cell. Biol. , vol.24 , Issue.19 , pp. 8408-8417
    • Wen, H.1    Watry, D.D.2    Marcondes, M.C.3    Fox, H.S.4
  • 107
    • 17744380785 scopus 로고    scopus 로고
    • Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29
    • Wilcox, E.R., Burton, Q.L., Naz, S., Riazuddin, S., Smith, T.N., Ploplis, B., et al., 2001. Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29. Cell 104, 165-172.
    • (2001) Cell , vol.104 , pp. 165-172
    • Wilcox, E.R.1    Burton, Q.L.2    Naz, S.3    Riazuddin, S.4    Smith, T.N.5    Ploplis, B.6
  • 108
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong, V., Gumbiner, B.M., 1997. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136, 399-409.
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 109
    • 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., 2003. Claudin-8 expression in Madin-Darby canine kidney cells augments the paracellular barrier to cation permeation. J. Biol. Chem. 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
  • 110
    • 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., Burgel, N., Gunzel, D., Richter, J., Mankertz, J., Wahnschaffe, U., et al., 2007. 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) Gut , vol.56 , pp. 61-72
    • Zeissig, S.1    Burgel, N.2    Gunzel, D.3    Richter, J.4    Mankertz, J.5    Wahnschaffe, U.6


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