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Volumn 51, Issue 3, 2000, Pages 280-301

Integrins as receptors for laminins

Author keywords

Epithelial cell adhesion; Laminin; Myoblast differentiation

Indexed keywords

BUILDINGS; CELL ADHESION; CELL PROLIFERATION;

EID: 0034333146     PISSN: 1059910X     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O     Document Type: Review
Times cited : (312)

References (279)
  • 1
    • 0024337558 scopus 로고
    • Identification and characterization of cell-substratum adhesion receptors on cultured human endothelial cells
    • Albelda SM, Daise M, Levine EM, Buck CA. 1989. Identification and characterization of cell-substratum adhesion receptors on cultured human endothelial cells. J Clin Invest 83:1992-2002.
    • (1989) J Clin Invest , vol.83 , pp. 1992-2002
    • Albelda, S.M.1    Daise, M.2    Levine, E.M.3    Buck, C.A.4
  • 2
    • 0032734174 scopus 로고    scopus 로고
    • Cell adhesion molecules, signal transduction and cell growth
    • Aplin AE, Howe AK, Juliano R. 1999. Cell adhesion molecules, signal transduction and cell growth. Curr Opin Cell Biol 11:737-744.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 737-744
    • Aplin, A.E.1    Howe, A.K.2    Juliano, R.3
  • 3
    • 0031030316 scopus 로고    scopus 로고
    • Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the α6β4 integrin
    • Ardini E, Tagliabue E, Magnifico A, Buto S, Castronovo V, Colnaghi MI, Menard S. 1997. Co-regulation and physical association of the 67-kDa monomeric laminin receptor and the α6β4 integrin. J Biol Chem 272:2342-2345.
    • (1997) J Biol Chem , vol.272 , pp. 2342-2345
    • Ardini, E.1    Tagliabue, E.2    Magnifico, A.3    Buto, S.4    Castronovo, V.5    Colnaghi, M.I.6    Menard, S.7
  • 5
    • 0027933266 scopus 로고
    • Transformation and tumor progression are frequently associated with expression of the α3β1 heterodimer in solid tumors
    • Bartolazzi A, Cerboni C, Nicotra MR, Mottolese M, Bigotti A, Natali PG. 1994. Transformation and tumor progression are frequently associated with expression of the α3β1 heterodimer in solid tumors. Int J Cancer 58:488-491.
    • (1994) Int J Cancer , vol.58 , pp. 488-491
    • Bartolazzi, A.1    Cerboni, C.2    Nicotra, M.R.3    Mottolese, M.4    Bigotti, A.5    Natali, P.G.6
  • 6
    • 0032521681 scopus 로고    scopus 로고
    • Knockout and knockin of the β1 exon D define distinct roles for integrin splice variants in heart function and embryonic development
    • Baudoin C, Goumans MJ, Mummery C, Sonnenberg A. 1998. Knockout and knockin of the β1 exon D define distinct roles for integrin splice variants in heart function and embryonic development. Genes Dev 12:1202-1216.
    • (1998) Genes Dev , vol.12 , pp. 1202-1216
    • Baudoin, C.1    Goumans, M.J.2    Mummery, C.3    Sonnenberg, A.4
  • 7
    • 0026471680 scopus 로고
    • In vitro model of angiogenesis using a human endothelium-derived permanent cell line: Contributions of induced gene expression, G-proteins and integrins
    • Bauer J, Margolis M, Schreiner C, Edgell CJ, Azizkhan J, Lazarowski E, Juliano RL. 1992. In vitro model of angiogenesis using a human endothelium-derived permanent cell line: contributions of induced gene expression, G-proteins and integrins. J Cell Physiol 153:437-449.
    • (1992) J Cell Physiol , vol.153 , pp. 437-449
    • Bauer, J.1    Margolis, M.2    Schreiner, C.3    Edgell, C.J.4    Azizkhan, J.5    Lazarowski, E.6    Juliano, R.L.7
  • 8
    • 0028804279 scopus 로고
    • Differential display and integrin α6 messenger RNA overexpression in hepatocellular carcinoma
    • Begum NA, Mori M, Matsumata T, Takenaka K, Sugimachi K, Barnard GF. 1995. Differential display and integrin α6 messenger RNA overexpression in hepatocellular carcinoma. Hepatology 22:1447-1455.
    • (1995) Hepatology , vol.22 , pp. 1447-1455
    • Begum, N.A.1    Mori, M.2    Matsumata, T.3    Takenaka, K.4    Sugimachi, K.5    Barnard, G.F.6
  • 9
    • 0032510837 scopus 로고    scopus 로고
    • β1D integrin inhibits cell cycle progression in normal myoblasts and fibroblasts
    • Belkin AM, Retta SF. 1998. β1D integrin inhibits cell cycle progression in normal myoblasts and fibroblasts. J Biol Chem 273:15234-15240.
    • (1998) J Biol Chem , vol.273 , pp. 15234-15240
    • Belkin, A.M.1    Retta, S.F.2
  • 10
    • 0029671374 scopus 로고    scopus 로고
    • β1D integrin displaces the β1A isoform in striated muscles: Localization at junctional structures and signaling potential in non-muscle cells
    • Belkin AM, Zhidkova NI, Balzac F, Altruda F, Tomatis D, Maier A, Tarone G, Koteliansky VE, Burridge K. 1996. β1D integrin displaces the β1A isoform in striated muscles: localization at junctional structures and signaling potential in non-muscle cells. J Cell Biol 132:211-226.
    • (1996) J Cell Biol , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 12
    • 0033606802 scopus 로고    scopus 로고
    • Characterization of integrin-tetraspanin adhesion complexes: Role of tetraspanins in integrin signaling
    • Berditchevski F, Odintsova E. 1999. Characterization of integrin-tetraspanin adhesion complexes: role of tetraspanins in integrin signaling. J Cell Biol 146:477-492.
    • (1999) J Cell Biol , vol.146 , pp. 477-492
    • Berditchevski, F.1    Odintsova, E.2
  • 13
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
    • Berditchevski F, Zutter MM, Hemler ME. 1996. Characterization of novel complexes on the surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol Biol Cell 7:1193-1207.
    • (1996) Mol Biol Cell , vol.7 , pp. 1193-1207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 16
    • 0031713433 scopus 로고    scopus 로고
    • Extracellular matrix signaling: Integration of form and function in normal and malignant cells
    • Boudreau N, Bissell MJ. 1998. Extracellular matrix signaling: integration of form and function in normal and malignant cells. Curr Opin Cell Biol 10:640-646.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 640-646
    • Boudreau, N.1    Bissell, M.J.2
  • 19
    • 0028246730 scopus 로고
    • Neural crest cell formation and migration in the developing embryo
    • Bronner-Fraser M. 1994. Neural crest cell formation and migration in the developing embryo. FASEB J 8:699-706.
    • (1994) FASEB J , vol.8 , pp. 699-706
    • Bronner-Fraser, M.1
  • 20
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • Brooks PC, Clark RA, Cheresh DA. 1994. Requirement of vascular integrin αvβ3 for angiogenesis. Science 264:569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 21
    • 0027619559 scopus 로고
    • Integrins hold Drosophila together
    • Brown NH. 1993. Integrins hold Drosophila together. Bioessays 15: 383-390.
    • (1993) Bioessays , vol.15 , pp. 383-390
    • Brown, N.H.1
  • 23
    • 0032538841 scopus 로고    scopus 로고
    • A functional role for specific spliced variants of the α7β1 integrin in acetylcholine receptor clustering
    • Burkin DJ, Gu M, Hodges BL, Campanelli JT, Kaufman SJ. 1998. A functional role for specific spliced variants of the α7β1 integrin in acetylcholine receptor clustering. J Cell Biol 143:1067-1075.
    • (1998) J Cell Biol , vol.143 , pp. 1067-1075
    • Burkin, D.J.1    Gu, M.2    Hodges, B.L.3    Campanelli, J.T.4    Kaufman, S.J.5
  • 25
    • 0030612224 scopus 로고    scopus 로고
    • The integrin α1 A-domain is a ligand binding site for collagens and laminin
    • Calderwood DA, Tuckwell DS, Eble J, Kuhn K, Humphries MJ. 1997. The integrin α1 A-domain is a ligand binding site for collagens and laminin. J Biol Chem 272:12311-12317.
    • (1997) J Biol Chem , vol.272 , pp. 12311-12317
    • Calderwood, D.A.1    Tuckwell, D.S.2    Eble, J.3    Kuhn, K.4    Humphries, M.J.5
  • 26
    • 0025999292 scopus 로고
    • Relationship between neuronal migration and cell-substratum adhesion: Laminin and merosin promote olfactory neuronal migration but are anti-adhesive
    • Calof AL, Lander AD. 1991. Relationship between neuronal migration and cell-substratum adhesion: laminin and merosin promote olfactory neuronal migration but are anti-adhesive. J Cell Biol 115:779-794.
    • (1991) J Cell Biol , vol.115 , pp. 779-794
    • Calof, A.L.1    Lander, A.D.2
  • 27
    • 0027991270 scopus 로고
    • Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin
    • Calof AL, Campanero MR, O'Rear JJ, Yurchenco PD, Lander AD. 1994. Domain-specific activation of neuronal migration and neurite outgrowth-promoting activities of laminin. Neuron 13:117-130.
    • (1994) Neuron , vol.13 , pp. 117-130
    • Calof, A.L.1    Campanero, M.R.2    O'Rear, J.J.3    Yurchenco, P.D.4    Lander, A.D.5
  • 28
    • 0033567948 scopus 로고    scopus 로고
    • The nonintegrin laminin binding protein (p67 LBP) is expressed on a subset of activated human T lymphocytes and, together with the integrin very late activation antigen-6, mediates avid cellular adherence to laminin
    • Canfield SM, Khakoo AY. 1999. The nonintegrin laminin binding protein (p67 LBP) is expressed on a subset of activated human T lymphocytes and, together with the integrin very late activation antigen-6, mediates avid cellular adherence to laminin. J Immunol 163:3430-3440.
    • (1999) J Immunol , vol.163 , pp. 3430-3440
    • Canfield, S.M.1    Khakoo, A.Y.2
  • 30
    • 0028575901 scopus 로고
    • Selective increase in the binding of the α1β1 integrin for collagen type IV during neurite outgrowth of human neuroblastoma TR 14 cells
    • Carmeliet G, Himpens B, Cassiman JJ. 1994. Selective increase in the binding of the α1β1 integrin for collagen type IV during neurite outgrowth of human neuroblastoma TR 14 cells. J Cell Sci 107: 3379-3392.
    • (1994) J Cell Sci , vol.107 , pp. 3379-3392
    • Carmeliet, G.1    Himpens, B.2    Cassiman, J.J.3
  • 31
    • 0025806141 scopus 로고
    • In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells
    • Chan BM, Matsuura N, Takada Y, Zetter BR, Hemler ME. 1991. In vitro and in vivo consequences of VLA-2 expression on rhabdomyosarcoma cells. Science 251:1600-1602.
    • (1991) Science , vol.251 , pp. 1600-1602
    • Chan, B.M.1    Matsuura, N.2    Takada, Y.3    Zetter, B.R.4    Hemler, M.E.5
  • 32
    • 0028983544 scopus 로고
    • α3β1 and α6β1 integrins mediate laminin/merosin binding and function as costimulatory molecules for human thymocyte proliferation
    • Chang AC, Salomon DR, Wadsworth S, Hong MJ, Mojcik CF, Otto S, Shevach EM, Coligan JE. 1995. α3β1 and α6β1 integrins mediate laminin/merosin binding and function as costimulatory molecules for human thymocyte proliferation. J Immunol 154:500-510.
    • (1995) J Immunol , vol.154 , pp. 500-510
    • Chang, A.C.1    Salomon, D.R.2    Wadsworth, S.3    Hong, M.J.4    Mojcik, C.F.5    Otto, S.6    Shevach, E.M.7    Coligan, J.E.8
  • 33
    • 0023294574 scopus 로고
    • Extension of neurites on axons is impaired by antibodies against specific neural cell surface glycoproteins
    • Chang S, Rathjen FG, Raper JA. 1987. Extension of neurites on axons is impaired by antibodies against specific neural cell surface glycoproteins. J Cell Biol 104:355-362.
    • (1987) J Cell Biol , vol.104 , pp. 355-362
    • Chang, S.1    Rathjen, F.G.2    Raper, J.A.3
  • 35
    • 0028326914 scopus 로고
    • Functional identification of integrin laminin receptors that mediate process outgrowth by human SY5Y neuroblastoma cells
    • Choi ES, Rettig WJ, Wayner EA, Srour ML, Clegg DO. 1994. Functional identification of integrin laminin receptors that mediate process outgrowth by human SY5Y neuroblastoma cells. J Neurosci Res 37:475-488.
    • (1994) J Neurosci Res , vol.37 , pp. 475-488
    • Choi, E.S.1    Rettig, W.J.2    Wayner, E.A.3    Srour, M.L.4    Clegg, D.O.5
  • 37
    • 0027245576 scopus 로고
    • Interaction between the 67 kilodalton metastasis-associated laminin receptor and laminin
    • Cioce V, Margulies IM, Sobel ME, Castronovo V. 1993. Interaction between the 67 kilodalton metastasis-associated laminin receptor and laminin. Kidney Int 43:30-37.
    • (1993) Kidney Int , vol.43 , pp. 30-37
    • Cioce, V.1    Margulies, I.M.2    Sobel, M.E.3    Castronovo, V.4
  • 38
    • 0031561481 scopus 로고    scopus 로고
    • Keystone symposium on signal transduction by cell adhesion receptors
    • Clark EA, Hynes RO. 1997. Keystone symposium on signal transduction by cell adhesion receptors. Biochim Biophys Acta 1333:R9-R16.
    • (1997) Biochim Biophys Acta , vol.1333
    • Clark, E.A.1    Hynes, R.O.2
  • 39
    • 0030444250 scopus 로고    scopus 로고
    • Identification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein
    • Clausse N, Jackers P, Jares P, Joris B, Sobel ME, Castronovo V. 1996. Identification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein. DNA Cell Biol 15: 1009-1023.
    • (1996) DNA Cell Biol , vol.15 , pp. 1009-1023
    • Clausse, N.1    Jackers, P.2    Jares, P.3    Joris, B.4    Sobel, M.E.5    Castronovo, V.6
  • 40
    • 0033084217 scopus 로고    scopus 로고
    • Secondary reduction of α7B integrin in laminin α2 deficient congenital muscular dystrophy supports an additional transmembrane link in skeletal muscle
    • Cohn RD, Mayer U, Saher G, Herrmann R, van der Flier A, Sonnenberg A, Sorokin L, Voit T. 1999. Secondary reduction of α7B integrin in laminin α2 deficient congenital muscular dystrophy supports an additional transmembrane link in skeletal muscle. J Neurol Sci 163:140-152.
    • (1999) J Neurol Sci , vol.163 , pp. 140-152
    • Cohn, R.D.1    Mayer, U.2    Saher, G.3    Herrmann, R.4    Van Der Flier, A.5    Sonnenberg, A.6    Sorokin, L.7    Voit, T.8
  • 41
    • 0033216630 scopus 로고    scopus 로고
    • Upregulation of integrin α6β1 and chemokine receptor CCR1 by interleukin-12 promotes the migration of human type 1 helper T cells
    • Colantonio L, Iellem A, Clissi B, Pardi R, Rogge L, Siniganglia F, D'Ambrosio D. 1999. Upregulation of integrin α6β1 and chemokine receptor CCR1 by interleukin-12 promotes the migration of human type 1 helper T cells. Blood 94:2981-2989.
    • (1999) Blood , vol.94 , pp. 2981-2989
    • Colantonio, L.1    Iellem, A.2    Clissi, B.3    Pardi, R.4    Rogge, L.5    Siniganglia, F.6    D'Ambrosio, D.7
  • 42
    • 0027247797 scopus 로고
    • A new isoform of the laminin receptor integrin α7β1 is developmentally regulated in skeletal muscle
    • Collo G, Starr L, Quaranta V. 1993. A new isoform of the laminin receptor integrin α7β1 is developmentally regulated in skeletal muscle. J Biol Chem 268:19019-19024.
    • (1993) J Biol Chem , vol.268 , pp. 19019-19024
    • Collo, G.1    Starr, L.2    Quaranta, V.3
  • 43
    • 0028984447 scopus 로고
    • Gradient of α6A in the myocardium during early heart development
    • Collo G, Domanico SZ, Klier G, Quaranta V. 1995. Gradient of α6A in the myocardium during early heart development. Cell Adhes Commun 3:101-113.
    • (1995) Cell Adhes Commun , vol.3 , pp. 101-113
    • Collo, G.1    Domanico, S.Z.2    Klier, G.3    Quaranta, V.4
  • 44
    • 0030613628 scopus 로고    scopus 로고
    • The laminin α2-chain short arm mediates cell adhesion through both the α1β1 and α2β1 integrins
    • Colognato H, MacCarrick M, O'Rear JJ, Yurchenco PD. 1997. The laminin α2-chain short arm mediates cell adhesion through both the α1β1 and α2β1 integrins. J Biol Chem 272:29330-29336.
    • (1997) J Biol Chem , vol.272 , pp. 29330-29336
    • Colognato, H.1    MacCarrick, M.2    O'Rear, J.J.3    Yurchenco, P.D.4
  • 45
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • Colognato H, Winkelmann DA, Yurchenco PD. 1999. Laminin polymerization induces a receptor-cytoskeleton network. J Cell Biol 145:619-631.
    • (1999) J Cell Biol , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 46
    • 0032746544 scopus 로고    scopus 로고
    • Syndecan-4 and integrins: Combinatorial signaling in cell adhesion
    • Couchman JR, Woods A. 1999. Syndecan-4 and integrins: combinatorial signaling in cell adhesion. J Cell Sci 112:3415-3420.
    • (1999) J Cell Sci , vol.112 , pp. 3415-3420
    • Couchman, J.R.1    Woods, A.2
  • 49
    • 0028169729 scopus 로고
    • The α6 and β4 integrin subunits are expressed by smooth muscle cells of human small vessels: A new localization in mesenchymal cells
    • Cremona O Savoia P, Marchisio PC, Gabbiani G, Chaponnier C. 1994. The α6 and β4 integrin subunits are expressed by smooth muscle cells of human small vessels: a new localization in mesenchymal cells. J Histochem Cytochem 42:1221-1228.
    • (1994) J Histochem Cytochem , vol.42 , pp. 1221-1228
    • Cremona, O.1    Savoia, P.2    Marchisio, P.C.3    Gabbiani, G.4    Chaponnier, C.5
  • 50
    • 0028954485 scopus 로고
    • Regulation of endothelial cell morphogenesis by integrins, mechanical forces, and matrix guidance pathways
    • Davis GE, Camarillo CW. 1995. Regulation of endothelial cell morphogenesis by integrins, mechanical forces, and matrix guidance pathways. Exp Cell Res 216:113-123.
    • (1995) Exp Cell Res , vol.216 , pp. 113-123
    • Davis, G.E.1    Camarillo, C.W.2
  • 51
    • 0027160707 scopus 로고
    • Function and spatial distribution in developing chick retina of the laminin receptor α6β1 and its isoforms
    • de Curtis I, Reichardt LF. 1993. Function and spatial distribution in developing chick retina of the laminin receptor α6β1 and its isoforms. Development 118:377-388.
    • (1993) Development , vol.118 , pp. 377-388
    • De Curtis, I.1    Reichardt, L.F.2
  • 52
    • 0033152940 scopus 로고    scopus 로고
    • Integrins: Alternative splicing as a mechanism to regulate ligand binding and integrin signaling events
    • de Melker AA, Sonnenberg A. 1999. Integrins: alternative splicing as a mechanism to regulate ligand binding and integrin signaling events. Bioessays 21:499-509.
    • (1999) Bioessays , vol.21 , pp. 499-509
    • De Melker, A.A.1    Sonnenberg, A.2
  • 54
    • 0025827302 scopus 로고
    • Differential distribution and modulation of expression of α1β1 integrin on human endothelial cells
    • Defilippi P, van Hisbergh V, Bertolotto A, Rossino P, Silengo L, Tarone G. 1991. Differential distribution and modulation of expression of α1β1 integrin on human endothelial cells. J Cell Biol 114: 855-863.
    • (1991) J Cell Biol , vol.114 , pp. 855-863
    • Defilippi, P.1    Van Hisbergh, V.2    Bertolotto, A.3    Rossino, P.4    Silengo, L.5    Tarone, G.6
  • 55
    • 0026611378 scopus 로고
    • α6β1 integrin (laminin receptor) is down-regulated by tumor necrosis factor α and interleukin-1 β in human endothelial cells
    • Defilippi P, Silengo L, Tarone G. 1992. α6β1 integrin (laminin receptor) is down-regulated by tumor necrosis factor α and interleukin-1 β in human endothelial cells. J Biol Chem 267:18303-18307.
    • (1992) J Biol Chem , vol.267 , pp. 18303-18307
    • Defilippi, P.1    Silengo, L.2    Tarone, G.3
  • 56
  • 58
    • 0029665071 scopus 로고    scopus 로고
    • Cleavage of the α6A subunit is essential for activation of the α6Aβ1 integrin by phorbol 12-myristate 13-acetate
    • Delwel GO, Hogervorst F, Sonnenberg A. 1996. Cleavage of the α6A subunit is essential for activation of the α6Aβ1 integrin by phorbol 12-myristate 13-acetate. J Biol Chem 271:7293-7296.
    • (1996) J Biol Chem , vol.271 , pp. 7293-7296
    • Delwel, G.O.1    Hogervorst, F.2    Sonnenberg, A.3
  • 59
    • 0030684146 scopus 로고    scopus 로고
    • Avian neural crest cell migration on laminin: Interaction of the α1β1 integrin with distinct laminin-1 domains mediates different adhesive responses
    • Desban N, Duband JL. 1997. Avian neural crest cell migration on laminin: interaction of the α1β1 integrin with distinct laminin-1 domains mediates different adhesive responses. J Cell Sci 110: 2729-2744.
    • (1997) J Cell Sci , vol.110 , pp. 2729-2744
    • Desban, N.1    Duband, J.L.2
  • 62
    • 0030730986 scopus 로고    scopus 로고
    • Integrin α6Aβ1 induces CD81-dependent cell motility without engaging the extracellular matrix migration substrate
    • Domanico SZ, Pelletier AJ, Havran WL, Quaranta V. 1997. Integrin α6Aβ1 induces CD81-dependent cell motility without engaging the extracellular matrix migration substrate. Mol Biol Cell 8:2253-2265.
    • (1997) Mol Biol Cell , vol.8 , pp. 2253-2265
    • Domanico, S.Z.1    Pelletier, A.J.2    Havran, W.L.3    Quaranta, V.4
  • 63
    • 0029666420 scopus 로고    scopus 로고
    • β4 integrin is required for hemidesmosome formation, cell adhesion, and cell survival
    • Dowling J, Yu QC, Fuchs E. 1996. β4 integrin is required for hemidesmosome formation, cell adhesion, and cell survival. J Cell Biol 134:559-572.
    • (1996) J Cell Biol , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 64
    • 0026481012 scopus 로고
    • Expression of α1 integrin, a laminin-collagen receptor, during myogenesis and neurogenesis in the avian embryo
    • Duband J-L, Belkin AM, Syfrig J, Thiery JP, Koteliansky VE. 1992. Expression of α1 integrin, a laminin-collagen receptor, during myogenesis and neurogenesis in the avian embryo. Development 116:585-600.
    • (1992) Development , vol.116 , pp. 585-600
    • Duband, J.-L.1    Belkin, A.M.2    Syfrig, J.3    Thiery, J.P.4    Koteliansky, V.E.5
  • 65
    • 0032483122 scopus 로고    scopus 로고
    • Recombinant soluble human α3β1 integrin: Purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner
    • Eble JA, Wucherpfennig KW, Gauthier L, Dersch P, Krukonis E, Isberg RR, Hemler ME. 1998. Recombinant soluble human α3β1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner. Biochemistry 37:10945-10955.
    • (1998) Biochemistry , vol.37 , pp. 10945-10955
    • Eble, J.A.1    Wucherpfennig, K.W.2    Gauthier, L.3    Dersch, P.4    Krukonis, E.5    Isberg, R.R.6    Hemler, M.E.7
  • 66
    • 0024847956 scopus 로고
    • The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor on others
    • Elices MJ, Hemler ME. 1989. The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor on others. Proc Natl Acad Sci USA 86:9906-9910.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9906-9910
    • Elices, M.J.1    Hemler, M.E.2
  • 67
    • 0026020583 scopus 로고
    • Receptor functions for the integrin VLA-3: Fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations
    • Elices MJ, Urry LA, Hemler ME. 1991. Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations. J Cell Biol 112:169-181.
    • (1991) J Cell Biol , vol.112 , pp. 169-181
    • Elices, M.J.1    Urry, L.A.2    Hemler, M.E.3
  • 68
    • 0027008419 scopus 로고
    • Basic FGF and TGF-beta differentially modulate integrin expression of human microvascular endothelial cells
    • Enenstein J, Waleh NS, Kramer RH. 1992. Basic FGF and TGF-beta differentially modulate integrin expression of human microvascular endothelial cells. Exp Cell Res 203:499-503.
    • (1992) Exp Cell Res , vol.203 , pp. 499-503
    • Enenstein, J.1    Waleh, N.S.2    Kramer, R.H.3
  • 69
    • 0026512402 scopus 로고
    • Merosin promotes cell attachment and neurite outgrowth and is a component of the neurite-promoting factor of RN22 schwannoma cells
    • Engvall E, Earwicker D, Day A, Muir D, Manthorpe M, Paulsson M. 1992. Merosin promotes cell attachment and neurite outgrowth and is a component of the neurite-promoting factor of RN22 schwannoma cells. Exp Cell Res 198:115-123.
    • (1992) Exp Cell Res , vol.198 , pp. 115-123
    • Engvall, E.1    Earwicker, D.2    Day, A.3    Muir, D.4    Manthorpe, M.5    Paulsson, M.6
  • 72
    • 0031258105 scopus 로고    scopus 로고
    • Alternatively spliced variants: A new view of the integrin cytoplasmic domain
    • Fornaro M, Languino LR. 1997. Alternatively spliced variants: a new view of the integrin cytoplasmic domain. Matrix Biol 16:185-193.
    • (1997) Matrix Biol , vol.16 , pp. 185-193
    • Fornaro, M.1    Languino, L.R.2
  • 73
    • 0033523879 scopus 로고    scopus 로고
    • Integrins mediate a neuronal survival signal for oligodendrocytes
    • Frost EE, Buttery PC, Milner R, ffrench-Constant C. 1999. Integrins mediate a neuronal survival signal for oligodendrocytes. Curr Biol 9:1251-1254.
    • (1999) Curr Biol , vol.9 , pp. 1251-1254
    • Frost, E.E.1    Buttery, P.C.2    Milner, R.3    Ffrench-Constant, C.4
  • 75
    • 0029894277 scopus 로고    scopus 로고
    • Deletion of integrin α1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion
    • Gardner H, Kreidberg J, Koteliansky V, Jaenisch R. 1996. Deletion of integrin α1 by homologous recombination permits normal murine development but gives rise to a specific deficit in cell adhesion. Dev Biol 175:301-313.
    • (1996) Dev Biol , vol.175 , pp. 301-313
    • Gardner, H.1    Kreidberg, J.2    Koteliansky, V.3    Jaenisch, R.4
  • 78
    • 0023721720 scopus 로고
    • The human laminin receptor is a member of the integrin family of cell adhesion receptors
    • Gehlsen KR, Dillner L, Engvall E, Ruoslahti E. 1988. The human laminin receptor is a member of the integrin family of cell adhesion receptors Science 241:1228-1229.
    • (1988) Science , vol.241 , pp. 1228-1229
    • Gehlsen, K.R.1    Dillner, L.2    Engvall, E.3    Ruoslahti, E.4
  • 81
  • 82
    • 0027409341 scopus 로고
    • In vitro and in vivo expression of α7 integrin and desmin define the primary and secondary myogenic lineages
    • George-Weinstein M, Foster RF, Gerhart JV, Kaufman SJ. 1993. In vitro and in vivo expression of α7 integrin and desmin define the primary and secondary myogenic lineages. Dev Biol 156:209-229.
    • (1993) Dev Biol , vol.156 , pp. 209-229
    • George-Weinstein, M.1    Foster, R.F.2    Gerhart, J.V.3    Kaufman, S.J.4
  • 83
    • 0033794569 scopus 로고    scopus 로고
    • Complexity and specificity of integrin signalling
    • Giancotti FG. 2000. Complexity and specificity of integrin signalling. Nat Cell Biol 2:E13-E14.
    • (2000) Nat Cell Biol , vol.2
    • Giancotti, F.G.1
  • 84
  • 86
    • 0032487578 scopus 로고    scopus 로고
    • Cre-loxP-mediated inactivation of the α6A integrin splice variant in vivo: Evidence for a specific functional role of α6A in lymphocyte migration but not in heart development
    • Gimond C, Baudoin C, van der Neut R, Kramer D, Calafat J, Sonnenberg A. 1998. Cre-loxP-mediated inactivation of the α6A integrin splice variant in vivo: evidence for a specific functional role of α6A in lymphocyte migration but not in heart development. J Cell Biol 143:253-266.
    • (1998) J Cell Biol , vol.143 , pp. 253-266
    • Gimond, C.1    Baudoin, C.2    Van Der Neut, R.3    Kramer, D.4    Calafat, J.5    Sonnenberg, A.6
  • 87
    • 0027318904 scopus 로고
    • Redistribution of the hemidesmosome components α6β4 integrin and bullous pemphigoid antigens during epithelial wound healing
    • Gipson IK, Spurr-Michaud S, Tisdale A, Elwell J, Stepp MA. 1993. Redistribution of the hemidesmosome components α6β4 integrin and bullous pemphigoid antigens during epithelial wound healing. Exp Cell Res 207:86-98.
    • (1993) Exp Cell Res , vol.207 , pp. 86-98
    • Gipson, I.K.1    Spurr-Michaud, S.2    Tisdale, A.3    Elwell, J.4    Stepp, M.A.5
  • 88
    • 0027197249 scopus 로고
    • Laminin variants and integrin laminin receptors in developing and adult human smooth muscle
    • Glukhova M, Koteliansky V, Fondacci C, Marotte F, Rappaport L. 1993. Laminin variants and integrin laminin receptors in developing and adult human smooth muscle. Dev Biol 157:437-447.
    • (1993) Dev Biol , vol.157 , pp. 437-447
    • Glukhova, M.1    Koteliansky, V.2    Fondacci, C.3    Marotte, F.4    Rappaport, L.5
  • 89
    • 0032841440 scopus 로고    scopus 로고
    • The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger LE, Hopkinson SB, deHart GW, Collawn S, Couchman JR, Jones JC. 1999. The α3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J Cell Sci 112:2615-2629.
    • (1999) J Cell Sci , vol.112 , pp. 2615-2629
    • Goldfinger, L.E.1    Hopkinson, S.B.2    DeHart, G.W.3    Collawn, S.4    Couchman, J.R.5    Jones, J.C.6
  • 90
    • 0032893678 scopus 로고    scopus 로고
    • A cell signal pathway involving laminin-5, α3β1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation
    • Gonzales M, Haan K, Baker SE, Fitchmun M, Todorov I, Weitzman S, Jones JC. 1999. A cell signal pathway involving laminin-5, α3β1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation. Mol Biol Cell 10:259-270.
    • (1999) Mol Biol Cell , vol.10 , pp. 259-270
    • Gonzales, M.1    Haan, K.2    Baker, S.E.3    Fitchmun, M.4    Todorov, I.5    Weitzman, S.6    Jones, J.C.7
  • 92
    • 0028053242 scopus 로고
    • Selective modulation of the interaction of α7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation
    • Gu M, Wang W, Song WK, Cooper DNW, Kaufman SJ. 1994. Selective modulation of the interaction of α7β1 integrin with fibronectin and laminin by L-14 lectin during skeletal muscle differentiation. J Cell Sci 107:175-181.
    • (1994) J Cell Sci , vol.107 , pp. 175-181
    • Gu, M.1    Wang, W.2    Song, W.K.3    Cooper, D.N.W.4    Kaufman, S.J.5
  • 93
    • 0028225439 scopus 로고
    • Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins
    • Habets GG, Scholtes EH, Zuydgeest D, van der Kammen RA, Stam JC, Berns A, Collard JG. 1994. Identification of an invasion-inducing gene, Tiam-1, that encodes a protein with homology to GDP-GTP exchangers for Rho-like proteins. Cell 77:537-549.
    • (1994) Cell , vol.77 , pp. 537-549
    • Habets, G.G.1    Scholtes, E.H.2    Zuydgeest, D.3    Van Der Kammen, R.A.4    Stam, J.C.5    Berns, A.6    Collard, J.G.7
  • 94
    • 0023407601 scopus 로고
    • Immunohistochemical localization of laminin, neural cell adhesion molecule, collagen type IV and T-61 antigen in the embryonic retina of the Japanese quail by in vivo injection of antibodies
    • Halfter W, Fua CS. 1987. Immunohistochemical localization of laminin, neural cell adhesion molecule, collagen type IV and T-61 antigen in the embryonic retina of the Japanese quail by in vivo injection of antibodies. Cell Tissue Res 249:487-496.
    • (1987) Cell Tissue Res , vol.249 , pp. 487-496
    • Halfter, W.1    Fua, C.S.2
  • 95
    • 0030828894 scopus 로고    scopus 로고
    • An epitope on VLA-6 (α6β1) integrin involved in migration but not adhesion is required for extravasation of murine melanoma B16F1 cells in liver
    • Hangan D, Morris VL, Boeters L, von Ballestrem C, Uniyal S, Chan BM. 1997. An epitope on VLA-6 (α6β1) integrin involved in migration but not adhesion is required for extravasation of murine melanoma B16F1 cells in liver. Cancer Res 57:3812-3817.
    • (1997) Cancer Res , vol.57 , pp. 3812-3817
    • Hangan, D.1    Morris, V.L.2    Boeters, L.3    Von Ballestrem, C.4    Uniyal, S.5    Chan, B.M.6
  • 97
    • 0031720629 scopus 로고    scopus 로고
    • Integrin associated proteins
    • Hemler ME. 1998. Integrin associated proteins. Curr Opin Cell Biol 10:578-585.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 578-585
    • Hemler, M.E.1
  • 98
    • 0033612299 scopus 로고    scopus 로고
    • Dystroglycan versatility
    • Hemler ME. 1999. Dystroglycan versatility. Cell 97:543-546.
    • (1999) Cell , vol.97 , pp. 543-546
    • Hemler, M.E.1
  • 99
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • Henry MD, Campbell KP. 1998. A role for dystroglycan in basement membrane assembly. Cell 95:859-870.
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 101
    • 0033084189 scopus 로고    scopus 로고
    • SU2, an epithelial integrin that binds laminin in the sea urchin embryo
    • Hertzler PL, McClay DR. 1999. aSU2, an epithelial integrin that binds laminin in the sea urchin embryo. Dev Biol 207:1-13.
    • (1999) Dev Biol , vol.207 , pp. 1-13
    • Hertzler, P.L.1    McClay, D.R.2
  • 102
    • 0031696484 scopus 로고    scopus 로고
    • Mouse myoblasts can fuse and form a normal sarcomere in the absence of β1 integrin expression
    • Hirsh E, Lohikangas L, Gullberg D, Johansson S, Fassler R. 1998. Mouse myoblasts can fuse and form a normal sarcomere in the absence of β1 integrin expression. J Cell Sci 111:2397-2409.
    • (1998) J Cell Sci , vol.111 , pp. 2397-2409
    • Hirsh, E.1    Lohikangas, L.2    Gullberg, D.3    Johansson, S.4    Fassler, R.5
  • 103
    • 0030809116 scopus 로고    scopus 로고
    • Altered expression of the α7β1 integrin in human and murine muscular dystrophies
    • Hodges BL, Hayashi YK, Nonaka I, Wang W, Arahata K, Kaufman S. 1997. Altered expression of the α7β1 integrin in human and murine muscular dystrophies. J Cell Sci 110:2873-2881.
    • (1997) J Cell Sci , vol.110 , pp. 2873-2881
    • Hodges, B.L.1    Hayashi, Y.K.2    Nonaka, I.3    Wang, W.4    Arahata, K.5    Kaufman, S.6
  • 104
    • 0032493934 scopus 로고    scopus 로고
    • Novel roles for alphα3betα1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes
    • Hodivala-Dilke KM, DiPersio CM, Kreidberg JA, Hynes RO. 1998. Novel roles for alphα3betα1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes. J Cell Biol 142:1357-1369.
    • (1998) J Cell Biol , vol.142 , pp. 1357-1369
    • Hodivala-Dilke, K.M.1    DiPersio, C.M.2    Kreidberg, J.A.3    Hynes, R.O.4
  • 105
    • 0032582650 scopus 로고    scopus 로고
    • Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line
    • Hoffman MP, Nomizu M, Roque E, Lee S, Jung DW, Yamada Y, Kleinman HK. 1998. Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line. J Biol Chem 273:28633-28641.
    • (1998) J Biol Chem , vol.273 , pp. 28633-28641
    • Hoffman, M.P.1    Nomizu, M.2    Roque, E.3    Lee, S.4    Jung, D.W.5    Yamada, Y.6    Kleinman, H.K.7
  • 106
    • 0032447962 scopus 로고    scopus 로고
    • Interaction of BP180 (type XVII collagen) and α6 integrin is necessary for stabilization of hemidesmosome structure
    • Hopkinson SB, Findlay K, deHart GW, Jones JC. 1998. Interaction of BP180 (type XVII collagen) and α6 integrin is necessary for stabilization of hemidesmosome structure. J Invest Dermatol 111:1015-1022.
    • (1998) J Invest Dermatol , vol.111 , pp. 1015-1022
    • Hopkinson, S.B.1    Findlay, K.2    DeHart, G.W.3    Jones, J.C.4
  • 107
    • 0025908468 scopus 로고
    • Molecular cloning of the human α6 integrin subunit. Alternative splicing of α6 mRNA and chromosomal localization of the α6 and β4 genes
    • Hogervorst F, Kuikman I, van Kessel AG, Sonnenberg A. 1991. Molecular cloning of the human α6 integrin subunit. Alternative splicing of α6 mRNA and chromosomal localization of the α6 and β4 genes. Eur J Biochem 199:425-433.
    • (1991) Eur J Biochem , vol.199 , pp. 425-433
    • Hogervorst, F.1    Kuikman, I.2    Van Kessel, A.G.3    Sonnenberg, A.4
  • 108
    • 0027301230 scopus 로고
    • The role of phosphorylation in activation of the α6Aβ1 laminin receptor
    • Hogervorst F, Kuikman I, Noteboom E, Sonnenberg A. 1993. The role of phosphorylation in activation of the α6Aβ1 laminin receptor. J Biol Chem 268:18427-18430.
    • (1993) J Biol Chem , vol.268 , pp. 18427-18430
    • Hogervorst, F.1    Kuikman, I.2    Noteboom, E.3    Sonnenberg, A.4
  • 110
    • 0033374678 scopus 로고    scopus 로고
    • Cell adhesion: Old and new questions
    • Hynes RO. 1999a. Cell adhesion: old and new questions Trends Cell Biol 9:M33-M37.
    • (1999) Trends Cell Biol , vol.9
    • Hynes, R.O.1
  • 111
    • 0033017948 scopus 로고    scopus 로고
    • The dynamic dialogue between cells and matrices: Implications of fibronectin's elasticity
    • Hynes RO. 1999b. The dynamic dialogue between cells and matrices: implications of fibronectin's elasticity. Proc Natl Acad Sci USA 96:2588-2590.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2588-2590
    • Hynes, R.O.1
  • 112
    • 0027406455 scopus 로고
    • Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA
    • Ikeyama S, Koyama M, Yamaoko M, Sasada R, Miyake M. 1993. Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. J Exp Med 177:1231-1237.
    • (1993) J Exp Med , vol.177 , pp. 1231-1237
    • Ikeyama, S.1    Koyama, M.2    Yamaoko, M.3    Sasada, R.4    Miyake, M.5
  • 114
    • 0028983943 scopus 로고
    • β1 integrins do not have a major role in keratinocyte intercellular adhesion
    • Jensen PJ, Wheelock MJ. 1995. β1 integrins do not have a major role in keratinocyte intercellular adhesion. Exp Cell Res 219:322-331.
    • (1995) Exp Cell Res , vol.219 , pp. 322-331
    • Jensen, P.J.1    Wheelock, M.J.2
  • 115
    • 0028901094 scopus 로고
    • Stimulation of tyrosine phosphorylation of distinct proteins in response to antibody-mediated ligation and clustering of α3 and α6 integrins
    • Jewell K, Kapron-Bras C, Jeevaratnam P, Dedhar S. 1995. Stimulation of tyrosine phosphorylation of distinct proteins in response to antibody-mediated ligation and clustering of α3 and α6 integrins. J Cell Sci 108:1165-1174.
    • (1995) J Cell Sci , vol.108 , pp. 1165-1174
    • Jewell, K.1    Kapron-Bras, C.2    Jeevaratnam, P.3    Dedhar, S.4
  • 117
    • 0029005076 scopus 로고
    • Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells
    • Kato M, Saunders S, Nguyen H, Bernfield M. 1995. Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells. Mol Biol Cell 6:559-576.
    • (1995) Mol Biol Cell , vol.6 , pp. 559-576
    • Kato, M.1    Saunders, S.2    Nguyen, H.3    Bernfield, M.4
  • 118
    • 0021801358 scopus 로고
    • Expression of a developmentally regulated antigen on the surface of skeletal and cardiac muscle cells
    • Kaufman SJ, George-Weinstein M, Foster RF. 1985. Expression of a developmentally regulated antigen on the surface of skeletal and cardiac muscle cells. J Cell Biol 100:1977-1987.
    • (1985) J Cell Biol , vol.100 , pp. 1977-1987
    • Kaufman, S.J.1    George-Weinstein, M.2    Foster, R.F.3
  • 119
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and Rac1 induce integrin-mediated cell motility and invasivenesss through PI(3)K
    • Keely PJ Westwick JK, Whitehead IP, Der CJ, Parise LV. 1997. Cdc42 and Rac1 induce integrin-mediated cell motility and invasivenesss through PI(3)K. Nature 390:632-636.
    • (1997) Nature , vol.390 , pp. 632-636
    • Keely, P.J.1    Westwick, J.K.2    Whitehead, I.P.3    Der, C.J.4    Parise, L.V.5
  • 120
    • 0033620657 scopus 로고    scopus 로고
    • R-Ras signals through specific integrin a cytoplasmic domains to promote migration and invasion of breast epithelial cells
    • Keely PJ, Rusyn EV, Cox AD, Parise LV. 1999. R-Ras signals through specific integrin a cytoplasmic domains to promote migration and invasion of breast epithelial cells. J Cell Biol 145:1077-1088.
    • (1999) J Cell Biol , vol.145 , pp. 1077-1088
    • Keely, P.J.1    Rusyn, E.V.2    Cox, A.D.3    Parise, L.V.4
  • 121
    • 0032546780 scopus 로고    scopus 로고
    • Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. Laminin-10/11 mediates cell adhesion through integrin α3β1
    • Kikkawa Y, Sanzen N, Sekiguchi K. 1998. Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. Laminin-10/11 mediates cell adhesion through integrin α3β1. J Biol Chem 273:15854-15859.
    • (1998) J Biol Chem , vol.273 , pp. 15854-15859
    • Kikkawa, Y.1    Sanzen, N.2    Sekiguchi, K.3
  • 122
    • 0034003019 scopus 로고    scopus 로고
    • Control of extracellular matrix assembly by syndecan-2 proteoglycan
    • Klass CM, Couchman JR, Woods A. 2000. Control of extracellular matrix assembly by syndecan-2 proteoglycan. J Cell Sci 113:493-506.
    • (2000) J Cell Sci , vol.113 , pp. 493-506
    • Klass, C.M.1    Couchman, J.R.2    Woods, A.3
  • 123
    • 0027442793 scopus 로고
    • Basic fibroblast growth factor modulates integrin expression in microvascular endothelial cells
    • Klein S, Giancotti FG, Presta M, Albelda SM, Buck CA, Rifkin DB. 1993. Basic fibroblast growth factor modulates integrin expression in microvascular endothelial cells. Mol Biol Cell 10:973-982.
    • (1993) Mol Biol Cell , vol.10 , pp. 973-982
    • Klein, S.1    Giancotti, F.G.2    Presta, M.3    Albelda, S.M.4    Buck, C.A.5    Rifkin, D.B.6
  • 124
    • 0031656747 scopus 로고    scopus 로고
    • Desmosomes: Intercellular adhesive junctions specialized for attachment of intermediate filaments
    • Kowalczyk AP, Bornslaeger EA, Norvell SM, Palka HL, Green KJ. 1999. Desmosomes: intercellular adhesive junctions specialized for attachment of intermediate filaments. Int Rev Cytol 185:237-302.
    • (1999) Int Rev Cytol , vol.185 , pp. 237-302
    • Kowalczyk, A.P.1    Bornslaeger, E.A.2    Norvell, S.M.3    Palka, H.L.4    Green, K.J.5
  • 125
    • 0025036252 scopus 로고
    • Human microvascular endothelial cells use β1 and β3 integrin receptor complexes to attach to laminin
    • Kramer RH, Cheng YF, Clyman R. 1990. Human microvascular endothelial cells use β1 and β3 integrin receptor complexes to attach to laminin. J Cell Biol 111:1233-1243.
    • (1990) J Cell Biol , vol.111 , pp. 1233-1243
    • Kramer, R.H.1    Cheng, Y.F.2    Clyman, R.3
  • 126
    • 0026236965 scopus 로고
    • Laminin-binding integrin α7β1: Functional characterization and expression in normal and malignant melanocytes
    • Kramer RH, Vu MP, Cheng YF, Ramos DM, Timpl R, Waleh N. 1991. Laminin-binding integrin α7β1: functional characterization and expression in normal and malignant melanocytes. Cell Regul 2:805-817.
    • (1991) Cell Regul , vol.2 , pp. 805-817
    • Kramer, R.H.1    Vu, M.P.2    Cheng, Y.F.3    Ramos, D.M.4    Timpl, R.5    Waleh, N.6
  • 128
    • 0028303125 scopus 로고
    • The structural basis of integrin ligand interactions
    • Kuhn K, Eble J. 1994. The structural basis of integrin ligand interactions. Trends Cell Biol 4:256-261.
    • (1994) Trends Cell Biol , vol.4 , pp. 256-261
    • Kuhn, K.1    Eble, J.2
  • 129
    • 0026327658 scopus 로고
    • Avian neural crest cell attachment to laminin: Involvement of divalent cation dependent and independent integrins
    • Lallier T, Bronner-Fraser M. 1991. Avian neural crest cell attachment to laminin: involvement of divalent cation dependent and independent integrins. Development 113:1069-1084.
    • (1991) Development , vol.113 , pp. 1069-1084
    • Lallier, T.1    Bronner-Fraser, M.2
  • 130
    • 0028204058 scopus 로고
    • Neural crest cell interactions with laminin: Structural requirements and localization of the binding site for α1β1 integrin
    • Lallier T, Deutzmann R, Perris R, Bronner-Fraser M. 1994. Neural crest cell interactions with laminin: structural requirements and localization of the binding site for α1β1 integrin. Dev Biol 162:451-464.
    • (1994) Dev Biol , vol.162 , pp. 451-464
    • Lallier, T.1    Deutzmann, R.2    Perris, R.3    Bronner-Fraser, M.4
  • 131
    • 0032517773 scopus 로고    scopus 로고
    • Cellular interaction of integrin α3β1 with laminin 5 promotes gap junctional communication
    • Lampe PD, Nguyen BP, Gil S, Usui M, Olerud J, Takada Y, Carter WG. 1998. Cellular interaction of integrin α3β1 with laminin 5 promotes gap junctional communication. J Cell Biol 143:1735-1747.
    • (1998) J Cell Biol , vol.143 , pp. 1735-1747
    • Lampe, P.D.1    Nguyen, B.P.2    Gil, S.3    Usui, M.4    Olerud, J.5    Takada, Y.6    Carter, W.G.7
  • 132
    • 0026013429 scopus 로고
    • The role of integrins in the maintenance of endothelial monolayer integrity
    • Lampugnani MG, Resnati M, Dejana E, Marchisio PC. 1991. The role of integrins in the maintenance of endothelial monolayer integrity. J Cell Biol 112:479-490.
    • (1991) J Cell Biol , vol.112 , pp. 479-490
    • Lampugnani, M.G.1    Resnati, M.2    Dejana, E.3    Marchisio, P.C.4
  • 133
    • 0344923326 scopus 로고
    • Laminin is associated with the "neurite outgrowth-promoting factors" found in conditioned media
    • Lander AD, Fujii DK, Reichardt LF. 1985a. Laminin is associated with the "neurite outgrowth-promoting factors" found in conditioned media. Proc Natl Acad Sci USA 82:2183-2187.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2183-2187
    • Lander, A.D.1    Fujii, D.K.2    Reichardt, L.F.3
  • 134
    • 0022201055 scopus 로고
    • Purification of a factor that promotes neurite outgrowth: Isolation of laminin and associated molecules
    • Lander AD, Fujii DK, Reichardt LF. 1985b. Purification of a factor that promotes neurite outgrowth: isolation of laminin and associated molecules. J Cell Biol 101:898-913.
    • (1985) J Cell Biol , vol.101 , pp. 898-913
    • Lander, A.D.1    Fujii, D.K.2    Reichardt, L.F.3
  • 137
    • 0028180208 scopus 로고
    • The integrin chains β1 and α6 associate with the chaperone calnexin prior to integrin assembly
    • Lenter M, Vestweber D. 1994. The integrin chains β1 and α6 associate with the chaperone calnexin prior to integrin assembly. J Biol Chem 269:12263-12268.
    • (1994) J Biol Chem , vol.269 , pp. 12263-12268
    • Lenter, M.1    Vestweber, D.2
  • 138
    • 0032481294 scopus 로고    scopus 로고
    • A novel extracellular domain variant of the human integrin α7 subunit generated by alternative intron splicing
    • Leung E, Lim SP, Berg R, Yang Y, Ni J, Wang SX, Krissansen GW. 1998. A novel extracellular domain variant of the human integrin α7 subunit generated by alternative intron splicing. Biochem Biophys Res Commun 243:317-325.
    • (1998) Biochem Biophys Res Commun , vol.243 , pp. 317-325
    • Leung, E.1    Lim, S.P.2    Berg, R.3    Yang, Y.4    Ni, J.5    Wang, S.X.6    Krissansen, G.W.7
  • 139
    • 0033611068 scopus 로고    scopus 로고
    • A novel muscle-specific β1 integrin binding protein (MIBP) that modulates myogenic differentiation
    • Li J, Mayne R, Wu C. 1999. A novel muscle-specific β1 integrin binding protein (MIBP) that modulates myogenic differentiation. J Cell Biol 147:1391-1397.
    • (1999) J Cell Biol , vol.147 , pp. 1391-1397
    • Li, J.1    Mayne, R.2    Wu, C.3
  • 141
    • 0027214012 scopus 로고
    • α6 integrin is up-regulated in step increments accompanying neoplastic transformation and tumorigenic conversion of human fibroblasts
    • Lin CS, Zhang K, Kramer R. 1993. α6 integrin is up-regulated in step increments accompanying neoplastic transformation and tumorigenic conversion of human fibroblasts. Cancer Res 53:2950-2953.
    • (1993) Cancer Res , vol.53 , pp. 2950-2953
    • Lin, C.S.1    Zhang, K.2    Kramer, R.3
  • 142
    • 0029043889 scopus 로고
    • The basal keratin network of stratified squamous epithelia: Defining K15 function in the absence of K14
    • Lloyd C, Yu QC, Cheng J, Turksen K, Degenstein L, Hutton E, Fuchs E. 1995. The basal keratin network of stratified squamous epithelia: defining K15 function in the absence of K14. J Cell Biol 129:1329-1344.
    • (1995) J Cell Biol , vol.129 , pp. 1329-1344
    • Lloyd, C.1    Yu, Q.C.2    Cheng, J.3    Turksen, K.4    Degenstein, L.5    Hutton, E.6    Fuchs, E.7
  • 143
    • 0029115343 scopus 로고
    • Signal transduction by the α6β4 integrin: Distinct β4 subunit sites mediate recruitment of Shc/Grβ2 and association with the cytoskeleton of hemidesmosomes
    • Mainiero F, Pepe A, Wary KK, Spinardi L, Mohammadi M, Schlessinger J, Giancotti FG. 1995. Signal transduction by the α6β4 integrin: distinct β4 subunit sites mediate recruitment of Shc/Grβ2 and association with the cytoskeleton of hemidesmosomes. EMBO J 14:4470-4481.
    • (1995) EMBO J , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.G.7
  • 144
    • 0020618286 scopus 로고
    • Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells
    • Malinoff HL, Wicha MS. 1983. Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells. J Cell Biol 96:1475-1479.
    • (1983) J Cell Biol , vol.96 , pp. 1475-1479
    • Malinoff, H.L.1    Wicha, M.S.2
  • 145
    • 0030176080 scopus 로고    scopus 로고
    • Tyrosine phosphorylation induced by integrin-mediated adhesion of retinal neurons to laminin
    • Malosio ML, Del Curtis I. 1996. Tyrosine phosphorylation induced by integrin-mediated adhesion of retinal neurons to laminin. Int J Dev Neurosci 14:269-281.
    • (1996) Int J Dev Neurosci , vol.14 , pp. 269-281
    • Malosio, M.L.1    Del Curtis, I.2
  • 146
    • 0029988437 scopus 로고    scopus 로고
    • Synaptic integrins:selective association of the α1 and α7A and α7B subunits with the neuromuscular junction
    • Martin PT, Kaufman SJ, Kramer RH, Sanes JR. 1996. Synaptic integrins:selective association of the α1 and α7A and α7B subunits with the neuromuscular junction. Dev Biol 174:125-139.
    • (1996) Dev Biol , vol.174 , pp. 125-139
    • Martin, P.T.1    Kaufman, S.J.2    Kramer, R.H.3    Sanes, J.R.4
  • 148
    • 0028890992 scopus 로고
    • αv and α3 integrin subunits are associated with myofibrils during myofibrillogenesis
    • McDonald KA, Lakonishok M, Horwitz AF. 1995. αv and α3 integrin subunits are associated with myofibrils during myofibrillogenesis. J Cell Sci 108:2573-2581.
    • (1995) J Cell Sci , vol.108 , pp. 2573-2581
    • McDonald, K.A.1    Lakonishok, M.2    Horwitz, A.F.3
  • 149
    • 0029670673 scopus 로고    scopus 로고
    • Mutagenesis of ser41 to ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: Effects on cell adhesion and the composition of neurite cytoskeleton and membrane
    • Meiri KF, Hammang JP, Dent EW, Baetge EE. 1996. Mutagenesis of ser41 to ala inhibits the association of GAP-43 with the membrane skeleton of GAP-43-deficient PC12B cells: effects on cell adhesion and the composition of neurite cytoskeleton and membrane. J Neurobiol 29:213-232.
    • (1996) J Neurobiol , vol.29 , pp. 213-232
    • Meiri, K.F.1    Hammang, J.P.2    Dent, E.W.3    Baetge, E.E.4
  • 151
    • 0028802948 scopus 로고
    • Laminin receptors: Achieving specificity through cooperation
    • Mercurio AM. 1995. Laminin receptors: achieving specificity through cooperation Trends Cell Biol 5:419-424.
    • (1995) Trends Cell Biol , vol.5 , pp. 419-424
    • Mercurio, A.M.1
  • 152
    • 0026671599 scopus 로고
    • Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies
    • Meyer RA, Laird DW, Revel JP, Johnson RG. 1992. Inhibition of gap junction and adherens junction assembly by connexin and A-CAM antibodies J Cell Biol 119:179-189.
    • (1992) J Cell Biol , vol.119 , pp. 179-189
    • Meyer, R.A.1    Laird, D.W.2    Revel, J.P.3    Johnson, R.G.4
  • 154
    • 0033372459 scopus 로고    scopus 로고
    • Organization of the myotendinous junction is dependent on the presence of α7β1 integrin
    • Miosge N, Klenczar C, Herken R, Willem M, Mayer U. 1999. Organization of the myotendinous junction is dependent on the presence of α7β1 integrin. Lab Invest 79:1591-1599.
    • (1999) Lab Invest , vol.79 , pp. 1591-1599
    • Miosge, N.1    Klenczar, C.2    Herken, R.3    Willem, M.4    Mayer, U.5
  • 155
  • 156
    • 0033553906 scopus 로고    scopus 로고
    • α-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability
    • Montanaro F, Lindenbaum M, Carbonetto S. 1999. α-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability. J Cell Biol 145:1325-1340.
    • (1999) J Cell Biol , vol.145 , pp. 1325-1340
    • Montanaro, F.1    Lindenbaum, M.2    Carbonetto, S.3
  • 158
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain
    • Murgia C, Blaikie P, Kim N, Dans M, Petrie HT, Giancotti FG. 1998. Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain. EMBO J 17:3940-3951.
    • (1998) EMBO J , vol.17 , pp. 3940-3951
    • Murgia, C.1    Blaikie, P.2    Kim, N.3    Dans, M.4    Petrie, H.T.5    Giancotti, F.G.6
  • 159
    • 0032586951 scopus 로고    scopus 로고
    • Division of labor among the α6β4 integrin, β1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells
    • Muschler J, Lochter A, Roskelley CD, Yurchenco P, Bissell MJ. 1999. Division of labor among the α6β4 integrin, β1 integrins, and an E3 laminin receptor to signal morphogenesis and beta-casein expression in mammary epithelial cells. Mol Biol Cell 10:2817-2828.
    • (1999) Mol Biol Cell , vol.10 , pp. 2817-2828
    • Muschler, J.1    Lochter, A.2    Roskelley, C.D.3    Yurchenco, P.4    Bissell, M.J.5
  • 160
    • 0029965589 scopus 로고    scopus 로고
    • A mechanism for regulation of melanoma invasion. Ligation of α6β1 integrin by laminin G peptides
    • Nakahara H, Nomizu M, Akiyama SK, Yamada Y, Yeh Y, Chen WT. 1996. A mechanism for regulation of melanoma invasion. Ligation of α6β1 integrin by laminin G peptides. J Biol Chem 271:27221-27224.
    • (1996) J Biol Chem , vol.271 , pp. 27221-27224
    • Nakahara, H.1    Nomizu, M.2    Akiyama, S.K.3    Yamada, Y.4    Yeh, Y.5    Chen, W.T.6
  • 161
    • 0031594710 scopus 로고    scopus 로고
    • Activation of beta1 integrin signaling stimulates tyrosine phosphorylation of p190RhoGAP and membrane-protrusive activities at invadopodia
    • Nakahara H, Mueller SC, Nomizu M, Yamada Y, Yeh Y, Chen WT. 1998. Activation of beta1 integrin signaling stimulates tyrosine phosphorylation of p190RhoGAP and membrane-protrusive activities at invadopodia. J Biol Chem 273:9-12.
    • (1998) J Biol Chem , vol.273 , pp. 9-12
    • Nakahara, H.1    Mueller, S.C.2    Nomizu, M.3    Yamada, Y.4    Yeh, Y.5    Chen, W.T.6
  • 162
    • 0032589363 scopus 로고    scopus 로고
    • α6β1 integrin expression in hepatocarcinoma cells: Regulation and role in cell adhesion and migration
    • Nejjari M, Hafdi Z, Dumortier J, Bringuier AF, Feldmann G, Scoazec JY. 1999. α6β1 integrin expression in hepatocarcinoma cells: regulation and role in cell adhesion and migration. Int J Cancer 83:518-525.
    • (1999) Int J Cancer , vol.83 , pp. 518-525
    • Nejjari, M.1    Hafdi, Z.2    Dumortier, J.3    Bringuier, A.F.4    Feldmann, G.5    Scoazec, J.Y.6
  • 165
    • 0029100640 scopus 로고
    • Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides
    • Nomizu M, Kim WH, Yamamura K, Utani A, Song SY, Otaka A, Roller PP, Kleinman HK, Yamada Y. 1995. Identification of cell binding sites in the laminin α1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides. J Biol Chem 270:20583-20590.
    • (1995) J Biol Chem , vol.270 , pp. 20583-20590
    • Nomizu, M.1    Kim, W.H.2    Yamamura, K.3    Utani, A.4    Song, S.Y.5    Otaka, A.6    Roller, P.P.7    Kleinman, H.K.8    Yamada, Y.9
  • 167
    • 0032517857 scopus 로고    scopus 로고
    • Release of cAMP gating by the α6β4 integrin stimulates lamellae formation and the chemotactoc migration of invasive carcinoma cells
    • O'Connor KL, Shaw LM, Mercurio AM. 1998. Release of cAMP gating by the α6β4 integrin stimulates lamellae formation and the chemotactoc migration of invasive carcinoma cells. J Cell Biol 143:1749-1760.
    • (1998) J Cell Biol , vol.143 , pp. 1749-1760
    • O'Connor, K.L.1    Shaw, L.M.2    Mercurio, A.M.3
  • 168
    • 0034707597 scopus 로고    scopus 로고
    • RhoA function in lamellae formation and migration is regulated by the α6β4 integrin and cAMP metabolism
    • O'Connor KL, Nguyen BK, Mercurio AM. 2000. RhoA function in lamellae formation and migration is regulated by the α6β4 integrin and cAMP metabolism. J Cell Biol 148:253-258.
    • (2000) J Cell Biol , vol.148 , pp. 253-258
    • O'Connor, K.L.1    Nguyen, B.K.2    Mercurio, A.M.3
  • 169
    • 0031448867 scopus 로고    scopus 로고
    • Expression of tetra-spans transmembrane family (CD9, CD37, CD53, CD63, CD81 and CD82) in normal and neoplastic human keratinocytes: An association of CD9 with α3β1 integrin
    • Okochi H, Kato M, Nashiro K, Yoshie O, Miyazono K, Furue M. 1997. Expression of tetra-spans transmembrane family (CD9, CD37, CD53, CD63, CD81 and CD82) in normal and neoplastic human keratinocytes: an association of CD9 with α3β1 integrin. Br J Dermatol 137:856-863.
    • (1997) Br J Dermatol , vol.137 , pp. 856-863
    • Okochi, H.1    Kato, M.2    Nashiro, K.3    Yoshie, O.4    Miyazono, K.5    Furue, M.6
  • 170
    • 0031868639 scopus 로고    scopus 로고
    • Human colonic cancer cells synthesize and adhere to laminin-5: Their adhesion to laminin-5 involves multiple receptors among which is integrin α2β1
    • Orian-Rousseau V, Aberdam D, Rousselle P, Messent A, Gavrilovic J, Meneguzzi G, Kedinger M, Simon-Assmann P. 1998. Human colonic cancer cells synthesize and adhere to laminin-5: Their adhesion to laminin-5 involves multiple receptors among which is integrin α2β1. J Cell Sci 111:1993-2004.
    • (1998) J Cell Sci , vol.111 , pp. 1993-2004
    • Orian-Rousseau, V.1    Aberdam, D.2    Rousselle, P.3    Messent, A.4    Gavrilovic, J.5    Meneguzzi, G.6    Kedinger, M.7    Simon-Assmann, P.8
  • 171
    • 0027981988 scopus 로고
    • Collagens, integrins and the mesenchymal drift in glioblastomas: A comparison of biopsy specimens, spheroid and early monolayer cultures
    • Paulus W, Huettner C, Tonn JC. 1994. Collagens, integrins and the mesenchymal drift in glioblastomas: a comparison of biopsy specimens, spheroid and early monolayer cultures. Int J Cancer 58:841-846.
    • (1994) Int J Cancer , vol.58 , pp. 841-846
    • Paulus, W.1    Huettner, C.2    Tonn, J.C.3
  • 174
    • 0030919887 scopus 로고    scopus 로고
    • Genomic organization of the integjrin β4 gene ITGB4: A homozygous splice-site mutation in a patient with junctional epidermolysis bullosa associated with pyloric atresia
    • Pulkkinen L, Kurtz K, Xu Y, Bruckner-Tuderman L, Uitto J. 1997. Genomic organization of the integjrin β4 gene ITGB4): a homozygous splice-site mutation in a patient with junctional epidermolysis bullosa associated with pyloric atresia. Lab Invest 76: 823-833.
    • (1997) Lab Invest , vol.76 , pp. 823-833
    • Pulkkinen, L.1    Kurtz, K.2    Xu, Y.3    Bruckner-Tuderman, L.4    Uitto, J.5
  • 175
    • 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. 1997. 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 139:1873-1884.
    • (1997) J Cell Biol , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 176
    • 0028970987 scopus 로고
    • Integrin α6 expression in human prostate carcinoma cells is associated with a migratory and invasive phenotype in vitro and in vivo
    • Rabinovitz I, Nagle RB, Cress AE. 1995. Integrin α6 expression in human prostate carcinoma cells is associated with a migratory and invasive phenotype in vitro and in vivo. Clin Exp Metast 13:481-491.
    • (1995) Clin Exp Metast , vol.13 , pp. 481-491
    • Rabinovitz, I.1    Nagle, R.B.2    Cress, A.E.3
  • 177
    • 0032845770 scopus 로고    scopus 로고
    • Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells
    • Rabinovitz I, Toker A, Mercurio AM. 1999. Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells. J Cell Biol 146:1147-1160.
    • (1999) J Cell Biol , vol.146 , pp. 1147-1160
    • Rabinovitz, I.1    Toker, A.2    Mercurio, A.M.3
  • 179
    • 0023150560 scopus 로고
    • Distribution of laminin and fibronectin along peripheral trigeminal axon pathways in the developing chick
    • Riggott MJ, Moody SA. 1987. Distribution of laminin and fibronectin along peripheral trigeminal axon pathways in the developing chick. J Comp Neurol 258:580-596.
    • (1987) J Comp Neurol , vol.258 , pp. 580-596
    • Riggott, M.J.1    Moody, S.A.2
  • 180
    • 0033121316 scopus 로고    scopus 로고
    • Biogenesis of α6β4 integrin in a human colonic adenocarcinoma cell line involvement of calnexin
    • Rigot V, Andre F, Lehmann M, Lissitzky JC, Marvaldi J, Luis J. 1999. Biogenesis of α6β4 integrin in a human colonic adenocarcinoma cell line involvement of calnexin. Eur J Biochem 261:659-666.
    • (1999) Eur J Biochem , vol.261 , pp. 659-666
    • Rigot, V.1    Andre, F.2    Lehmann, M.3    Lissitzky, J.C.4    Marvaldi, J.5    Luis, J.6
  • 181
    • 0032529848 scopus 로고    scopus 로고
    • Loss of β1 integrin function results in retardation of myogenic, but an acceleration of neuronal, differentiation of embryonic stem cells in vitro
    • Rohwedel J, Guan K, Zuschratter W, Jin S, Ahnert-Hilger G, Fursyt D, Fassler R, Wobus AM. 1998. Loss of β1 integrin function results in retardation of myogenic, but an acceleration of neuronal, differentiation of embryonic stem cells in vitro. Dev Biol 201:167-184.
    • (1998) Dev Biol , vol.201 , pp. 167-184
    • Rohwedel, J.1    Guan, K.2    Zuschratter, W.3    Jin, S.4    Ahnert-Hilger, G.5    Fursyt, D.6    Fassler, R.7    Wobus, A.M.8
  • 182
    • 0034651015 scopus 로고    scopus 로고
    • Soluble VCAM-1 binding to α4 integrins is cell-type specific and activation dependent and is disrupted during apoptosis in T cells
    • Rose DM, Cardarelli PM, Cobb RR, Ginsberg MH. 2000. Soluble VCAM-1 binding to α4 integrins is cell-type specific and activation dependent and is disrupted during apoptosis in T cells. Blood 95: 602-609.
    • (2000) Blood , vol.95 , pp. 602-609
    • Rose, D.M.1    Cardarelli, P.M.2    Cobb, R.R.3    Ginsberg, M.H.4
  • 183
    • 0026266264 scopus 로고
    • Up-regulation of the integrin α1β1 in human neuroblastoma cells differentiated by retinoic acid: Correlation with increased neurite outgrowth response to laminin
    • Rossino P, Defilippi P, Silengo L, Tarone G. 1991. Up-regulation of the integrin α1β1 in human neuroblastoma cells differentiated by retinoic acid: correlation with increased neurite outgrowth response to laminin. Cell Regul 2:1021-1033.
    • (1991) Cell Regul , vol.2 , pp. 1021-1033
    • Rossino, P.1    Defilippi, P.2    Silengo, L.3    Tarone, G.4
  • 184
    • 0030816279 scopus 로고    scopus 로고
    • Transendothelial migration induces rapid expression on neutrophils of granule-release VLA6 used for tissue infiltration
    • Roussel E, Gingras MC. 1997. Transendothelial migration induces rapid expression on neutrophils of granule-release VLA6 used for tissue infiltration. J Leuk Biol 62:356-362.
    • (1997) J Leuk Biol , vol.62 , pp. 356-362
    • Roussel, E.1    Gingras, M.C.2
  • 185
    • 0028979458 scopus 로고
    • α6 integrins participate in pro-T cell homing to the thymus
    • Ruiz P, Wiles MV, Imhof BA. 1995. α6 integrins participate in pro-T cell homing to the thymus. Eur J Immunol 25:2034-2041.
    • (1995) Eur J Immunol , vol.25 , pp. 2034-2041
    • Ruiz, P.1    Wiles, M.V.2    Imhof, B.A.3
  • 187
    • 0033600748 scopus 로고    scopus 로고
    • Activation of c-Raf-1 kinase signal transduction pathway in α7 integrin-deficient mice
    • Saher G, Hildt E. 1999. Activation of c-Raf-1 kinase signal transduction pathway in α7 integrin-deficient mice. J Biol Chem 274:27651-27657.
    • (1999) J Biol Chem , vol.274 , pp. 27651-27657
    • Saher, G.1    Hildt, E.2
  • 188
    • 0028007259 scopus 로고
    • A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells
    • Salmivirta M, Mali M, Heino J, Hermonen J, Jalkanen M. 1994. A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells. Exp Cell Res 215:180-188.
    • (1994) Exp Cell Res , vol.215 , pp. 180-188
    • Salmivirta, M.1    Mali, M.2    Heino, J.3    Hermonen, J.4    Jalkanen, M.5
  • 190
    • 0031846576 scopus 로고    scopus 로고
    • Deficiency of β1 integrins in teratoma interferes with basement membrane assembly and laminin-1 expression
    • Sasaki T, Forsberg E, Bloch W, Addicks K, Fassler R, Timpl R. 1998. Deficiency of β1 integrins in teratoma interferes with basement membrane assembly and laminin-1 expression. Exp Cell Res 238:70-81.
    • (1998) Exp Cell Res , vol.238 , pp. 70-81
    • Sasaki, T.1    Forsberg, E.2    Bloch, W.3    Addicks, K.4    Fassler, R.5    Timpl, R.6
  • 191
    • 0029664439 scopus 로고    scopus 로고
    • Integrin α subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation
    • Sastry SK, Lakonishok M, Thomas DA, Muschler J, Horwitz AF. 1996. Integrin α subunit ratios, cytoplasmic domains, and growth factor synergy regulate muscle proliferation and differentiation. J Cell Biol 133:169-184.
    • (1996) J Cell Biol , vol.133 , pp. 169-184
    • Sastry, S.K.1    Lakonishok, M.2    Thomas, D.A.3    Muschler, J.4    Horwitz, A.F.5
  • 193
    • 0032514156 scopus 로고    scopus 로고
    • Hemidesmosome formation is initiated by the β4 integrin subunit, requires complex formation of β4 and HD1/plectin, and involves a direct interaction between β4 and the bullous pemphigoid antigen 180
    • Schaapveld RQ, Borradori L, Geerts D, van Leusden MR, Kuikman I, Nievers MG, Niessen CM, Steenbergen RD, Snijders PJ, Sonnenberg A. 1998. Hemidesmosome formation is initiated by the β4 integrin subunit, requires complex formation of β4 and HD1/plectin, and involves a direct interaction between β4 and the bullous pemphigoid antigen 180. J Cell Biol 142:271-284.
    • (1998) J Cell Biol , vol.142 , pp. 271-284
    • Schaapveld, R.Q.1    Borradori, L.2    Geerts, D.3    Van Leusden, M.R.4    Kuikman, I.5    Nievers, M.G.6    Niessen, C.M.7    Steenbergen, R.D.8    Snijders, P.J.9    Sonnenberg, A.10
  • 194
    • 0030021514 scopus 로고    scopus 로고
    • CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6β1 integrin and the neural adhesion molecule L1
    • Schmidt C, Kunemund V, Wintergerst ES, Schmitz B, Schachner M. 1996. CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6β1 integrin and the neural adhesion molecule L1. J Neurosci Res 43:12-31.
    • (1996) J Neurosci Res , vol.43 , pp. 12-31
    • Schmidt, C.1    Kunemund, V.2    Wintergerst, E.S.3    Schmitz, B.4    Schachner, M.5
  • 195
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder SM, Burridge K. 1999. Bidirectional signaling between the cytoskeleton and integrins. Curr Opin Cell Biol 11:274-286.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 196
    • 0032910337 scopus 로고    scopus 로고
    • Interactions between mitogenic stimuli, or, a thousand and one connections
    • Schwartz MA, Baron V. 1999. Interactions between mitogenic stimuli, or, a thousand and one connections. Curr Opin Cell Biol 11:197-202.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 197-202
    • Schwartz, M.A.1    Baron, V.2
  • 197
    • 0033535485 scopus 로고    scopus 로고
    • Basement membranes: Putting up the barriers
    • Schwarzbauer J. 1999. Basement membranes: putting up the barriers. Curr Biol 9:R242-R244.
    • (1999) Curr Biol , vol.9
    • Schwarzbauer, J.1
  • 198
    • 0031459892 scopus 로고    scopus 로고
    • Angiogenesis promoted by vascular endothelial growth factor: Regulation through α1β1 and α2β1 integrins
    • Senger DR, Claffey KP, Benes JE, Perruzzi CA, Sergiou AP, Detmar M. 1997. Angiogenesis promoted by vascular endothelial growth factor: regulation through α1β1 and α2β1 integrins. Proc Natl Acad Sci USA 94:13612-13617.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13612-13617
    • Senger, D.R.1    Claffey, K.P.2    Benes, J.E.3    Perruzzi, C.A.4    Sergiou, A.P.5    Detmar, M.6
  • 199
    • 0028855095 scopus 로고
    • Polarized expression and basic fibroblast growth factor-induced downregulation of the α6β4 integrin complex on human microvascular endothelial cells
    • Sepp NT, Cornelius LA, Romani N, Li LJ, Caughman SW, Lawley TJ, Swerlick RA. 1995. Polarized expression and basic fibroblast growth factor-induced downregulation of the α6β4 integrin complex on human microvascular endothelial cells. J Invest Dermatol 104: 266-270.
    • (1995) J Invest Dermatol , vol.104 , pp. 266-270
    • Sepp, N.T.1    Cornelius, L.A.2    Romani, N.3    Li, L.J.4    Caughman, S.W.5    Lawley, T.J.6    Swerlick, R.A.7
  • 200
    • 0032979447 scopus 로고    scopus 로고
    • The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway
    • Sethi T, Ginsberg MH, Downward J, Hughes PE. 1999. The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway. Mol Biol Cell 10:1799-1809.
    • (1999) Mol Biol Cell , vol.10 , pp. 1799-1809
    • Sethi, T.1    Ginsberg, M.H.2    Downward, J.3    Hughes, P.E.4
  • 201
    • 0031471678 scopus 로고    scopus 로고
    • Integrin signaling in vascular biology
    • Shattil SJ, Ginsberg MH. 1997. Integrin signaling in vascular biology. J Clin Invest 100:591-595.
    • (1997) J Clin Invest , vol.100 , pp. 591-595
    • Shattil, S.J.1    Ginsberg, M.H.2
  • 202
    • 0029874916 scopus 로고    scopus 로고
    • Analysis of integrin expression on oligodendrocytes during axo-glial interaction by using rat-mouse xenocultures
    • Shaw CE, Milner R, Compston AS, ffrench-Constant C. 1996. Analysis of integrin expression on oligodendrocytes during axo-glial interaction by using rat-mouse xenocultures. J Neurosci 16:1163-1172.
    • (1996) J Neurosci , vol.16 , pp. 1163-1172
    • Shaw, C.E.1    Milner, R.2    Compston, A.S.3    Ffrench-Constant, C.4
  • 203
    • 0027332373 scopus 로고
    • Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of the α6 subunit
    • Shaw LM, Mercurio AM. 1993. Regulation of α6β1 integrin laminin receptor function by the cytoplasmic domain of the α6 subunit. J Cell Biol 123:1017-1025.
    • (1993) J Cell Biol , vol.123 , pp. 1017-1025
    • Shaw, L.M.1    Mercurio, A.M.2
  • 204
    • 0028356999 scopus 로고
    • Regulation of cellular interactions with laminin by integrin cytoplasmic domains: The A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology and migration of macrophages
    • Shaw LM, Mercurio AM. 1994. Regulation of cellular interactions with laminin by integrin cytoplasmic domains: the A and B structural variants of the α6β1 integrin differentially modulate the adhesive strength, morphology and migration of macrophages. Mol Biol Cell 5:679-690.
    • (1994) Mol Biol Cell , vol.5 , pp. 679-690
    • Shaw, L.M.1    Mercurio, A.M.2
  • 205
    • 0025336326 scopus 로고
    • The activation dependent adhesion of macrophages to laminin involves cytoskeletal anchoring and phosphorylate of the α6β1 integrin
    • Shaw LM, Messier JM, Mercurio AM. 1990. The activation dependent adhesion of macrophages to laminin involves cytoskeletal anchoring and phosphorylate of the α6β1 integrin. J Cell Biol 110:2167-2174.
    • (1990) J Cell Biol , vol.110 , pp. 2167-2174
    • Shaw, L.M.1    Messier, J.M.2    Mercurio, A.M.3
  • 206
    • 0027258613 scopus 로고
    • Inside-out integrin signaling in macrophages. Analysis of the role of the α6Aβ1 and α6Bβ1 integrin variants in laminin adhesion by cDNA expression in an α6 integrin-deficient macrophage cell line
    • Shaw LM, Lotz MM, Mercurio AM. 1993. Inside-out integrin signaling in macrophages. Analysis of the role of the α6Aβ1 and α6Bβ1 integrin variants in laminin adhesion by cDNA expression in an α6 integrin-deficient macrophage cell line. J Biol Chem 268:11401-11408.
    • (1993) J Biol Chem , vol.268 , pp. 11401-11408
    • Shaw, L.M.1    Lotz, M.M.2    Mercurio, A.M.3
  • 207
    • 0028970786 scopus 로고
    • The α6Aβ1 and α6Bβ1 integrin variants signal differences in the tyrosine phosphorylation of paxillin and other proteins
    • Shaw LM, Turner CE, Mercurio AM. 1995. The α6Aβ1 and α6Bβ1 integrin variants signal differences in the tyrosine phosphorylation of paxillin and other proteins. J Biol Chem 270:23648-23652.
    • (1995) J Biol Chem , vol.270 , pp. 23648-23652
    • Shaw, L.M.1    Turner, C.E.2    Mercurio, A.M.3
  • 208
    • 0030063313 scopus 로고    scopus 로고
    • Function of the integrin α6β1 in metastatic breast carcinoma cells assessed by expression of a dominant-negative receptor
    • Shaw LM, Chao C, Wewer UM, Mercurio AM. 1996. Function of the integrin α6β1 in metastatic breast carcinoma cells assessed by expression of a dominant-negative receptor. Cancer Res 56:959-963.
    • (1996) Cancer Res , vol.56 , pp. 959-963
    • Shaw, L.M.1    Chao, C.2    Wewer, U.M.3    Mercurio, A.M.4
  • 209
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma cell invasion
    • Shaw LM, Rabinovitz I, Wang HH-F, Toker A, Mercurio AM. 1997. Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma cell invasion. Cell 91:949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.-F.3    Toker, A.4    Mercurio, A.M.5
  • 210
    • 0033597343 scopus 로고    scopus 로고
    • Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan
    • Shimizu H, Hosokawa H, Ninomiya H, Miner JH, Masaki T. 1999. Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J Biol Chem 274:11995-12000.
    • (1999) J Biol Chem , vol.274 , pp. 11995-12000
    • Shimizu, H.1    Hosokawa, H.2    Ninomiya, H.3    Miner, J.H.4    Masaki, T.5
  • 211
    • 0025363922 scopus 로고
    • Regulated expression and binding of three VLA (β1) integrin receptors on T cells
    • Shimizu Y, van Seventer GA, Horgan KJ, Shaw S. 1990. Regulated expression and binding of three VLA (β1) integrin receptors on T cells. Nature 345:250-253.
    • (1990) Nature , vol.345 , pp. 250-253
    • Shimizu, Y.1    Van Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 212
    • 0031765429 scopus 로고    scopus 로고
    • Diverse functions of vertebrate gap junctions
    • Simon AM, Goodenough DA. Diverse functions of vertebrate gap junctions. 1998. Trends Cell Biol 8:477-483.
    • (1998) Trends Cell Biol , vol.8 , pp. 477-483
    • Simon, A.M.1    Goodenough, D.A.2
  • 213
    • 0026347812 scopus 로고
    • Synthetic peptides from the carboxy-terminal globular domain of the A chain of laminin: Their ability to promote cell adhesion and neurite outgrowth, and interact with heparan and the β1 integrin subunit
    • Skubitz AP, Letourneau PC, Wayner E, Furcht LT. 1991. Synthetic peptides from the carboxy-terminal globular domain of the A chain of laminin: their ability to promote cell adhesion and neurite outgrowth, and interact with heparan and the β1 integrin subunit. J Cell Biol 115:1137-1148.
    • (1991) J Cell Biol , vol.115 , pp. 1137-1148
    • Skubitz, A.P.1    Letourneau, P.C.2    Wayner, E.3    Furcht, L.T.4
  • 214
    • 0029896841 scopus 로고    scopus 로고
    • Human SY5Y neuroblastoma cell interactions with laminin isoforms: Neurite outgrowth on laminin-5 is mediated by integrin α3β1
    • Smith BE, Bradshaw AD, Choi ES, Rouselle P, Wayner EA, Clegg DO. 1996. Human SY5Y neuroblastoma cell interactions with laminin isoforms: neurite outgrowth on laminin-5 is mediated by integrin α3β1. Cell Adhes Commun 3:451-462.
    • (1996) Cell Adhes Commun , vol.3 , pp. 451-462
    • Smith, B.E.1    Bradshaw, A.D.2    Choi, E.S.3    Rouselle, P.4    Wayner, E.A.5    Clegg, D.O.6
  • 215
    • 0026591586 scopus 로고
    • H36-α7 is a novel integrin a chain that is developmentally regulated during skeletal myogenesis
    • Song WK, Wang W, Foster RF, Bielser DA, Kaufman SJ. 1992. H36-α7 is a novel integrin a chain that is developmentally regulated during skeletal myogenesis. J Cell Biol 117:643-657.
    • (1992) J Cell Biol , vol.117 , pp. 643-657
    • Song, W.K.1    Wang, W.2    Foster, R.F.3    Bielser, D.A.4    Kaufman, S.J.5
  • 216
    • 0027787640 scopus 로고
    • Expression of α7 integrin cytoplasmic domains during skeletal muscle development: Alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases
    • Song WK, Wang W, Sato H, Bielser DA, Kaufman SJ. 1993. Expression of α7 integrin cytoplasmic domains during skeletal muscle development: alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases. J Cell Sci 106:1139-1152.
    • (1993) J Cell Sci , vol.106 , pp. 1139-1152
    • Song, W.K.1    Wang, W.2    Sato, H.3    Bielser, D.A.4    Kaufman, S.J.5
  • 217
    • 0023812375 scopus 로고
    • Laminin receptor on platelets is the integrin VLA-6
    • Sonnenberg A, Modderman PW, Hogervorst F. 1988. Laminin receptor on platelets is the integrin VLA-6. Nature 336:487-489.
    • (1988) Nature , vol.336 , pp. 487-489
    • Sonnenberg, A.1    Modderman, P.W.2    Hogervorst, F.3
  • 219
    • 0026338891 scopus 로고
    • Isolation of α6β1 integrins from platelets and adherent cells by affinity chromatography on mouse laminin fragment E8 and human laminin pepsin fragment
    • Sonnenberg A, Gehlsen KR, Aumailley M, Timpl R. 1991b. Isolation of α6β1 integrins from platelets and adherent cells by affinity chromatography on mouse laminin fragment E8 and human laminin pepsin fragment. Exp Cell Res 197:234-244.
    • (1991) Exp Cell Res , vol.197 , pp. 234-244
    • Sonnenberg, A.1    Gehlsen, K.R.2    Aumailley, M.3    Timpl, R.4
  • 220
    • 0034071069 scopus 로고    scopus 로고
    • Disruption of the basement membrane after corneal debridement
    • Sta Iglesia DD, Stepp MA. 2000. Disruption of the basement membrane after corneal debridement. Invest Ophthalmol Vis Sci (41: 1045-1053).
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 1045-1053
    • Sta Iglesia, D.D.1    Stepp, M.A.2
  • 221
    • 0033053121 scopus 로고    scopus 로고
    • Plectin: A cytolinker by design
    • Steinbock FA, Wiche G. 1999. Plectin: a cytolinker by design. Biol Chem 380:151-158.
    • (1999) Biol Chem , vol.380 , pp. 151-158
    • Steinbock, F.A.1    Wiche, G.2
  • 223
    • 84907112148 scopus 로고
    • Expression of α4 integrin mRNA and protein and fibronectin in the early chicken embryo
    • Stepp MA, Urry LA, Hynes RO. 1994. Expression of α4 integrin mRNA and protein and fibronectin in the early chicken embryo. Cell Adhes Commun 2:359-375.
    • (1994) Cell Adhes Commun , vol.2 , pp. 359-375
    • Stepp, M.A.1    Urry, L.A.2    Hynes, R.O.3
  • 224
    • 0029739492 scopus 로고    scopus 로고
    • Changes in β4 integrin expression and localization in vivo in response to corneal epithelial injury
    • Stepp MA, Zhu L, Cranfill R. 1996. Changes in β4 integrin expression and localization in vivo in response to corneal epithelial injury. Invest Ophthalmol Vis Sci 37:1593-1601.
    • (1996) Invest Ophthalmol Vis Sci , vol.37 , pp. 1593-1601
    • Stepp, M.A.1    Zhu, L.2    Cranfill, R.3
  • 226
    • 0033588545 scopus 로고    scopus 로고
    • Function of alphα3beta1-tetraspanin protein complexes in tumor cell invasion. Evidence for the role of the complexes in production of matrix metalloproteinase 2 (MMP-2)
    • Sugiura T, Berditchevski F. 1999. Function of alphα3beta1-tetraspanin protein complexes in tumor cell invasion. Evidence for the role of the complexes in production of matrix metalloproteinase 2 (MMP-2). J Cell Biol 146:1375-1389.
    • (1999) J Cell Biol , vol.146 , pp. 1375-1389
    • Sugiura, T.1    Berditchevski, F.2
  • 227
    • 0028945659 scopus 로고
    • Modulation of epidermal differentiation by epiligrin and integrin α3β1
    • Symington BE, Carter WG. 1995. Modulation of epidermal differentiation by epiligrin and integrin α3β1. J Cell Sci 108:831-838.
    • (1995) J Cell Sci , vol.108 , pp. 831-838
    • Symington, B.E.1    Carter, W.G.2
  • 228
    • 0027535633 scopus 로고
    • Interaction of integrins α3β1 and α2β1: Potential role in keratinocyte intercellular adhesion
    • Symington BE, Takada Y, Carter WG. 1993. Interaction of integrins α3β1 and α2β1: potential role in keratinocyte intercellular adhesion. J Cell Biol 120:523-535.
    • (1993) J Cell Biol , vol.120 , pp. 523-535
    • Symington, B.E.1    Takada, Y.2    Carter, W.G.3
  • 229
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • Tachibana I, Hemler ME. 1999. Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J Cell Biol 146:893-904.
    • (1999) J Cell Biol , vol.146 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 230
    • 0032847081 scopus 로고    scopus 로고
    • Mutation of a basic sequence in the laminin α2LG3 module leads to a lack of proteolytic processing and has different effects on β1 integrin-mediated cell adhesion and α-dystroglycan binding
    • Talts JF, Timpl R. 1999. Mutation of a basic sequence in the laminin α2LG3 module leads to a lack of proteolytic processing and has different effects on β1 integrin-mediated cell adhesion and α-dystroglycan binding. FEBS Lett 458:319-323.
    • (1999) FEBS Lett , vol.458 , pp. 319-323
    • Talts, J.F.1    Timpl, R.2
  • 231
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin alpha1 and alphα2 chains and perlecan to heparan, sulfatides, alpha-dystroglycan and several extracellular matrix proteins
    • Talts JF, Andac Z, Gohring W, Brancaccio A, Timpl R. 1999. Binding of the G domains of laminin alpha1 and alphα2 chains and perlecan to heparan, sulfatides, alpha-dystroglycan and several extracellular matrix proteins. EMBO J 18:863-870.
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Gohring, W.3    Brancaccio, A.4    Timpl, R.5
  • 233
    • 0025720737 scopus 로고
    • Cell type-specific integrin variants with alternative α chain cytoplasmic domains
    • Tamura RN, Cooper HM, Collo G, Quaranta V. 1991. Cell type-specific integrin variants with alternative α chain cytoplasmic domains. Proc Natl Acad Sci USA 88:10183-10187.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10183-10187
    • Tamura, R.N.1    Cooper, H.M.2    Collo, G.3    Quaranta, V.4
  • 234
    • 0033562972 scopus 로고    scopus 로고
    • An IKLLI-containing peptide derived from the laminin α1 chain mediating heparan-binding, cell adhesion, neurite outgrowth and proliferation, represents a binding site for integrin α3β1 and heparan sulphate proteoglycan
    • Tashiro K, Monji A, Yoshida I, Hayashi Y, Matsuda K, Tashiro N, Mitsuyama Y. 1999. An IKLLI-containing peptide derived from the laminin α1 chain mediating heparan-binding, cell adhesion, neurite outgrowth and proliferation, represents a binding site for integrin α3β1 and heparan sulphate proteoglycan. Biochem J 340:119-126.
    • (1999) Biochem J , vol.340 , pp. 119-126
    • Tashiro, K.1    Monji, A.2    Yoshida, I.3    Hayashi, Y.4    Matsuda, K.5    Tashiro, N.6    Mitsuyama, Y.7
  • 237
    • 0028828282 scopus 로고
    • Expression patterns of laminin receptor splice variants α6Aβ1 and α6Bβ1 suggest different roles in mouse development
    • Thorsteinsdottir S, Roelen BA, Freund E, Gaspar AC, Sonnenberg A, Mummery CL. 1995. Expression patterns of laminin receptor splice variants α6Aβ1 and α6Bβ1 suggest different roles in mouse development. Dev Dyn 204:240-258.
    • (1995) Dev Dyn , vol.204 , pp. 240-258
    • Thorsteinsdottir, S.1    Roelen, B.A.2    Freund, E.3    Gaspar, A.C.4    Sonnenberg, A.5    Mummery, C.L.6
  • 238
    • 0027332964 scopus 로고
    • Expression of β1 integrins in sensory neurons of the dorsal root ganglion and their functions in neurite outgrowth on two laminin isoforms
    • Tomaselli KJ, Doherty P, Emmett CJ, Damsky CH, Walsh FS, Reichardt LF. 1993. Expression of β1 integrins in sensory neurons of the dorsal root ganglion and their functions in neurite outgrowth on two laminin isoforms. J Neurosci 13:4880-4888.
    • (1993) J Neurosci , vol.13 , pp. 4880-4888
    • Tomaselli, K.J.1    Doherty, P.2    Emmett, C.J.3    Damsky, C.H.4    Walsh, F.S.5    Reichardt, L.F.6
  • 239
    • 0029143059 scopus 로고
    • Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin
    • Underwood PA, Bennett FA, Kirkpatrick A, Bean PA, Moss BA. 1995. Evidence for the location of a binding sequence for the α2β1 integrin of endothelial cells, in the β1 subunit of laminin. Biochem J 309:765-771.
    • (1995) Biochem J , vol.309 , pp. 765-771
    • Underwood, P.A.1    Bennett, F.A.2    Kirkpatrick, A.3    Bean, P.A.4    Moss, B.A.5
  • 240
    • 0027153138 scopus 로고
    • Melanocyte tumor progression is associated with changes in angiogenesis and expression of the 67-kilodalton laminin receptor
    • Vacca A, Ribatti D, Roncali L, Lospalluti M, Serio G, Carrel S, Dammacco F. 1993. Melanocyte tumor progression is associated with changes in angiogenesis and expression of the 67-kilodalton laminin receptor. Cancer 72:455-61
    • (1993) Cancer , vol.72 , pp. 455-461
    • Vacca, A.1    Ribatti, D.2    Roncali, L.3    Lospalluti, M.4    Serio, G.5    Carrel, S.6    Dammacco, F.7
  • 241
    • 0029794008 scopus 로고    scopus 로고
    • Merosin and laminin in myogenesis: Specific requirement for merosin in myotube stability and survival
    • Vachon PH, Loechel F, Xu H, Wewer UM, Engvall E. 1996. Merosin and laminin in myogenesis: specific requirement for merosin in myotube stability and survival. J Cell Biol 134:1483-1497.
    • (1996) J Cell Biol , vol.134 , pp. 1483-1497
    • Vachon, P.H.1    Loechel, F.2    Xu, H.3    Wewer, U.M.4    Engvall, E.5
  • 242
    • 0030610576 scopus 로고    scopus 로고
    • Integrin α7β1 in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy
    • Vachon PH, Xu H, Liu L, Loechel F, Hayashi Y, Arahata K, Reed JC, Wewer UM, Engvall E. 1997. Integrin α7β1 in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy. J Clin Invest 100:1870-1881.
    • (1997) J Clin Invest , vol.100 , pp. 1870-1881
    • Vachon, P.H.1    Xu, H.2    Liu, L.3    Loechel, F.4    Hayashi, Y.5    Arahata, K.6    Reed, J.C.7    Wewer, U.M.8    Engvall, E.9
  • 243
    • 0028984183 scopus 로고
    • A novel β1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle
    • van der Flier A, Kuikman I, Baudoin C, van der Neut R, Sonnenberg A. 1995. A novel β1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle. FEBS Lett 369:340-344.
    • (1995) FEBS Lett , vol.369 , pp. 340-344
    • Van Der Flier, A.1    Kuikman, I.2    Baudoin, C.3    Van Der Neut, R.4    Sonnenberg, A.5
  • 247
    • 0030658939 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor Tiam1 affects neuronal morphology; opposing roles for the small GTPases Rac and Rho
    • van Leeuwen FN, Kain HET, van der Kammen RA, Michiels F, Kranenburg OW, Collard JG. 1997. The guanine nucleotide exchange factor Tiam1 affects neuronal morphology; opposing roles for the small GTPases Rac and Rho. J Cell Biol 139:797-807.
    • (1997) J Cell Biol , vol.139 , pp. 797-807
    • Van Leeuwen, F.N.1    Kain, H.E.T.2    Van Der Kammen, R.A.3    Michiels, F.4    Kranenburg, O.W.5    Collard, J.G.6
  • 248
    • 0029958564 scopus 로고    scopus 로고
    • Distinct α7Aβ1 and α7Bβ1 integrin expression patterns during mouse development: α7A is restricted to skeletal muscle but α7B is expressed in striated muscle, vasculature and nervous system
    • Velling T, Collo G, Sorokin L, Durbeej M, Zhang H, Gullberg D. 1996. Distinct α7Aβ1 and α7Bβ1 integrin expression patterns during mouse development: α7A is restricted to skeletal muscle but α7B is expressed in striated muscle, vasculature and nervous system. Dev Dyn 207: 355-371.
    • (1996) Dev Dyn , vol.207 , pp. 355-371
    • Velling, T.1    Collo, G.2    Sorokin, L.3    Durbeej, M.4    Zhang, H.5    Gullberg, D.6
  • 251
    • 0027773003 scopus 로고
    • Integrins as differential cell lineage markers of primary liver tumors
    • Volpes R, van den Oord JJ, Desmet VJ. 1993. Integrins as differential cell lineage markers of primary liver tumors. Am J Pathol 142: 1483-1492.
    • (1993) Am J Pathol , vol.142 , pp. 1483-1492
    • Volpes, R.1    Van Den Oord, J.J.2    Desmet, V.J.3
  • 252
    • 0026354979 scopus 로고
    • Skeletal myoblasts utilize a novel β1-series integrin and not α6β1 for binding to the E8 and T8 fragments of laminin
    • von der Mark H, Durr A, Sonnenberg A, von der Mark K, Deutzmann R, Goodman SL. 1991. Skeletal myoblasts utilize a novel β1-series integrin and not α6β1 for binding to the E8 and T8 fragments of laminin. J Biol Chem 266:23593-23601.
    • (1991) J Biol Chem , vol.266 , pp. 23593-23601
    • Von Der Mark, H.1    Durr, A.2    Sonnenberg, A.3    Von Der Mark, K.4    Deutzmann, R.5    Goodman, S.L.6
  • 254
    • 0030584077 scopus 로고    scopus 로고
    • The adaptor protein She couples a class of integrins to the control of cell cycle progression
    • Wary KK, Mainiero F, Isakoff SJ, Marcantonio EE, Giancotti FG. 1996. The adaptor protein She couples a class of integrins to the control of cell cycle progression. Cell 87:733-743.
    • (1996) Cell , vol.87 , pp. 733-743
    • Wary, K.K.1    Mainiero, F.2    Isakoff, S.J.3    Marcantonio, E.E.4    Giancotti, F.G.5
  • 255
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • Wary KK, Mariotti A, Zurzolo C, Giancotti FG. 1998. A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell 94:625-634.
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 256
    • 0023555151 scopus 로고
    • Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique α and common β subunits
    • Wayner EA, Carter WG. 1987. Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique α and common β subunits. J Cell Biol 105:1873-1884.
    • (1987) J Cell Biol , vol.105 , pp. 1873-1884
    • Wayner, E.A.1    Carter, W.G.2
  • 257
    • 0027278234 scopus 로고
    • Epiligrin, a component of epithelial basement membranes, is an adhesive ligand for α3β1 positive T lymphocytes
    • Wayner EA, Gil SG, Murphy GF, Wilke MS, Carter WG. 1993. Epiligrin, a component of epithelial basement membranes, is an adhesive ligand for α3β1 positive T lymphocytes. J Cell Biol 121:1141-1152.
    • (1993) J Cell Biol , vol.121 , pp. 1141-1152
    • Wayner, E.A.1    Gil, S.G.2    Murphy, G.F.3    Wilke, M.S.4    Carter, W.G.5
  • 258
    • 0030936450 scopus 로고    scopus 로고
    • Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies
    • Weaver VM, Petersen OW, Wang F, Larabell CA, Briand P, Damsky C, Bissell MJ. 1997. Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies. J Cell Biol 137:231-245.
    • (1997) J Cell Biol , vol.137 , pp. 231-245
    • Weaver, V.M.1    Petersen, O.W.2    Wang, F.3    Larabell, C.A.4    Briand, P.5    Damsky, C.6    Bissell, M.J.7
  • 259
    • 0030902384 scopus 로고    scopus 로고
    • Integrin signaling in leukocytes: Lessons from the α6β1 integrin
    • Wei J, Shaw LM, Mercurio AM. 1997. Integrin signaling in leukocytes: lessons from the α6β1 integrin. J Leukoc Biol 61:397-407.
    • (1997) J Leukoc Biol , vol.61 , pp. 397-407
    • Wei, J.1    Shaw, L.M.2    Mercurio, A.M.3
  • 260
    • 0032489532 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinase activation by the cytoplasmic domain of the α6 integrin subunit
    • Wei J, Shaw LM, Mercurio AM. 1998. Regulation of mitogen-activated protein kinase activation by the cytoplasmic domain of the α6 integrin subunit. J Biol Chem 273:5903-5907.
    • (1998) J Biol Chem , vol.273 , pp. 5903-5907
    • Wei, J.1    Shaw, L.M.2    Mercurio, A.M.3
  • 261
    • 0030695152 scopus 로고    scopus 로고
    • The integrin α6β1 promotes the survival of metastatic human breast carcinoma cells in mice
    • Wewer UM, Shaw LM, Albrechtsen R, Mercurio AM. 1997. The integrin α6β1 promotes the survival of metastatic human breast carcinoma cells in mice. Am J Pathol 151:1191-1198.
    • (1997) Am J Pathol , vol.151 , pp. 1191-1198
    • Wewer, U.M.1    Shaw, L.M.2    Albrechtsen, R.3    Mercurio, A.M.4
  • 262
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche G. 1998. Role of plectin in cytoskeleton organization and dynamics. J Cell Sci 111:2477-2486.
    • (1998) J Cell Sci , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 263
    • 0033557895 scopus 로고    scopus 로고
    • Origin of the integrin-mediated signal transduction. Functional studies with cell cultures from the sponge Suberites domuncula
    • Wimmer W, Perovic S, Kruse M, Schroder HC, Krasko A, Batel R, Muller WE. 1999. Origin of the integrin-mediated signal transduction. Functional studies with cell cultures from the sponge Suberites domuncula. Eur J Biochem 260:156-165.
    • (1999) Eur J Biochem , vol.260 , pp. 156-165
    • Wimmer, W.1    Perovic, S.2    Kruse, M.3    Schroder, H.C.4    Krasko, A.5    Batel, R.6    Muller, W.E.7
  • 264
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada KM, Geiger B. 1997. Molecular interactions in cell adhesion complexes. Curr Opin Cell Biol 9:76-85.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 265
    • 0032482216 scopus 로고    scopus 로고
    • Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions
    • Yanez-Mo M, Alfranca A, Cabanas C, Marazuela M, Tejedor R, Ursa MA, Ashman LK, de Landazuri MO, Sanchez-Madrid F. 1998. Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions. J Cell Biol 141:791-804.
    • (1998) J Cell Biol , vol.141 , pp. 791-804
    • Yanez-Mo, M.1    Alfranca, A.2    Cabanas, C.3    Marazuela, M.4    Tejedor, R.5    Ursa, M.A.6    Ashman, L.K.7    De Landazuri, M.O.8    Sanchez-Madrid, F.9
  • 266
    • 0029661978 scopus 로고    scopus 로고
    • α7 integrin mediates cell adhesion and migration on specific laminin isoforms
    • Yao CC, Ziober BL, Squillace RM, Kramer RH. 1996a. α7 integrin mediates cell adhesion and migration on specific laminin isoforms. J Biol Chem 271:25598-25603.
    • (1996) J Biol Chem , vol.271 , pp. 25598-25603
    • Yao, C.C.1    Ziober, B.L.2    Squillace, R.M.3    Kramer, R.H.4
  • 267
    • 0030451425 scopus 로고    scopus 로고
    • Laminins promote the locomotion of skeletal myoblasts via the α7 integrin receptor
    • Yao CC, Ziober BL, Sutherland AE, Mendrick DL, Kramer RH. 1996b. Laminins promote the locomotion of skeletal myoblasts via the α7 integrin receptor. J Cell Sci 109:3139-3150.
    • (1996) J Cell Sci , vol.109 , pp. 3139-3150
    • Yao, C.C.1    Ziober, B.L.2    Sutherland, A.E.3    Mendrick, D.L.4    Kramer, R.H.5
  • 268
    • 0030835890 scopus 로고    scopus 로고
    • Functional expression of the α7 integrin receptor in differentiated smooth muscle cells
    • Yao CC, Breuss J, Pytela R, Kramer RH. 1997. Functional expression of the α7 integrin receptor in differentiated smooth muscle cells. J Cell Sci 110:1477-1487.
    • (1997) J Cell Sci , vol.110 , pp. 1477-1487
    • Yao, C.C.1    Breuss, J.2    Pytela, R.3    Kramer, R.H.4
  • 269
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable, and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration
    • Yauch RL, Berditchevski F, Harler MB, Reichner J, Hemler ME. 1998. Highly stoichiometric, stable, and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration. Mol Biol Cell 9:2751-2765.
    • (1998) Mol Biol Cell , vol.9 , pp. 2751-2765
    • Yauch, R.L.1    Berditchevski, F.2    Harler, M.B.3    Reichner, J.4    Hemler, M.E.5
  • 270
    • 0023190051 scopus 로고
    • In vivo guidance of regenerating nerve by laminin-coated filaments
    • Yoshii S, Yamamuro T, Ito S, Hayashi M. 1987. In vivo guidance of regenerating nerve by laminin-coated filaments. Exp Neurol 96: 469-473.
    • (1987) Exp Neurol , vol.96 , pp. 469-473
    • Yoshii, S.1    Yamamuro, T.2    Ito, S.3    Hayashi, M.4
  • 271
    • 0027471434 scopus 로고
    • Expression of integrin α1β1 is regulated by nerve growth factor and dexamethasone in PC12 cells. Functional consequences for adhesion and neurite outgrowth
    • Zhang Z, Tarone G, Turner DC. 1993. Expression of integrin α1β1 is regulated by nerve growth factor and dexamethasone in PC12 cells. Functional consequences for adhesion and neurite outgrowth. J Biol Chem 268:5557-5565.
    • (1993) J Biol Chem , vol.268 , pp. 5557-5565
    • Zhang, Z.1    Tarone, G.2    Turner, D.C.3
  • 273
    • 0028978745 scopus 로고
    • Novel isoform of β1 integrin expressed in skeletal and cardiac muscle
    • Zhidkova NI, Belkin AM, Mayne R. 1995. Novel isoform of β1 integrin expressed in skeletal and cardiac muscle. Biochem Biophys Res Commun 214:279-285.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 279-285
    • Zhidkova, N.I.1    Belkin, A.M.2    Mayne, R.3
  • 274
    • 0032920936 scopus 로고    scopus 로고
    • The syndecans, tuners of transmembrane signaling
    • Zimmermann P, David G. 1999. The syndecans, tuners of transmembrane signaling. FASEB J 13(Suppl):S91-S100.
    • (1999) FASEB J , vol.13 , Issue.SUPPL.
    • Zimmermann, P.1    David, G.2
  • 275
    • 0027454265 scopus 로고
    • Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development
    • Ziober BL, Vu MP, Waleh N, Crawford J, Lin CS, Kramer RH. 1993. Alternative extracellular and cytoplasmic domains of the integrin α7 subunit are differentially expressed during development. J Biol Chem 268:26773-26783.
    • (1993) J Biol Chem , vol.268 , pp. 26773-26783
    • Ziober, B.L.1    Vu, M.P.2    Waleh, N.3    Crawford, J.4    Lin, C.S.5    Kramer, R.H.6
  • 276
    • 0030840417 scopus 로고    scopus 로고
    • The laminin-binding activity of the α7 integin receptor is defined by developmentally regulated splicing in the extracellular domain
    • Ziober BL, Chen Y, Kramer RH. 1997. The laminin-binding activity of the α7 integin receptor is defined by developmentally regulated splicing in the extracellular domain. Mol Biol Cell 8:1723-1734.
    • (1997) Mol Biol Cell , vol.8 , pp. 1723-1734
    • Ziober, B.L.1    Chen, Y.2    Kramer, R.H.3
  • 277
    • 0033158929 scopus 로고    scopus 로고
    • Expression of the α7β1 laminin receptor suppresses melanoma growth and metastatic potential
    • Ziober BL, Chen Y, Ramos DM, Waleh N, Kramer RH. 1999. Expression of the α7β1 laminin receptor suppresses melanoma growth and metastatic potential. Cell Growth Differ 10:479-490.
    • (1999) Cell Growth Differ , vol.10 , pp. 479-490
    • Ziober, B.L.1    Chen, Y.2    Ramos, D.M.3    Waleh, N.4    Kramer, R.H.5
  • 278
    • 0027331555 scopus 로고
    • Integrin α7 as substrate for a glycosylphosphatidyl-inositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells
    • Zolkiewska A, Moss J. 1993. Integrin α7 as substrate for a glycosylphosphatidyl-inositol-anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J Biol Chem 268:25273-25276.
    • (1993) J Biol Chem , vol.268 , pp. 25273-25276
    • Zolkiewska, A.1    Moss, J.2


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