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Volumn 81, Issue 1, 2003, Pages 1-44

Tight junction proteins

Author keywords

Cingulin; Claudin; JAM, MAGUK, ZO; Occludin; Tight junctions

Indexed keywords

IMMUNOGLOBULIN; LIPID;

EID: 0037212701     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(02)00037-8     Document Type: Review
Times cited : (1001)

References (273)
  • 1
    • 0035665517 scopus 로고    scopus 로고
    • Lung epithelial barrier function and wound healing are decreased by IL-4 and IL-13 and enhanced by IFN-gamma
    • Ahdieh M., Vandenbos T., Youakim A. Lung epithelial barrier function and wound healing are decreased by IL-4 and IL-13 and enhanced by IFN-gamma. Am. J. Physiol. Cell Physiol. 281:2001;C2029-C2038.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Ahdieh, M.1    Vandenbos, T.2    Youakim, A.3
  • 2
    • 0037129361 scopus 로고    scopus 로고
    • Identification of genes associated with head and neck carcinogenesis by cDNA microarray comparison between matched primary normal epithelial and squamous carcinoma cells
    • Al Moustafa A.E., Alaoui-Jamali M.A., Batist G., Hernandez-Perez M., Serruya C., Alpert L., Black M.J., Sladek R., Foulkes W.D. Identification of genes associated with head and neck carcinogenesis by cDNA microarray comparison between matched primary normal epithelial and squamous carcinoma cells. Oncogene. 21:2002;2634-2640.
    • (2002) Oncogene , vol.21 , pp. 2634-2640
    • Al Moustafa, A.E.1    Alaoui-Jamali, M.A.2    Batist, G.3    Hernandez-Perez, M.4    Serruya, C.5    Alpert, L.6    Black, M.J.7    Sladek, R.8    Foulkes, W.D.9
  • 4
    • 0032941962 scopus 로고    scopus 로고
    • Differential behavior of E-cadherin and occludin in their colocalization with ZO-1 during the establishment of epithelial cell polarity
    • Ando-Akatsuka Y., Yonemura S., Itoh M., Furuse M., Tsukita S. Differential behavior of E-cadherin and occludin in their colocalization with ZO-1 during the establishment of epithelial cell polarity. J. Cell Physiol. 179:1999;115-125.
    • (1999) J. Cell Physiol. , vol.179 , pp. 115-125
    • Ando-Akatsuka, Y.1    Yonemura, S.2    Itoh, M.3    Furuse, M.4    Tsukita, S.5
  • 5
    • 0035914359 scopus 로고    scopus 로고
    • Protein kinase C regulates the phosphorylation and cellular localization of occludin
    • Andreeva A.Y., Krause E., Muller E.C., Blasig I.E., Utepbergenov D.I. Protein kinase C regulates the phosphorylation and cellular localization of occludin. J. Biol. Chem. 276:2001;38480-38486.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38480-38486
    • Andreeva, A.Y.1    Krause, E.2    Muller, E.C.3    Blasig, I.E.4    Utepbergenov, D.I.5
  • 6
    • 0026022395 scopus 로고
    • Differential expression of two cadherins in Xenopus laevis
    • Angres B., Muller A.H., Kellermann J., Hausen P. Differential expression of two cadherins in Xenopus laevis. Development. 111:1991;829-844.
    • (1991) Development , vol.111 , pp. 829-844
    • Angres, B.1    Muller, A.H.2    Kellermann, J.3    Hausen, P.4
  • 7
    • 0033551811 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occluden 1, A potential mechanism for vascular permeability in diabetic retinopathy and tumors
    • Antonetti D.A., Barber A.J., Hollinger L.A., Wolpert E.B., Gardner T.W. Vascular endothelial growth factor induces rapid phosphorylation of tight junction proteins occludin and zonula occluden 1, A potential mechanism for vascular permeability in diabetic retinopathy and tumors. J. Biol. Chem. 274:1999;23463-23467.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23463-23467
    • Antonetti, D.A.1    Barber, A.J.2    Hollinger, L.A.3    Wolpert, E.B.4    Gardner, T.W.5
  • 8
    • 0035824527 scopus 로고    scopus 로고
    • Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor
    • Arrate M.P., Rodriguez J.M., Tran T.M., Brock T.A., Cunningham S.A. Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. J. Biol. Chem. 276:2001;45826-45832.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45826-45832
    • Arrate, M.P.1    Rodriguez, J.M.2    Tran, T.M.3    Brock, T.A.4    Cunningham, S.A.5
  • 9
    • 0032753450 scopus 로고    scopus 로고
    • Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells
    • Asakura T., Nakanishi H., Sakisaka T., Takahashi K., Mandai K., Nishimura M., Sasaki T., Takai Y. Similar and differential behaviour between the nectin-afadin-ponsin and cadherin-catenin systems during the formation and disruption of the polarized junctional alignment in epithelial cells. Genes Cells. 4:1999;573-581.
    • (1999) Genes Cells , vol.4 , pp. 573-581
    • Asakura, T.1    Nakanishi, H.2    Sakisaka, T.3    Takahashi, K.4    Mandai, K.5    Nishimura, M.6    Sasaki, T.7    Takai, Y.8
  • 11
    • 0029588323 scopus 로고
    • Widespread expression of the peripheral myelin protein-22 gene (PMP22) in neural and non-neural tissues during murine development
    • Baechner D., Liehr T., Hameister H., Altenberger H., Grehl H., Suter U., Rautenstrauss B. Widespread expression of the peripheral myelin protein-22 gene (PMP22) in neural and non-neural tissues during murine development. J. Neurosci. Res. 42:1995;733-741.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 733-741
    • Baechner, D.1    Liehr, T.2    Hameister, H.3    Altenberger, H.4    Grehl, H.5    Suter, U.6    Rautenstrauss, B.7
  • 12
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Balda M.S., Anderson J.M. Two classes of tight junctions are revealed by ZO-1 isoforms. Am. J. Physiol. 264:1993;C918-C924.
    • (1993) Am. J. Physiol. , vol.264
    • Balda, M.S.1    Anderson, J.M.2
  • 13
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda M.S., Matter K. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J. 19:2000;2024-2033.
    • (2000) EMBO J. , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 16
    • 0030590868 scopus 로고    scopus 로고
    • The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain
    • Balda M.S., Anderson J.M., Matter K. The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain. FEBS Lett. 399:1996;326-332.
    • (1996) FEBS Lett. , vol.399 , pp. 326-332
    • Balda, M.S.1    Anderson, J.M.2    Matter, K.3
  • 17
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda M.S., Whitney J.A., Flores C., Gonzalez S., Cereijido M., Matter K. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J. Cell Biol. 134:1996;1031-1049.
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 18
    • 0032769698 scopus 로고    scopus 로고
    • A dominant mutant of occludin disrupts tight junction structure and function
    • Bamforth S.D., Kniesel U., Wolburg H., Engelhardt B., Risau W. A dominant mutant of occludin disrupts tight junction structure and function. J. Cell Sci. 112(Pt. 12):1999;1879-1888.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 12 , pp. 1879-1888
    • Bamforth, S.D.1    Kniesel, U.2    Wolburg, H.3    Engelhardt, B.4    Risau, W.5
  • 19
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • Barker R.J., Price R.L., Gourdie R.G. Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions. Circ. Res. 90:2002;317-324.
    • (2002) Circ. Res. , vol.90 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 22
    • 0039027605 scopus 로고    scopus 로고
    • Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin
    • Bazzoni G., Martinez-Estrada O.M., Orsenigo F., Cordenonsi M., Citi S., Dejana E. Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin. J. Biol. Chem. 275:2000;20520-20526.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20520-20526
    • Bazzoni, G.1    Martinez-Estrada, O.M.2    Orsenigo, F.3    Cordenonsi, M.4    Citi, S.5    Dejana, E.6
  • 23
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins. more than meets the eye J. Cell Sci. 114:2001;4143-4151.
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 24
    • 4243507704 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 associates with Jun, Fos and C/E[beta]P transcription factors in epithelial cells
    • Betanzos A., Amerena J.A., Azuara E., Lopez-Bayghen E., Gonzalez-Mariscal L. The tight junction protein ZO-2 associates with Jun, Fos and C/E[beta]P transcription factors in epithelial cells. Mol. Biol. Cell. 12S:2001;219a.
    • (2001) Mol. Biol. Cell , vol.12 S
    • Betanzos, A.1    Amerena, J.A.2    Azuara, E.3    Lopez-Bayghen, E.4    Gonzalez-Mariscal, L.5
  • 25
    • 0035861856 scopus 로고    scopus 로고
    • Classification of PDZ domains
    • Bezprozvanny I., Maximov A. Classification of PDZ domains. FEBS Lett. 509:2001;457-462.
    • (2001) FEBS Lett. , vol.509 , pp. 457-462
    • Bezprozvanny, I.1    Maximov, A.2
  • 27
    • 0034254923 scopus 로고    scopus 로고
    • The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin
    • Boettner B., Govek E.E., Cross J., Van Aelst L. The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin. Proc. Natl. Acad. Sci. USA. 97:2000;9064-9069.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9064-9069
    • Boettner, B.1    Govek, E.E.2    Cross, J.3    Van Aelst, L.4
  • 28
    • 0030780536 scopus 로고    scopus 로고
    • The maternal par genes and the segregation of cell fate specification activities in early Caenorhabditis elegans embryos
    • Bowerman B., Ingram M.K., Hunter C.P. The maternal par genes and the segregation of cell fate specification activities in early Caenorhabditis elegans embryos. Development. 124:1997;3815-3826.
    • (1997) Development , vol.124 , pp. 3815-3826
    • Bowerman, B.1    Ingram, M.K.2    Hunter, C.P.3
  • 30
    • 0025999560 scopus 로고
    • Isolation and characterization of transcripts induced by androgen withdrawal and apoptotic cell death in the rat ventral prostate
    • Briehl M.M., Miesfeld R.L. Isolation and characterization of transcripts induced by androgen withdrawal and apoptotic cell death in the rat ventral prostate. Mol. Endocrinol. 5:1991;1381-1388.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1381-1388
    • Briehl, M.M.1    Miesfeld, R.L.2
  • 31
    • 0035865044 scopus 로고    scopus 로고
    • Overexpression of the Xenopus tight-junction protein claudin causes randomization of the left-right body axis
    • Brizuela B.J., Wessely O., De Robertis E.M. Overexpression of the Xenopus tight-junction protein claudin causes randomization of the left-right body axis. Dev. Biol. 230:2001;217-229.
    • (2001) Dev. Biol. , vol.230 , pp. 217-229
    • Brizuela, B.J.1    Wessely, O.2    De Robertis, E.M.3
  • 32
    • 0030695395 scopus 로고    scopus 로고
    • Oligodendrocyte-specific protein (OSP) is a major component of CNS myelin
    • Bronstein J.M., Micevych P.E., Chen K. Oligodendrocyte-specific protein (OSP) is a major component of CNS myelin. J. Neurosci. Res. 50:1997;713-720.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 713-720
    • Bronstein, J.M.1    Micevych, P.E.2    Chen, K.3
  • 34
    • 0033601747 scopus 로고    scopus 로고
    • The junction-associated protein AF-6 interacts and clusters with specific Eph receptor tyrosine kinases at specialized sites of cell-cell contact in the brain
    • Buchert M., Schneider S., Meskenaite V., Adams M.T., Canaani E., Baechi T., Moelling K., Hovens C.M. The junction-associated protein AF-6 interacts and clusters with specific Eph receptor tyrosine kinases at specialized sites of cell-cell contact in the brain. J. Cell Biol. 144:1999;361-371.
    • (1999) J. Cell Biol. , vol.144 , pp. 361-371
    • Buchert, M.1    Schneider, S.2    Meskenaite, V.3    Adams, M.T.4    Canaani, E.5    Baechi, T.6    Moelling, K.7    Hovens, C.M.8
  • 36
    • 0029756510 scopus 로고    scopus 로고
    • Tight junctions in early amphibian development: Detection of junctional cingulin from the 2-cell stage and its localization at the boundary of distinct membrane domains in dividing blastomeres in low calcium
    • Cardellini P., Davanzo G., Citi S. Tight junctions in early amphibian development. detection of junctional cingulin from the 2-cell stage and its localization at the boundary of distinct membrane domains in dividing blastomeres in low calcium Dev. Dyn. 207:1996;104-113.
    • (1996) Dev. Dyn. , vol.207 , pp. 104-113
    • Cardellini, P.1    Davanzo, G.2    Citi, S.3
  • 37
    • 0035807869 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor (CAR) binds immunoglobulins
    • Carson S.D., Chapman N.M. Coxsackievirus and adenovirus receptor (CAR) binds immunoglobulins. Biochemistry. 40:2001;14324-14329.
    • (2001) Biochemistry , vol.40 , pp. 14324-14329
    • Carson, S.D.1    Chapman, N.M.2
  • 38
  • 39
    • 0034099223 scopus 로고    scopus 로고
    • Restoration of tight junction structure and barrier function by down-regulation of the nitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells
    • Chen Y., Lu Q., Schneeberger E.E., Goodenough D.A. Restoration of tight junction structure and barrier function by down-regulation of the nitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells. Mol. Biol. Cell. 11:2000;849-862.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 849-862
    • Chen, Y.1    Lu, Q.2    Schneeberger, E.E.3    Goodenough, D.A.4
  • 40
    • 0037040188 scopus 로고    scopus 로고
    • Protein kinase C signaling regulates ZO-1 translocation and increased paracellular flux of T84 colonocytes exposed to Clostridium difficile toxin A
    • Chen M.L., Pothoulakis C., LaMont J.T. Protein kinase C signaling regulates ZO-1 translocation and increased paracellular flux of T84 colonocytes exposed to Clostridium difficile toxin A. J. Biol. Chem. 277:2002;4247-4254.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4247-4254
    • Chen, M.L.1    Pothoulakis, C.2    LaMont, J.T.3
  • 41
    • 0036226069 scopus 로고    scopus 로고
    • Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight jnction formation in canine kidney epithelial cells
    • Chen Y.H., Lu Q., Goodenough D.A., Jeansonne B. Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight jnction formation in canine kidney epithelial cells. Mol. Biol. Cell. 13:2002;1227-1237.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1227-1237
    • Chen, Y.H.1    Lu, Q.2    Goodenough, D.A.3    Jeansonne, B.4
  • 43
    • 0033516532 scopus 로고    scopus 로고
    • Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma
    • Chlenski A., Ketels K.V., Tsao M.S., Talamonti M.S., Anderson M.R., Oyasu R., Scarpelli D.G. Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma. Int. J. Cancer. 82:1999;137-144.
    • (1999) Int. J. Cancer , vol.82 , pp. 137-144
    • Chlenski, A.1    Ketels, K.V.2    Tsao, M.S.3    Talamonti, M.S.4    Anderson, M.R.5    Oyasu, R.6    Scarpelli, D.G.7
  • 45
    • 0034755902 scopus 로고    scopus 로고
    • A 22-amino acid synthetic peptide corresponding to the second extracellular loop of rat occludin perturbs the blood-testis barrier and disrupts spermatogenesis reversibly in vivo
    • Chung N.P., Mruk D., Mo M.Y., Lee W.M., Cheng C.Y. A 22-amino acid synthetic peptide corresponding to the second extracellular loop of rat occludin perturbs the blood-testis barrier and disrupts spermatogenesis reversibly in vivo. Biol. Reprod. 65:2001;1340-1351.
    • (2001) Biol. Reprod. , vol.65 , pp. 1340-1351
    • Chung, N.P.1    Mruk, D.2    Mo, M.Y.3    Lee, W.M.4    Cheng, C.Y.5
  • 46
    • 0029122307 scopus 로고
    • Phosphorylation of the tight junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells
    • Citi S., Denisenko N. Phosphorylation of the tight junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells. J. Cell Sci. 108(Pt. 8):1995;2917-2926.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 8 , pp. 2917-2926
    • Citi, S.1    Denisenko, N.2
  • 48
    • 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. 39:1978;219-232.
    • (1978) J. Membr. Biol. , vol.39 , pp. 219-232
    • Claude, P.1
  • 50
    • 0031457495 scopus 로고    scopus 로고
    • Occludin dephosphorylation in early development of Xenopus laevis
    • Cordenonsi M., Mazzon E., De Rigo L., Baraldo S., Meggio F., Citi S. Occludin dephosphorylation in early development of Xenopus laevis. J. Cell Sci. 110(Pt. 24):1997;3131-3139.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 24 , pp. 3131-3139
    • Cordenonsi, M.1    Mazzon, E.2    De Rigo, L.3    Baraldo, S.4    Meggio, F.5    Citi, S.6
  • 51
  • 52
    • 0033199904 scopus 로고    scopus 로고
    • Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin
    • Cordenonsi M., Turco F., D'Atri F., Hammar E., Martinucci G., Meggio F., Citi S. Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin. Eur. J. Biochem. 264:1999;374-384.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 374-384
    • Cordenonsi, M.1    Turco, F.2    D'Atri, F.3    Hammar, E.4    Martinucci, G.5    Meggio, F.6    Citi, S.7
  • 54
    • 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. 507:2001;21-24.
    • (2001) FEBS Lett. , vol.507 , pp. 21-24
    • D'Atri, F.1    Citi, S.2
  • 55
    • 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. 277:2002;27757-27764.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27757-27764
    • D'Atri, F.1    Nadalutti, F.2    Citi, S.3
  • 56
    • 0025253083 scopus 로고
    • Protein zero of peripheral nerve myelin: Biosynthesis, membrane insertion, and evidence for homotypic interaction
    • D'Urso D., Brophy P.J., Staugaitis S.M., Gillespie C.S., Frey A.B., Stempak J.G., Colman D.R. Protein zero of peripheral nerve myelin. biosynthesis, membrane insertion, and evidence for homotypic interaction Neuron. 4:1990;449-460.
    • (1990) Neuron , vol.4 , pp. 449-460
    • D'Urso, D.1    Brophy, P.J.2    Staugaitis, S.M.3    Gillespie, C.S.4    Frey, A.B.5    Stempak, J.G.6    Colman, D.R.7
  • 57
    • 0033134949 scopus 로고    scopus 로고
    • Peripheral myelin protein 22 and protein zero: A novel association in peripheral nervous system myelin
    • D'Urso D., Ehrhardt P., Muller H.W. Peripheral myelin protein 22 and protein zero. a novel association in peripheral nervous system myelin J. Neurosci. 19:1999;3396-3403.
    • (1999) J. Neurosci. , vol.19 , pp. 3396-3403
    • D'Urso, D.1    Ehrhardt, P.2    Muller, H.W.3
  • 60
    • 0029862538 scopus 로고    scopus 로고
    • Involvement of a heterotrimeric G protein alpha subunit in tight junction biogenesis
    • Denker B.M., Saha C., Khawaja S., Nigam S.K. Involvement of a heterotrimeric G protein alpha subunit in tight junction biogenesis. J. Biol. Chem. 271:1996;25750-25753.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25750-25753
    • Denker, B.M.1    Saha, C.2    Khawaja, S.3    Nigam, S.K.4
  • 61
    • 0031440289 scopus 로고    scopus 로고
    • MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains
    • Dobrosotskaya I., Guy R.K., James G.L. MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains. J. Biol. Chem. 272:1997;31589-31597.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31589-31597
    • Dobrosotskaya, I.1    Guy, R.K.2    James, G.L.3
  • 62
    • 0034696822 scopus 로고    scopus 로고
    • MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures
    • Dobrosotskaya I.Y., James G.L. MAGI-1 interacts with beta-catenin and is associated with cell-cell adhesion structures. Biochem. Biophys. Res. Commun. 270:2000;903-909.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 903-909
    • Dobrosotskaya, I.Y.1    James, G.L.2
  • 63
    • 0029883798 scopus 로고    scopus 로고
    • Identification of isoforms of G proteins and PKC that colocalize with tight junctions
    • Dodane V., Kachar B. Identification of isoforms of G proteins and PKC that colocalize with tight junctions. J. Membr. Biol. 149:1996;199-209.
    • (1996) J. Membr. Biol. , vol.149 , pp. 199-209
    • Dodane, V.1    Kachar, B.2
  • 64
    • 0028802652 scopus 로고
    • Protein zero, a nervous system adhesion molecule, triggers epithelial reversion in host carcinoma cells
    • Doyle J.P., Stempak J.G., Cowin P., Colman D.R., D'Urso D. Protein zero, a nervous system adhesion molecule, triggers epithelial reversion in host carcinoma cells. J. Cell Biol. 131:1995;465-482.
    • (1995) J. Cell Biol. , vol.131 , pp. 465-482
    • Doyle, J.P.1    Stempak, J.G.2    Cowin, P.3    Colman, D.R.4    D'Urso, D.5
  • 65
    • 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. Membrane asymmetry in epithelia. is the tight junction a barrier to diffusion in the plasma membrane? Nature. 294:1981;718-722.
    • (1981) Nature , vol.294 , pp. 718-722
    • Dragsten, P.R.1    Blumenthal, R.2    Handler, J.S.3
  • 66
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K., Schulz C.U., Meyer Zu Brickwedde M.K., Pendl G.G., Vestweber D. Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J. Biol. Chem. 275:2000;27979-27988.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3    Pendl, G.G.4    Vestweber, D.5
  • 68
    • 0026523921 scopus 로고
    • Rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain
    • Elferink L.A., Anzai K., Scheller R.H. rab15, a novel low molecular weight GTP-binding protein specifically expressed in rat brain. J. Biol. Chem. 267:1992;22693.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22693
    • Elferink, L.A.1    Anzai, K.2    Scheller, R.H.3
  • 69
    • 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. Claudin-2 is selectively expressed in proximal nephron in mouse kidney. Am. J. Physiol. Renal Physiol. 281:2001;F966-F974.
    • (2001) Am. J. Physiol. Renal Physiol. , vol.281
    • Enck, A.H.1    Berger, U.V.2    Yu, A.S.3
  • 70
    • 0029556584 scopus 로고
    • Isolation of cDNA encoding 7H6-reactive polypeptide defines a new class of protein with [alpha]-helical coiled-coil structure and DA-box similar to yeast chromosomal segregation proteins
    • Ezoe E., Kokai Y., Konishi Y., Kuwahara K., Zhong Y., Enomoto K., Sawada N., Hirata K., Mori M. Isolation of cDNA encoding 7H6-reactive polypeptide defines a new class of protein with [alpha]-helical coiled-coil structure and DA-box similar to yeast chromosomal segregation proteins. Tumor Res. 30:1995;21-36.
    • (1995) Tumor Res. , vol.30 , pp. 21-36
    • Ezoe, E.1    Kokai, Y.2    Konishi, Y.3    Kuwahara, K.4    Zhong, Y.5    Enomoto, K.6    Sawada, N.7    Hirata, K.8    Mori, M.9
  • 71
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning A.S., Jameson B.J., Jesaitis L.A., Anderson J.M. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J. Biol. Chem. 273:1998;29745-29753.
    • (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
  • 74
    • 0036354737 scopus 로고    scopus 로고
    • Hypoxia-induced hyperpermeability in brain microvessel endothelial cells involves VEGF-mediated changes in the expression of zonula occludens-1
    • Fischer S., Wobben M., Marti H.H., Renz D., Schaper W. Hypoxia-induced hyperpermeability in brain microvessel endothelial cells involves VEGF-mediated changes in the expression of zonula occludens-1. Microvasc. Res. 63:2002;70-80.
    • (2002) Microvasc. Res. , vol.63 , pp. 70-80
    • Fischer, S.1    Wobben, M.2    Marti, H.H.3    Renz, D.4    Schaper, W.5
  • 75
    • 0024505997 scopus 로고
    • Development of tight junctions de novo in the mouse early embryo: Control of assembly of the tight junction-specific protein, ZO-1
    • Fleming T.P., McConnell J., Johnson M.H., Stevenson B.R. Development of tight junctions de novo in the mouse early embryo. control of assembly of the tight junction-specific protein, ZO-1 J. Cell Biol. 108:1989;1407-1418.
    • (1989) J. Cell Biol. , vol.108 , pp. 1407-1418
    • Fleming, T.P.1    McConnell, J.2    Johnson, M.H.3    Stevenson, B.R.4
  • 76
    • 0027411236 scopus 로고
    • Localisation of tight junction protein cingulin is temporally and spatially regulated during early mouse development
    • Fleming T.P., Hay M., Javed Q., Citi S. Localisation of tight junction protein cingulin is temporally and spatially regulated during early mouse development. Development. 117:1993;1135-1144.
    • (1993) Development , vol.117 , pp. 1135-1144
    • Fleming, T.P.1    Hay, M.2    Javed, Q.3    Citi, S.4
  • 77
    • 0001821649 scopus 로고    scopus 로고
    • Developmental assembly of the tight junction
    • Cereijido, M., Anderson, J. (Eds.), Boca Raton
    • Fleming, T.P., Sheth, B., Thomas, F., Fesenko, I., Eckert, J., 2001. Developmental assembly of the tight junction. In: Cereijido, M., Anderson, J. (Eds.), Tight Junctions, Boca Raton, pp. 285-303.
    • (2001) Tight Junctions , pp. 285-303
    • Fleming, T.P.1    Sheth, B.2    Thomas, F.3    Fesenko, I.4    Eckert, J.5
  • 78
    • 0032840311 scopus 로고    scopus 로고
    • Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance
    • Francis S.A., Kelly J.M., McCormack J., Rogers R.A., Lai J., Schneeberger E.E., Lynch R.D. Rapid reduction of MDCK cell cholesterol by methyl-beta-cyclodextrin alters steady state transepithelial electrical resistance. Eur. J. Cell Biol. 78:1999;473-484.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 473-484
    • Francis, S.A.1    Kelly, J.M.2    McCormack, J.3    Rogers, R.A.4    Lai, J.5    Schneeberger, E.E.6    Lynch, R.D.7
  • 79
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes
    • Fujimoto K. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes. J. Cell Sci. 108(Pt. 11):1995;3443-3449.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 11 , pp. 3443-3449
    • Fujimoto, K.1
  • 81
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse M., Itoh M., Hirase T., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127:1994;1617-1626.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 82
    • 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. Claudin-1 and -2. novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin J. Cell Biol. 141:1998;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
  • 83
    • 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. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143:1998;391-401.
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 84
    • 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. 147:1999;891-903.
    • (1999) J. Cell Biol. , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 85
    • 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. 153:2001;263-272.
    • (2001) J. Cell Biol. , vol.153 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 86
    • 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. 156:2002;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    Noda, T.7    Kubo, A.8    Tsukita, S.9
  • 87
    • 0037022122 scopus 로고    scopus 로고
    • Assembly of epithelial tight junctions is negatively regulated by Par6
    • Gao L., Joberty G., Macara I.G. Assembly of epithelial tight junctions is negatively regulated by Par6. Curr. Biol. 12:2002;221-225.
    • (2002) Curr. Biol. , vol.12 , pp. 221-225
    • Gao, L.1    Joberty, G.2    Macara, I.G.3
  • 88
    • 0026090748 scopus 로고
    • Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and early Xenopus embryos
    • Ginsberg D., DeSimone D., Geiger B. Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and early Xenopus embryos. Development. 111:1991;315-325.
    • (1991) Development , vol.111 , pp. 315-325
    • Ginsberg, D.1    DeSimone, D.2    Geiger, B.3
  • 89
    • 0034597533 scopus 로고    scopus 로고
    • Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins
    • Glaunsinger B.A., Lee S.S., Thomas M., Banks L., Javier R. Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins. Oncogene. 19:2000;5270-5280.
    • (2000) Oncogene , vol.19 , pp. 5270-5280
    • Glaunsinger, B.A.1    Lee, S.S.2    Thomas, M.3    Banks, L.4    Javier, R.5
  • 90
    • 0035887255 scopus 로고    scopus 로고
    • Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2
    • Glaunsinger B.A., Weiss R.S., Lee S.S., Javier R. Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2. EMBO J. 20:2001;5578-5586.
    • (2001) EMBO J. , vol.20 , pp. 5578-5586
    • Glaunsinger, B.A.1    Weiss, R.S.2    Lee, S.S.3    Javier, R.4
  • 91
  • 94
    • 85008146432 scopus 로고    scopus 로고
    • The relationship between structure and function of tight junctions
    • Cereijido, M., Anderson, J.M. (Eds.), Boca Raton
    • Gonzalez-Mariscal, L., Avila-Flores, A., Betanzos, A., 2001. The relationship between structure and function of tight junctions. In: Cereijido, M., Anderson, J.M. (Eds.), Tight Junctions, Boca Raton, pp. 89-119.
    • (2001) Tight Junctions , pp. 89-119
    • Gonzalez-Mariscal, L.1    Avila-Flores, A.2    Betanzos, A.3
  • 95
    • 0345188815 scopus 로고    scopus 로고
    • Paracellular channels!
    • Goodenough D.A., Wong V. Paracellular channels! Science. 285:1999;62.
    • (1999) Science , vol.285 , pp. 62
    • Goodenough, D.A.1    Wong, V.2
  • 96
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts
    • Gottardi C.J., Arpin M., Fanning A.S., Louvard D. The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts. Proc. Natl. Acad. Sci. USA. 93:1996;10779-10784.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 98
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff K.K., Yeaman C., Anandasabapathy N., Hsu S.C., Rodriguez-Boulan E., Scheller R.H., Nelson W.J. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell. 93:1998;731-740.
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 99
    • 0024095524 scopus 로고
    • The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex
    • Gumbiner B., Stevenson B., Grimaldi A. The role of the cell adhesion molecule uvomorulin in the formation and maintenance of the epithelial junctional complex. J. Cell Biol. 107:1988;1575-1587.
    • (1988) J. Cell Biol. , vol.107 , pp. 1575-1587
    • Gumbiner, B.1    Stevenson, B.2    Grimaldi, A.3
  • 100
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B., Lowenkopf T., Apatira D. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci. USA. 88:1991;3460-3464.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 101
    • 0030217996 scopus 로고    scopus 로고
    • Molecular genetics of asymmetric cleavage in the early Caenorhabditis elegans embryo
    • Guo S., Kemphues K.J. Molecular genetics of asymmetric cleavage in the early Caenorhabditis elegans embryo. Curr. Opin. Genet. Dev. 6:1996;408-415.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 408-415
    • Guo, S.1    Kemphues, K.J.2
  • 102
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo W., Roth D., Walch-Solimena C., Novick P. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18:1999;1071-1080.
    • (1999) EMBO J. , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 103
    • 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. 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. 277:2002;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
  • 104
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • Haskins J., Gu L., Wittchen E.S., Hibbard J., Stevenson B.R. ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J. Cell Biol. 141:1998;199-208.
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 105
    • 0034463144 scopus 로고    scopus 로고
    • Developmental and hormonal regulation of the expression of oligodendrocyte-specific protein/claudin 11 in mouse testis
    • Hellani A., Ji J., Mauduit C., Deschildre C., Tabone E., Benahmed M. Developmental and hormonal regulation of the expression of oligodendrocyte-specific protein/claudin 11 in mouse testis. Endocrinology. 141:2000;3012-3019.
    • (2000) Endocrinology , vol.141 , pp. 3012-3019
    • Hellani, A.1    Ji, J.2    Mauduit, C.3    Deschildre, C.4    Tabone, E.5    Benahmed, M.6
  • 107
    • 0025744383 scopus 로고
    • Expression of XBcad, a novel cadherin, during oogenesis and early development of Xenopus
    • Herzberg F., Wildermuth V., Wedlich D. Expression of XBcad, a novel cadherin, during oogenesis and early development of Xenopus. Mech. Dev. 35:1991;33-42.
    • (1991) Mech. Dev. , vol.35 , pp. 33-42
    • Herzberg, F.1    Wildermuth, V.2    Wedlich, D.3
  • 108
    • 0032516885 scopus 로고    scopus 로고
    • A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins
    • Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M., Toyoda A., Sudhof T.C., Takai Y. A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins. J. Biol. Chem. 273:1998;21105-21110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21105-21110
    • Hirao, K.1    Hata, Y.2    Ide, N.3    Takeuchi, M.4    Irie, M.5    Yao, I.6    Deguchi, M.7    Toyoda, A.8    Sudhof, T.C.9    Takai, Y.10
  • 109
    • 0034723359 scopus 로고    scopus 로고
    • Three isoforms of synaptic scaffolding molecule and their characterization. Multimerization between the isoforms and their interaction with N-methyl-D-aspartate receptors and SAP90/PSD-95- associated protein
    • Hirao K., Hata Y., Yao I., Deguchi M., Kawabe H., Mizoguchi A., Takai Y. Three isoforms of synaptic scaffolding molecule and their characterization. Multimerization between the isoforms and their interaction with N-methyl-D-aspartate receptors and SAP90/PSD-95- associated protein. J. Biol. Chem. 275:2000;2966-2972.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2966-2972
    • Hirao, K.1    Hata, Y.2    Yao, I.3    Deguchi, M.4    Kawabe, H.5    Mizoguchi, A.6    Takai, Y.7
  • 110
    • 0036197421 scopus 로고    scopus 로고
    • Expression and targeting of the tight junction protein CLDN1 in CLDN1-negative human breast tumor cells
    • Hoevel T., Macek R., Mundigl O., Swisshelm K., Kubbies M. Expression and targeting of the tight junction protein CLDN1 in CLDN1-negative human breast tumor cells. J. Cell Physiol. 191:2002;60-68.
    • (2002) J. Cell Physiol. , vol.191 , pp. 60-68
    • Hoevel, T.1    Macek, R.2    Mundigl, O.3    Swisshelm, K.4    Kubbies, M.5
  • 111
    • 0036000009 scopus 로고    scopus 로고
    • Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes
    • Hofmann I., Schnolzer M., Kaufmann I., Franke W.W. Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes. Mol. Biol. Cell. 13:2002;1665-1676.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1665-1676
    • Hofmann, I.1    Schnolzer, M.2    Kaufmann, I.3    Franke, W.W.4
  • 112
    • 0031773440 scopus 로고    scopus 로고
    • Loss of the tight junction MAGUK ZO-1 in breast cancer: Relationship to glandular differentiation and loss of heterozygosity
    • Hoover K.B., Liao S.Y., Bryant P.J. Loss of the tight junction MAGUK ZO-1 in breast cancer. relationship to glandular differentiation and loss of heterozygosity Am. J. Pathol. 153:1998;1767-1773.
    • (1998) Am. J. Pathol. , vol.153 , pp. 1767-1773
    • Hoover, K.B.1    Liao, S.Y.2    Bryant, P.J.3
  • 113
    • 0028221689 scopus 로고
    • Analysis of the distribution and phosphorylation state of ZO-1 in MDCK and nonepithelial cells
    • Howarth A.G., Singer K.L., Stevenson B.R. Analysis of the distribution and phosphorylation state of ZO-1 in MDCK and nonepithelial cells. J. Membr. Biol. 137:1994;261-270.
    • (1994) J. Membr. Biol. , vol.137 , pp. 261-270
    • Howarth, A.G.1    Singer, K.L.2    Stevenson, B.R.3
  • 114
    • 0034102426 scopus 로고    scopus 로고
    • Occludin modulates transepithelial migration of neutrophils
    • Huber D., Balda M.S., Matter K. Occludin modulates transepithelial migration of neutrophils. J. Biol. Chem. 275:2000;5773-5778.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5773-5778
    • Huber, D.1    Balda, M.S.2    Matter, K.3
  • 115
    • 0017176592 scopus 로고
    • Junctions in developing human and rat kidney: A freeze-fracture study
    • Humbert F., Montesano R., Perrelet A., Orci L. Junctions in developing human and rat kidney. a freeze-fracture study J. Ultrastruct. Res. 56:1976;202-214.
    • (1976) J. Ultrastruct. Res. , vol.56 , pp. 202-214
    • Humbert, F.1    Montesano, R.2    Perrelet, A.3    Orci, L.4
  • 116
    • 0033599549 scopus 로고    scopus 로고
    • Interaction of S-SCAM with neural plakophilin-related Armadillo-repeat protein/delta-catenin
    • Ide N., Hata Y., Deguchi M., Hirao K., Yao I., Takai Y. Interaction of S-SCAM with neural plakophilin-related Armadillo-repeat protein/delta-catenin. Biochem. Biophys. Res. Commun. 256:1999;456-461.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 456-461
    • Ide, N.1    Hata, Y.2    Deguchi, M.3    Hirao, K.4    Yao, I.5    Takai, Y.6
  • 118
    • 0036343646 scopus 로고    scopus 로고
    • Nuclear localization of the tight junction protein ZO-2 in epithelial cells
    • Islas S., Vega J., Ponce L., Gonzalez-Mariscal L. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Exp. Cell Res. 274:2002;138-148.
    • (2002) Exp. Cell Res. , vol.274 , pp. 138-148
    • Islas, S.1    Vega, J.2    Ponce, L.3    Gonzalez-Mariscal, L.4
  • 120
    • 0027300689 scopus 로고
    • The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: CDNA cloning and immunoelectron microscopy
    • Itoh M., Nagafuchi A., Yonemura S., Kitani-Yasuda T., Tsukita S., Tsukita S. The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells. cDNA cloning and immunoelectron microscopy J. Cell Biol. 121:1993;491-502.
    • (1993) J. Cell Biol. , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3    Kitani-Yasuda, T.4    Tsukita, S.5    Tsukita, S.6
  • 121
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments
    • Itoh M., Nagafuchi A., Moroi S., Tsukita S. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to alpha catenin and actin filaments. J. Cell Biol. 138:1997;181-192.
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 122
    • 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. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J. Cell Biol. 147:1999;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
  • 123
    • 0033605347 scopus 로고    scopus 로고
    • Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin
    • Itoh M., Morita K., Tsukita S. Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin. J. Biol. Chem. 274:1999;5981-5986.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5981-5986
    • Itoh, M.1    Morita, K.2    Tsukita, S.3
  • 124
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
    • Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S. Junctional adhesion molecule (JAM) binds to PAR-3. a possible mechanism for the recruitment of PAR-3 to tight junctions J. Cell Biol. 154:2001;491-497.
    • (2001) J. Cell Biol. , vol.154 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 125
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y., Hirose T., Tamai Y., Hirai S., Nagashima Y., Fujimoto T., Tabuse Y., Kemphues K.J., Ohno S. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143:1998;95-106.
    • (1998) J. Cell Biol. , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5    Fujimoto, T.6    Tabuse, Y.7    Kemphues, K.J.8    Ohno, S.9
  • 126
    • 0027459534 scopus 로고
    • Tight junction protein cingulin is expressed by maternal and embryonic genomes during early mouse development
    • Javed Q., Fleming T.P., Hay M., Citi S. Tight junction protein cingulin is expressed by maternal and embryonic genomes during early mouse development. Development. 117:1993;1145-1151.
    • (1993) Development , vol.117 , pp. 1145-1151
    • Javed, Q.1    Fleming, T.P.2    Hay, M.3    Citi, S.4
  • 127
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein
    • Jesaitis L.A., Goodenough D.A. Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. J. Cell Biol. 124:1994;949-961.
    • (1994) J. Cell Biol. , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 128
    • 0033631414 scopus 로고    scopus 로고
    • The peripheral myelin protein 22 and epithelial membrane protein family
    • Jetten A.M., Suter U. The peripheral myelin protein 22 and epithelial membrane protein family. Prog. Nucleic Acid Res. Mol. Biol. 64:2000;97-129.
    • (2000) Prog. Nucleic Acid Res. Mol. Biol. , vol.64 , pp. 97-129
    • Jetten, A.M.1    Suter, U.2
  • 129
    • 0027248397 scopus 로고
    • Isoprenylation of Rab proteins possessing a C-terminal CaaX motif
    • Joberty G., Tavitian A., Zahraoui A. Isoprenylation of Rab proteins possessing a C-terminal CaaX motif. FEBS Lett. 330:1993;323-328.
    • (1993) FEBS Lett. , vol.330 , pp. 323-328
    • Joberty, G.1    Tavitian, A.2    Zahraoui, A.3
  • 130
    • 0033790539 scopus 로고    scopus 로고
    • The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1
    • Johansson A., Driessens M., Aspenstrom P. The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J. Cell Sci. 113(Pt. 18):2000;3267-3275.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 18 , pp. 3267-3275
    • Johansson, A.1    Driessens, M.2    Aspenstrom, P.3
  • 131
    • 0020058236 scopus 로고
    • Evidence for the lipidic nature of tight junction strands
    • Kachar B., Reese T.S. Evidence for the lipidic nature of tight junction strands. Nature. 296:1982;464-466.
    • (1982) Nature , vol.296 , pp. 464-466
    • Kachar, B.1    Reese, T.S.2
  • 132
    • 0032544565 scopus 로고    scopus 로고
    • The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
    • Kaech S.M., Whitfield C.W., Kim S.K. The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells. Cell. 94:1998;761-771.
    • (1998) Cell , vol.94 , pp. 761-771
    • Kaech, S.M.1    Whitfield, C.W.2    Kim, S.K.3
  • 134
    • 0035823043 scopus 로고    scopus 로고
    • Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells
    • Kausalya P.J., Reichert M., Hunziker W. Connexin45 directly binds to ZO-1 and localizes to the tight junction region in epithelial MDCK cells. FEBS Lett. 505:2001;92-96.
    • (2001) FEBS Lett. , vol.505 , pp. 92-96
    • Kausalya, P.J.1    Reichert, M.2    Hunziker, W.3
  • 137
  • 138
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
    • Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M. Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases. Nature. 378:1995;85-88.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, M.2    Rothschild, A.3    Jan, Y.N.4    Sheng, M.5
  • 139
    • 0031052970 scopus 로고    scopus 로고
    • GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules
    • Kim E., Naisbitt S., Hsueh Y.P., Rao A., Rothschild A., Craig A.M., Sheng M. GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules. J. Cell Biol. 136:1997;669-678.
    • (1997) J. Cell Biol. , vol.136 , pp. 669-678
    • Kim, E.1    Naisbitt, S.2    Hsueh, Y.P.3    Rao, A.4    Rothschild, A.5    Craig, A.M.6    Sheng, M.7
  • 140
    • 0029867955 scopus 로고    scopus 로고
    • Comparison between the distribution of 7H6 tight junction-associated antigen and occludin during the development of chick intestine
    • Kimura M., Sawada N., Kimura H., Isomura H., Hirata K., Mori M. Comparison between the distribution of 7H6 tight junction-associated antigen and occludin during the development of chick intestine. Cell Struct. Funct. 21:1996;91-96.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 91-96
    • Kimura, M.1    Sawada, N.2    Kimura, H.3    Isomura, H.4    Hirata, K.5    Mori, M.6
  • 141
    • 0030998325 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide reduced intestinal barrier function and altered localization of 7H6 antigen in IEC-6 rat intestinal crypt cells
    • Kimura H., Sawada N., Tobioka H., Isomura H., Kokai Y., Hirata K., Mori M. Bacterial lipopolysaccharide reduced intestinal barrier function and altered localization of 7H6 antigen in IEC-6 rat intestinal crypt cells. J. Cell Physiol. 171:1997;284-290.
    • (1997) J. Cell Physiol. , vol.171 , pp. 284-290
    • Kimura, H.1    Sawada, N.2    Tobioka, H.3    Isomura, H.4    Kokai, Y.5    Hirata, K.6    Mori, M.7
  • 142
    • 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. 13:2002;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
  • 143
    • 0034802020 scopus 로고    scopus 로고
    • Altered expression and localization of the tight junction protein ZO-1 in primary and metastatic pancreatic cancer
    • Kleeff J., Shi X., Bode H.P., Hoover K., Shrikhande S., Bryant P.J., Korc M., Buchler M.W., Friess H. Altered expression and localization of the tight junction protein ZO-1 in primary and metastatic pancreatic cancer. Pancreas. 23:2001;259-265.
    • (2001) Pancreas , vol.23 , pp. 259-265
    • Kleeff, J.1    Shi, X.2    Bode, H.P.3    Hoover, K.4    Shrikhande, S.5    Bryant, P.J.6    Korc, M.7    Buchler, M.W.8    Friess, H.9
  • 144
    • 0037087291 scopus 로고    scopus 로고
    • Claudin 5 is transiently expressed during the development of the retinal pigment epithelium
    • Kojima S., Rahner C., Peng S., Rizzolo L.J. Claudin 5 is transiently expressed during the development of the retinal pigment epithelium. J. Membr. Biol. 186:2002;81-88.
    • (2002) J. Membr. Biol. , vol.186 , pp. 81-88
    • Kojima, S.1    Rahner, C.2    Peng, S.3    Rizzolo, L.J.4
  • 146
    • 0033780963 scopus 로고    scopus 로고
    • Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer
    • Kramer F., White K., Kubbies M., Swisshelm K., Weber B.H. Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer. Hum. Genet. 107:2000;249-256.
    • (2000) Hum. Genet. , vol.107 , pp. 249-256
    • Kramer, F.1    White, K.2    Kubbies, M.3    Swisshelm, K.4    Weber, B.H.5
  • 147
    • 0026736220 scopus 로고
    • Diversity among tight junctions in rat kidney: Glomerular slit diaphragms and endothelial junctions express only one isoform of the tight junction protein ZO-1
    • Kurihara H., Anderson J.M., Farquhar M.G. Diversity among tight junctions in rat kidney. glomerular slit diaphragms and endothelial junctions express only one isoform of the tight junction protein ZO-1 Proc. Natl. Acad. Sci. USA. 89:1992;7075-7079.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7075-7079
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 148
    • 0032922584 scopus 로고    scopus 로고
    • Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing
    • Lacaz-Vieira F., Jaeger M.M., Farshori P., Kachar B. Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing. J. Membr. Biol. 168:1999;289-297.
    • (1999) J. Membr. Biol. , vol.168 , pp. 289-297
    • Lacaz-Vieira, F.1    Jaeger, M.M.2    Farshori, P.3    Kachar, B.4
  • 149
    • 0033823684 scopus 로고    scopus 로고
    • Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and do not prevent leukocyte influx into the meninges after viral or bacterial infection
    • Lechner F., Sahrbacher U., Suter T., Frei K., Brockhaus M., Koedel U., Fontana A. Antibodies to the junctional adhesion molecule cause disruption of endothelial cells and do not prevent leukocyte influx into the meninges after viral or bacterial infection. J. Infect. Dis. 182:2000;978-982.
    • (2000) J. Infect. Dis. , vol.182 , pp. 978-982
    • Lechner, F.1    Sahrbacher, U.2    Suter, T.3    Frei, K.4    Brockhaus, M.5    Koedel, U.6    Fontana, A.7
  • 150
    • 0033815457 scopus 로고    scopus 로고
    • Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins
    • Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T. Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins. J. Virol. 74:2000;9680-9693.
    • (2000) J. Virol. , vol.74 , pp. 9680-9693
    • Lee, S.S.1    Glaunsinger, B.2    Mantovani, F.3    Banks, L.4    Javier, R.T.5
  • 151
    • 0037067320 scopus 로고    scopus 로고
    • HINADl/PATJ, a homolog of Discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells
    • Lemmers C., Medina E., Delgrossi M.H., Michel D., Arsanto J.P., Le Bivic A. hINADl/PATJ, a homolog of Discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells. J. Biol. Chem. 277:2002;25408-25415.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25408-25415
    • Lemmers, C.1    Medina, E.2    Delgrossi, M.H.3    Michel, D.4    Arsanto, J.P.5    Le Bivic, A.6
  • 152
    • 0034042424 scopus 로고    scopus 로고
    • Entamoeba histolytica disturbs the tight junction complex in human enteric T84 cell layers
    • Leroy A., Lauwaet T., De Bruyne G., Cornelissen M., Mareel M. Entamoeba histolytica disturbs the tight junction complex in human enteric T84 cell layers. FASEB J. 14:2000;1139-1146.
    • (2000) FASEB J. , vol.14 , pp. 1139-1146
    • Leroy, A.1    Lauwaet, T.2    De Bruyne, G.3    Cornelissen, M.4    Mareel, M.5
  • 153
    • 0033902942 scopus 로고    scopus 로고
    • Human junction adhesion molecule regulates tight junction resealing in epithelia
    • Liu Y., Nusrat A., Schnell F.J., Reaves T.A., Walsh S., Pochet M., Parkos C.A. Human junction adhesion molecule regulates tight junction resealing in epithelia. J. Cell Sci. 113(Pt. 13):2000;2363-2374.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 13 , pp. 2363-2374
    • Liu, Y.1    Nusrat, A.2    Schnell, F.J.3    Reaves, T.A.4    Walsh, S.5    Pochet, M.6    Parkos, C.A.7
  • 154
    • 0035503028 scopus 로고    scopus 로고
    • Expression of Clostridium perfringens enterotoxin receptors claudin-3 and claudin-4 in prostate cancer epithelium
    • Long H., Crean C.D., Lee W.H., Cummings O.W., Gabig T.G. Expression of Clostridium perfringens enterotoxin receptors claudin-3 and claudin-4 in prostate cancer epithelium. Cancer Res. 61:2001;7878-7881.
    • (2001) Cancer Res. , vol.61 , pp. 7878-7881
    • Long, H.1    Crean, C.D.2    Lee, W.H.3    Cummings, O.W.4    Gabig, T.G.5
  • 155
    • 0029768928 scopus 로고    scopus 로고
    • Differential expression of rab3 isoforms in oligodendrocytes and astrocytes
    • Madison D.L., Kruger W.H., Kim T., Pfeiffer S.E. Differential expression of rab3 isoforms in oligodendrocytes and astrocytes. J. Neurosci. Res. 45:1996;258-268.
    • (1996) J. Neurosci. Res. , vol.45 , pp. 258-268
    • Madison, D.L.1    Kruger, W.H.2    Kim, T.3    Pfeiffer, S.E.4
  • 156
    • 0034730837 scopus 로고    scopus 로고
    • The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity
    • Mancini A., Koch A., Stefan M., Niemann H., Tamura T. The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity. FEBS Lett. 482:2000;54-58.
    • (2000) FEBS Lett. , vol.482 , pp. 54-58
    • Mancini, A.1    Koch, A.2    Stefan, M.3    Niemann, H.4    Tamura, T.5
  • 158
    • 0033535163 scopus 로고    scopus 로고
    • Ponsin/SH3P12: An l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions
    • Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., Takai Y. Ponsin/SH3P12. an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions J. Cell Biol. 144:1999;1001-1017.
    • (1999) J. Cell Biol. , vol.144 , pp. 1001-1017
    • Mandai, K.1    Nakanishi, H.2    Satoh, A.3    Takahashi, K.4    Satoh, K.5    Nishioka, H.6    Mizoguchi, A.7    Takai, Y.8
  • 159
    • 0027339375 scopus 로고
    • Uncoupling of the molecular 'fence' and paracellular 'gate' functions in epithelial tight junctions
    • Mandel L.J., Bacallao R., Zampighi G. Uncoupling of the molecular 'fence' and paracellular 'gate' functions in epithelial tight junctions. Nature. 361:1993;552-555.
    • (1993) Nature , vol.361 , pp. 552-555
    • Mandel, L.J.1    Bacallao, R.2    Zampighi, G.3
  • 161
    • 0032575637 scopus 로고    scopus 로고
    • The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes
    • Marzesco A.M., Galli T., Louvard D., Zahraoui A. The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes. J. Biol. Chem. 273:1998;22340-22345.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22340-22345
    • Marzesco, A.M.1    Galli, T.2    Louvard, D.3    Zahraoui, A.4
  • 162
    • 0034730515 scopus 로고    scopus 로고
    • Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton
    • Mattagajasingh S.N., Huang S.C., Hartenstein J.S., Benz E.J. Jr. Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton. J. Biol. Chem. 275:2000;30573-30585.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30573-30585
    • Mattagajasingh, S.N.1    Huang, S.C.2    Hartenstein, J.S.3    Benz E.J., Jr.4
  • 163
    • 0031886504 scopus 로고    scopus 로고
    • Biogenesis of tight junctions: The C-terminal domain of occludin mediates basolateral targeting
    • Matter K., Balda M.S. Biogenesis of tight junctions. the C-terminal domain of occludin mediates basolateral targeting J. Cell Sci. 111(Pt. 4):1998;511-519.
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 4 , pp. 511-519
    • Matter, K.1    Balda, M.S.2
  • 164
    • 0035955627 scopus 로고    scopus 로고
    • IGF-I receptor-induced cell-cell adhesion of MCF-7 breast cancer cells requires the expression of junction protein ZO-1
    • Mauro L., Bartucci M., Morelli C., Ando' S., Surmacz E. IGF-I receptor-induced cell-cell adhesion of MCF-7 breast cancer cells requires the expression of junction protein ZO-1. J. Biol. Chem. 276:2001;39892-39897.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39892-39897
    • Mauro, L.1    Bartucci, M.2    Morelli, C.3    Ando', S.4    Surmacz, E.5
  • 166
    • 0034388122 scopus 로고    scopus 로고
    • Occludin localization at the tight junction requires the second extracellular loop
    • Medina R., Rahner C., Mitic L.L., Anderson J.M., Van Itallie C.M. Occludin localization at the tight junction requires the second extracellular loop. J. Membr. Biol. 178:2000;235-247.
    • (2000) J. Membr. Biol. , vol.178 , pp. 235-247
    • Medina, R.1    Rahner, C.2    Mitic, L.L.3    Anderson, J.M.4    Van Itallie, C.M.5
  • 167
    • 0032521458 scopus 로고    scopus 로고
    • Formation of functional tight junctions in Xenopus embryos
    • Merzdorf C.S., Chen Y.H., Goodenough D.A. Formation of functional tight junctions in Xenopus embryos. Dev. Biol. 195:1998;187-203.
    • (1998) Dev. Biol. , vol.195 , pp. 187-203
    • Merzdorf, C.S.1    Chen, Y.H.2    Goodenough, D.A.3
  • 169
    • 0034485413 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions
    • Mino A., Ohtsuka T., Inoue E., Takai Y. Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAP1) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions. Genes Cells. 5:2000;1009-1016.
    • (2000) Genes Cells , vol.5 , pp. 1009-1016
    • Mino, A.1    Ohtsuka, T.2    Inoue, E.3    Takai, Y.4
  • 170
    • 0002899825 scopus 로고    scopus 로고
    • Occludin and claudins: Transmembrane proteins of the tight junction
    • Cereijido, M., Anderson, J.M. (Eds.). Boca Raton
    • Mitic, L., Van Itallie, C.M., 2001. Occludin and claudins: Transmembrane proteins of the tight junction. In: Cereijido, M., Anderson, J.M. (Eds.), Tight Junctions. Boca Raton, pp. 213-230.
    • (2001) Tight Junctions , pp. 213-230
    • Mitic, L.1    Van Itallie, C.M.2
  • 171
    • 0034468689 scopus 로고    scopus 로고
    • Glycoprotein E of varicella-zoster virus enhances cell-cell contact in polarized epithelial cells
    • Mo C., Schneeberger E.E., Arvin A.M. Glycoprotein E of varicella-zoster virus enhances cell-cell contact in polarized epithelial cells. J. Virol. 74:2000;11377-11387.
    • (2000) J. Virol. , vol.74 , pp. 11377-11387
    • Mo, C.1    Schneeberger, E.E.2    Arvin, A.M.3
  • 172
  • 173
    • 0033519348 scopus 로고    scopus 로고
    • Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis
    • Morita K., Sasaki H., Fujimoto K., Furuse M., Tsukita S. Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. J. Cell Biol. 145:1999;579-588.
    • (1999) J. Cell Biol. , vol.145 , pp. 579-588
    • Morita, K.1    Sasaki, H.2    Fujimoto, K.3    Furuse, M.4    Tsukita, S.5
  • 174
    • 0033523758 scopus 로고    scopus 로고
    • Endothelial claudin: Claudin-5/TMVCF constitutes tight junction strands in endothelial cells
    • Morita K., Sasaki H., Furuse M., Tsukita S. Endothelial claudin. claudin-5/TMVCF constitutes tight junction strands in endothelial cells J. Cell Biol. 147:1999;185-194.
    • (1999) J. Cell Biol. , vol.147 , pp. 185-194
    • Morita, K.1    Sasaki, H.2    Furuse, M.3    Tsukita, S.4
  • 175
    • 0033996784 scopus 로고    scopus 로고
    • Occludin 1B, a variant of the tight junction protein occludin
    • Muresan Z., Paul D.L., Goodenough D.A. Occludin 1B, a variant of the tight junction protein occludin. Mol. Biol. Cell. 11:2000;627-634.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 627-634
    • Muresan, Z.1    Paul, D.L.2    Goodenough, D.A.3
  • 176
    • 0033728777 scopus 로고    scopus 로고
    • HGF/SF-induced spreading of MDCK cells correlates with disappearance of barmotin/7H6, a tight junction-associated protein, from the cell membrane
    • Muto S., Sato Y., Umeki Y., Yoshida K., Yoshioka T., Nishikawa Y., Nakamura T., Mori M., Koyama K., Enomoto K. HGF/SF-induced spreading of MDCK cells correlates with disappearance of barmotin/7H6, a tight junction-associated protein, from the cell membrane. Cell Biol. Int. 24:2000;439-446.
    • (2000) Cell Biol. Int. , vol.24 , pp. 439-446
    • Muto, S.1    Sato, Y.2    Umeki, Y.3    Yoshida, K.4    Yoshioka, T.5    Nishikawa, Y.6    Nakamura, T.7    Mori, M.8    Koyama, K.9    Enomoto, K.10
  • 177
    • 12944262412 scopus 로고    scopus 로고
    • HuASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions
    • Nakamura T., Blechman J., Tada S., Rozovskaia T., Itoyama T., Bullrich F., Mazo A., Croce C.M., Geiger B., Canaani E. huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions. Proc. Natl. Acad. Sci. USA. 97:2000;7284-7289.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7284-7289
    • Nakamura, T.1    Blechman, J.2    Tada, S.3    Rozovskaia, T.4    Itoyama, T.5    Bullrich, F.6    Mazo, A.7    Croce, C.M.8    Geiger, B.9    Canaani, E.10
  • 178
    • 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 J.M., Minoo P., Zimonjic D.B., Popescu N.C., 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. 21:2001;7380-7390.
    • (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
  • 180
    • 0035929649 scopus 로고    scopus 로고
    • Interleukin-2 receptor beta subunit-dependent and -independent regulation of intestinal epithelial tight junctions
    • Nishiyama R., Sakaguchi T., Kinugasa T., Gu X., MacDermott R.P., Podolsky D.K., Reinecker H.C. Interleukin-2 receptor beta subunit-dependent and -independent regulation of intestinal epithelial tight junctions. J. Biol. Chem. 276:2001;35571-35580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35571-35580
    • Nishiyama, R.1    Sakaguchi, T.2    Kinugasa, T.3    Gu, X.4    MacDermott, R.P.5    Podolsky, D.K.6    Reinecker, H.C.7
  • 182
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick P., Zerial M. The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9:1997;496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 183
    • 0034703027 scopus 로고    scopus 로고
    • The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction
    • Nusrat A., Chen J.A., Foley C.S., Liang T.W., Tom J., Cromwell M., Quan C., Mrsny R.J. The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction. J. Biol. Chem. 275:2000;29816-29822.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29816-29822
    • Nusrat, A.1    Chen, J.A.2    Foley, C.S.3    Liang, T.W.4    Tom, J.5    Cromwell, M.6    Quan, C.7    Mrsny, R.J.8
  • 184
    • 0033547353 scopus 로고    scopus 로고
    • NRap GEP: A novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM)
    • Ohtsuka T., Hata Y., Ide N., Yasuda T., Inoue E., Inoue T., Mizoguchi A., Takai Y. nRap GEP. a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM) Biochem. Biophys. Res. Commun. 265:1999;38-44.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 38-44
    • Ohtsuka, T.1    Hata, Y.2    Ide, N.3    Yasuda, T.4    Inoue, E.5    Inoue, T.6    Mizoguchi, A.7    Takai, Y.8
  • 186
    • 0034705379 scopus 로고    scopus 로고
    • Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells
    • Palmeri D., van Zante A., Huang C.C., Hemmerich S., Rosen S.D. Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells. J. Biol. Chem. 275:2000;19139-19145.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19139-19145
    • Palmeri, D.1    Van Zante, A.2    Huang, C.C.3    Hemmerich, S.4    Rosen, S.D.5
  • 187
    • 0031736990 scopus 로고    scopus 로고
    • The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes
    • Papoulas O., Beek S.J., Moseley S.L., McCallum C.M., Sarte M., Shearn A., Tamkun J.W. The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes. Development. 125:1998;3955-3966.
    • (1998) Development , vol.125 , pp. 3955-3966
    • Papoulas, O.1    Beek, S.J.2    Moseley, S.L.3    McCallum, C.M.4    Sarte, M.5    Shearn, A.6    Tamkun, J.W.7
  • 188
    • 0035082651 scopus 로고    scopus 로고
    • The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes
    • Patrie K.M., Drescher A.J., Goyal M., Wiggins R.C., Margolis B. The membrane-associated guanylate kinase protein MAGI-1 binds megalin and is present in glomerular podocytes. J. Am. Soc. Nephrol. 12:2001;667-677.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 667-677
    • Patrie, K.M.1    Drescher, A.J.2    Goyal, M.3    Wiggins, R.C.4    Margolis, B.5
  • 189
    • 0030820681 scopus 로고    scopus 로고
    • Molecular characterization of a novel human PDZ domain protein with homology to INAD from Drosophila melanogaster
    • Philipp S., Flockerzi V. Molecular characterization of a novel human PDZ domain protein with homology to INAD from Drosophila melanogaster. FEBS Lett. 413:1997;243-248.
    • (1997) FEBS Lett. , vol.413 , pp. 243-248
    • Philipp, S.1    Flockerzi, V.2
  • 190
    • 0020079785 scopus 로고
    • On tight-junction structure
    • Pinto d.S., Kachar B. On tight-junction structure. Cell. 28:1982;441-450.
    • (1982) Cell , vol.28 , pp. 441-450
    • Pinto, d.S.1    Kachar, B.2
  • 191
    • 0027373678 scopus 로고
    • Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation
    • Prasad R., Gu Y., Alder H., Nakamura T., Canaani O., Saito H., Huebner K., Gale R.P., Nowell P.C., Kuriyama K. Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation. Cancer Res. 53:1993;5624-5628.
    • (1993) Cancer Res. , vol.53 , pp. 5624-5628
    • Prasad, R.1    Gu, Y.2    Alder, H.3    Nakamura, T.4    Canaani, O.5    Saito, H.6    Huebner, K.7    Gale, R.P.8    Nowell, P.C.9    Kuriyama, K.10
  • 192
    • 0033588299 scopus 로고    scopus 로고
    • M-Ras/R-Ras3, a transforming ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6
    • Quilliam L.A., Castro A.F., Rogers-Graham K.S., Martin C.B., Der C.J., Bi C. M-Ras/R-Ras3, a transforming ras protein regulated by Sos1, GRF1, and p120 Ras GTPase-activating protein, interacts with the putative Ras effector AF6. J. Biol. Chem. 274:1999;23850-23857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23850-23857
    • Quilliam, L.A.1    Castro, A.F.2    Rogers-Graham, K.S.3    Martin, C.B.4    Der, C.J.5    Bi, C.6
  • 194
    • 0037178864 scopus 로고    scopus 로고
    • The carboxy-terminus of zona Occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions
    • Roh, M.H., Liu, C.J., Laurinec, S., Margolis, B., 2002a. The carboxy-terminus of zona Occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions. J. Biol. Chem.
    • (2002) J. Biol. Chem.
    • Roh, M.H.1    Liu, C.J.2    Laurinec, S.3    Margolis, B.4
  • 196
    • 0034030506 scopus 로고    scopus 로고
    • Truncation mutants of the tight junction protein ZO-1 disrupt corneal epithelial cell morphology
    • Ryeom S.W., Paul D., Goodenough D.A. Truncation mutants of the tight junction protein ZO-1 disrupt corneal epithelial cell morphology. Mol. Biol. Cell. 11:2000;1687-1696.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 1687-1696
    • Ryeom, S.W.1    Paul, D.2    Goodenough, D.A.3
  • 197
    • 0032555295 scopus 로고    scopus 로고
    • Involvement of Galphai2 in the maintenance and biogenesis of epithelial cell tight junctions
    • Saha C., Nigam S.K., Denker B.M. Involvement of Galphai2 in the maintenance and biogenesis of epithelial cell tight junctions. J. Biol. Chem. 273:1998;21629-21633.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21629-21633
    • Saha, C.1    Nigam, S.K.2    Denker, B.M.3
  • 198
    • 0034804853 scopus 로고    scopus 로고
    • Expanding role of G proteins in tight junction regulation: Galpha(s) stimulates TJ assembly
    • Saha C., Nigam S.K., Denker B.M. Expanding role of G proteins in tight junction regulation. Galpha(s) stimulates TJ assembly Biochem. Biophys. Res. Commun. 285:2001;250-256.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 250-256
    • Saha, C.1    Nigam, S.K.2    Denker, B.M.3
  • 200
    • 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. 137:1997;1393-1401.
    • (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
  • 202
    • 0030027609 scopus 로고    scopus 로고
    • Localization of 7H6 tight junction-associated antigen along the cell border of vascular endothelial cells correlates with paracellular barrier function against ions, large molecules, and cancer cells
    • Satoh H., Zhong Y., Isomura H., Saitoh M., Enomoto K., Sawada N., Mori M. Localization of 7H6 tight junction-associated antigen along the cell border of vascular endothelial cells correlates with paracellular barrier function against ions, large molecules, and cancer cells. Exp. Cell Res. 222:1996;269-274.
    • (1996) Exp. Cell Res. , vol.222 , pp. 269-274
    • Satoh, H.1    Zhong, Y.2    Isomura, H.3    Saitoh, M.4    Enomoto, K.5    Sawada, N.6    Mori, M.7
  • 203
    • 0035900576 scopus 로고    scopus 로고
    • Use of surface plasmon resonance for real-time analysis of the interaction of ZO-1 and occludin
    • Schmidt A., Utepbergenov D.I., Krause G., Blasig I.E. Use of surface plasmon resonance for real-time analysis of the interaction of ZO-1 and occludin. Biochem. Biophys. Res. Commun. 288:2001;1194-1199.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 1194-1199
    • Schmidt, A.1    Utepbergenov, D.I.2    Krause, G.3    Blasig, I.E.4
  • 204
    • 0023765743 scopus 로고
    • Genes specifically expressed at growth arrest of mammalian cells
    • Schneider C., King R.M., Philipson L. Genes specifically expressed at growth arrest of mammalian cells. Cell. 54:1988;787-793.
    • (1988) Cell , vol.54 , pp. 787-793
    • Schneider, C.1    King, R.M.2    Philipson, L.3
  • 206
    • 0030246987 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin
    • Shapiro L., Doyle J.P., Hensley P., Colman D.R., Hendrickson W.A. Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin. Neuron. 17:1996;435-449.
    • (1996) Neuron , vol.17 , pp. 435-449
    • Shapiro, L.1    Doyle, J.P.2    Hensley, P.3    Colman, D.R.4    Hendrickson, W.A.5
  • 207
    • 0030962073 scopus 로고    scopus 로고
    • Tight junction assembly during mouse blastocyst formation is regulated by late expression of ZO-1 alpha+ isoform
    • Sheth B., Fesenko I., Collins J.E., Moran B., Wild A.E., Anderson J.M., Fleming T.P. Tight junction assembly during mouse blastocyst formation is regulated by late expression of ZO-1 alpha+ isoform. Development. 124:1997;2027-2037.
    • (1997) Development , vol.124 , pp. 2027-2037
    • Sheth, B.1    Fesenko, I.2    Collins, J.E.3    Moran, B.4    Wild, A.E.5    Anderson, J.M.6    Fleming, T.P.7
  • 208
    • 0342409279 scopus 로고    scopus 로고
    • Differentiation of the epithelial apical junctional complex during mouse preimplantation development: A role for rab13 in the early maturation of the tight junction
    • Sheth B., Fontaine J.J., Ponza E., McCallum A., Page A., Citi S., Louvard D., Zahraoui A., Fleming T.P. Differentiation of the epithelial apical junctional complex during mouse preimplantation development. a role for rab13 in the early maturation of the tight junction Mech. Dev. 97:2000;93-104.
    • (2000) Mech. Dev. , vol.97 , pp. 93-104
    • Sheth, B.1    Fontaine, J.J.2    Ponza, E.3    McCallum, A.4    Page, A.5    Citi, S.6    Louvard, D.7    Zahraoui, A.8    Fleming, T.P.9
  • 209
    • 0034012846 scopus 로고    scopus 로고
    • Post-translational control of occludin membrane assembly in mouse trophectoderm: A mechanism to regulate timing of tight junction biogenesis and blastocyst formation
    • Sheth B., Moran B., Anderson J.M., Fleming T.P. Post-translational control of occludin membrane assembly in mouse trophectoderm. a mechanism to regulate timing of tight junction biogenesis and blastocyst formation Development. 127:2000;831-840.
    • (2000) Development , vol.127 , pp. 831-840
    • Sheth, B.1    Moran, B.2    Anderson, J.M.3    Fleming, T.P.4
  • 210
    • 0029664550 scopus 로고    scopus 로고
    • Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors
    • Shieh B.H., Zhu M.Y. Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors. Neuron. 16:1996;991-998.
    • (1996) Neuron , vol.16 , pp. 991-998
    • Shieh, B.H.1    Zhu, M.Y.2
  • 212
    • 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 G.R., Patanjali S.R., Skoultchi A., Weissman S.M., Kucherlapati R. 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. 42:1997;245-251.
    • (1997) Genomics , vol.42 , pp. 245-251
    • Sirotkin, H.1    Morrow, B.2    Saint-Jore, B.3    Puech, A.4    Das, G.R.5    Patanjali, S.R.6    Skoultchi, A.7    Weissman, S.M.8    Kucherlapati, R.9
  • 214
    • 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. 147:1999;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    Tsukita, S.7
  • 215
    • 0011982478 scopus 로고    scopus 로고
    • Functions of OSP/claudin-11-containing parallel tight junctions: Implications from the knockout mouse
    • M. Cereijido, & J.M. Anderson. Boca Raton: CRC Press
    • Southwood C.M., Gow A. Functions of OSP/claudin-11-containing parallel tight junctions: implications from the knockout mouse. Cereijido M., Anderson J.M. Tight Junctions. 2001;723-745 CRC Press, Boca Raton.
    • (2001) Tight Junctions , pp. 723-745
    • Southwood, C.M.1    Gow, A.2
  • 216
    • 0004009318 scopus 로고    scopus 로고
    • Preparation of nuclei from tissues and suspension cells
    • CSHL Press, Cold Spring Harbor
    • Spector, D.L., Goldman, R.D., Leinwand, L.A., 1998. Preparation of nuclei from tissues and suspension cells. In: Cells: a Laboratory Manual. CSHL Press, Cold Spring Harbor, pp. 43.1-43.6.
    • (1998) Cells: A Laboratory Manual , pp. 431-436
    • Spector, D.L.1    Goldman, R.D.2    Leinwand, L.A.3
  • 217
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson B.R., Siliciano J.D., Mooseker M.S., Goodenough D.A. Identification of ZO-1. a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia J. Cell Biol. 103:1986;755-766.
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 218
    • 0024456733 scopus 로고
    • Phosphorylation of the tight-junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance
    • Stevenson B.R., Anderson J.M., Braun I.D., Mooseker M.S. Phosphorylation of the tight-junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Biochem. J. 263:1989;597-599.
    • (1989) Biochem. J. , vol.263 , pp. 597-599
    • Stevenson, B.R.1    Anderson, J.M.2    Braun, I.D.3    Mooseker, M.S.4
  • 219
    • 0026003089 scopus 로고
    • G alpha 12 and G alpha 13 subunits define a fourth class of G protein alpha subunits
    • Strathmann M.P., Simon M.I. G alpha 12 and G alpha 13 subunits define a fourth class of G protein alpha subunits. Proc. Natl. Acad. Sci. USA. 88:1991;5582-5586.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5582-5586
    • Strathmann, M.P.1    Simon, M.I.2
  • 220
    • 0035947760 scopus 로고    scopus 로고
    • MAGI-1c: A synaptic MAGUK interacting with muSK at the vertebrate neuromuscular junction
    • Strochlic L., Cartaud A., Labas V., Hoch W., Rossier J., Cartaud J. MAGI-1c. a synaptic MAGUK interacting with muSK at the vertebrate neuromuscular junction J. Cell Biol. 153:2001;1127-1132.
    • (2001) J. Cell Biol. , vol.153 , pp. 1127-1132
    • Strochlic, L.1    Cartaud, A.2    Labas, V.3    Hoch, W.4    Rossier, J.5    Cartaud, J.6
  • 221
    • 0034713369 scopus 로고    scopus 로고
    • Rab3B regulates ZO-1 targeting and actin organization in PC12 neuroendocrine cells
    • Sunshine C., Francis S., Kirk K.L. Rab3B regulates ZO-1 targeting and actin organization in PC12 neuroendocrine cells. Exp. Cell Res. 257:2000;1-10.
    • (2000) Exp. Cell Res. , vol.257 , pp. 1-10
    • Sunshine, C.1    Francis, S.2    Kirk, K.L.3
  • 222
    • 0033554318 scopus 로고    scopus 로고
    • Transgenic mouse models of CMT1A and HNPP
    • Suter U., Nave K.A. Transgenic mouse models of CMT1A and HNPP. Ann. N. Y. Acad. Sci. 883:1999;247-253.
    • (1999) Ann. N. Y. Acad. Sci. , vol.883 , pp. 247-253
    • Suter, U.1    Nave, K.A.2
  • 223
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M., Akimoto K., Izumi Y., Ohnishi T., Ohno S. Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152:2001;1183-1196.
    • (2001) J. Cell Biol. , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 224
    • 0036120691 scopus 로고    scopus 로고
    • SS1 Helicobacter pylori disrupts the paracellular barrier of the gastric mucosa and leads to neutrophilic gastritis in mice
    • Suzuki K.K., Kokai Y., Sawada N., Takakuwa R., Kuwahara K., Isogai E., Isogai H., Mori M. SS1 Helicobacter pylori disrupts the paracellular barrier of the gastric mucosa and leads to neutrophilic gastritis in mice. Virchows Arch. 440:2002;318-324.
    • (2002) Virchows Arch. , vol.440 , pp. 318-324
    • Suzuki, K.K.1    Kokai, Y.2    Sawada, N.3    Takakuwa, R.4    Kuwahara, K.5    Isogai, E.6    Isogai, H.7    Mori, M.8
  • 225
    • 0033984159 scopus 로고    scopus 로고
    • Complex protein interactions within the human polyadenylation machinery identify a novel component
    • Takagaki Y., Manley J.L. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol. Cell Biol. 20:2000;1515-1525.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 1515-1525
    • Takagaki, Y.1    Manley, J.L.2
  • 226
    • 0031648724 scopus 로고    scopus 로고
    • Direct binding between two PDZ domain proteins Canoe and ZO-1 and their roles in regulation of the jun N-terminal kinase pathway in Drosophila morphogenesis
    • Takahashi K., Matsuo T., Katsube T., Ueda R., Yamamoto D. Direct binding between two PDZ domain proteins Canoe and ZO-1 and their roles in regulation of the jun N-terminal kinase pathway in Drosophila morphogenesis. Mech. Dev. 78:1998;97-111.
    • (1998) Mech. Dev. , vol.78 , pp. 97-111
    • Takahashi, K.1    Matsuo, T.2    Katsube, T.3    Ueda, R.4    Yamamoto, D.5
  • 227
    • 0033519211 scopus 로고    scopus 로고
    • Nectin/PRR: An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein
    • Takahashi K., Nakanishi H., Miyahara M., Mandai K., Satoh K., Satoh A., Nishioka H., Aoki J., Nomoto A., Mizoguchi A., Takai Y. Nectin/PRR. an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein J. Cell Biol. 145:1999;539-549.
    • (1999) J. Cell Biol. , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3    Mandai, K.4    Satoh, K.5    Satoh, A.6    Nishioka, H.7    Aoki, J.8    Nomoto, A.9    Mizoguchi, A.10    Takai, Y.11
  • 228
    • 0029762186 scopus 로고    scopus 로고
    • The Drosophila tamou gene, a component of the activating pathway of extramacrochaetae expression, encodes a protein homologous to mammalian cell-cell junction-associated protein ZO-1
    • Takahisa M., Togashi S., Suzuki T., Kobayashi M., Murayama A., Kondo K., Miyake T., Ueda R. The Drosophila tamou gene, a component of the activating pathway of extramacrochaetae expression, encodes a protein homologous to mammalian cell-cell junction-associated protein ZO-1. Genes Dev. 10:1996;1783-1795.
    • (1996) Genes Dev. , vol.10 , pp. 1783-1795
    • Takahisa, M.1    Togashi, S.2    Suzuki, T.3    Kobayashi, M.4    Murayama, A.5    Kondo, K.6    Miyake, T.7    Ueda, R.8
  • 229
    • 0028819708 scopus 로고
    • Effects of tyrosine phosphorylation on tight junctions in temperature- sensitive v-src-transfected MDCK cells
    • Takeda H., Tsukita S. Effects of tyrosine phosphorylation on tight junctions in temperature- sensitive v-src-transfected MDCK cells. Cell Struct. Funct. 20:1995;387-393.
    • (1995) Cell Struct. Funct. , vol.20 , pp. 387-393
    • Takeda, H.1    Tsukita, S.2
  • 230
    • 0034871268 scopus 로고    scopus 로고
    • Functional analysis for peripheral myelin protein PASII/PMP22: Is it a member of claudin superfamily?
    • Takeda Y., Notsu T., Kitamura K., Uyemura K. Functional analysis for peripheral myelin protein PASII/PMP22. is it a member of claudin superfamily? Neurochem. Res. 26:2001;599-607.
    • (2001) Neurochem. Res. , vol.26 , pp. 599-607
    • Takeda, Y.1    Notsu, T.2    Kitamura, K.3    Uyemura, K.4
  • 233
    • 0017738144 scopus 로고
    • Tracer and freeze fracture observations on developing tight junctions in fetal rat thyroid
    • Tice L.W., Carter R.L., Cahill M.C. Tracer and freeze fracture observations on developing tight junctions in fetal rat thyroid. Tissue Cell. 9:1977;395-417.
    • (1977) Tissue Cell , vol.9 , pp. 395-417
    • Tice, L.W.1    Carter, R.L.2    Cahill, M.C.3
  • 234
    • 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., Bronstein J.M. 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. 153:2001;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    Bronstein, J.M.7
  • 235
    • 0030016641 scopus 로고    scopus 로고
    • Enhanced paracellular barrier function of rat mesothelial cells partially protects against cancer cell penetration
    • Tobioka H., Sawada N., Zhong Y., Mori M. Enhanced paracellular barrier function of rat mesothelial cells partially protects against cancer cell penetration. Br. J. Cancer. 74:1996;439-445.
    • (1996) Br. J. Cancer , vol.74 , pp. 439-445
    • Tobioka, H.1    Sawada, N.2    Zhong, Y.3    Mori, M.4
  • 236
    • 0030915715 scopus 로고    scopus 로고
    • HCAR and MCAR: The human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
    • Tomko R.P., Xu R., Philipson L. HCAR and MCAR. the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses Proc. Natl. Acad. Sci. USA. 94:1997;3352-3356.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3352-3356
    • Tomko, R.P.1    Xu, R.2    Philipson, L.3
  • 237
    • 0032557460 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T., Yabuki M., Otsu K., Kuzuya T., Hori M., Tada M. Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. J. Biol. Chem. 273:1998;12725-12731.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12725-12731
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Kuzuya, T.4    Hori, M.5    Tada, M.6
  • 238
  • 239
    • 0033004247 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins
    • Tsukamoto T., Nigam S.K. Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins. Am. J. Physiol. 276:1999;F737-F750.
    • (1999) Am. J. Physiol. , vol.276
    • Tsukamoto, T.1    Nigam, S.K.2
  • 241
    • 0034796342 scopus 로고    scopus 로고
    • Claudin-6: A novel tight junction molecule is developmentally regulated in mouse embryonic epithelium
    • Turksen K., Troy T.C. Claudin-6. a novel tight junction molecule is developmentally regulated in mouse embryonic epithelium Dev. Dyn. 222:2001;292-300.
    • (2001) Dev. Dyn. , vol.222 , pp. 292-300
    • Turksen, K.1    Troy, T.C.2
  • 242
    • 0036336486 scopus 로고    scopus 로고
    • Permeability barrier dysfunction in transgenic mice overexpressing claudin 6
    • Turksen K., Troy T.C. Permeability barrier dysfunction in transgenic mice overexpressing claudin 6. Development. 129:2002;1775-1784.
    • (2002) Development , vol.129 , pp. 1775-1784
    • Turksen, K.1    Troy, T.C.2
  • 244
    • 0032489347 scopus 로고    scopus 로고
    • Cloning and characterization of MUPP1, a novel PDZ domain protein
    • Ullmer C., Schmuck K., Figge A., Lubbert H. Cloning and characterization of MUPP1, a novel PDZ domain protein. FEBS Lett. 424:1998;63-68.
    • (1998) FEBS Lett. , vol.424 , pp. 63-68
    • Ullmer, C.1    Schmuck, K.2    Figge, A.3    Lubbert, H.4
  • 246
    • 0030983484 scopus 로고    scopus 로고
    • Occludin confers adhesiveness when expressed in fibroblasts
    • Van Itallie C.M., Anderson J.M. Occludin confers adhesiveness when expressed in fibroblasts. J. Cell Sci. 110(Pt. 9):1997;1113-1121.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 9 , pp. 1113-1121
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 247
    • 0028922237 scopus 로고
    • Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells
    • Van Itallie C.M., Balda M.S., Anderson J.M. Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells. J. Cell Sci. 108(Pt. 4):1995;1735-1742.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 4 , pp. 1735-1742
    • Van Itallie, C.M.1    Balda, M.S.2    Anderson, J.M.3
  • 248
    • 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. Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J. Clin. Invest. 107:2001;1319-1327.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 249
    • 0035966127 scopus 로고    scopus 로고
    • Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex
    • Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N., Sellers W.R. Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J. Biol. Chem. 276:2001;48627-48630.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48627-48630
    • Vazquez, F.1    Grossman, S.R.2    Takahashi, Y.3    Rokas, M.V.4    Nakamura, N.5    Sellers, W.R.6
  • 250
    • 0023518424 scopus 로고
    • Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos
    • Vestweber D., Gossler A., Boller K., Kemler R. Expression and distribution of cell adhesion molecule uvomorulin in mouse preimplantation embryos. Dev. Biol. 124:1987;451-456.
    • (1987) Dev. Biol. , vol.124 , pp. 451-456
    • Vestweber, D.1    Gossler, A.2    Boller, K.3    Kemler, R.4
  • 251
    • 0035038783 scopus 로고    scopus 로고
    • Perturbation of the tight junction permeability barrier by occludin loop peptides activates beta-catenin/TCF/LEF-mediated transcription
    • Vietor I., Bader T., Paiha K., Huber L.A. Perturbation of the tight junction permeability barrier by occludin loop peptides activates beta-catenin/TCF/LEF-mediated transcription. EMBO Rep. 2:2001;306-312.
    • (2001) EMBO Rep. , vol.2 , pp. 306-312
    • Vietor, I.1    Bader, T.2    Paiha, K.3    Huber, L.A.4
  • 254
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions
    • Willott E., Balda M.S., Fanning A.S., Jameson B., Van Itallie C., Anderson J.M. The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions. Proc. Natl. Acad. Sci. USA. 90:1993;7834-7838.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7834-7838
    • Willott, E.1    Balda, M.S.2    Fanning, A.S.3    Jameson, B.4    Van Itallie, C.5    Anderson, J.M.6
  • 255
    • 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 E.S., Haskins J., Stevenson B.R. 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. 274:1999;35179-35185.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 256
    • 0034645048 scopus 로고    scopus 로고
    • Exogenous expression of the amino-terminal half of the tight junction protein ZO-3 perturbs junctional complex assembly
    • Wittchen E.S., Haskins J., Stevenson B.R. Exogenous expression of the amino-terminal half of the tight junction protein ZO-3 perturbs junctional complex assembly. J. Cell Biol. 151:2000;825-836.
    • (2000) J. Cell Biol. , vol.151 , pp. 825-836
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 257
    • 0035854606 scopus 로고    scopus 로고
    • Claudin-1, claudin-2 and claudin-11 are present in tight junctions of choroid plexus epithelium of the mouse
    • Wolburg H., Wolburg-Buchholz K., Liebner S., Engelhardt B. Claudin-1, claudin-2 and claudin-11 are present in tight junctions of choroid plexus epithelium of the mouse. Neurosci. Lett. 307:2001;77-80.
    • (2001) Neurosci. Lett. , vol.307 , pp. 77-80
    • Wolburg, H.1    Wolburg-Buchholz, K.2    Liebner, S.3    Engelhardt, B.4
  • 258
    • 0031425958 scopus 로고    scopus 로고
    • Phosphorylation of occludin correlates with occludin localization and function at the tight junction
    • Wong V. Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Am. J. Physiol. 273:1997;C1859-C1867.
    • (1997) Am. J. Physiol. , vol.273
    • Wong, V.1
  • 259
    • 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. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136:1997;399-409.
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 262
    • 0034647496 scopus 로고    scopus 로고
    • Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase
    • Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A. Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase. J. Biol. Chem. 275:2000;21477-21485.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21477-21485
    • Wu, Y.1    Dowbenko, D.2    Spencer, S.3    Laura, R.4    Lee, J.5    Gu, Q.6    Lasky, L.A.7
  • 263
    • 0035798618 scopus 로고    scopus 로고
    • Beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95
    • Xu J., Paquet M., Lau A.G., Wood J.D., Ross C.A., Hall R.A. Beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95. J. Biol. Chem. 276:2001;41310-41317.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41310-41317
    • Xu, J.1    Paquet, M.2    Lau, A.G.3    Wood, J.D.4    Ross, C.A.5    Hall, R.A.6
  • 268
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization: Similarities and differences between non-polarized fibroblasts and polarized epithelial cells
    • Yonemura S., Itoh M., Nagafuchi A., Tsukita S. Cell-to-cell adherens junction formation and actin filament organization. similarities and differences between non-polarized fibroblasts and polarized epithelial cells J. Cell Sci. 108(Pt. 1):1995;127-142.
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 1 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, S.4
  • 269
    • 0028008838 scopus 로고
    • A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells
    • Zahraoui A., Joberty G., Arpin M., Fontaine J.J., Hellio R., Tavitian A., Louvard D. A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells. J. Cell Biol. 124:1994;101-115.
    • (1994) J. Cell Biol. , vol.124 , pp. 101-115
    • Zahraoui, A.1    Joberty, G.2    Arpin, M.3    Fontaine, J.J.4    Hellio, R.5    Tavitian, A.6    Louvard, D.7
  • 270
  • 271
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2
    • Zhong Y., Saitoh T., Minase T., Sawada N., Enomoto K., Mori M. Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2. J. Cell Biol. 120:1993;477-483.
    • (1993) J. Cell Biol. , vol.120 , pp. 477-483
    • Zhong, Y.1    Saitoh, T.2    Minase, T.3    Sawada, N.4    Enomoto, K.5    Mori, M.6
  • 272
    • 0028109285 scopus 로고
    • Localization of the 7H6 antigen at tight junctions correlates with the paracellular barrier function of MDCK cells
    • Zhong Y., Enomoto K., Isomura H., Sawada N., Minase T., Oyamada M., Konishi Y., Mori M. Localization of the 7H6 antigen at tight junctions correlates with the paracellular barrier function of MDCK cells. Exp. Cell Res. 214:1994;614-620.
    • (1994) Exp. Cell Res. , vol.214 , pp. 614-620
    • Zhong, Y.1    Enomoto, K.2    Isomura, H.3    Sawada, N.4    Minase, T.5    Oyamada, M.6    Konishi, Y.7    Mori, M.8
  • 273
    • 0028331789 scopus 로고
    • Sequential decrease in tight junctions as revealed by 7H6 tight junction-associated protein during rat hepatocarcinogenesis
    • Zhong Y., Enomoto K., Tobioka H., Konishi Y., Satoh M., Mori M. Sequential decrease in tight junctions as revealed by 7H6 tight junction-associated protein during rat hepatocarcinogenesis. Jpn. J. Cancer Res. 85:1994;351-356.
    • (1994) Jpn. J. Cancer Res. , vol.85 , pp. 351-356
    • Zhong, Y.1    Enomoto, K.2    Tobioka, H.3    Konishi, Y.4    Satoh, M.5    Mori, M.6


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