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Volumn 24, Issue 1, 2003, Pages 1-14

Adherens junction dynamics in the testis and spermatogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA 2 MACROGLOBULIN; APROTININ; CADHERIN; CATENIN; INTEGRIN; LAMININ; PROTEINASE INHIBITOR;

EID: 0038025642     PISSN: 01963635     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (40)

References (172)
  • 3
    • 0034010129 scopus 로고    scopus 로고
    • The p120 catenin family: Complex roles in adhesion, signaling and cancer
    • Anastasiadis PZ, Reynolds AB. The p120 catenin family: complex roles in adhesion, signaling and cancer. J Cell Sci. 2000;113:1319-1334.
    • (2000) J Cell Sci , vol.113 , pp. 1319-1334
    • Anastasiadis, P.Z.1    Reynolds, A.B.2
  • 4
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Aplin AE, Howe A, Alahari SK, Juliano RL. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev. 1998;50:197-263.
    • (1998) Pharmacol Rev , vol.50 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 5
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of PTP1B-like phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of β-catenin
    • Balsamo J, Leung T, Ernst H, Zanin MK, Hoffman S, Lilien J. Regulated binding of PTP1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of β-catenin. J Cell Biol. 1996;134:801-813.
    • (1996) J Cell Biol , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung, T.2    Ernst, H.3    Zanin, M.K.4    Hoffman, S.5    Lilien, J.6
  • 6
    • 0029896454 scopus 로고    scopus 로고
    • Identification and characterization of espin, an actin-binding protein localized to the F-actin-rich junctional plaques of Sertoli cell ectoplasmic specializations
    • Bartles JR, Wierda A, Zheng L. Identification and characterization of espin, an actin-binding protein localized to the F-actin-rich junctional plaques of Sertoli cell ectoplasmic specializations. J Cell Sci. 1996;109:1229-1239.
    • (1996) J Cell Sci , vol.109 , pp. 1229-1239
    • Bartles, J.R.1    Wierda, A.2    Zheng, L.3
  • 7
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-src gene
    • Behrens J, Vakaet L, Friis R, Winterhager E, van Roy F, Mareel MM, Birchmeier W. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-src gene. J Cell Biol. 1993;120:757-766.
    • (1993) J Cell Biol , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 9
    • 0034029901 scopus 로고    scopus 로고
    • Defects in nuclear and cytoskeletal morphology and mitochondrial localization in spermatozoa of mice lacking nectin-2, a component of cell-cell adherens junctions
    • Bouchard MJ, Dong Y, McDermott BM Jr, Lam DH, Brown KR, Shelanski M, Bellve AR, Racaniello VR. Defects in nuclear and cytoskeletal morphology and mitochondrial localization in spermatozoa of mice lacking nectin-2, a component of cell-cell adherens junctions. Mol Cell Biol. 2000;20:2865-2873.
    • (2000) Mol Cell Biol , vol.20 , pp. 2865-2873
    • Bouchard, M.J.1    Dong, Y.2    McDermott Jr., B.M.3    Lam, D.H.4    Brown, K.R.5    Shelanski, M.6    Bellve, A.R.7    Racaniello, V.R.8
  • 10
    • 0029149746 scopus 로고
    • Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo
    • Brady-Kalnay SM, Rimm DL, Tonks NK. Receptor protein tyrosine phosphatase PTPμ associates with cadherins and catenins in vivo. J Cell Biol. 1995;130:977-986.
    • (1995) J Cell Biol , vol.130 , pp. 977-986
    • Brady-Kalnay, S.M.1    Rimm, D.L.2    Tonks, N.K.3
  • 11
    • 0026532667 scopus 로고
    • Isolation and characterization of a human gene that encodes a new subclass of protein tyrosine kinases
    • Brauninger A, Holtrich U, Strebhardt K, Rubsamen-Waigmann H. Isolation and characterization of a human gene that encodes a new subclass of protein tyrosine kinases. Gene. 1992;110:205-211.
    • (1992) Gene , vol.110 , pp. 205-211
    • Brauninger, A.1    Holtrich, U.2    Strebhardt, K.3    Rubsamen-Waigmann, H.4
  • 12
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • Brown MT, Cooper JA. Regulation, substrates and functions of Src. Biochim Biophys Acta. 1996;1287:121-149.
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 14
    • 0002503883 scopus 로고
    • Sertoli cell junctions and the seminiferous epithelium barrier
    • Russell LD, Griswold MD, eds. Clearwater, Fla: Cache River Press
    • Byers S, Pelletier RM, Suarez-Quian C. Sertoli cell junctions and the seminiferous epithelium barrier. In: Russell LD, Griswold MD, eds. The Sertoli cell. Clearwater, Fla: Cache River Press; 1993:431-446.
    • (1993) The Sertoli Cell , pp. 431-446
    • Byers, S.1    Pelletier, R.M.2    Suarez-Quian, C.3
  • 16
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • Calderwood DA, Shattil SJ, Ginsberg MH. Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling. J Biol Chem. 2000;275:22607-22610.
    • (2000) J Biol Chem , vol.275 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 17
    • 0025990027 scopus 로고
    • Hormonal regulation of spermatid binding
    • Cameron DF, Muffly KE. Hormonal regulation of spermatid binding. J Cell Sci. 1991;100:623-633.
    • (1991) J Cell Sci , vol.100 , pp. 623-633
    • Cameron, D.F.1    Muffly, K.E.2
  • 18
    • 0034749410 scopus 로고    scopus 로고
    • Structure and control of a cell-cell adhesion complex associated with spermiation in rat seminiferous epithelium
    • Chapin RE, Wine RN, Harris MW, Borchers CH, Haseman JK. Structure and control of a cell-cell adhesion complex associated with spermiation in rat seminiferous epithelium. J Androl. 2001;22:1030-1052.
    • (2001) J Androl , vol.22 , pp. 1030-1052
    • Chapin, R.E.1    Wine, R.N.2    Harris, M.W.3    Borchers, C.H.4    Haseman, J.K.5
  • 20
    • 0036788073 scopus 로고    scopus 로고
    • Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive developments
    • Cheng CY, Mruk DD. Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive developments. Physiol Rev. 2002;82:825-874.
    • (2002) Physiol Rev , vol.82 , pp. 825-874
    • Cheng, C.Y.1    Mruk, D.D.2
  • 21
    • 0030904004 scopus 로고    scopus 로고
    • A novel protein-tyrosine phosphatase related to the homotypically ad hering κ and μ receptors
    • Cheng J, Wu K, Armanini M, O'Rourke N, Dowbenko D, Lasky LA. A novel protein-tyrosine phosphatase related to the homotypically ad hering κ and μ receptors. J Biol Chem. 1997;272:7264-7277.
    • (1997) J Biol Chem , vol.272 , pp. 7264-7277
    • Cheng, J.1    Wu, K.2    Armanini, M.3    O'Rourke, N.4    Dowbenko, D.5    Lasky, L.A.6
  • 22
    • 0032876725 scopus 로고    scopus 로고
    • Study on the formation of specialized inter-Sertoli cell junctions m vitro
    • Chung SSW, Lee WM, Cheng CY. Study on the formation of specialized inter-Sertoli cell junctions m vitro. J Cell Physiol. 1999a;181:258-272.
    • (1999) J Cell Physiol , vol.181 , pp. 258-272
    • Chung, S.S.W.1    Lee, W.M.2    Cheng, C.Y.3
  • 23
    • 0031732607 scopus 로고    scopus 로고
    • Rat testicular N-cadherin: Its complementary deoxyribonucleic acid cloning and regulation
    • Chung SSW, Mo MY, Silvestrini B, Lee WM, Cheng CY. Rat testicular N-cadherin: its complementary deoxyribonucleic acid cloning and regulation. Endocrinology. 1998a;139:1853-1862.
    • (1998) Endocrinology , vol.139 , pp. 1853-1862
    • Chung, S.S.W.1    Mo, M.Y.2    Silvestrini, B.3    Lee, W.M.4    Cheng, C.Y.5
  • 24
    • 0032891770 scopus 로고    scopus 로고
    • Identification and purification of proteins from germ cell-conditioned medium (GCCM)
    • Chung SSW, Mruk D, Lee WM, Cheng CY. Identification and purification of proteins from germ cell-conditioned medium (GCCM). Biochem Mol Biol Int. 1999b;47:479-491.
    • (1999) Biochem Mol Biol Int , vol.47 , pp. 479-491
    • Chung, S.S.W.1    Mruk, D.2    Lee, W.M.3    Cheng, C.Y.4
  • 25
    • 0032407875 scopus 로고    scopus 로고
    • Evidence for cross-talk between Sertoli and germ cells using selected cathepsins as markers
    • Chung SSW, Zhu LJ, Mo MY, Silvestrini B, Lee WM, Cheng CY. Evidence for cross-talk between Sertoli and germ cells using selected cathepsins as markers. J Androl. 1998b;19:686-703.
    • (1998) J Androl , vol.19 , pp. 686-703
    • Chung, S.S.W.1    Zhu, L.J.2    Mo, M.Y.3    Silvestrini, B.4    Lee, W.M.5    Cheng, C.Y.6
  • 26
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark EA, Brugge JS. Integrins and signal transduction pathways: the road taken. Science. 1995;268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 27
    • 0031797729 scopus 로고    scopus 로고
    • The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells
    • Cocchi F, Menotti L, Mirandola P, Lopez M, Campadelli-Fiume G. The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. J Virol. 1998;72:9992-10002.
    • (1998) J Virol , vol.72 , pp. 9992-10002
    • Cocchi, F.1    Menotti, L.2    Mirandola, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 28
    • 0035160210 scopus 로고    scopus 로고
    • Mice devoid of Fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation
    • Craig AWB, Zirngibl R, Williams K, Cole LA, Greer PA. Mice devoid of Fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation. Mol Cell Biol. 2001;21:603-613.
    • (2001) Mol Cell Biol , vol.21 , pp. 603-613
    • Craig, A.W.B.1    Zirngibl, R.2    Williams, K.3    Cole, L.A.4    Greer, P.A.5
  • 29
    • 0033152940 scopus 로고    scopus 로고
    • Integrins: Alternative splicing as a mechanism to regulate ligand binding and integrin signaling events
    • de Melker AA, Sonnenberg A. Integrins: alternative splicing as a mechanism to regulate ligand binding and integrin signaling events. Bioessays. 1999;21:499-509.
    • (1999) Bioessays , vol.21 , pp. 499-509
    • De Melker, A.A.1    Sonnenberg, A.2
  • 30
    • 0035879015 scopus 로고    scopus 로고
    • Autocatalytic tyrosine-phosphorylation of protein kinase CK2 α and α′ subunits: Implication of Tyr182
    • Donella-Deana A, Cesaro L, Sarno S, Brunati AM, Ruzzene M, Pinna LA. Autocatalytic tyrosine-phosphorylation of protein kinase CK2 α and α′ subunits: implication of Tyr182. Biochem J. 2001;357:563-567.
    • (2001) Biochem J , vol.357 , pp. 563-567
    • Donella-Deana, A.1    Cesaro, L.2    Sarno, S.3    Brunati, A.M.4    Ruzzene, M.5    Pinna, L.A.6
  • 31
    • 0027958088 scopus 로고
    • Basement membrane regulation of Sertoli cells
    • Dym M. Basement membrane regulation of Sertoli cells. Endocr Rev. 1994;15:102-115.
    • (1994) Endocr Rev , vol.15 , pp. 102-115
    • Dym, M.1
  • 32
    • 0023935414 scopus 로고    scopus 로고
    • Pachytene spermatocyte and round spermatid binding to Sertoli cells in vitro
    • Enders GC, Millette CF. Pachytene spermatocyte and round spermatid binding to Sertoli cells in vitro. J Cell Sci. 1998;90:105-114.
    • (1998) J Cell Sci , vol.90 , pp. 105-114
    • Enders, G.C.1    Millette, C.F.2
  • 33
    • 0031825437 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces VE-cadherin tyrosine phosphorylation in endothelial cells
    • Esser S, Lampugnani MG, Corada M, Dejana E, Risau W. Vascular endothelial growth factor induces VE-cadherin tyrosine phosphorylation in endothelial cells. J Cell Sci. 1998;111:1853-1865.
    • (1998) J Cell Sci , vol.111 , pp. 1853-1865
    • Esser, S.1    Lampugnani, M.G.2    Corada, M.3    Dejana, E.4    Risau, W.5
  • 34
    • 0028979154 scopus 로고
    • Consequences of lack of β1 integrin gene expression in mice
    • Fassler R, Meyer M. Consequences of lack of β1 integrin gene expression in mice. Genes Dev. 1995;9:1896-1908.
    • (1995) Genes Dev , vol.9 , pp. 1896-1908
    • Fassler, R.1    Meyer, M.2
  • 35
    • 0030960388 scopus 로고    scopus 로고
    • Uncoupling of XB/U-cadherin-catenin complex formation from its function in cell-cell adhesion
    • Finnemann S, Mitrik I, Hess M, Otto G, Wedlich D. Uncoupling of XB/U-cadherin-catenin complex formation from its function in cell-cell adhesion. J Biol Chem. 1997;272:11856-11862.
    • (1997) J Biol Chem , vol.272 , pp. 11856-11862
    • Finnemann, S.1    Mitrik, I.2    Hess, M.3    Otto, G.4    Wedlich, D.5
  • 37
    • 0000888012 scopus 로고
    • Proteases and antiproteases in the seminiferous tubule
    • Russell LD, Griswold MD, eds. Clearwater, Fla: Cache River Press
    • Fritz IB, Tung PS, Ailenberg M. Proteases and antiproteases in the seminiferous tubule. In: Russell LD, Griswold MD, eds. The Sertoli Cell. Clearwater, Fla: Cache River Press; 1993:305-330.
    • (1993) The Sertoli Cell , pp. 305-330
    • Fritz, I.B.1    Tung, P.S.2    Ailenberg, M.3
  • 38
    • 0030012613 scopus 로고    scopus 로고
    • Association of human protein-tyrosine phosphatase κ with members of the armadillo family
    • Fuchs M, Müller T, Lerch MM, Ullrich A. Association of human protein-tyrosine phosphatase κ with members of the armadillo family. J Biol Chem. 1996;271:16712-16719.
    • (1996) J Biol Chem , vol.271 , pp. 16712-16719
    • Fuchs, M.1    Müller, T.2    Lerch, M.M.3    Ullrich, A.4
  • 39
    • 0028954815 scopus 로고
    • Embryonic axis induction by the armadillo repeat domain of β-catenin: Evidence for intracellular signaling
    • Funayama N, Fagotto F, McCrea P, Gumbiner BM. Embryonic axis induction by the armadillo repeat domain of β-catenin: evidence for intracellular signaling. J Cell Biol. 1995;128:959-968.
    • (1995) J Cell Biol , vol.128 , pp. 959-968
    • Funayama, N.1    Fagotto, F.2    McCrea, P.3    Gumbiner, B.M.4
  • 41
    • 0025234672 scopus 로고
    • Immunofluorescence localization of vinculin in ectoplasmic ("junctional") specializations of rat Sertoli cells
    • Grove BD, Pfeiffer DC, Allen S, Vogl AW. Immunofluorescence localization of vinculin in ectoplasmic ("junctional") specializations of rat Sertoli cells. Am J Anat. 1990;188:44-56.
    • (1990) Am J Anat , vol.188 , pp. 44-56
    • Grove, B.D.1    Pfeiffer, D.C.2    Allen, S.3    Vogl, A.W.4
  • 42
    • 0024325594 scopus 로고
    • Sertoli cell ectoplasmic specialization: A type of actin-associated adhesion junction?
    • Grove BD, Vogl AW. Sertoli cell ectoplasmic specialization: a type of actin-associated adhesion junction? J Cell Sci. 1989;93:309-323.
    • (1989) J Cell Sci , vol.93 , pp. 309-323
    • Grove, B.D.1    Vogl, A.W.2
  • 43
    • 0032725769 scopus 로고    scopus 로고
    • Protein kinase CK2: Evidence for a protein kinase CK2β subunit fraction, devoid of the catalytic CK2α subunit, in mouse brain and testicles
    • Guerra B, Siemer S, Boldyreff B, Issinger OG. Protein kinase CK2: evidence for a protein kinase CK2β subunit fraction, devoid of the catalytic CK2α subunit, in mouse brain and testicles. FEBS Lett. 1999;462:353-357.
    • (1999) FEBS Lett , vol.462 , pp. 353-357
    • Guerra, B.1    Siemer, S.2    Boldyreff, B.3    Issinger, O.G.4
  • 44
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell. 1996;84:345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 45
    • 0036473058 scopus 로고    scopus 로고
    • Gelsolin-evidence for a role in turnover of junction-related actin filaments in Sertoli cells
    • Guttman JA, Janmey P, Vogl AW. Gelsolin-evidence for a role in turnover of junction-related actin filaments in Sertoli cells. J Cell Sci. 2002;115:499-505.
    • (2002) J Cell Sci , vol.115 , pp. 499-505
    • Guttman, J.A.1    Janmey, P.2    Vogl, A.W.3
  • 47
    • 0024500460 scopus 로고
    • Isolation and sequence analysis of a novel human tyrosine kinase gene
    • Hao QL, Heisterkamp N, Groffen J. Isolation and sequence analysis of a novel human tyrosine kinase gene. Mol Cell Biol. 1989;9:1587-1593.
    • (1989) Mol Cell Biol , vol.9 , pp. 1587-1593
    • Hao, Q.L.1    Heisterkamp, N.2    Groffen, J.3
  • 49
    • 0023838733 scopus 로고
    • Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: Its identity in the cadherin gene family
    • Hatta K, Nose A, Nagafuchi A, Takeichi M. Cloning and expression of cDNA encoding a neural calcium-dependent cell adhesion molecule: its identity in the cadherin gene family. J Cell Biol. 1988;106:873-881.
    • (1988) J Cell Biol , vol.106 , pp. 873-881
    • Hatta, K.1    Nose, A.2    Nagafuchi, A.3    Takeichi, M.4
  • 50
    • 0032502669 scopus 로고    scopus 로고
    • The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton
    • Hazan RB, Norton L. The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton. J Biol Chem. 1998;273:9078-9084.
    • (1998) J Biol Chem , vol.273 , pp. 9078-9084
    • Hazan, R.B.1    Norton, L.2
  • 52
    • 0022965058 scopus 로고
    • Hormonal stimulation alters the type of plasminogen activator produced by Sertoli cells
    • Hettle JA, Waller EK, Fritz IB. Hormonal stimulation alters the type of plasminogen activator produced by Sertoli cells. Biol Reprod. 1986;34:895-904.
    • (1986) Biol Reprod , vol.34 , pp. 895-904
    • Hettle, J.A.1    Waller, E.K.2    Fritz, I.B.3
  • 53
    • 0026630994 scopus 로고
    • Identification of a neural α-catenin as a key regulator of cadherin function and multicellular organization
    • Hirano S, Kimoto N, Shimoyama Y, Hirohashi S, Takeichi M. Identification of a neural α-catenin as a key regulator of cadherin function and multicellular organization. Cell. 1992;70:293-301.
    • (1992) Cell , vol.70 , pp. 293-301
    • Hirano, S.1    Kimoto, N.2    Shimoyama, Y.3    Hirohashi, S.4    Takeichi, M.5
  • 54
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton
    • Hülsken J, Birchmeier W, Behrens J. E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton. J Cell Biol. 1994;127:2061-2069.
    • (1994) J Cell Biol , vol.127 , pp. 2061-2069
    • Hülsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 55
    • 0033430117 scopus 로고    scopus 로고
    • Cell adhesion: Old and new questions
    • Hynes RO. Cell adhesion: old and new questions. Trends Cell Biol. 1999;9:M33-M37.
    • (1999) Trends Cell Biol , vol.9
    • Hynes, R.O.1
  • 56
    • 0032822081 scopus 로고    scopus 로고
    • Afadin: A key molecule essential for structural organization of cell-cell junctions of polarized epithelia during embryogenesis
    • Ikeda W, Nakanishi H, Miyoshi J, et al. Afadin: a key molecule essential for structural organization of cell-cell junctions of polarized epithelia during embryogenesis. J Cell Biol. 1999;146:1117-1132.
    • (1999) J Cell Biol , vol.146 , pp. 1117-1132
    • Ikeda, W.1    Nakanishi, H.2    Miyoshi, J.3
  • 57
    • 0019879656 scopus 로고
    • Purification and characterization of tow cyclic AMP-independent casein/glycogen synthase kinases from rat liver cytosol
    • Itarte E, Mor MA, Salavert A, Pena JM, Bertomeu JF, Guinovart JJ. Purification and characterization of tow cyclic AMP-independent casein/glycogen synthase kinases from rat liver cytosol. Biochim Biophys Acta. 1981;658:334-347.
    • (1981) Biochim Biophys Acta , vol.658 , pp. 334-347
    • Itarte, E.1    Mor, M.A.2    Salavert, A.3    Pena, J.M.4    Bertomeu, J.F.5    Guinovart, J.J.6
  • 59
    • 0034982962 scopus 로고    scopus 로고
    • Phosphorylation of the Fas associated factor FAF1 by protein kinase CK2 and identification of serines 289 and 291 as the in vitro phosphorylation sites
    • Jensen HH, Hjerrild M, Guerra B, Larsen MR, Hojrup P, Boldyreff B. Phosphorylation of the Fas associated factor FAF1 by protein kinase CK2 and identification of serines 289 and 291 as the in vitro phosphorylation sites. Int J Biochem Cell Biol. 2001;33:577-589.
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 577-589
    • Jensen, H.H.1    Hjerrild, M.2    Guerra, B.3    Larsen, M.R.4    Hojrup, P.5    Boldyreff, B.6
  • 60
    • 0031729612 scopus 로고    scopus 로고
    • Expression of Src family kinases and their putative substrates in the human preosteoclastic cell line FLG 29.1
    • Jeschke M, Brandi ML, Susa M. Expression of Src family kinases and their putative substrates in the human preosteoclastic cell line FLG 29.1. J Bone Miner Res. 1998;13:1880-1889.
    • (1998) J Bone Miner Res , vol.13 , pp. 1880-1889
    • Jeschke, M.1    Brandi, M.L.2    Susa, M.3
  • 61
    • 0036196242 scopus 로고    scopus 로고
    • Dynamic testicular adhesion junctions are immunologically unique. I. Localization of p120 catenin in rat testis
    • Johnson KJ, Boekelheide K. Dynamic testicular adhesion junctions are immunologically unique. I. Localization of p120 catenin in rat testis. Biol Reprod. 2002a;66:983-991.
    • (2002) Biol Reprod , vol.66 , pp. 983-991
    • Johnson, K.J.1    Boekelheide, K.2
  • 62
    • 0036196243 scopus 로고    scopus 로고
    • Dynamic testicular adhesion junctions are immunologically unique. II. Localization of classic cadherins in rat testis
    • Johnson KJ, Boekelheide K. Dynamic testicular adhesion junctions are immunologically unique. II. Localization of classic cadherins in rat testis. Biol Reprod. 2002b;66:992-1000.
    • (2002) Biol Reprod , vol.66 , pp. 992-1000
    • Johnson, K.J.1    Boekelheide, K.2
  • 63
    • 0034465552 scopus 로고    scopus 로고
    • Multiple cadherin superfamily members with unique expression profiles are produced in rat testis
    • Johnson KJ, Patel SR, Boekelheide K. Multiple cadherin superfamily members with unique expression profiles are produced in rat testis. Endocrinology. 2000;141:675-683.
    • (2000) Endocrinology , vol.141 , pp. 675-683
    • Johnson, K.J.1    Patel, S.R.2    Boekelheide, K.3
  • 64
    • 0029040123 scopus 로고
    • Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex
    • Jou TS, Stewart DB, Stappert J, Nelson WJ, Marrs JA. Genetic and biochemical dissection of protein linkages in the cadherin-catenin complex. Proc Natl Acad Sci USA. 1995;92:5067-5071.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5067-5071
    • Jou, T.S.1    Stewart, D.B.2    Stappert, J.3    Nelson, W.J.4    Marrs, J.A.5
  • 65
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano RL. Signal transduction by cell adhesion receptors and the cytoskeleton: functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu Rev Pharmacol Toxicol. 2002;42:283-323.
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 66
    • 0028918979 scopus 로고
    • Presence of alternative 5′ untranslated sequence and identification of cells expressing ctk transcripts in the brain and testis
    • Kaneko Y, Nonoguchi K, Fukuyama H, et al. Presence of alternative 5′ untranslated sequence and identification of cells expressing ctk transcripts in the brain and testis. Oncogene. 1995;10:945-952.
    • (1995) Oncogene , vol.10 , pp. 945-952
    • Kaneko, Y.1    Nonoguchi, K.2    Fukuyama, H.3
  • 67
    • 0034644776 scopus 로고    scopus 로고
    • Cell volume-dependent phosphorylation of proteins of the cortical cytoskeleton and cell-cell contact sites. The role of Fyn and FER kinases
    • Kapus A, Di Ciano C, Sun J, Zhan X, Kim L, Wong TW, Rotstein OD. Cell volume-dependent phosphorylation of proteins of the cortical cytoskeleton and cell-cell contact sites. The role of Fyn and FER kinases. J Biol Chem. 2000;275:32289-32298.
    • (2000) J Biol Chem , vol.275 , pp. 32289-32298
    • Kapus, A.1    Di Ciano, C.2    Sun, J.3    Zhan, X.4    Kim, L.5    Wong, T.W.6    Rotstein, O.D.7
  • 68
    • 0027185632 scopus 로고
    • From cadherins to catenins: Cytoplasmic protein interactions and regulation of cell adhesion
    • Kemler R. From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion. Trends Genet. 1993;9:317-321.
    • (1993) Trends Genet , vol.9 , pp. 317-321
    • Kemler, R.1
  • 69
    • 0025161207 scopus 로고
    • The testis-specific transcript (ferT) of the tyrosine kinase FER is expressed during spermatogenesis in a stage-specific manner
    • Keshet E, Itin A, Fischman K, Nir U. The testis-specific transcript (ferT) of the tyrosine kinase FER is expressed during spermatogenesis in a stage-specific manner. Mol Cell Biol. 1990;10:5021-5025.
    • (1990) Mol Cell Biol , vol.10 , pp. 5021-5025
    • Keshet, E.1    Itin, A.2    Fischman, K.3    Nir, U.4
  • 70
    • 0034680059 scopus 로고    scopus 로고
    • Cell-cell adhesion-mediated tyrosine phosphorylation of nectin-25, an immunoglobulin-like cell adhesion molecule at adherens junctions
    • Kikyo M, Matozaki T, Kodama A, Kawabe H, Nakanishi H, Takai Y. Cell-cell adhesion-mediated tyrosine phosphorylation of nectin-25, an immunoglobulin-like cell adhesion molecule at adherens junctions. Oncogene. 2000;19:4022-4028.
    • (2000) Oncogene , vol.19 , pp. 4022-4028
    • Kikyo, M.1    Matozaki, T.2    Kodama, A.3    Kawabe, H.4    Nakanishi, H.5    Takai, Y.6
  • 71
    • 0029003669 scopus 로고
    • The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors
    • Kim L, Wong TW. The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors. Mol Cell Biol. 1995;15:4553-4561.
    • (1995) Mol Cell Biol , vol.15 , pp. 4553-4561
    • Kim, L.1    Wong, T.W.2
  • 73
    • 0028979956 scopus 로고
    • Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via α-catenin
    • Knudsen KA, Soler AP, Johnson KR, Wheelock MJ. Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via α-catenin. J Cell Biol. 1995;130:67-77.
    • (1995) J Cell Biol , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 75
    • 0029797378 scopus 로고    scopus 로고
    • Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex
    • Kypta RM, Su H, Reichardt LF. Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex. J Cell Biol. 1996;134:1519-1529.
    • (1996) J Cell Biol , vol.134 , pp. 1519-1529
    • Kypta, R.M.1    Su, H.2    Reichardt, L.F.3
  • 76
    • 0034669042 scopus 로고    scopus 로고
    • Vezatin, a novel transmembrane protein, bridges myosin Vila to the cadherin-catenins complex
    • Küssel-Andermann P, El-Amraoui A, Safieddine S, et al. Vezatin, a novel transmembrane protein, bridges myosin Vila to the cadherin-catenins complex. EMBO J. 2000;19:6020-6029.
    • (2000) EMBO J , vol.19 , pp. 6020-6029
    • Küssel-Andermann, P.1    El-Amraoui, A.2    Safieddine, S.3
  • 77
    • 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. 1994;91:8263-8267.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8263-8267
    • Larue, L.1    Ohsugi, M.2    Hirchenhain, J.3    Kemler, R.4
  • 78
    • 33750690974 scopus 로고    scopus 로고
    • Is the cadherin/catenin complex a functional unit of cell-cell actin-based adherens junction (AJ) in the rat testis?
    • In press
    • Lee NPY, Mruk D, Lee WM, Cheng CY. Is the cadherin/catenin complex a functional unit of cell-cell actin-based adherens junction (AJ) in the rat testis? Biol Reprod. In press.
    • Biol Reprod
    • Lee, N.P.Y.1    Mruk, D.2    Lee, W.M.3    Cheng, C.Y.4
  • 79
    • 0035113674 scopus 로고    scopus 로고
    • Regulation of Sertoli cell myotubularin (rMTM) expression by germ cells in vitro
    • Li JCH, Lee WM, Mruk D, Cheng CY. Regulation of Sertoli cell myotubularin (rMTM) expression by germ cells in vitro. J Androl. 2001a;22:266-277.
    • (2001) J Androl , vol.22 , pp. 266-277
    • Li, J.C.H.1    Lee, W.M.2    Mruk, D.3    Cheng, C.Y.4
  • 80
    • 0034850977 scopus 로고    scopus 로고
    • The inter-Sertoli tight junction permeability barrier is regulated by the interplay of protein phosphatases and kinases: An in vitro study
    • Li JCH, Mruk D, Cheng CY. The inter-Sertoli tight junction permeability barrier is regulated by the interplay of protein phosphatases and kinases: an in vitro study. J Androl. 2001b;22:847-856.
    • (2001) J Androl , vol.22 , pp. 847-856
    • Li, J.C.H.1    Mruk, D.2    Cheng, C.Y.3
  • 81
    • 0033773233 scopus 로고    scopus 로고
    • Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis
    • Li JCH, Samy ET, Grima J, Chung SSW, Mruk D, Lee WM, Silvestrini B, Cheng CY. Rat testicular myotubularin, a protein tyrosine phosphatase expressed by Sertoli and germ cells, is a potential marker for studying cell-cell interactions in the rat testis. J Cell Physiol. 2000;185:366-385.
    • (2000) J Cell Physiol , vol.185 , pp. 366-385
    • Li, J.C.H.1    Samy, E.T.2    Grima, J.3    Chung, S.S.W.4    Mruk, D.5    Lee, W.M.6    Silvestrini, B.7    Cheng, C.Y.8
  • 82
    • 0026497659 scopus 로고
    • Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
    • Lipfert L, Haimovich B, Schaller MD, Cobb BS, Parsons JT, Brugge JS. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J Cell Biol. 1992;119:905-912.
    • (1992) J Cell Biol , vol.119 , pp. 905-912
    • Lipfert, L.1    Haimovich, B.2    Schaller, M.D.3    Cobb, B.S.4    Parsons, J.T.5    Brugge, J.S.6
  • 83
    • 0035047036 scopus 로고    scopus 로고
    • Transforming growth factor-β3 (TGF-β3) perturbs the inter-Sertoli tight junction permeability barrier in vitro possibly mediated its effects on occludin, zonula-occludin-1, and claudin-11
    • Lui WY, Lee WM, Cheng CY. Transforming growth factor-β3 (TGF-β3) perturbs the inter-Sertoli tight junction permeability barrier in vitro possibly mediated its effects on occludin, zonula-occludin-1, and claudin-11. Endocrinology. 2001;142:1865-1877.
    • (2001) Endocrinology , vol.142 , pp. 1865-1877
    • Lui, W.Y.1    Lee, W.M.2    Cheng, C.Y.3
  • 84
    • 0242500358 scopus 로고    scopus 로고
    • Transforming growth factor-β regulates the dynamics of Sertoli cell tight junctions via the p38 mitogen-activated protein kinase pathway
    • In press
    • Lui WY, Lee WM, Cheng CY. Transforming growth factor-β regulates the dynamics of Sertoli cell tight junctions via the p38 mitogen-activated protein kinase pathway. Biol Reprod. In press.
    • Biol Reprod
    • Lui, W.Y.1    Lee, W.M.2    Cheng, C.Y.3
  • 86
    • 14444271574 scopus 로고    scopus 로고
    • Afadin: A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction
    • Mandai K, Nakanishi H, Satoh A, et al. Afadin: a novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction. J Cell Biol. 1997;139:517-528.
    • (1997) J Cell Biol , vol.139 , pp. 517-528
    • Mandai, K.1    Nakanishi, H.2    Satoh, A.3
  • 87
    • 0033535163 scopus 로고    scopus 로고
    • Ponsin/SH3P12: An I-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions
    • Mandai K, Nakanishi H, Satoh A, Takahashi T, Satoh K, Nishioka H, Mizoguchi A, Takai Y. Ponsin/SH3P12: an I-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions. J Cell Biol. 1999;144:1001-1017.
    • (1999) J Cell Biol , vol.144 , pp. 1001-1017
    • Mandai, K.1    Nakanishi, H.2    Satoh, A.3    Takahashi, T.4    Satoh, K.5    Nishioka, H.6    Mizoguchi, A.7    Takai, Y.8
  • 88
    • 0035374609 scopus 로고    scopus 로고
    • The hunting of the Src
    • Martin GS. The hunting of the Src. Nat Rev Mol Cell Biol. 2001;2:467-475.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 467-475
    • Martin, G.S.1
  • 91
    • 0036114872 scopus 로고    scopus 로고
    • Immunhistochemical analysis of β3 integrin (CD61): Expression in pig tissues and human tumors
    • Merono A, Lucena C, Lopez A, Garrido JJ, Perez de LL, Llanes D. Immunhistochemical analysis of β3 integrin (CD61): expression in pig tissues and human tumors. Histol Histopathol. 2002;17:347-352.
    • (2002) Histol Histopathol , vol.17 , pp. 347-352
    • Merono, A.1    Lucena, C.2    Lopez, A.3    Garrido, J.J.4    De Perez, L.L.5    Llanes, D.6
  • 92
    • 0034614555 scopus 로고    scopus 로고
    • Interaction of nectin and afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction
    • Miyahara M, Nakanishi H, Takahashi K, Satoh-Horikawa K, Tachibana K, Takai Y. Interaction of nectin and afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction. J Biol Chem. 2000;275:613-618.
    • (2000) J Biol Chem , vol.275 , pp. 613-618
    • Miyahara, M.1    Nakanishi, H.2    Takahashi, K.3    Satoh-Horikawa, K.4    Tachibana, K.5    Takai, Y.6
  • 94
    • 0037017401 scopus 로고    scopus 로고
    • Nectin: An adhesion molecule involved in formation of synapses
    • Mizoguchi A, Nakanishi H, Kimura K, et al. Nectin: an adhesion molecule involved in formation of synapses. J Cell Biol. 2002;156:555-565.
    • (2002) J Cell Biol , vol.156 , pp. 555-565
    • Mizoguchi, A.1    Nakanishi, H.2    Kimura, K.3
  • 95
    • 0029896440 scopus 로고    scopus 로고
    • Identification of murine p120 isoforms and heterogeneous expression of p 120cas isoforms in human tumor cell lines
    • Mo YY, Reynolds AB. Identification of murine p120 isoforms and heterogeneous expression of p 120cas isoforms in human tumor cell lines. Cancer Res. 1996;56:2633-2640.
    • (1996) Cancer Res , vol.56 , pp. 2633-2640
    • Mo, Y.Y.1    Reynolds, A.B.2
  • 96
    • 0026560656 scopus 로고
    • Molecular cloning and expression of a murine homolog of the human poliovirus receptor gene
    • Morrison ME, Racaniello VR. Molecular cloning and expression of a murine homolog of the human poliovirus receptor gene. J Virol. 1992;66:2807-2813.
    • (1992) J Virol , vol.66 , pp. 2807-2813
    • Morrison, M.E.1    Racaniello, V.R.2
  • 97
    • 0033578753 scopus 로고    scopus 로고
    • Sertolin is a novel gene maker of cell-cell interactions in the rat testis
    • Mruk DD, Cheng CY. Sertolin is a novel gene maker of cell-cell interactions in the rat testis. J Biol Chem. 1999;274:27056-27068.
    • (1999) J Biol Chem , vol.274 , pp. 27056-27068
    • Mruk, D.D.1    Cheng, C.Y.2
  • 98
    • 0002992293 scopus 로고    scopus 로고
    • Sertoli cell proteins in testicular paracriny
    • Jegou B, Pineau C, Saez J, eds. Heidelberg, Germany: Springer-Verlag
    • Mruk DD, Cheng CY. Sertoli cell proteins in testicular paracriny. In: Jegou B, Pineau C, Saez J, eds. Testis, Epididymis and Technologies in the Year 2000. Heidelberg, Germany: Springer-Verlag; 2000:197-228.
    • (2000) Testis, Epididymis and Technologies in the Year 2000 , pp. 197-228
    • Mruk, D.D.1    Cheng, C.Y.2
  • 100
    • 0031424610 scopus 로고    scopus 로고
    • Interactions of proteases and protease inhibitors in Sertoli-germ cell cocultures preceding the formation of specialized Sertoli-germ cell junction in vitro
    • Mruk DD, Zhu LJ, Silvestrini B, Lee WM, Cheng CY. Interactions of proteases and protease inhibitors in Sertoli-germ cell cocultures preceding the formation of specialized Sertoli-germ cell junction in vitro. J Androl. 1997;18:612-622.
    • (1997) J Androl , vol.18 , pp. 612-622
    • Mruk, D.D.1    Zhu, L.J.2    Silvestrini, B.3    Lee, W.M.4    Cheng, C.Y.5
  • 101
    • 0035160160 scopus 로고    scopus 로고
    • Rat seminiferous epithelium contains a unique junction (ectoplasmic specialization) with signaling properties both of cell/cell and cell/matrix junctions
    • Mulholland DJ, Dedhar S, Vogl AW. Rat seminiferous epithelium contains a unique junction (ectoplasmic specialization) with signaling properties both of cell/cell and cell/matrix junctions. Biol Reprod. 2001;64:396-407.
    • (2001) Biol Reprod , vol.64 , pp. 396-407
    • Mulholland, D.J.1    Dedhar, S.2    Vogl, A.W.3
  • 102
    • 0028087729 scopus 로고
    • The roles of catenins in the cadherin-mediated cell adhesion: Functional analysis of E-cadherin-α-catenin fusion molecules
    • Nagafuchi A, Ishihara S, Tsukita S. The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-α- catenin fusion molecules. J Cell Biol. 1994;127:235-245.
    • (1994) J Cell Biol , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 103
    • 0024755646 scopus 로고
    • Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin
    • Nagafuchi A, Takeichi M. Transmembrane control of cadherin-mediated cell adhesion: a 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin. Cell Regul. 1989;1:37-44.
    • (1989) Cell Regul , vol.1 , pp. 37-44
    • Nagafuchi, A.1    Takeichi, M.2
  • 104
    • 0028289669 scopus 로고
    • Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells
    • Nathke IS, Hinck L, Swedlow JR, Papkoff J, Nelson WJ. Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells. J Cell Biol. 1994;125:1341-1352.
    • (1994) J Cell Biol , vol.125 , pp. 1341-1352
    • Nathke, I.S.1    Hinck, L.2    Swedlow, J.R.3    Papkoff, J.4    Nelson, W.J.5
  • 105
    • 0030926845 scopus 로고    scopus 로고
    • Characterization of the interactions of α-catenin with α-actinin and β-catenin/plakoglobin
    • Nieset JE, Redfield AR, Jin F, Knudsen KA, Johnson KR, Wheelock MJ. Characterization of the interactions of α-catenin with α-actinin and β-catenin/plakoglobin. J Cell Sci. 1997;110:1013-1022.
    • (1997) J Cell Sci , vol.110 , pp. 1013-1022
    • Nieset, J.E.1    Redfield, A.R.2    Jin, F.3    Knudsen, K.A.4    Johnson, K.R.5    Wheelock, M.J.6
  • 107
    • 0026355723 scopus 로고
    • CSK: A protein-tyrosine kinase involved in regulation of src family kinases
    • Okada M, Nada S, Yamanashi Y, Yamamoto T, Nakagawa H. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J Biol Chem. 1991;266:24249-24252.
    • (1991) J Biol Chem , vol.266 , pp. 24249-24252
    • Okada, M.1    Nada, S.2    Yamanashi, Y.3    Yamamoto, T.4    Nakagawa, H.5
  • 109
    • 0037046811 scopus 로고    scopus 로고
    • Nectin couples cell-cell adhesion and the actin scaffold at heterotypic testicular junctions
    • Ozaki-Kuroda K, Nakanishi H, Ohta H, et al. Nectin couples cell-cell adhesion and the actin scaffold at heterotypic testicular junctions. Curr Biol. 2002;12:1145-1150.
    • (2002) Curr Biol , vol.12 , pp. 1145-1150
    • Ozaki-Kuroda, K.1    Nakanishi, H.2    Ohta, H.3
  • 110
    • 0024451982 scopus 로고
    • The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species
    • Ozawa M, Baribault H, Kemler R. The cytoplasmic domain of the cell adhesion molecule uvomorulin associates with three independent proteins structurally related in different species. EMBO J. 1989;8:1711-1717.
    • (1989) EMBO J , vol.8 , pp. 1711-1717
    • Ozawa, M.1    Baribault, H.2    Kemler, R.3
  • 111
    • 0032513297 scopus 로고    scopus 로고
    • Altered cell adhesion activity by pervanadate due to the dissociation of α-catenin from the E-cadherin-catenin complex
    • Ozawa M, Kemler R. Altered cell adhesion activity by pervanadate due to the dissociation of α-catenin from the E-cadherin-catenin complex. J Biol Chem. 1998;273:6166-6170.
    • (1998) J Biol Chem , vol.273 , pp. 6166-6170
    • Ozawa, M.1    Kemler, R.2
  • 112
    • 0026492397 scopus 로고
    • Distribution of β1 integrin subunit in rat seminiferous epithelium
    • Palombi F, Salanova M, Tarone G, Farini D, Stefanini M. Distribution of β1 integrin subunit in rat seminiferous epithelium. Biol Reprod. 1992;47:1173-1182.
    • (1992) Biol Reprod , vol.47 , pp. 1173-1182
    • Palombi, F.1    Salanova, M.2    Tarone, G.3    Farini, D.4    Stefanini, M.5
  • 113
    • 0019848801 scopus 로고
    • Cellular homologue (c-src) of the transforming gene of Rous sarcoma virus: Isolation, mapping, and transcriptional analysis of c-src and flanking regions
    • Parker RC, Varmus HF, Bishop JM. Cellular homologue (c-src) of the transforming gene of Rous sarcoma virus: isolation, mapping, and transcriptional analysis of c-src and flanking regions. Proc Natl Acad Sci USA. 1981;78:5842-8546.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 5842-8546
    • Parker, R.C.1    Varmus, H.F.2    Bishop, J.M.3
  • 114
    • 0024378678 scopus 로고
    • The FER gene is evolutionarily conserved and encodes a widely expressed member of the FPS/FES protein-tyrosine kinase family
    • Pawson T, Letwin K, Lee TL, Hao QL, Heisterkamp N, Groffen J. The FER gene is evolutionarily conserved and encodes a widely expressed member of the FPS/FES protein-tyrosine kinase family. Mol Cell Biol. 1989;9:5722-5725.
    • (1989) Mol Cell Biol , vol.9 , pp. 5722-5725
    • Pawson, T.1    Letwin, K.2    Lee, T.L.3    Hao, Q.L.4    Heisterkamp, N.5    Groffen, J.6
  • 115
    • 0345126549 scopus 로고
    • Characterization of antigens recognized by monoclonal and polyclonal antibodies directed against uvomorulin
    • Peyrieras N, Louvard D, Jacob F. Characterization of antigens recognized by monoclonal and polyclonal antibodies directed against uvomorulin. Proc Natl Acad Sci USA. 1985;82:8067-8071.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8067-8071
    • Peyrieras, N.1    Louvard, D.2    Jacob, F.3
  • 116
    • 0025944757 scopus 로고
    • Evidence that vinculin is co-distributed with actin bundles in ectoplasmic ("junctional") specializations of mammalian Sertoli cells
    • Pfeiffer DC, Vogl AW. Evidence that vinculin is co-distributed with actin bundles in ectoplasmic ("junctional") specializations of mammalian Sertoli cells. Anat Rec. 1991;231:89-100.
    • (1991) Anat Rec , vol.231 , pp. 89-100
    • Pfeiffer, D.C.1    Vogl, A.W.2
  • 118
    • 0037166245 scopus 로고    scopus 로고
    • Biochemical and structural definition of the I-afadin- and actin-binding sites of α-catenin
    • Pokutta S, Drees F, Takai Y, Nelson WJ, Weis WI. Biochemical and structural definition of the I-afadin- and actin-binding sites of α-catenin. J Biol Chem. 2002;277:18868-18874.
    • (2002) J Biol Chem , vol.277 , pp. 18868-18874
    • Pokutta, S.1    Drees, F.2    Takai, Y.3    Nelson, W.J.4    Weis, W.I.5
  • 119
    • 0032792155 scopus 로고    scopus 로고
    • The cadherin-catenin system: Implications for growth and differentiation of endocrine tissues
    • Pötter E, Bergwitz C, Brabant G. The cadherin-catenin system: implications for growth and differentiation of endocrine tissues. Endocr Rev. 1999;20:207-239.
    • (1999) Endocr Rev , vol.20 , pp. 207-239
    • Pötter, E.1    Bergwitz, C.2    Brabant, G.3
  • 120
    • 0031283128 scopus 로고    scopus 로고
    • The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures
    • Rabinovitz I, Mercurio AM. The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures. J Cell Biol. 1997;139:1873-1884.
    • (1997) J Cell Biol , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 122
    • 0028019276 scopus 로고
    • Identification of a new catenin: The tyrosine kinase substrate p120cas associates with E-cadherin complexes
    • Reynolds AB, Daniel J, McCrea PD, Wheelock MJ, Wu J, Zhang Z. Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes. Mol Cell Biol. 1994;14:8333-8342.
    • (1994) Mol Cell Biol , vol.14 , pp. 8333-8342
    • Reynolds, A.B.1    Daniel, J.2    McCrea, P.D.3    Wheelock, M.J.4    Wu, J.5    Zhang, Z.6
  • 123
    • 0026441267 scopus 로고
    • p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors β-catenin, plakoglobin and armadillo
    • Reynolds AB, Herbert L, Cleveland JL, Berg ST, Gaut JR. p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors β-catenin, plakoglobin and armadillo. Oncogene. 1992;7:2439-2445.
    • (1992) Oncogene , vol.7 , pp. 2439-2445
    • Reynolds, A.B.1    Herbert, L.2    Cleveland, J.L.3    Berg, S.T.4    Gaut, J.R.5
  • 124
    • 0028821380 scopus 로고
    • A targeted mutation in the mouse E-cadherin gene results in defective preimplantation development
    • Riethmacher D, Brinkmann V, Birchmeier C. A targeted mutation in the mouse E-cadherin gene results in defective preimplantation development. Proc Natl Acad Sci USA. 1995;92:855-859.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 855-859
    • Riethmacher, D.1    Brinkmann, V.2    Birchmeier, C.3
  • 125
    • 0028981208 scopus 로고
    • α1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • Rimm DL, Koslov ER, Kebriaei P, Cianci CD, Morrow JS. α1(E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc Natl Acad Sci USA. 1995;92:8813-8817.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 126
    • 0026410424 scopus 로고
    • The structure of the gene coding for the mouse cell adhesion molecule uvomorulin
    • Ringwald M, Baribault H, Schmidt C, Kemler R. The structure of the gene coding for the mouse cell adhesion molecule uvomorulin. Nucleic Acids Res. 1991;19:6533-6539.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6533-6539
    • Ringwald, M.1    Baribault, H.2    Schmidt, C.3    Kemler, R.4
  • 128
  • 129
    • 0033978582 scopus 로고    scopus 로고
    • Cadherins: Crucial regulators of structure and function in reproductive tissues
    • Rowlands TM, Symonds JM, Farookhi R, Blaschuk OW. Cadherins: crucial regulators of structure and function in reproductive tissues. Rev Reprod. 2000;5:53-61.
    • (2000) Rev Reprod , vol.5 , pp. 53-61
    • Rowlands, T.M.1    Symonds, J.M.2    Farookhi, R.3    Blaschuk, O.W.4
  • 130
    • 0017709496 scopus 로고
    • Observations on rat Sertoli ectoplasmic ("junctional") specializations in their association with germ cells of the rat testis
    • Russell L. Observations on rat Sertoli ectoplasmic (" junctional") specializations in their association with germ cells of the rat testis. Tissue Cell. 1977a;9:475-498.
    • (1977) Tissue Cell , vol.9 , pp. 475-498
    • Russell, L.1
  • 131
    • 0017578731 scopus 로고
    • Movement of spermatocytes from the basal to the adluminal compartment of the rat testis
    • Russell LD. Movement of spermatocytes from the basal to the adluminal compartment of the rat testis. Am J Anal. 1977b;148:313-328.
    • (1977) Am J Anal , vol.148 , pp. 313-328
    • Russell, L.D.1
  • 132
    • 0019119141 scopus 로고
    • Sertoli-germ cell interactions: A review
    • Russell LD. Sertoli-germ cell interactions: a review. Gamete Res. 1980;3:179-202.
    • (1980) Gamete Res , vol.3 , pp. 179-202
    • Russell, L.D.1
  • 133
    • 0002546050 scopus 로고
    • Morphological and functional evidence for Sertoli-germ cell relationships
    • Russell LD, Griswold MD, eds. Clearwater, Fla: Cache River Press
    • Russell LD. Morphological and functional evidence for Sertoli-germ cell relationships. In: Russell LD, Griswold MD, eds. The Sertoli Cell. Clearwater, Fla: Cache River Press; 1993:365-390.
    • (1993) The Sertoli Cell , pp. 365-390
    • Russell, L.D.1
  • 134
    • 0017082439 scopus 로고
    • Anchoring device between Sertoli cells and late spermatids in rat seminiferous tubules
    • Russell L, Clermont Y. Anchoring device between Sertoli cells and late spermatids in rat seminiferous tubules. Anat Rec. 1976;185:259-278.
    • (1976) Anat Rec , vol.185 , pp. 259-278
    • Russell, L.1    Clermont, Y.2
  • 136
    • 0010456037 scopus 로고    scopus 로고
    • Localization of actinin in the rat testis: Preliminary observations
    • Parvinen M, Huhtaniemi I, Pelliniemi LJ, eds. New York: Raven Press
    • Russell LD, Goh JC. Localization of actinin in the rat testis: preliminary observations. In: Parvinen M, Huhtaniemi I, Pelliniemi LJ, eds. Development and Function of the Reproductive Organs, VII Ares-Serono Symposia Series. New York: Raven Press; 1998:237-244.
    • (1998) Development and Function of the Reproductive Organs, VII Ares-Serono Symposia Series , pp. 237-244
    • Russell, L.D.1    Goh, J.C.2
  • 137
    • 0021892796 scopus 로고
    • Sertoli cell junctions: Morphological and functional correlates
    • Russell LD, Peterson RN. Sertoli cell junctions: morphological and functional correlates. Int Rev Cytol. 1985;94:177-211.
    • (1985) Int Rev Cytol , vol.94 , pp. 177-211
    • Russell, L.D.1    Peterson, R.N.2
  • 138
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai R, Iwamatsu A, Hirano N, Ogawa S, Tanaka T, Mano H, Yazaki Y, Hirai H. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 1994;13:3748-3756.
    • (1994) EMBO J , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 139
    • 0028984244 scopus 로고
    • Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium
    • Salanova M, Stefanini M, de Curtis I, Palombi F. Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium. Biol Reprod. 1995;52:79-87.
    • (1995) Biol Reprod , vol.52 , pp. 79-87
    • Salanova, M.1    Stefanini, M.2    De Curtis, I.3    Palombi, F.4
  • 140
    • 0033918217 scopus 로고    scopus 로고
    • Immunofluorescence distribution of actin-associated proteins in human seminiferous tubules of adolescent testes, normal and pathologic
    • Santoro G, Romeo C, Impellizzeri O, Cutroneo G, Micali A, Trimarchi F, Gentile C. Immunofluorescence distribution of actin-associated proteins in human seminiferous tubules of adolescent testes, normal and pathologic. J Endocrinol Invest. 2000;23:369-375.
    • (2000) J Endocrinol Invest , vol.23 , pp. 369-375
    • Santoro, G.1    Romeo, C.2    Impellizzeri, O.3    Cutroneo, G.4    Micali, A.5    Trimarchi, F.6    Gentile, C.7
  • 141
    • 0034616002 scopus 로고    scopus 로고
    • Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities
    • Satoh-Horikawa K, Nakanishi H, Takahashi K, Miyahara M, Nishimura M, Tachibana K, Mizoguchi A, Takai Y. Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities. J Biol Chem. 2000;275:10291-10299.
    • (2000) J Biol Chem , vol.275 , pp. 10291-10299
    • Satoh-Horikawa, K.1    Nakanishi, H.2    Takahashi, K.3    Miyahara, M.4    Nishimura, M.5    Tachibana, K.6    Mizoguchi, A.7    Takai, Y.8
  • 142
    • 0027424784 scopus 로고
    • Evidence of β1 integrins and fibronectin on spermatogenic cells in human testis
    • Schaller J, Glander HJ, Dethloff J. Evidence of β1 integrins and fibronectin on spermatogenic cells in human testis. Hum Reprod. 1993;8:1873-1878.
    • (1993) Hum Reprod , vol.8 , pp. 1873-1878
    • Schaller, J.1    Glander, H.J.2    Dethloff, J.3
  • 143
  • 144
    • 0027332373 scopus 로고
    • Regulation of αβ1 integrin laminin receptor function by the cytoplasmic domain of the 06 subunit
    • Shaw LM, Mercurio AM. Regulation of αβ1 integrin laminin receptor function by the cytoplasmic domain of the 06 subunit. J Cell Biol. 1993;123:1017-1025.
    • (1993) J Cell Biol , vol.123 , pp. 1017-1025
    • Shaw, L.M.1    Mercurio, A.M.2
  • 145
    • 84907115825 scopus 로고
    • Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells
    • Shibamoto S, Hayakawa M, Takeuchi K, et al. Tyrosine phosphorylation of β-catenin and plakoglobin enhanced by hepatocyte growth factor and epidermal growth factor in human carcinoma cells. Cell Adhes Commun. 1994;1:295-305.
    • (1994) Cell Adhes Commun , vol.1 , pp. 295-305
    • Shibamoto, S.1    Hayakawa, M.2    Takeuchi, K.3
  • 146
    • 0038070531 scopus 로고    scopus 로고
    • The adhering junction dynamics in the testis are regulated by an interplay of β1-integrin and the focal adhesion complex (FAC)-associated proteins
    • In press
    • Siu MKY, Mruk DD, Lee WM, Cheng CY. The adhering junction dynamics in the testis are regulated by an interplay of β1-integrin and the focal adhesion complex (FAC)-associated proteins. Endocrinology In press.
    • Endocrinology
    • Siu, M.K.Y.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 147
    • 0029887541 scopus 로고    scopus 로고
    • Intestinal HT-29 cells with dysfunction of E-cadherin show increased pp60src activity and tyrosine phosphorylation of p120-catenin
    • Skoudy A, Llosas MD, Garcia de Herreros A. Intestinal HT-29 cells with dysfunction of E-cadherin show increased pp60src activity and tyrosine phosphorylation of p120-catenin. Biochem J. 1996;317:279-284.
    • (1996) Biochem J , vol.317 , pp. 279-284
    • Skoudy, A.1    Llosas, M.D.2    Garcia De Herreros, A.3
  • 148
    • 0033600568 scopus 로고    scopus 로고
    • Domain interactions in protein tyrosine kinase Csk
    • Sondhi D, Cole PA. Domain interactions in protein tyrosine kinase Csk. Biochemistry. 1999;38:11147-11155.
    • (1999) Biochemistry , vol.38 , pp. 11147-11155
    • Sondhi, D.1    Cole, P.A.2
  • 149
    • 0027938682 scopus 로고
    • A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated
    • Stappert J, Kemler R. A short core region of E-cadherin is essential for catenin binding and is highly phosphorylated. Cell Adhes Commun. 1994;2:319-327.
    • (1994) Cell Adhes Commun , vol.2 , pp. 319-327
    • Stappert, J.1    Kemler, R.2
  • 151
    • 0034605062 scopus 로고    scopus 로고
    • Two cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domain-associated proteins
    • Tachibana K, Nakanishi H, Mandai K, et al. Two cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domain-associated proteins. J Cell Biol. 2000;150:1161-1176.
    • (2000) J Cell Biol , vol.150 , pp. 1161-1176
    • Tachibana, K.1    Nakanishi, H.2    Mandai, K.3
  • 152
    • 0031841622 scopus 로고    scopus 로고
    • Cell adhesion and reproduction. An overview
    • Taga M, Suginami H. Cell adhesion and reproduction. An overview. Horm Res. 1998;50:2-6.
    • (1998) Horm Res , vol.50 , pp. 2-6
    • Taga, M.1    Suginami, H.2
  • 153
    • 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, et al. 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. 1999;145:539-549.
    • (1999) J Cell Biol , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3
  • 154
    • 0025325167 scopus 로고
    • Cadherins: A molecular family important in selective cell-cell adhesion
    • Takeichi M. Cadherins: a molecular family important in selective cell-cell adhesion. Annu Rev Biochem. 1990;59:237-252.
    • (1990) Annu Rev Biochem , vol.59 , pp. 237-252
    • Takeichi, M.1
  • 155
    • 0029160437 scopus 로고
    • Morphogenetic roles of classical cadherins
    • Takeichi M. Morphogenetic roles of classical cadherins. Curr Opin Cell Biol. 1995;7:619-627.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 157
    • 0033214110 scopus 로고    scopus 로고
    • Morphogenesis of the acrosome during final steps of rat spermiogenesis with special reference to tubulobulbar complexes
    • Tanii I, Yoshinaga K, Toshimori K. Morphogenesis of the acrosome during final steps of rat spermiogenesis with special reference to tubulobulbar complexes. Anat Rec. 1999;256:195-201.
    • (1999) Anat Rec , vol.256 , pp. 195-201
    • Tanii, I.1    Yoshinaga, K.2    Toshimori, K.3
  • 158
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas SM, Brugge JS. Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol. 1997;12:513-609.
    • (1997) Annu Rev Cell Dev Biol , vol.12 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 159
    • 0032698223 scopus 로고    scopus 로고
    • Expression of protein tyrosine phosphatase PTP-RL10 and its isoform in the mouse testis
    • Tokuchi H, Higashitsuji H, Nishiyama H, et al. Expression of protein tyrosine phosphatase PTP-RL10 and its isoform in the mouse testis. Int J Urol. 1999;6:572-577.
    • (1999) Int J Urol , vol.6 , pp. 572-577
    • Tokuchi, H.1    Higashitsuji, H.2    Nishiyama, H.3
  • 162
    • 0024499823 scopus 로고
    • Regulation of urokinase- and tissue-type plasminogen activator gene expression in the rat seminiferous epithelium
    • Vihko KK, Penttila TL, Parvinen M, Belin D. Regulation of urokinase- and tissue-type plasminogen activator gene expression in the rat seminiferous epithelium. Mol Endocrinol. 1989;3:52-59.
    • (1989) Mol Endocrinol , vol.3 , pp. 52-59
    • Vihko, K.K.1    Penttila, T.L.2    Parvinen, M.3    Belin, D.4
  • 163
    • 0034115882 scopus 로고    scopus 로고
    • Unique and multifunctional adhesion junctions in the testis: Ectoplasmic specializations
    • Vogl AW, Pfeiffer DC, Mulholland D, Kimel G, Guttman J. Unique and multifunctional adhesion junctions in the testis: ectoplasmic specializations. Arch Histol Cytol. 2000;63:1-15.
    • (2000) Arch Histol Cytol , vol.63 , pp. 1-15
    • Vogl, A.W.1    Pfeiffer, D.C.2    Mulholland, D.3    Kimel, G.4    Guttman, J.5
  • 164
    • 0035916292 scopus 로고    scopus 로고
    • Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail
    • Wang D, Huang XY, Cole PA. Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail. Biochemistry. 2001;40:2004-2010.
    • (2001) Biochemistry , vol.40 , pp. 2004-2010
    • Wang, D.1    Huang, X.Y.2    Cole, P.A.3
  • 165
    • 0028129695 scopus 로고
    • Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin-catenin adhesion system in a dispersed carcinoma line
    • Watabe M, Nagafuchi A, Tsukita S, Takeichi M. Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin-catenin adhesion system in a dispersed carcinoma line. J Cell Biol. 1994;127:247-256.
    • (1994) J Cell Biol , vol.127 , pp. 247-256
    • Watabe, M.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4
  • 166
    • 0028972871 scopus 로고
    • Investigation of the role of β1 integrins in cell-cell adhesion
    • Weitzman JB, Chen A, Hemler ME. Investigation of the role of β1 integrins in cell-cell adhesion. J Cell Sci. 1995;108:3635-3644.
    • (1995) J Cell Sci , vol.108 , pp. 3635-3644
    • Weitzman, J.B.1    Chen, A.2    Hemler, M.E.3
  • 167
    • 0020082249 scopus 로고
    • High-affinity interaction of vinculin with actin filaments in vitro
    • Wilkins JA, Lin S. High-affinity interaction of vinculin with actin filaments in vitro. Cell. 1982;28:83-90.
    • (1982) Cell , vol.28 , pp. 83-90
    • Wilkins, J.A.1    Lin, S.2
  • 168
    • 0032932582 scopus 로고    scopus 로고
    • Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat
    • Wine RN, Chapin RE. Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat. J Androl. 1999;20:198-213.
    • (1999) J Androl , vol.20 , pp. 198-213
    • Wine, R.N.1    Chapin, R.E.2
  • 169
    • 0034652234 scopus 로고    scopus 로고
    • Vascular endothelial growth factor stimulates dephosphorylation of the catenins p120 and p100 in endothelial cells
    • Wong EYM, Morgan L, Smales C, Lang P, Gubby SE, Stabbon JM. Vascular endothelial growth factor stimulates dephosphorylation of the catenins p120 and p100 in endothelial cells. Biochem J. 2000;346:209-216.
    • (2000) Biochem J , vol.346 , pp. 209-216
    • Wong, E.Y.M.1    Morgan, L.2    Smales, C.3    Lang, P.4    Gubby, S.E.5    Stabbon, J.M.6
  • 170
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap AS, Brieher WM, Gumbiner BM. Molecular and functional analysis of cadherin-based adherens junctions. Annu Rev Cell Dev Biol. 1997;13:119-146.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 119-146
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 172
    • 0035172522 scopus 로고    scopus 로고
    • α-catenin-independent recruitment of ZO-1 to nectin-based cell-cell adhesion sites through afadin
    • Yokoyama S, Tachibana K, Nakanishi H, et al. α-catenin-independent recruitment of ZO-1 to nectin-based cell-cell adhesion sites through afadin. Mol Biol Cell. 2001;12:1595-1609.
    • (2001) Mol Biol Cell , vol.12 , pp. 1595-1609
    • Yokoyama, S.1    Tachibana, K.2    Nakanishi, H.3


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