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Volumn 163, Issue 3, 1998, Pages 159-167

Molecular analyses of tight junction physiology: Insights and paradoxes

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; OCCLUDIN;

EID: 0032102036     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900380     Document Type: Review
Times cited : (72)

References (63)
  • 3
    • 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., Whitney, J.A., Flores, C., Gonzalez, S., Cereijido, M., Matter, K. 1996. 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. 134:1031-1049
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 4
    • 0030962405 scopus 로고    scopus 로고
    • The chloride conductance of tight junctions of rat ileum can be increased by cAMP but not by carbachol
    • Bijlsma, P.B., Bakker, R., Groot, J.A. 1997. The chloride conductance of tight junctions of rat ileum can be increased by cAMP but not by carbachol. J. Membrane Biol. 157:127-17.
    • (1997) J. Membrane Biol. , vol.157 , pp. 127-217
    • Bijlsma, P.B.1    Bakker, R.2    Groot, J.A.3
  • 6
    • 0002436442 scopus 로고
    • Tight junction: Barrier between higher organisms and environment
    • Cereijido, M., Gonzalez-Mariscal, L., Contreras, G. 1989. Tight junction: barrier between higher organisms and environment. NIPS 4:72-75
    • (1989) NIPS , vol.4 , pp. 72-75
    • Cereijido, M.1    Gonzalez-Mariscal, L.2    Contreras, G.3
  • 7
    • 0030748172 scopus 로고    scopus 로고
    • COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos
    • Chen, Y.-H., Merzdorf, C., Paul, D.L., Goodenough, D.A. 1997. COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos. J. Cell Biol. 138:891-899
    • (1997) J. Cell Biol. , vol.138 , pp. 891-899
    • Chen, Y.-H.1    Merzdorf, C.2    Paul, D.L.3    Goodenough, D.A.4
  • 8
  • 9
    • 0017855840 scopus 로고
    • Morphological factors influencing transepithelial permeability: A model for the resistance of the zonula occludens
    • Claude, P. 1978. Morphological factors influencing transepithelial permeability: a model for the resistance of the zonula occludens. J. Membrane Biol. 39:219-232
    • (1978) J. Membrane Biol. , vol.39 , pp. 219-232
    • Claude, P.1
  • 10
    • 0017459472 scopus 로고
    • The epithelial junction: Bridge, gate, and fence
    • Diamond, J. 1977. The epithelial junction: bridge, gate, and fence. Physiologist 20:10-18
    • (1977) Physiologist , vol.20 , pp. 10-18
    • Diamond, J.1
  • 11
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar, M.G., Palade, G.E. 1963. Junctional complexes in various epithelia. J. Cell Biol. 17:375-412
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 12
    • 0015350947 scopus 로고
    • Variations in tight and gap junctions in mammalian tissues
    • Friend, D.S., Gilula, N.B. 1972. Variations in tight and gap junctions in mammalian tissues. J. Cell Biol. 53:758-776
    • (1972) J. Cell Biol. , vol.53 , pp. 758-776
    • Friend, D.S.1    Gilula, N.B.2
  • 13
    • 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. 1995. 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 Science 108:3443-3449
    • (1995) J. Cell Science , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 14
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of multilamellar bodies bearing tight junction-like structures
    • Furuse, M., Fujimoto, K., Sato, N., Hirase, T., Tsukita, S., Tsukita, S. 1996. Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of multilamellar bodies bearing tight junction-like structures. J. Cell Science 109:429-435
    • (1996) J. Cell Science , vol.109 , pp. 429-435
    • Furuse, M.1    Fujimoto, K.2    Sato, N.3    Hirase, T.4    Tsukita, S.5    Tsukita, S.6
  • 16
    • 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. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127:1617-1626
    • (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
  • 17
    • 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. 1996. 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 93:10799-10784
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10799-110784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 18
    • 0025083621 scopus 로고
    • Generation and maintenance of epithelial cell polarity
    • Gumbiner, B. 1990. Generation and maintenance of epithelial cell polarity. Curr. Opin. Cell Biol., 2:881-887
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 881-887
    • Gumbiner, B.1
  • 19
    • 0027715358 scopus 로고
    • Breaking through the tight junction barrier
    • Gumbiner, B.M. 1993. Breaking through the tight junction barrier. J. Cell Biol. 123:1631-1633
    • (1993) J. Cell Biol. , vol.123 , pp. 1631-1633
    • Gumbiner, B.M.1
  • 20
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner, B., Lowenkopf, T., Apatira, D. 1991. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci. USA 88:3460-3464
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 21
    • 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. 1998. ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J. Cell Biol. 141:199-208
    • (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
  • 22
    • 0030760530 scopus 로고    scopus 로고
    • + transport and shunt conductance in A6 epithelia
    • + transport and shunt conductance in A6 epithelia. 1997. Am. J. Physiol. 273 42:C434-C441
    • (1997) Am. J. Physiol. , vol.273 , Issue.42
    • Helman, S.I.1    Liu, X.2
  • 23
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz I. 1987. Functional inactivation of genes by dominant negative mutations. Nature 329:219-222
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 24
    • 0026603087 scopus 로고
    • Detection of the tight junction-associated protein ZO-1 in astrocytes and other non-epithelial cell types
    • Howarth, A. G., Hughes, M.R., Stevenson, B.R. 1992. Detection of the tight junction-associated protein ZO-1 in astrocytes and other non-epithelial cell types. Am. J. Physiol. 262:C461-C469
    • (1992) Am. J. Physiol. , vol.262
    • Howarth, A.G.1    Hughes, M.R.2    Stevenson, B.R.3
  • 25
    • 0030748548 scopus 로고    scopus 로고
    • Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to a Catenin and actin filaments
    • Itoh, M., Nagafuchi, A., Moroi, S., Tsukita, S. 1997. Involvement of ZO-1 in cadherin-based cell adhesion through its direct binding to a Catenin and actin filaments. J. Cell Biol. 138:181-192
    • (1997) J. Cell Biol. , vol.138 , pp. 181-192
    • Itoh, M.1    Nagafuchi, A.2    Moroi, S.3    Tsukita, S.4
  • 26
    • 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. 1994. 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. 124:949-961
    • (1994) J. Cell Biol. , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 28
    • 0029840160 scopus 로고    scopus 로고
    • Symplekin, a novel type of tight junction plaque protein
    • Keon, B.H., Schafer, S., Kuhn, C., Grund, C., Francke, W.W. 1996. Symplekin, a novel type of tight junction plaque protein. J. Cell Biol. 134:1003-1018
    • (1996) J. Cell Biol. , vol.134 , pp. 1003-1018
    • Keon, B.H.1    Schafer, S.2    Kuhn, C.3    Grund, C.4    Francke, W.W.5
  • 29
    • 0025691638 scopus 로고
    • Determination of paracellular shunt conductance in epithelia
    • Kottra, G., Fromter, E. 1990. Determination of paracellular shunt conductance in epithelia. Meth. Enzymol. 191:4-27
    • (1990) Meth. Enzymol. , vol.191 , pp. 4-27
    • Kottra, G.1    Fromter, E.2
  • 31
    • 0027757028 scopus 로고
    • 2+. I. Microscopic and general electrophysiological observations
    • 2+. I. Microscopic and general electrophysiological observations. Pfluegers Arch. 425:528-534
    • (1993) Pfluegers Arch. , vol.425 , pp. 528-534
    • Kottra, G.1    Haase, W.2    Fromter, E.3
  • 32
    • 0029610648 scopus 로고
    • Determination of the Na permeability of the tight junction of MDCK cells by fluorescence microscopy
    • Kovbasnujuk, O., Chatton, J.-Y., Friauf, W.S., Spring, K.R. 1995. Determination of the Na permeability of the tight junction of MDCK cells by fluorescence microscopy. J. Membrane Biol. 148:223-232
    • (1995) J. Membrane Biol. , vol.148 , pp. 223-232
    • Kovbasnujuk, O.1    Chatton, J.-Y.2    Friauf, W.S.3    Spring, K.R.4
  • 33
    • 0029074142 scopus 로고
    • Modulation of epithelial permeability by extracellular molecules
    • Lewis, S.A., Berg, J.R., Kline, T.J. 1995. Modulation of epithelial permeability by extracellular molecules. Physiol. Rev. 75:561-589
    • (1995) Physiol. Rev. , vol.75 , pp. 561-589
    • Lewis, S.A.1    Berg, J.R.2    Kline, T.J.3
  • 34
    • 0023176321 scopus 로고
    • Intestinal absorptive cell tight junctions are linked to the cytoskeleton
    • Madara, J.L. 1987. Intestinal absorptive cell tight junctions are linked to the cytoskeleton. Am. J. Physiol. 253:C171-C175
    • (1987) Am. J. Physiol. , vol.253
    • Madara, J.L.1
  • 35
    • 0022393433 scopus 로고
    • Occluding junction structure function relationships in a cultured epithelial monolayer
    • Madara, J.L., Dharmsathaphorn, K. 1985. Occluding junction structure function relationships in a cultured epithelial monolayer. J. Cell Biol. 101:2124-2133
    • (1985) J. Cell Biol. , vol.101 , pp. 2124-2133
    • Madara, J.L.1    Dharmsathaphorn, K.2
  • 37
    • 0023949917 scopus 로고
    • Functional coupling of tight junctions and microfilaments in T84 monolayers
    • Madara, J.L., Stafford, J., Barenberg, D., Carlson, S. 1988. Functional coupling of tight junctions and microfilaments in T84 monolayers. Am. J. Physiol. 254:G416-G423
    • (1988) Am. J. Physiol. , vol.254
    • Madara, J.L.1    Stafford, J.2    Barenberg, D.3    Carlson, S.4
  • 38
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., Mellman, I. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6:545-554
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 40
    • 0030994411 scopus 로고    scopus 로고
    • Different size limitations for increased transepithelial paracellular solute flux across phorbol ester and tumor necrosis factor-treated epithelial cell sheets
    • Mullin, J.M., Marano, C.W., Laughlin, K.V., Nuciglio, M., Stevenson, B.R., Peralta Soler, A. 1997. Different size limitations for increased transepithelial paracellular solute flux across phorbol ester and tumor necrosis factor-treated epithelial cell sheets. J. Cellular Physiol. 171:226-233
    • (1997) J. Cellular Physiol. , vol.171 , pp. 226-233
    • Mullin, J.M.1    Marano, C.W.2    Laughlin, K.V.3    Nuciglio, M.4    Stevenson, B.R.5    Peralta Soler, A.6
  • 41
    • 0026446341 scopus 로고
    • Regulation of cell surface polarity from bacteria to mammals
    • Nelson, W.J. 1992. Regulation of cell surface polarity from bacteria to mammals. Science 258:949-954
    • (1992) Science , vol.258 , pp. 949-954
    • Nelson, W.J.1
  • 43
    • 0026682741 scopus 로고
    • Neutrophil migration across a cultured epithelial monolayer elicits a biphasic resistance response representing sequential effects on transcellular and paracellular pathways
    • Parkos, C.A., Colgan, S.P., Delp, C., Arnaout, M.A., Madara, J.L. 1992. Neutrophil migration across a cultured epithelial monolayer elicits a biphasic resistance response representing sequential effects on transcellular and paracellular pathways. J. Cell Biol. 117:757-764
    • (1992) J. Cell Biol. , vol.117 , pp. 757-764
    • Parkos, C.A.1    Colgan, S.P.2    Delp, C.3    Arnaout, M.A.4    Madara, J.L.5
  • 44
    • 0017177752 scopus 로고
    • Redistribution of surface macromolecules in dissociated epithelial cells
    • Pisam, M., Ripoche, P. 1976. Redistribution of surface macromolecules in dissociated epithelial cells. J. Cell Biol. 71:907-920
    • (1976) J. Cell Biol. , vol.71 , pp. 907-920
    • Pisam, M.1    Ripoche, P.2
  • 45
    • 0001901261 scopus 로고
    • Tight junction permeability to ions and water
    • M. Cereijido, editor, CRC Press, Boca Raton
    • Reuss, L. 1992. Tight junction permeability to ions and water. In: Tight Junctions. M. Cereijido, editor, pp. 49-66. CRC Press, Boca Raton
    • (1992) Tight Junctions , pp. 49-66
    • Reuss, L.1
  • 47
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., Ikonen, E. 1997. Functional rafts in cell membranes. Nature 387:569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 48
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • Staehelin, L.A. 1974. Structure and function of intercellular junctions. Int Rev. Cytol. 39:191-283
    • (1974) Int Rev. Cytol. , vol.39 , pp. 191-283
    • Staehelin, L.A.1
  • 49
    • 0023715186 scopus 로고
    • The epithelial tight junction: Structure, function and preliminary biochemical characterization
    • Stevenson, B.R., Anderson, J.M., Bullivant, S. 1988. The epithelial tight junction: structure, function and preliminary biochemical characterization. Mol. Cell. Biochem. 83:129-145
    • (1988) Mol. Cell. Biochem. , vol.83 , pp. 129-145
    • Stevenson, B.R.1    Anderson, J.M.2    Bullivant, S.3
  • 50
    • 0028289263 scopus 로고
    • Concentration-dependent effects of cytochalasin D on tight junctions and actin filaments in MDCK epithelial cells
    • Stevenson, B.R., Begg, D.A. 1994. Concentration-dependent effects of cytochalasin D on tight junctions and actin filaments in MDCK epithelial cells. J. Cell Science 107:367-375
    • (1994) J. Cell Science , vol.107 , pp. 367-375
    • Stevenson, B.R.1    Begg, D.A.2
  • 51
    • 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. 1986. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103:755-766
    • (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
  • 52
    • 0023748364 scopus 로고
    • Voltage- and time dependence of apical membrane conductance during current clamp in Necturus gallbladder epithelium
    • Stoddard, J.S., Reuss, L. 1988. Voltage- and time dependence of apical membrane conductance during current clamp in Necturus gallbladder epithelium. J. Membrane Biol. 103:191-204
    • (1988) J. Membrane Biol. , vol.103 , pp. 191-204
    • Stoddard, J.S.1    Reuss, L.2
  • 53
    • 0030983484 scopus 로고    scopus 로고
    • Occludin confers adhesiveness when expressed in fibroblasts
    • van Itallie, C.M., Anderson, J.M. 1997. Occludin confers adhesiveness when expressed in fibroblasts. J. Cell Science 110:1113-1121
    • (1997) J. Cell Science , vol.110 , pp. 1113-1121
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 54
    • 0022748005 scopus 로고
    • The function of tight junctions in maintaining differences in lipid composition between the apical and basolateral cell surface domains of MDCK cells
    • van Meer, G., Simons, K. 1986. The function of tight junctions in maintaining differences in lipid composition between the apical and basolateral cell surface domains of MDCK cells. EMBO J. 5:1455-1464
    • (1986) EMBO J. , vol.5 , pp. 1455-1464
    • Van Meer, G.1    Simons, K.2
  • 56
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophila disc-large tumor suppressor protein of septate junctions
    • Willott, E., Balda, M.S., Fanning, A.S., Jameson, B., van Itallie, C., Anderson, J.M. 1993. The tight junction protein ZO-1 is homologous to the Drosophila disc-large tumor suppressor protein of septate junctions. Proc. Natl. Acad. Sci. USA 90:7834-7838
    • (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
  • 57
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong, V., Gumbiner, B.M. 1997. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136:399-409
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 58
    • 0025941465 scopus 로고
    • The disc-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods, D.R., Bryant, P.J. 1992. The disc-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell 66:451-464
    • (1992) Cell , vol.66 , pp. 451-464
    • Woods, D.R.1    Bryant, P.J.2
  • 59
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • in press
    • Yap, A.S., Brieher, W.M., Gumbiner, B.M. 1997. Molecular and functional analysis of cadherin-based adherens junctions. Ann. Rev. Cell Develop. Biol. 13:(in press)
    • (1997) Ann. Rev. Cell Develop. Biol. , vol.13
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 60
    • 0029074302 scopus 로고
    • Microtubule integrity is necessary for the barrier function of cultured thyroid cell monolayers
    • Yap, A.S., Stevenson, B.R., Abel, K.C., Cragoe, E.J., Jr., Manley, S.W. 1995a. Microtubule integrity is necessary for the barrier function of cultured thyroid cell monolayers. Exp. Cell Res. 218:540-550
    • (1995) Exp. Cell Res. , vol.218 , pp. 540-550
    • Yap, A.S.1    Stevenson, B.R.2    Abel, K.C.3    Cragoe Jr., E.J.4    Manley, S.W.5
  • 61
    • 0028868366 scopus 로고
    • Vinculin localization and actin stress fibers differ in thyroid cells organized as monolayers or follicles
    • Yap, A.S., Stevenson, B.R., Waters, M.J., Keast, J.R., Manley, S.W. 1995b. Vinculin localization and actin stress fibers differ in thyroid cells organized as monolayers or follicles. Cell Motil. Cytoskel. 32:318-331
    • (1995) Cell Motil. Cytoskel. , vol.32 , pp. 318-331
    • Yap, A.S.1    Stevenson, B.R.2    Waters, M.J.3    Keast, J.R.4    Manley, S.W.5
  • 62
    • 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. 1994. 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. 124:101-115
    • (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
  • 63
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 react 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. 1993. Monoclonal antibody 7H6 react with a novel tight junction-associated protein distinct from ZO-1, cingulin, and ZO-2. J. Cell Biol. 120:477-483.
    • (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


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