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Volumn 9, Issue 4, 1998, Pages 715-731

β-Integrin cytoplasmic subdomains involved in dominant negative function

Author keywords

[No Author keywords available]

Indexed keywords

FOCAL ADHESION KINASE; INTEGRIN; ISOPROTEIN; MANGANESE; MUTANT PROTEIN; ACTININ; ALPHA5 INTEGRIN; BETA1 INTEGRIN; BETA3 INTEGRIN; CD51 ANTIGEN; CELL ADHESION MOLECULE; FIBRINOGEN RECEPTOR; FIBRONECTIN; FOCAL ADHESION KINASE 1; LEUKOCYTE ANTIGEN; PROTEIN TYROSINE KINASE; PTK2 PROTEIN, MOUSE; RECOMBINANT PROTEIN; TALIN;

EID: 0031594784     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.4.715     Document Type: Article
Times cited : (63)

References (61)
  • 1
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama, S.K., Yamada, S.S., Chen, W.T., and Yamada, K.M. (1989). Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J. Cell Biol. 109, 863-875.
    • (1989) J. Cell Biol. , vol.109 , pp. 863-875
    • Akiyama, S.K.1    Yamada, S.S.2    Chen, W.T.3    Yamada, K.M.4
  • 2
    • 0028343192 scopus 로고
    • Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras
    • Akiyama, S.K., Yamada, S.S., Yamada, K.M., and LaFlamme, S.E. (1994). Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras. J. Biol. Chem. 269, 15961-15964.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15961-15964
    • Akiyama, S.K.1    Yamada, S.S.2    Yamada, K.M.3    LaFlamme, S.E.4
  • 3
    • 0025203926 scopus 로고
    • A human integrin β1 with a unique cytoplasmic domain generated by alternative mRNA processing
    • Altruda, F., Cervella, P., Tarone, G., Botta, C., Balzac, F., Stefanuto, G., and Silengo, L. (1990). A human integrin β1 with a unique cytoplasmic domain generated by alternative mRNA processing. Gene 95, 261-266.
    • (1990) Gene , vol.95 , pp. 261-266
    • Altruda, F.1    Cervella, P.2    Tarone, G.3    Botta, C.4    Balzac, F.5    Stefanuto, G.6    Silengo, L.7
  • 4
    • 0027406474 scopus 로고
    • Expression and functional analysis of a cytoplasmic domain variant of the β1 integrin subunit
    • Balzac, F., Belkin, A., Koteliansky, V., Balabanow, Y., Altruda, F., Silengo, L., and Tarone, G. (1993). Expression and functional analysis of a cytoplasmic domain variant of the β1 integrin subunit. J. Cell Biol. 211, 171-178.
    • (1993) J. Cell Biol. , vol.211 , pp. 171-178
    • Balzac, F.1    Belkin, A.2    Koteliansky, V.3    Balabanow, Y.4    Altruda, F.5    Silengo, L.6    Tarone, G.7
  • 5
    • 0028171267 scopus 로고
    • Expression of β1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility
    • Balzac, F., Retta, S.F., Albini, A., Melchiorri, A., Koteliansky, V., Geuna, M., Silengo, L., and Tarone, G. (1994). Expression of β1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility. J. Cell. Biol. 127, 557-565.
    • (1994) J. Cell. Biol. , vol.127 , pp. 557-565
    • Balzac, F.1    Retta, S.F.2    Albini, A.3    Melchiorri, A.4    Koteliansky, V.5    Geuna, M.6    Silengo, L.7    Tarone, G.8
  • 6
    • 0029837731 scopus 로고    scopus 로고
    • Genomic organization of the mouse beta 1 gene: Conservation of the beta1D but not of the beta 1B and beta 1C integrin splice variants
    • Baudoin, C., Van der Flier, A., Borradori, L., and Sonnenberg, A. (1996). Genomic organization of the mouse beta 1 gene: conservation of the beta1D but not of the beta 1B and beta 1C integrin splice variants. Cell Adhes. Commun. 4, 1-11.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 1-11
    • Baudoin, C.1    Van Der Flier, A.2    Borradori, L.3    Sonnenberg, A.4
  • 7
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni, G., Shih, D.T., Buck, C.A., and Hemler, M.E. (1995). Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270, 25570-25577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 8
    • 0029671374 scopus 로고    scopus 로고
    • β1D integrin displaced the β1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin, A.M., Zhidkova, N.I., Balzac, F., Altruda, F., Tomatis, D., Maier, A., Tarone, G., Koteliansky, V.E., and Burridge, K. (1996). β1D integrin displaced the β1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle 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
  • 9
    • 0024817189 scopus 로고
    • Construction and properties of an Epstein-Barr-virus-derived cDNA expression vector for human cells
    • Belt, P.B., Groeneveld, H., Teubel, W.J., Putte, v.d.P., and Backendorf, C. (1989). Construction and properties of an Epstein-Barr-virus-derived cDNA expression vector for human cells. Gene 84, 407-417.
    • (1989) Gene , vol.84 , pp. 407-417
    • Belt, P.B.1    Groeneveld, H.2    Teubel, W.J.3    Putte, V.D.P.4    Backendorf, C.5
  • 10
    • 0027154651 scopus 로고
    • Ligand-dependent and -independent integrin focal contact localization: The role of the a chain cytoplasmic domain
    • Briesewitz, R., Kern, A., and Marcantonio, E.E. (1993). Ligand-dependent and -independent integrin focal contact localization: the role of the a chain cytoplasmic domain. Mol. Biol. Cell 4, 593-604.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 593-604
    • Briesewitz, R.1    Kern, A.2    Marcantonio, E.E.3
  • 12
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and p125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • Burridge, K., Turner, C.E., and Romer, L.H. (1992). Tyrosine phosphorylation of paxillin and p125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119, 893-904.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-904
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 14
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and Brugge, J.S. (1995). Integrins and signal transduction pathways: the road taken. Science 268, 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 15
    • 0024325593 scopus 로고
    • Fibroblast contractility and actin organization are stimulated by microtubule inhibitors
    • Danowski, B.A. (1989). Fibroblast contractility and actin organization are stimulated by microtubule inhibitors. J. Cell Sci. 93, 255-266.
    • (1989) J. Cell Sci. , vol.93 , pp. 255-266
    • Danowski, B.A.1
  • 16
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signaling
    • Dedhar, S., and Hannigan, G.E. (1996). Integrin cytoplasmic interactions and bidirectional transmembrane signaling. Curr. Opin. Cell Biol. 8, 657-669.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 17
    • 0028792065 scopus 로고
    • p125FAK tyrosine phosphorylation and focal adhesion assembly: Studies with phosphotyrosine phosphatase inhibitors
    • Defilippi, P., Retta, S.F., Olivo, C., Palmieri, M., Venturino, M., Silengo, L., and Tarone, G. (1995). p125FAK tyrosine phosphorylation and focal adhesion assembly: studies with phosphotyrosine phosphatase inhibitors. Exp. Cell Res. 221, 141-152.
    • (1995) Exp. Cell Res. , vol.221 , pp. 141-152
    • Defilippi, P.1    Retta, S.F.2    Olivo, C.3    Palmieri, M.4    Venturino, M.5    Silengo, L.6    Tarone, G.7
  • 18
    • 0026611378 scopus 로고
    • α6/β1 integrin (laminin-receptor) is down-regulated by tumor necrosis factor β1 and interleukin-1β in human endothelial cells
    • Defilippi, P., Silengo, L., and Tarone, G. (1992). α6/β1 integrin (laminin-receptor) is down-regulated by tumor necrosis factor β1 and interleukin-1β 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
  • 19
    • 0025827302 scopus 로고
    • Differential distribution and modulation of expression of a1β1 integrin on human endothelial cells
    • Defilippi P, van Hinsbergh V, Bertolotto A, Rossino P, Silengo L, and Tarone G, (1991). Differential distribution and modulation of expression of a1β1 integrin on human endothelial cells. J Cell Biol 114, 855-863.
    • (1991) J Cell Biol , vol.114 , pp. 855-863
    • Defilippi, P.1    Van Hinsbergh, V.2    Bertolotto, A.3    Rossino, P.4    Silengo, L.5    Tarone, G.6
  • 20
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine residues 1162 and 1163 compromise insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis, L., Clauser, E., Morgan, D.O., Edery, M., Roth, R.A., and Rutter, W.J. (1986). Replacement of insulin receptor tyrosine residues 1162 and 1163 compromise insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45, 721-732.
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.A.5    Rutter, W.J.6
  • 21
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall, E., and Ruoslahti, E. (1977). Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int. J. Cancer 20, 1-5.
    • (1977) Int. J. Cancer , vol.20 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 22
    • 0028985980 scopus 로고
    • Lack of beta 1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts
    • Fässler, R., Pfaff, M., Murphy, J., Noegel, A.A., Johansson, S., Timpl, R., and Albrecht, R. (1995). Lack of beta 1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts. J. Cell Biol. 128, 979-988.
    • (1995) J. Cell Biol. , vol.128 , pp. 979-988
    • Fässler, R.1    Pfaff, M.2    Murphy, J.3    Noegel, A.A.4    Johansson, S.5    Timpl, R.6    Albrecht, R.7
  • 23
    • 0028879643 scopus 로고
    • The novel structural motif Gln795-Gln802 in the integrin β1C cytoplasmic domain regulates cell proliferation
    • Fornaro, M., Zheng, D.Q., and Languino, L.R. (1995). The novel structural motif Gln795-Gln802 in the integrin β1C cytoplasmic domain regulates cell proliferation. J. Biol. Chem. 270, 24666-24669.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24666-24669
    • Fornaro, M.1    Zheng, D.Q.2    Languino, L.R.3
  • 24
    • 0023730954 scopus 로고
    • Regulation of the fibronectin receptor affinity by divalent cations
    • Gailit, J., and Ruoslahti, E. (1988). Regulation of the fibronectin receptor affinity by divalent cations. J. Biol. Chem. 263, 12927-12932.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12927-12932
    • Gailit, J.1    Ruoslahti, E.2
  • 25
    • 0025214421 scopus 로고
    • Elevated levels of alpha5/ beta1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti, F., and Ruoslahti, E. (1990). Elevated levels of alpha5/ beta1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell 60, 849-859.
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.1    Ruoslahti, E.2
  • 27
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kD protein
    • Guan, J.L., Trevethick, J.E., and Hynes, R.O. (1991). Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kD protein. Cell Regul. 2, 951-964.
    • (1991) Cell Regul. , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevethick, J.E.2    Hynes, R.O.3
  • 29
    • 0018838995 scopus 로고
    • Silicone rubber substrata: A new wrinkle in the study of cell locomotion
    • Harris, A.K., Wild, P., and Stopak, D. (1980). Silicone rubber substrata: a new wrinkle in the study of cell locomotion. Science 208, 177-179.
    • (1980) Science , vol.208 , pp. 177-179
    • Harris, A.K.1    Wild, P.2    Stopak, D.3
  • 30
    • 0021267104 scopus 로고
    • Glycoproteins of 210,000 and 130,000 m. w. on activated T cells: Cell distribution and antigenic relation to components on resting cells and T cell lines
    • Hemler, M.E., Sanchez-Madrid, F., Flotte, T.J., Krensky, A.M., Burakoff, S.J., Bhan, A.K., Springer, T.A., and Strominger, J.L. (1984). Glycoproteins of 210,000 and 130,000 m. w. on activated T cells: cell distribution and antigenic relation to components on resting cells and T cell lines. J. Immunol. 132, 3011-3018.
    • (1984) J. Immunol. , vol.132 , pp. 3011-3018
    • Hemler, M.E.1    Sanchez-Madrid, F.2    Flotte, T.J.3    Krensky, A.M.4    Burakoff, S.J.5    Bhan, A.K.6    Springer, T.A.7    Strominger, J.L.8
  • 31
    • 0025806144 scopus 로고
    • Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 β-subunit
    • Hibbs, M.L., Xu Stacker, H.S.A., and Springer, T.A. (1991). Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 β-subunit. Science 251, 1611-1613.
    • (1991) Science , vol.251 , pp. 1611-1613
    • Hibbs, M.L.1    Xu Stacker, H.S.A.2    Springer, T.A.3
  • 32
    • 0001823786 scopus 로고
    • Recombinant PCR
    • ed. M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, San Diego: Academic Press
    • Higuchi, R. (1990). Recombinant PCR. In: PCR Protocols: A Guide to Methods and Applications, ed. M.A. Innis, D.H. Gelfand, J.J. Sninsky, and T.J. White, San Diego: Academic Press, 177-183.
    • (1990) PCR Protocols: A Guide to Methods and Applications , pp. 177-183
    • Higuchi, R.1
  • 34
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes, R.O. (1992). Integrins: versatility, modulation and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 35
    • 0026535449 scopus 로고
    • Regulation of fibronectin receptor distribution
    • LaFlamme, S.E., Akiyama, S.K., and Yamada, K.M. (1992). Regulation of fibronectin receptor distribution. J. Cell Biol. 117, 437-447.
    • (1992) J. Cell Biol. , vol.117 , pp. 437-447
    • LaFlamme, S.E.1    Akiyama, S.K.2    Yamada, K.M.3
  • 36
    • 0027421094 scopus 로고
    • A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1
    • Lenter, M., Uhlig, H., Hamann, A., Jeno, P., Imhof, B., and Vestweber, D. (1993). A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1. Proc. Natl. Acad. Sci. USA 90, 9051-9055.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9051-9055
    • Lenter, M.1    Uhlig, H.2    Hamann, A.3    Jeno, P.4    Imhof, B.5    Vestweber, D.6
  • 37
    • 0028238346 scopus 로고
    • Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain
    • Lukashev, M.E., Sheppard, D., and Pytela, R. (1994). Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain. J. Biol. Chem. 269, 18311-18314.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18311-18314
    • Lukashev, M.E.1    Sheppard, D.2    Pytela, R.3
  • 38
    • 0027360771 scopus 로고
    • Panning transfected cells for electrophysiological studies
    • Margolskee, R.F., McHendry-Rinde, B., and Horn, R. (1993). Panning transfected cells for electrophysiological studies. BioTechniques 15, 906-911.
    • (1993) BioTechniques , vol.15 , pp. 906-911
    • Margolskee, R.F.1    McHendry-Rinde, B.2    Horn, R.3
  • 39
    • 0021926873 scopus 로고
    • Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts
    • McKeown-Longo, P.J., and Mosher, D.F. (1985). Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts. J. Cell Biol. 100, 364-374.
    • (1985) J. Cell Biol. , vol.100 , pp. 364-374
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 40
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., Akiyama, S.K., and Yamada, K.M. (1995a). Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267, 883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 42
    • 0028944308 scopus 로고
    • Identification of a novel anti-integrin monoclonal antibody that recognizes a ligand-induced binding site epitope on β1 subunit
    • Mould, A.P., Garrat, A.N., Askari, J.A., Akiyama, S.K., and Humphries, M.J. (1995). Identification of a novel anti-integrin monoclonal antibody that recognizes a ligand-induced binding site epitope on β1 subunit. FEBS Lett. 363, 118-122.
    • (1995) FEBS Lett. , vol.363 , pp. 118-122
    • Mould, A.P.1    Garrat, A.N.2    Askari, J.A.3    Akiyama, S.K.4    Humphries, M.J.5
  • 43
    • 0025959811 scopus 로고
    • The mouse vitronectin receptor is a T cell activation antigen
    • Moulder, K., Roberts, K., Shevach, E.M., and Coligan, J.E. (1991). The mouse vitronectin receptor is a T cell activation antigen. J. Exp. Med. 173, 343-347.
    • (1991) J. Exp. Med. , vol.173 , pp. 343-347
    • Moulder, K.1    Roberts, K.2    Shevach, E.M.3    Coligan, J.E.4
  • 45
    • 0028954275 scopus 로고
    • Regulation of integrin affinity states through an NPXY motif in the β subunit cytoplasmic domain
    • O'Toole, T.E., Ylanne, J., and Culley, B.M. (1995). Regulation of integrin affinity states through an NPXY motif in the β subunit cytoplasmic domain. J. Biol. Chem. 270, 8553-8558.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8553-8558
    • O'Toole, T.E.1    Ylanne, J.2    Culley, B.M.3
  • 46
    • 0027454485 scopus 로고
    • Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain
    • Otey, C.A., Vasquez, G.B., Burridge, K., and Erickson, B.W. (1993). Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain. J. Biol. Chem. 268, 21193-21197.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21193-21197
    • Otey, C.A.1    Vasquez, G.B.2    Burridge, K.3    Erickson, B.W.4
  • 47
    • 0026642556 scopus 로고
    • Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association
    • Reszka, A.A., Hayashi, R.A., and Horwitz, A.F. (1992). Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association. J. Cell Biol. 117, 1321-1330.
    • (1992) J. Cell Biol. , vol.117 , pp. 1321-1330
    • Reszka, A.A.1    Hayashi, R.A.2    Horwitz, A.F.3
  • 48
    • 0030589481 scopus 로고    scopus 로고
    • Focal adhesion and stress fiber formation is regulated by tyrosine phosphatase activity
    • Retta, S.F., Barry, S.T., Critchley, D.R., Defilippi, P., Silengo, L., and Tarone, G. (1996). Focal adhesion and stress fiber formation is regulated by tyrosine phosphatase activity. Exp. Cell Res. 229, 307-317.
    • (1996) Exp. Cell Res. , vol.229 , pp. 307-317
    • Retta, S.F.1    Barry, S.T.2    Critchley, D.R.3    Defilippi, P.4    Silengo, L.5    Tarone, G.6
  • 50
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti, E., and Reed, J.C. (1994). Anchorage dependence, integrins, and apoptosis. Cell 77, 477-478.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 52
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller, M.D., Otey, C.A., Hildebrand, J.D., and Parsons, J.T. (1995). Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell Biol. 230, 1181-1187.
    • (1995) J. Cell Biol. , vol.230 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 53
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller, M.D., and Parson J.T. (1994). Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol. 6, 705-710.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parson, J.T.2
  • 54
    • 0023771015 scopus 로고
    • Identification and characterization of a novel antigen complex on mouse mammary tumor cells using a monoclonal antibody against platelet glycoprotein Ic
    • Sonnenberg, A., Hogervorst, F., Osterop, A., and Veltman, F.E.M. (1988). Identification and characterization of a novel antigen complex on mouse mammary tumor cells using a monoclonal antibody against platelet glycoprotein Ic. J. Biol. Chem. 263, 14030-14038.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14030-14038
    • Sonnenberg, A.1    Hogervorst, F.2    Osterop, A.3    Veltman, F.E.M.4
  • 55
    • 0021237798 scopus 로고
    • A cell surface, integral, membrane glycoprotein of 85,000 D (GP85) associated with Triton X100-insoluble cell skeleton
    • Tarone, G., Ferracini, R., Galetto, G., and Comoglio, P.M. (1984). A cell surface, integral, membrane glycoprotein of 85,000 D (GP85) associated With Triton X100-insoluble cell skeleton. J. Cell Biol. 99, 512-519.
    • (1984) J. Cell Biol. , vol.99 , pp. 512-519
    • Tarone, G.1    Ferracini, R.2    Galetto, G.3    Comoglio, P.M.4
  • 57
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., Tremble, P.M., Behrendsen, O., Crowley, E., and Damsky, C.D. (1989). Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J. Cell Biol. 109, 877-889.
    • (1989) J. Cell Biol. , vol.109 , pp. 877-889
    • Werb, Z.1    Tremble, P.M.2    Behrendsen, O.3    Crowley, E.4    Damsky, C.D.5
  • 58
    • 0027422170 scopus 로고
    • The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly
    • Wu, C., Bauer, J.S., Juliano, R.L., and McDonald, J.A. (1993). The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly. J. Biol. Chem. 268, 21883-21888.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21883-21888
    • Wu, C.1    Bauer, J.S.2    Juliano, R.L.3    McDonald, J.A.4
  • 59
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu, C., Keivens, V.M., O'Toole, T.E., McDonald, J.A., and Ginsberg, M.H. (1995). Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 83, 715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 60
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada, K.M., and Miyamoto, S. (1995). Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7, 681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 61
    • 0027263655 scopus 로고
    • Distinct functions of integrin a and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions
    • Ylanne, J., Chen, Y., O' Toole, T.E., Lofrus, J.C., Takada, Y., and Ginsberg M.H. (1993). Distinct functions of integrin a and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J. Cell Biol. 122, 223-233.
    • (1993) J. Cell Biol. , vol.122 , pp. 223-233
    • Ylanne, J.1    Chen, Y.2    O' Toole, T.E.3    Lofrus, J.C.4    Takada, Y.5    Ginsberg, M.H.6


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