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Volumn 292, Issue 3, 2007, Pages

Cell-cell adhesion in lung endothelium

Author keywords

Cadherin; Immunoglobulin like

Indexed keywords

ACTIN; ALPHA CATENIN; BETA CATENIN; CD146 ANTIGEN; CELL PROTEIN; CLAUDIN; DENSITY ENHANCED PROTEIN; DESMOPLAKIN; ENDOGLIN; ENDOTHELIUM SELECTIVE ADHESION MOLECULE; EPHRIN; GUANINE NUCLEOTIDE BINDING PROTEIN; JUNCTIONAL ADHESION MOLECULE; NECTIN 1; NERVE CELL ADHESION MOLECULE; OCCLUDIN; PHOSPHATASE; PHOSPHOTRANSFERASE; PLAKOGLOBIN; PLATELET ENDOTHELIAL CELL ADHESION MOLECULE; PROTEIN P120; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; UNCLASSIFIED DRUG; UVOMORULIN; VASCULAR ENDOTHELIAL CADHERIN;

EID: 33847763996     PISSN: 10400605     EISSN: 15221504     Source Type: Journal    
DOI: 10.1152/ajplung.00386.2006     Document Type: Review
Times cited : (19)

References (150)
  • 4
    • 0033519239 scopus 로고    scopus 로고
    • p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells
    • Aono S, Nakagawa S, Reynolds AB, Takeichi M. p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells. J Cell Biol 145: 551-562, 1999.
    • (1999) J Cell Biol , vol.145 , pp. 551-562
    • Aono, S.1    Nakagawa, S.2    Reynolds, A.B.3    Takeichi, M.4
  • 5
    • 0035895081 scopus 로고    scopus 로고
    • Identification of CD146 as a component of the endothelial junction involved in the control of cell-cell cohesion
    • Bardin N, Anfosso F, Masse JM, Cramer E, Sabatier F, Le Bivic A, Sampol J, Dignat-George F. Identification of CD146 as a component of the endothelial junction involved in the control of cell-cell cohesion. Blood 98: 3677-3684, 2001.
    • (2001) Blood , vol.98 , pp. 3677-3684
    • Bardin, N.1    Anfosso, F.2    Masse, J.M.3    Cramer, E.4    Sabatier, F.5    Le Bivic, A.6    Sampol, J.7    Dignat-George, F.8
  • 8
    • 0141644213 scopus 로고    scopus 로고
    • The JAM family of junctional adhesion molecules
    • Bazzoni G. The JAM family of junctional adhesion molecules. Curr Opin Cell Biol 15: 525-530, 2003.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 525-530
    • Bazzoni, G.1
  • 9
    • 3042590902 scopus 로고    scopus 로고
    • Endothelial cell-to-cell junctions: Molecular organization and role in vascular homeostasis
    • Bazzoni G, Dejana E. Endothelial cell-to-cell junctions: molecular organization and role in vascular homeostasis. Physiol Rev 84: 869-901, 2004.
    • (2004) Physiol Rev , vol.84 , pp. 869-901
    • Bazzoni, G.1    Dejana, E.2
  • 10
    • 0019051615 scopus 로고
    • A cell surface molecule involved in aggregation of embryonic liver cells
    • Bertolotti R, Rutishauser U, Edelman GM. A cell surface molecule involved in aggregation of embryonic liver cells. Proc Natl Acad Sci USA 77: 4831-4835, 1980.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 4831-4835
    • Bertolotti, R.1    Rutishauser, U.2    Edelman, G.M.3
  • 11
    • 0033730417 scopus 로고    scopus 로고
    • Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes
    • Braga VM, Betson M, Li X, Lamarche-Vane N. Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes. Mol Biol Cell 11: 3703-3721, 2000.
    • (2000) Mol Biol Cell , vol.11 , pp. 3703-3721
    • Braga, V.M.1    Betson, M.2    Li, X.3    Lamarche-Vane, N.4
  • 12
    • 0032948289 scopus 로고    scopus 로고
    • Regulation of cadherin function by Rho and Rac: Modulation by junction maturation and cellular context
    • Braga VM, Del Maschio A, Machesky L, Dejana E. Regulation of cadherin function by Rho and Rac: modulation by junction maturation and cellular context. Mol Biol Cell 10: 9-22, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 9-22
    • Braga, V.M.1    Del Maschio, A.2    Machesky, L.3    Dejana, E.4
  • 17
    • 0017891781 scopus 로고
    • Polarized monolayers formed by epithelial cells on a permeable and translucent support
    • Cereijido M, Robbins ES, Dolan WJ, Rotunno CA, Sabatini DD. Polarized monolayers formed by epithelial cells on a permeable and translucent support. J Cell Biol 77: 853-880, 1978.
    • (1978) J Cell Biol , vol.77 , pp. 853-880
    • Cereijido, M.1    Robbins, E.S.2    Dolan, W.J.3    Rotunno, C.A.4    Sabatini, D.D.5
  • 18
    • 11244290381 scopus 로고    scopus 로고
    • Critical roles of CD146 in zebrafish vascular development
    • Chan B, Sinha S, Cho D, Ramchandran R, Sukhatme VP. Critical roles of CD146 in zebrafish vascular development. Dev Dyn 232: 232-244, 2005.
    • (2005) Dev Dyn , vol.232 , pp. 232-244
    • Chan, B.1    Sinha, S.2    Cho, D.3    Ramchandran, R.4    Sukhatme, V.P.5
  • 19
    • 0036226069 scopus 로고    scopus 로고
    • Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells
    • Chen YH, Lu Q, Goodenough DA, Jeansonne B. Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells. Mol Biol Cell 13: 1227-1237, 2002.
    • (2002) Mol Biol Cell , vol.13 , pp. 1227-1237
    • Chen, Y.H.1    Lu, Q.2    Goodenough, D.A.3    Jeansonne, B.4
  • 20
    • 33644859739 scopus 로고    scopus 로고
    • Thermodynamics of beta-catenin-ligand interactions: The roles of the N- and C-terminal tails in modulating binding affinity
    • Choi HJ, Huber AH, Weis WI. Thermodynamics of beta-catenin-ligand interactions: the roles of the N- and C-terminal tails in modulating binding affinity. J Biol Chem 281: 1027-1038, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 1027-1038
    • Choi, H.J.1    Huber, A.H.2    Weis, W.I.3
  • 25
    • 15944404246 scopus 로고    scopus 로고
    • VE-cadherin is not required for the formation of nascent blood vessels but acts to prevent their disassembly
    • Crosby CV, Fleming PA, Argraves WS, Corada M, Zanetta L, Dejana E, Drake CJ. VE-cadherin is not required for the formation of nascent blood vessels but acts to prevent their disassembly. Blood 105: 2771-2776, 2005.
    • (2005) Blood , vol.105 , pp. 2771-2776
    • Crosby, C.V.1    Fleming, P.A.2    Argraves, W.S.3    Corada, M.4    Zanetta, L.5    Dejana, E.6    Drake, C.J.7
  • 26
    • 29744437549 scopus 로고    scopus 로고
    • Blocked acinar development, E-cadherin reduction, and intraepithelial neoplasia upon ablation of p120-catenin in the mouse salivary gland
    • Davis MA, Reynolds AB. Blocked acinar development, E-cadherin reduction, and intraepithelial neoplasia upon ablation of p120-catenin in the mouse salivary gland. Dev Cell 10: 21-31, 2006.
    • (2006) Dev Cell , vol.10 , pp. 21-31
    • Davis, M.A.1    Reynolds, A.B.2
  • 28
    • 1842632667 scopus 로고    scopus 로고
    • Endothelial cell-cell junctions: Happy together
    • Dejana E. Endothelial cell-cell junctions: happy together. Nat Rev Mol Cell Biol 5: 261-270, 2004.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 261-270
    • Dejana, E.1
  • 30
    • 28344439885 scopus 로고    scopus 로고
    • Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly
    • Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell 123: 903-915, 2005.
    • (2005) Cell , vol.123 , pp. 903-915
    • Drees, F.1    Pokutta, S.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 32
    • 0346025727 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs): More molecules with dual functions?
    • Ebnet K, Suzuki A, Ohno S, Vestweber D. Junctional adhesion molecules (JAMs): more molecules with dual functions? J Cell Sci 117: 19-29, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 19-29
    • Ebnet, K.1    Suzuki, A.2    Ohno, S.3    Vestweber, D.4
  • 33
  • 34
    • 0036121308 scopus 로고    scopus 로고
    • Fujita Y, Krause G, Scheffner M, Zechner D, Leddy HE, Behrens J, Sommer T, Birchmeier W. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. Nat Cell Biol 4: 222-231, 2002.
    • Fujita Y, Krause G, Scheffner M, Zechner D, Leddy HE, Behrens J, Sommer T, Birchmeier W. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. Nat Cell Biol 4: 222-231, 2002.
  • 38
    • 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: 1539-1550, 1998.
    • (1998) J Cell Biol , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 39
    • 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: 263-272, 2001.
    • (2001) J Cell Biol , vol.153 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 40
    • 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: 391-401, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 41
    • 0035066688 scopus 로고    scopus 로고
    • Rescuing desmoplakin function in extra-embryonic ectoderm reveals the importance of this protein in embryonic heart, neuroepithelium, skin and vasculature
    • Gallicano GI, Bauer C, Fuchs E. Rescuing desmoplakin function in extra-embryonic ectoderm reveals the importance of this protein in embryonic heart, neuroepithelium, skin and vasculature. Development 128: 929-941, 2001.
    • (2001) Development , vol.128 , pp. 929-941
    • Gallicano, G.I.1    Bauer, C.2    Fuchs, E.3
  • 42
    • 0022974366 scopus 로고
    • Antibodies to liver cell adhesion molecule perturb inductive interactions and alter feather pattern and structure
    • Gallin WJ, Chuong CM, Finkel LH, Edelman GM. Antibodies to liver cell adhesion molecule perturb inductive interactions and alter feather pattern and structure. Proc Natl Acad Sci USA 83: 8235-8239, 1986.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8235-8239
    • Gallin, W.J.1    Chuong, C.M.2    Finkel, L.H.3    Edelman, G.M.4
  • 43
    • 0037743623 scopus 로고    scopus 로고
    • Minimal mutation of the cytoplasmic tail inhibits the ability of E-cadherin to activate Rac but not phosphatidylinositol 3-kinase: Direct evidence of a role for cadherin-activated Rac signaling in adhesion and contact formation
    • Goodwin M, Kovacs EM, Thoreson MA, Reynolds AB, Yap AS. Minimal mutation of the cytoplasmic tail inhibits the ability of E-cadherin to activate Rac but not phosphatidylinositol 3-kinase: direct evidence of a role for cadherin-activated Rac signaling in adhesion and contact formation. J Biol Chem 278: 20533-20539, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 20533-20539
    • Goodwin, M.1    Kovacs, E.M.2    Thoreson, M.A.3    Reynolds, A.B.4    Yap, A.S.5
  • 46
    • 0022569860 scopus 로고
    • A functional assay for proteins involved in establishing an epithelial occluding barrier: Identification of a uvomorulin-like polypeptide
    • Gumbiner B, Simons K. A functional assay for proteins involved in establishing an epithelial occluding barrier: identification of a uvomorulin-like polypeptide. J Cell Biol 102: 457-468, 1986.
    • (1986) J Cell Biol , vol.102 , pp. 457-468
    • Gumbiner, B.1    Simons, K.2
  • 47
    • 0347756750 scopus 로고    scopus 로고
    • Transference of recombinant VE-cadherin cytoplasmic domain alters endothelial junctional integrity and porcine microvascular permeability
    • Guo M, Wu MH, Granger HJ, Yuan SY. Transference of recombinant VE-cadherin cytoplasmic domain alters endothelial junctional integrity and porcine microvascular permeability. J Physiol 554: 78-88, 2004.
    • (2004) J Physiol , vol.554 , pp. 78-88
    • Guo, M.1    Wu, M.H.2    Granger, H.J.3    Yuan, S.Y.4
  • 48
    • 0039113557 scopus 로고
    • A monoclonal antibody disrupting calcium-dependent cell-cell adhesion of brain tissues: Possible role of its target antigen in animal pattern formation
    • Hatta K, Okada TS, Takeichi M. A monoclonal antibody disrupting calcium-dependent cell-cell adhesion of brain tissues: possible role of its target antigen in animal pattern formation. Proc Natl Acad Sci USA 82: 2789-2793, 1985.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2789-2793
    • Hatta, K.1    Okada, T.S.2    Takeichi, M.3
  • 49
    • 0141865704 scopus 로고    scopus 로고
    • Untangling desmosomal knots with electron tomography
    • He W, Cowin P, Stokes DL. Untangling desmosomal knots with electron tomography. Science 302: 109-113, 2003.
    • (2003) Science , vol.302 , pp. 109-113
    • He, W.1    Cowin, P.2    Stokes, D.L.3
  • 50
    • 0025195196 scopus 로고
    • 2+-dependent cell-cell adhesion molecule in endothelial cells
    • 2+-dependent cell-cell adhesion molecule in endothelial cells. J Cell Biol 110: 1745-1756, 1990.
    • (1990) J Cell Biol , vol.110 , pp. 1745-1756
    • Heimark, R.L.1    Degner, M.2    Schwartz, S.M.3
  • 51
    • 0037192854 scopus 로고    scopus 로고
    • Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells
    • Hellberg CB, Burden-Gulley SM, Pietz GE, Brady-Kalnay SM. Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells. J Biol Chem 277: 11165-11173, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 11165-11173
    • Hellberg, C.B.1    Burden-Gulley, S.M.2    Pietz, G.E.3    Brady-Kalnay, S.M.4
  • 53
    • 0035844164 scopus 로고    scopus 로고
    • Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells
    • Hirata K, Ishida T, Penta K, Rezaee M, Yang E, Wohlgemuth J, Quertermous T. Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells. J Biol Chem 276: 16223-16231, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 16223-16231
    • Hirata, K.1    Ishida, T.2    Penta, K.3    Rezaee, M.4    Yang, E.5    Wohlgemuth, J.6    Quertermous, T.7
  • 55
    • 0035853847 scopus 로고    scopus 로고
    • The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover
    • Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. J Biol Chem 276: 12301-12309, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 12301-12309
    • Huber, A.H.1    Stewart, D.B.2    Laurents, D.V.3    Nelson, W.J.4    Weis, W.I.5
  • 56
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin
    • Huber AH, Weis WI. The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin. Cell 105: 391-402, 2001.
    • (2001) Cell , vol.105 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 57
    • 0019771667 scopus 로고
    • Cell-cell interactions in early embryogenesis: A molecular approach to the role of calcium
    • Hyafil F, Babinet C, Jacob F. Cell-cell interactions in early embryogenesis: a molecular approach to the role of calcium. Cell 26: 447-454, 1981.
    • (1981) Cell , vol.26 , pp. 447-454
    • Hyafil, F.1    Babinet, C.2    Jacob, F.3
  • 58
    • 0141867737 scopus 로고    scopus 로고
    • PECAM1: Old friend, new partners
    • Ilan N, Madri JA. PECAM1: old friend, new partners. Curr Opin Cell Biol 15: 515-524, 2003.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 515-524
    • Ilan, N.1    Madri, J.A.2
  • 59
    • 0032877293 scopus 로고    scopus 로고
    • PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated beta-catenin
    • Ilan N, Mahooti S, Rimm DL, Madri JA. PECAM-1 (CD31) functions as a reservoir for and a modulator of tyrosine-phosphorylated beta-catenin. J Cell Sci 112: 3005-3014, 1999.
    • (1999) J Cell Sci , vol.112 , pp. 3005-3014
    • Ilan, N.1    Mahooti, S.2    Rimm, D.L.3    Madri, J.A.4
  • 61
    • 0141594945 scopus 로고    scopus 로고
    • Targeted disruption of endothelial cell-selective adhesion molecule inhibits angiogenic processes in vitro and in vivo
    • Ishida T, Kundu RK, Yang E, Hirata K, Ho YD, Quertermous T. Targeted disruption of endothelial cell-selective adhesion molecule inhibits angiogenic processes in vitro and in vivo. J Biol Chem 278: 34598-34604, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 34598-34604
    • Ishida, T.1    Kundu, R.K.2    Yang, E.3    Hirata, K.4    Ho, Y.D.5    Quertermous, T.6
  • 62
    • 3342986329 scopus 로고    scopus 로고
    • Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments
    • Izumi G, Sakisaka T, Baba T, Tanaka S, Morimoto K, Takai Y. Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments. J Cell Biol 166: 237-248, 2004.
    • (2004) J Cell Biol , vol.166 , pp. 237-248
    • Izumi, G.1    Sakisaka, T.2    Baba, T.3    Tanaka, S.4    Morimoto, K.5    Takai, Y.6
  • 63
    • 4143131016 scopus 로고    scopus 로고
    • The cross-Rho'ds of cell-cell adhesion
    • Jaffer ZM, Chernoff J. The cross-Rho'ds of cell-cell adhesion. J Biol Chem 279: 35123-35126, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 35123-35126
    • Jaffer, Z.M.1    Chernoff, J.2
  • 64
    • 0031588368 scopus 로고    scopus 로고
    • Melanoma progression-associated glycoprotein MUC18/MCAM mediates homotypic cell adhesion through interaction with a heterophilic ligand
    • Johnson JP, Bar-Eli M, Jansen B, Markhof E. Melanoma progression-associated glycoprotein MUC18/MCAM mediates homotypic cell adhesion through interaction with a heterophilic ligand. Int J Cancer 73: 769-774, 1997.
    • (1997) Int J Cancer , vol.73 , pp. 769-774
    • Johnson, J.P.1    Bar-Eli, M.2    Jansen, B.3    Markhof, E.4
  • 65
    • 0032254486 scopus 로고    scopus 로고
    • Expression of zonula occludens and adherens junctional proteins in human venous and arterial endothelial cells: Role of occludin in endothelial solute barriers
    • Kevil CG, Okayama N, Trocha SD, Kalogeris TJ, Coe LL, Specian RD, Davis CP, Alexander JS. Expression of zonula occludens and adherens junctional proteins in human venous and arterial endothelial cells: role of occludin in endothelial solute barriers. Microcirculation 5: 197-210, 1998.
    • (1998) Microcirculation , vol.5 , pp. 197-210
    • Kevil, C.G.1    Okayama, N.2    Trocha, S.D.3    Kalogeris, T.J.4    Coe, L.L.5    Specian, R.D.6    Davis, C.P.7    Alexander, J.S.8
  • 67
    • 4444317116 scopus 로고    scopus 로고
    • Protecting your tail: Regulation of cadherin degradation by p120-catenin
    • Kowalczyk AP, Reynolds AB. Protecting your tail: regulation of cadherin degradation by p120-catenin. Curr Opin Cell Biol 16: 522-527, 2004.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 522-527
    • Kowalczyk, A.P.1    Reynolds, A.B.2
  • 70
    • 0028900299 scopus 로고
    • The molecular organization of endothelial cell to cell junctions: Differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular endothelial cadherin (VE-cadherin)
    • Lampugnani MG, Corada M, Caveda L, Breviario F, Ayalon O, Geiger B, Dejana E. The molecular organization of endothelial cell to cell junctions: differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular endothelial cadherin (VE-cadherin). J Cell Biol 129: 203-217, 1995.
    • (1995) J Cell Biol , vol.129 , pp. 203-217
    • Lampugnani, M.G.1    Corada, M.2    Caveda, L.3    Breviario, F.4    Ayalon, O.5    Geiger, B.6    Dejana, E.7
  • 73
    • 0028059290 scopus 로고
    • E-cadherin null mutant embryos fail to form a trophectoderm epithelium
    • Larue L, Ohsugi M, Hirchenhain J, Kemler R. E-cadherin null mutant embryos fail to form a trophectoderm epithelium. Proc Natl Acad Sci USA 91: 8263-8267, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8263-8267
    • Larue, L.1    Ohsugi, M.2    Hirchenhain, J.3    Kemler, R.4
  • 74
    • 0001331879 scopus 로고    scopus 로고
    • Recycling of E-cadherin: A potential mechanism for regulating cadherin dynamics
    • Le TL, Yap AS, Stow JL. Recycling of E-cadherin: a potential mechanism for regulating cadherin dynamics. J Cell Biol 146: 219-232, 1999.
    • (1999) J Cell Biol , vol.146 , pp. 219-232
    • TL, L.1    Yap, A.S.2    Stow, J.L.3
  • 77
    • 24644447079 scopus 로고    scopus 로고
    • The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of beta-catenin
    • Lilien J, Balsamo J. The regulation of cadherin-mediated adhesion by tyrosine phosphorylation/dephosphorylation of beta-catenin. Curr Opin Cell Biol 17: 459-465, 2005.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 459-465
    • Lilien, J.1    Balsamo, J.2
  • 78
    • 0036234842 scopus 로고    scopus 로고
    • Turn-off, drop-out: Functional state switching of cadherins
    • Lilien J, Balsamo J, Arregui C, Xu G. Turn-off, drop-out: functional state switching of cadherins. Dev Dyn 224: 18-29, 2002.
    • (2002) Dev Dyn , vol.224 , pp. 18-29
    • Lilien, J.1    Balsamo, J.2    Arregui, C.3    Xu, G.4
  • 81
    • 17644379624 scopus 로고    scopus 로고
    • N-cadherin acts upstream of VE-cadherin in controlling vascular morphogenesis
    • Luo Y, Radice GL. N-cadherin acts upstream of VE-cadherin in controlling vascular morphogenesis. J Cell Biol 169: 29-34, 2005.
    • (2005) J Cell Biol , vol.169 , pp. 29-34
    • Luo, Y.1    Radice, G.L.2
  • 84
    • 7044239314 scopus 로고    scopus 로고
    • Vascular remodeling in the circulations of the lung
    • Mitzner W, Wagner EM. Vascular remodeling in the circulations of the lung. J Appl Physiol 97: 1999-2004, 2004.
    • (2004) J Appl Physiol , vol.97 , pp. 1999-2004
    • Mitzner, W.1    Wagner, E.M.2
  • 86
    • 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: 185-194, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 185-194
    • Morita, K.1    Sasaki, H.2    Furuse, M.3    Tsukita, S.4
  • 88
    • 0023225108 scopus 로고
    • Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA
    • Nagafuchi A, Shirayoshi Y, Okazaki K, Yasuda K, Takeichi M. Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA. Nature 329: 341-343, 1987.
    • (1987) Nature , vol.329 , pp. 341-343
    • Nagafuchi, A.1    Shirayoshi, Y.2    Okazaki, K.3    Yasuda, K.4    Takeichi, M.5
  • 89
    • 1842390685 scopus 로고
    • Cell binding function of E-cadherin is regulated by the cytoplasmic domain
    • Nagafuchi A, Takeichi M. Cell binding function of E-cadherin is regulated by the cytoplasmic domain. EMBO J 7: 3679-3684, 1988.
    • (1988) EMBO J , vol.7 , pp. 3679-3684
    • Nagafuchi, A.1    Takeichi, M.2
  • 90
    • 0141679018 scopus 로고    scopus 로고
    • Signaling through JAM-1 and alphavbeta3 is required for the angiogenic action of bFGF: Dissociation of the JAM-1 and alphavbeta3 complex
    • Naik MU, Mousa SA, Parkos CA, Naik UP. Signaling through JAM-1 and alphavbeta3 is required for the angiogenic action of bFGF: dissociation of the JAM-1 and alphavbeta3 complex. Blood 102: 2108-2114, 2003.
    • (2003) Blood , vol.102 , pp. 2108-2114
    • Naik, M.U.1    Mousa, S.A.2    Parkos, C.A.3    Naik, U.P.4
  • 94
    • 8644277271 scopus 로고    scopus 로고
    • NADPH oxidase mediates vascular endothelial cadherin phosphorylation and endothelial dysfunction
    • Nwariaku FE, Liu Z, Zhu X, Nahari D, Ingle C, Wu RF, Gu Y, Sarosi G, Terada LS. NADPH oxidase mediates vascular endothelial cadherin phosphorylation and endothelial dysfunction. Blood 104: 3214-3220, 2004.
    • (2004) Blood , vol.104 , pp. 3214-3220
    • Nwariaku, F.E.1    Liu, Z.2    Zhu, X.3    Nahari, D.4    Ingle, C.5    Wu, R.F.6    Gu, Y.7    Sarosi, G.8    Terada, L.S.9
  • 95
    • 0033597896 scopus 로고    scopus 로고
    • p120(ctn) binds to the membrane-proximal region of the E-cadherin cytoplasmic domain and is involved in modulation of adhesion activity
    • Ohkubo T, Ozawa M. p120(ctn) binds to the membrane-proximal region of the E-cadherin cytoplasmic domain and is involved in modulation of adhesion activity. J Biol Chem 274: 21409-21415, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 21409-21415
    • Ohkubo, T.1    Ozawa, M.2
  • 96
    • 0037135988 scopus 로고    scopus 로고
    • Evidence for a role of platelet endothelial cell adhesion molecule-1 in endothelial cell mechanosignal transduction: Is it a mechanoresponsive molecule?
    • Osawa M, Masuda M, Kusano K, Fujiwara K. Evidence for a role of platelet endothelial cell adhesion molecule-1 in endothelial cell mechanosignal transduction: is it a mechanoresponsive molecule? J Cell Biol 158: 773-785, 2002.
    • (2002) J Cell Biol , vol.158 , pp. 773-785
    • Osawa, M.1    Masuda, M.2    Kusano, K.3    Fujiwara, K.4
  • 97
    • 0031049535 scopus 로고    scopus 로고
    • Modulation of cellular adhesion in bovine brain microvessel endothelial cells by a decapeptide
    • Pal D, Audus KL, Siahaan TJ. Modulation of cellular adhesion in bovine brain microvessel endothelial cells by a decapeptide. Brain Res 747: 103-113, 1997.
    • (1997) Brain Res , vol.747 , pp. 103-113
    • Pal, D.1    Audus, K.L.2    Siahaan, T.J.3
  • 99
    • 33644830571 scopus 로고    scopus 로고
    • Tightening the barrier: Mechanical forces and the control of endothelial permeability
    • Pearson JD. Tightening the barrier: mechanical forces and the control of endothelial permeability. Arterioscler Thromb Vasc Biol 26: 10-11, 2006.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 10-11
    • Pearson, J.D.1
  • 100
    • 0033119626 scopus 로고    scopus 로고
    • 2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation
    • 2+ dependence and mutational analysis reveal molecular details of E-cadherin homoassociation. EMBO J 18: 1738-1747, 1999.
    • (1999) EMBO J , vol.18 , pp. 1738-1747
    • Pertz, O.1    Bozic, D.2    Koch, A.W.3    Fauser, C.4    Brancaccio, A.5
  • 103
    • 0037378505 scopus 로고    scopus 로고
    • p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin interaction
    • Piedra J, Miravet S, Castano J, Palmer HG, Heisterkamp N, Garcia de Herreros A, Dunach M. p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin interaction. Mol Cell Biol 23: 2287-2297, 2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 2287-2297
    • Piedra, J.1    Miravet, S.2    Castano, J.3    Palmer, H.G.4    Heisterkamp, N.5    Garcia de Herreros, A.6    Dunach, M.7
  • 104
    • 33746706949 scopus 로고    scopus 로고
    • Spatial control of actin organization at adherens junctions by the synaptogamin-like protein Btsz
    • Pilot F, Phillippe J-M, Lemmers C, Lecuit T. Spatial control of actin organization at adherens junctions by the synaptogamin-like protein Btsz. Nature 442: 580-584, 2006.
    • (2006) Nature , vol.442 , pp. 580-584
    • Pilot, F.1    Phillippe, J.-M.2    Lemmers, C.3    Lecuit, T.4
  • 105
    • 33744949095 scopus 로고    scopus 로고
    • Calcium site mutations in cadherin: Impact on adhesion and evidence of cooperativity
    • Prakasam A, Chien YH, Maruthamuthu V, Leckband DE. Calcium site mutations in cadherin: impact on adhesion and evidence of cooperativity. Biochemistry 45: 6930-6939, 2006.
    • (2006) Biochemistry , vol.45 , pp. 6930-6939
    • Prakasam, A.1    Chien, Y.H.2    Maruthamuthu, V.3    Leckband, D.E.4
  • 106
    • 33646153988 scopus 로고    scopus 로고
    • The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis
    • Raschperger E, Thyberg J, Pettersson S, Philipson L, Fuxe J, Pettersson RF. The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis. Exp Cell Res 312: 1566-1580, 2006.
    • (2006) Exp Cell Res , vol.312 , pp. 1566-1580
    • Raschperger, E.1    Thyberg, J.2    Pettersson, S.3    Philipson, L.4    Fuxe, J.5    Pettersson, R.F.6
  • 108
    • 0036800124 scopus 로고    scopus 로고
    • Activation of the repulsive receptor Roundabout inhibits N-cadherin-mediated cell adhesion
    • Rhee J, Mahfooz NS, Arregui C, Lilien J, Balsamo J, VanBerkum MF. Activation of the repulsive receptor Roundabout inhibits N-cadherin-mediated cell adhesion. Nat Cell Biol 4: 798-805, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 798-805
    • Rhee, J.1    Mahfooz, N.S.2    Arregui, C.3    Lilien, J.4    Balsamo, J.5    VanBerkum, M.F.6
  • 109
    • 0033579480 scopus 로고    scopus 로고
    • Regulation of E-cadherin/catenin association by tyrosine phosphorylation
    • Roura S, Miravet S, Piedra J, Garcia de Herreros A, Dunach M. Regulation of E-cadherin/catenin association by tyrosine phosphorylation. J Biol Chem 274: 36734-36740, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 36734-36740
    • Roura, S.1    Miravet, S.2    Piedra, J.3    Garcia de Herreros, A.4    Dunach, M.5
  • 112
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • Sahai E, Marshall CJ. ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat Cell Biol 4: 408-415, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 114
    • 31944446602 scopus 로고    scopus 로고
    • MAGI-1 is required for Rap1 activation upon cell-cell contact and for enhancement of vascular endothelial cadherin-mediated cell adhesion
    • Sakurai A, Fukuhara S, Yamagishi A, Sako K, Kamioka Y, Masuda M, Nakaoka Y, Mochizuki N. MAGI-1 is required for Rap1 activation upon cell-cell contact and for enhancement of vascular endothelial cadherin-mediated cell adhesion. Mol Biol Cell 17: 966-976, 2006.
    • (2006) Mol Biol Cell , vol.17 , pp. 966-976
    • Sakurai, A.1    Fukuhara, S.2    Yamagishi, A.3    Sako, K.4    Kamioka, Y.5    Masuda, M.6    Nakaoka, Y.7    Mochizuki, N.8
  • 115
    • 0026740788 scopus 로고
    • Extrajunctional distribution of N-cadherin in cultured human endothelial cells
    • Salomon D, Ayalon O, Patel-King R, Hynes RO, Geiger B. Extrajunctional distribution of N-cadherin in cultured human endothelial cells. J Cell Sci 102: 7-17, 1992.
    • (1992) J Cell Sci , vol.102 , pp. 7-17
    • Salomon, D.1    Ayalon, O.2    Patel-King, R.3    Hynes, R.O.4    Geiger, B.5
  • 116
    • 27744551068 scopus 로고    scopus 로고
    • The homophilic binding of junctional adhesion molecule-C mediates tumor cell-endothelial cell interactions
    • Santoso S, Orlova VV, Song K, Sachs UJ, Andrei-Selmer CL, Chavakis T. The homophilic binding of junctional adhesion molecule-C mediates tumor cell-endothelial cell interactions. J Biol Chem 280: 36326-36333, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 36326-36333
    • Santoso, S.1    Orlova, V.V.2    Song, K.3    Sachs, U.J.4    Andrei-Selmer, C.L.5    Chavakis, T.6
  • 117
    • 8444224950 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule deficiency or blockade significantly reduces leukocyte emigration in a majority of mouse strains
    • Schenkel AR, Chew TW, Muller WA. Platelet endothelial cell adhesion molecule deficiency or blockade significantly reduces leukocyte emigration in a majority of mouse strains. J Immunol 173: 6403-6408, 2004.
    • (2004) J Immunol , vol.173 , pp. 6403-6408
    • Schenkel, A.R.1    Chew, T.W.2    Muller, W.A.3
  • 119
    • 0036087205 scopus 로고    scopus 로고
    • Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin
    • Shasby DM, Ries DR, Shasby SS, Winter MC. Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin. Am J Physiol Lung Cell Mol Physiol 282: L1330-L1338, 2002.
    • (2002) Am J Physiol Lung Cell Mol Physiol , vol.282
    • Shasby, D.M.1    Ries, D.R.2    Shasby, S.S.3    Winter, M.C.4
  • 120
    • 0022461861 scopus 로고
    • Effects of calcium on transendothelial albumin transfer and electrical resistance
    • Shasby DM, Shasby SS. Effects of calcium on transendothelial albumin transfer and electrical resistance. J Appl Physiol 60: 71-79, 1986.
    • (1986) J Appl Physiol , vol.60 , pp. 71-79
    • Shasby, D.M.1    Shasby, S.S.2
  • 121
    • 32044450585 scopus 로고    scopus 로고
    • Genomic structure, organization and promoter analysis of the human F11R/F11 receptor/junctional adhesion molecule-1/JAM-A
    • Sobocki T, Sobocka MB, Babinska A, Ehrlich YH, Banerjee P, Kornecki E. Genomic structure, organization and promoter analysis of the human F11R/F11 receptor/junctional adhesion molecule-1/JAM-A. Gene 366: 128-144, 2006.
    • (2006) Gene , vol.366 , pp. 128-144
    • Sobocki, T.1    Sobocka, M.B.2    Babinska, A.3    Ehrlich, Y.H.4    Banerjee, P.5    Kornecki, E.6
  • 123
    • 15744369759 scopus 로고    scopus 로고
    • MAPKs (ERK1/2, p38) and AKT can be phosphorylated by shear stress independently of platelet endothelial cell adhesion molecule-1 (CD31) in vascular endothelial cells
    • Sumpio BE, Yun S, Cordova AC, Haga M, Zhang J, Koh Y, Madri JA. MAPKs (ERK1/2, p38) and AKT can be phosphorylated by shear stress independently of platelet endothelial cell adhesion molecule-1 (CD31) in vascular endothelial cells. J Biol Chem 280: 11185-11191, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 11185-11191
    • Sumpio, B.E.1    Yun, S.2    Cordova, A.C.3    Haga, M.4    Zhang, J.5    Koh, Y.6    Madri, J.A.7
  • 124
    • 0026146968 scopus 로고
    • Diversity of the cadherin family: Evidence for eight new cadherins in nervous tissue
    • Suzuki S, Sano K, Tanihara H. Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue. Cell Regul 2: 261-270, 1991.
    • (1991) Cell Regul , vol.2 , pp. 261-270
    • Suzuki, S.1    Sano, K.2    Tanihara, H.3
  • 126
    • 0141813527 scopus 로고    scopus 로고
    • Nectins and nectin-like molecules: Roles in cell adhesion, migration, and polarization
    • Takai Y, Irie K, Shimizu K, Sakisaka T, Ikeda W. Nectins and nectin-like molecules: roles in cell adhesion, migration, and polarization. Cancer Sci 94: 655-667, 2003.
    • (2003) Cancer Sci , vol.94 , pp. 655-667
    • Takai, Y.1    Irie, K.2    Shimizu, K.3    Sakisaka, T.4    Ikeda, W.5
  • 127
    • 0037232646 scopus 로고    scopus 로고
    • Nectin and afadin: Novel organizers of intercellular junctions
    • Takai Y, Nakanishi H. Nectin and afadin: novel organizers of intercellular junctions. J Cell Sci 116: 17-27, 2003.
    • (2003) J Cell Sci , vol.116 , pp. 17-27
    • Takai, Y.1    Nakanishi, H.2
  • 128
    • 0017660974 scopus 로고
    • Adhesion among neural cells of the chick embryo. II. Purification and characterization of a cell adhesion molecule from neural retina
    • Thiery JP, Brackenbury R, Rutishauser U, Edelman GM. Adhesion among neural cells of the chick embryo. II. Purification and characterization of a cell adhesion molecule from neural retina. J Biol Chem 252: 6841-6845, 1977.
    • (1977) J Biol Chem , vol.252 , pp. 6841-6845
    • Thiery, J.P.1    Brackenbury, R.2    Rutishauser, U.3    Edelman, G.M.4
  • 130
    • 0034050458 scopus 로고    scopus 로고
    • SHP2 association with VE-cadherin complexes in human endothelial cells is regulated by thrombin
    • Ukropec JA, Hollinger MK, Salva SM, Woolkalis MJ. SHP2 association with VE-cadherin complexes in human endothelial cells is regulated by thrombin. J Biol Chem 275: 5983-5986, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 5983-5986
    • Ukropec, J.A.1    Hollinger, M.K.2    Salva, S.M.3    Woolkalis, M.J.4
  • 132
    • 20444418138 scopus 로고    scopus 로고
    • Proline-rich tyrosine kinase 2 (Pyk2) mediates vascular endothelial-cadherin-based cell-cell adhesion by regulating beta-catenin tyrosine phosphorylation
    • van Buul JD, Anthony EC, Fernandez-Borja M, Burridge K, Hordijk PL. Proline-rich tyrosine kinase 2 (Pyk2) mediates vascular endothelial-cadherin-based cell-cell adhesion by regulating beta-catenin tyrosine phosphorylation. J Biol Chem 280: 21129-21136, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 21129-21136
    • van Buul, J.D.1    Anthony, E.C.2    Fernandez-Borja, M.3    Burridge, K.4    Hordijk, P.L.5
  • 133
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie CM, Anderson JM. Claudins and epithelial paracellular transport. Annu Rev Physiol 68: 403-429, 2006.
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 135
    • 0032577446 scopus 로고    scopus 로고
    • Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4
    • Wang HU, Chen ZF, Anderson DJ. Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell 93: 741-753, 1998.
    • (1998) Cell , vol.93 , pp. 741-753
    • Wang, H.U.1    Chen, Z.F.2    Anderson, D.J.3
  • 136
    • 32444440870 scopus 로고    scopus 로고
    • Integrins regulate VE-cadherin and catenins: Dependence of this regulation on Src, but not on Ras
    • Wang Y, Jin G, Miao H, Li JY, Usami S, Chien S. Integrins regulate VE-cadherin and catenins: dependence of this regulation on Src, but not on Ras. Proc Natl Acad Sci USA 103: 1774-1779, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1774-1779
    • Wang, Y.1    Jin, G.2    Miao, H.3    Li, J.Y.4    Usami, S.5    Chien, S.6
  • 138
    • 25644449640 scopus 로고    scopus 로고
    • Pathophysiological consequences of VEGF-induced vascular permeability
    • Weis SM, Cheresh DA. Pathophysiological consequences of VEGF-induced vascular permeability. Nature 437: 497-504, 2005.
    • (2005) Nature , vol.437 , pp. 497-504
    • Weis, S.M.1    Cheresh, D.A.2
  • 139
    • 0141651204 scopus 로고    scopus 로고
    • Cadherins as modulators of cellular phenotype
    • Wheelock MJ, Johnson KR. Cadherins as modulators of cellular phenotype. Annu Rev Cell Dev Biol 19: 207-235, 2003.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 207-235
    • Wheelock, M.J.1    Johnson, K.R.2
  • 141
    • 4544345026 scopus 로고    scopus 로고
    • Histamine selectively interrupts VE-cadherin adhesion independently of capacitive calcium entry
    • Winter MC, Shasby SS, Ries DR, Shasby DM. Histamine selectively interrupts VE-cadherin adhesion independently of capacitive calcium entry. Am J Physiol Lung Cell Mol Physiol 287: L816-L823, 2004.
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.287
    • Winter, M.C.1    Shasby, S.S.2    Ries, D.R.3    Shasby, D.M.4
  • 142
    • 33749370682 scopus 로고    scopus 로고
    • PAR2 activation interrupts E-cadherin adhesion and compromises the airway epithelial barrier: Protective effect of beta-agonists
    • Winter MC, Shasby SS, Ries DR, Shasby DM. PAR2 activation interrupts E-cadherin adhesion and compromises the airway epithelial barrier: protective effect of beta-agonists. Am J Physiol Lung Cell Mol Physiol 291: L628-L635, 2006.
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.291
    • Winter, M.C.1    Shasby, S.S.2    Ries, D.R.3    Shasby, D.M.4
  • 144
  • 146
    • 0032577571 scopus 로고    scopus 로고
    • Vasculogenesis, angiogenesis, and growth factors: Ephrins enter the fray at the border
    • Yancopoulos GD, Klagsbrun M, Folkman J. Vasculogenesis, angiogenesis, and growth factors: ephrins enter the fray at the border. Cell 93: 661-664, 1998.
    • (1998) Cell , vol.93 , pp. 661-664
    • Yancopoulos, G.D.1    Klagsbrun, M.2    Folkman, J.3
  • 147
    • 0032482201 scopus 로고    scopus 로고
    • The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn
    • Yap AS, Niessen CM, Gumbiner BM. The juxtamembrane region of the cadherin cytoplasmic tail supports lateral clustering, adhesive strengthening, and interaction with p120ctn. J Cell Biol 141: 779-789, 1998.
    • (1998) J Cell Biol , vol.141 , pp. 779-789
    • Yap, A.S.1    Niessen, C.M.2    Gumbiner, B.M.3
  • 148
    • 0021298451 scopus 로고
    • Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody
    • Yoshida-Noro C, Suzuki N, Takeichi M. Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody. Dev Biol 101: 19-27, 1984.
    • (1984) Dev Biol , vol.101 , pp. 19-27
    • Yoshida-Noro, C.1    Suzuki, N.2    Takeichi, M.3


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