메뉴 건너뛰기




Volumn 19, Issue 2, 1997, Pages 137-145

Signaling through focal adhesion kinase

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0031081425     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950190208     Document Type: Review
Times cited : (443)

References (70)
  • 1
    • 0346481004 scopus 로고
    • Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product
    • Rohrschneider, L.R. (1980). Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc. Natl Acad. Sci. USA 77, 3514-3518.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 3514-3518
    • Rohrschneider, L.R.1
  • 2
    • 0020189847 scopus 로고
    • Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide
    • Nigg, E.A., Sefton, B.M., Hunter, T., Walter, G. and Singer, S.J. (1982). Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proc. Natl Acad. Sci. USA 79, 5322-5326.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5322-5326
    • Nigg, E.A.1    Sefton, B.M.2    Hunter, T.3    Walter, G.4    Singer, S.J.5
  • 3
    • 0012108774 scopus 로고
    • Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells
    • Maher, P.A., Pasquale, E.B., Wang, J.Y.J. and Singer, S.J. (1985). Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc. Natl Acad. Sci. USA 82, 6576-6580.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 6576-6580
    • Maher, P.A.1    Pasquale, E.B.2    Wang, J.Y.J.3    Singer, S.J.4
  • 4
    • 3142588838 scopus 로고
    • Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets
    • Ferrell, J.E. Jr. and Martin, G.S. (1989). Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets. Proc. Natl Acad. Sci. USA 86, 2234-2238.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 2234-2238
    • Ferrell J.E., Jr.1    Martin, G.S.2
  • 5
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein
    • Guan, J.-L., Trevithick, J.E. and Hynes, R.O. (1991). Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kDa protein. Cell. Regulation 2, 951-964.
    • (1991) Cell. Regulation , vol.2 , pp. 951-964
    • Guan, J.-L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 6
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of β1 integrins
    • Kornberg, L.J., Earp, H.S., Turner, C.E., Prockop, C. and Juliano, R.L. (1991). Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of β1 integrins. Proc. Natl Acad. Sci. USA 88, 8392-8396.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 8
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S.K., Calalb, M.B., Harper, M.C. and Patel, S.K. (1992). Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl Acad. Sci. USA 89, 8487-8491.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 9
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner, S.B., Reynolds, A.B., Vines, R.R. and Parsons, J.T. (1990). Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl Acad. Sci. USA 87, 3328-3332.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 11
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand, J.D., Schaller, M.D. and Parsons, J.T. (1995). Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 6, 637-647.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 13
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan, J.-L. and Shalloway, D. (1992). Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358, 690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.-L.1    Shalloway, D.2
  • 14
    • 0026497659 scopus 로고
    • FAK in platelets
    • FAK in platelets. J. Cell Biol. 119, 905-912.
    • (1992) J. Cell Biol. , vol.119 , pp. 905-912
    • Lipfert, L.1
  • 16
    • 0029026697 scopus 로고
    • Convergent signalling in the action of integrins, neuropeptides, growth factors and oncogenes
    • Rozengurt, E. (1995). Convergent signalling in the action of integrins, neuropeptides, growth factors and oncogenes. Cancer Surveys 24, 81-96.
    • (1995) Cancer Surveys , vol.24 , pp. 81-96
    • Rozengurt, E.1
  • 17
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M. and Burridge, K. (1996). Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 18
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic, D. et al. (1995). Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377, 539-544.
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1
  • 19
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary, L. A., Chang, J.F. and Guan, J.-L. (1996). Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J. Cell. Sci. 109, 1787-1794..
    • (1996) J. Cell. Sci. , vol.109 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.-L.3
  • 20
    • 0028018234 scopus 로고
    • Potential role for focal adhesion kinase in migrating and proliferating keratinocytes near epidermal wounds and in culture
    • Gates, R.E., King, L.E. Jr., Hanks, S.K. and Nanney, L.B. (1994). Potential role for focal adhesion kinase in migrating and proliferating keratinocytes near epidermal wounds and in culture. Cell Growth Differ. 5, 891-899.
    • (1994) Cell Growth Differ. , vol.5 , pp. 891-899
    • Gates, R.E.1    King L.E., Jr.2    Hanks, S.K.3    Nanney, L.B.4
  • 21
    • 0029039421 scopus 로고
    • FAK) in invasive human tumors
    • FAK) in invasive human tumors. Canc. Res. 55, 2752-2755.
    • (1995) Canc. Res. , vol.55 , pp. 2752-2755
    • Owens, L.V.1
  • 23
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch, S.M., Vuori, K., Ruoslahti, E. and Chan-Hui, P.-Y. (1996). Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell. Biol. 134, 793-799.
    • (1996) J. Cell. Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.-Y.4
  • 24
    • 0029848157 scopus 로고    scopus 로고
    • Attenuation of the expression of the focal adhesion kinase induces apoptosis in tumor cells
    • Xu, L.H. et al. (1996). Attenuation of the expression of the focal adhesion kinase induces apoptosis in tumor cells. Cell Growth Differ. 7, 413-418.
    • (1996) Cell Growth Differ. , vol.7 , pp. 413-418
    • Xu, L.H.1
  • 26
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src-family kinases
    • Calalb, M.B., Polte, T.R. and Hanks, S.K. (1995). Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src-family kinases. Mol. Cell. Biol. 15, 954-963.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 27
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D.D., Hanks, S.K., Hunter, T. and van der Geer, P. (1994). Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372, 786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 28
    • 0029834447 scopus 로고    scopus 로고
    • Evidence for the in vivo phosphorylation of the Grb2 SH2 binding site on the focal adhesion kinase (FAK) by Src-family protein-tyrosine kinases
    • Schlaepfer, D.D. and Hunter, T. (1996). Evidence for the in vivo phosphorylation of the Grb2 SH2 binding site on the focal adhesion kinase (FAK) by Src-family protein-tyrosine kinases. Mol. Cell. Biol. 16, 5623-5633.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 29
    • 0028598744 scopus 로고
    • Specificity in recognition of phosphopeptides by src-homology 2 domains
    • Cantley, L.C. and Songyang, Z. (1994). Specificity in recognition of phosphopeptides by src-homology 2 domains. J. Cell Sci. (Suppl.) 18, 121-126.
    • (1994) J. Cell Sci. (Suppl.) , vol.18 , pp. 121-126
    • Cantley, L.C.1    Songyang, Z.2
  • 32
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β 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 β integrin cytoplasmic domains. J. Cell Biol. 130, 1181-1187.
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 33
    • 0029046858 scopus 로고
    • Interaction of focal adhesion kinase with cytoskeletal protein talin
    • Chen, H.-C. et al. (1995). Interaction of focal adhesion kinase with cytoskeletal protein talin. J. Biol. Chem. 270, 16995-16999.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16995-16999
    • Chen, H.-C.1
  • 34
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of Src
    • Brown, M.T. and Cooper, J.A. (1996). Regulation, substrates and functions of Src. Biochim. Biophys. Acta 1287, 121-149.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 35
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan, K. B. et al. (1994). Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 13, 4745-4756.
    • (1994) EMBO J. , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1
  • 36
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • Taylor, S.S. and Radzio-Andzelm, E. (1994). Three protein kinase structures define a common motif. Structure 2, 345-355.
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 37
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S.R., Wei, L., Ellis, L. and Hendrickson, W.A. (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 38
    • 0027957728 scopus 로고
    • The GRB2/Sem-5 adaptor protein
    • Downward, J. (1994). The GRB2/Sem-5 adaptor protein. FEBS Lett. 338, 113-117.
    • (1994) FEBS Lett. , vol.338 , pp. 113-117
    • Downward, J.1
  • 39
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen, Q., Kinch, M.S., Lin, T.H., Burridge, K. and Juliano, R.L. (1994). Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269, 26602-26605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.L.5
  • 41
    • 0028904784 scopus 로고
    • Integrin-dependent activation of MAP kinase: A link to shape-dependent cell proliferation
    • Zhu, X. and Assoian, R.K. (1995). Integrin-dependent activation of MAP kinase: a link to shape-dependent cell proliferation. Mol. Biol. Cell 6, 273-282.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 273-282
    • Zhu, X.1    Assoian, R.K.2
  • 43
    • 0027938974 scopus 로고
    • Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
    • Chen, H.-C. and Guan, J.-L. (1994). Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc. Natl Acad. Sci. USA 91, 10148-10152.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10148-10152
    • Chen, H.-C.1    Guan, J.-L.2
  • 44
    • 0029873045 scopus 로고    scopus 로고
    • Association of phosphatidylinositol 3-kinase, via the SH2 domains of p85, with focal adhesion kinase in polyoma middle t-transformed fibroblasts
    • Bachelot, C., Rameh, L., Parsons, T. and Cantley, L.C. (1996). Association of phosphatidylinositol 3-kinase, via the SH2 domains of p85, with focal adhesion kinase in polyoma middle t-transformed fibroblasts. Biochim. Biophys. Acta 1311, 45-52.
    • (1996) Biochim. Biophys. Acta , vol.1311 , pp. 45-52
    • Bachelot, C.1    Rameh, L.2    Parsons, T.3    Cantley, L.C.4
  • 45
    • 0027970468 scopus 로고
    • Stimulation of phosphatidylinositol 3′-kinase association with focal adhesion kinase by platelet-derived growth factor
    • Chen, H.-C. and Guan, J.-L. (1994). Stimulation of phosphatidylinositol 3′-kinase association with focal adhesion kinase by platelet-derived growth factor. J. Biol. Chem. 269, 31229-31233.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31229-31233
    • Chen, H.-C.1    Guan, J.-L.2
  • 46
    • 0028123778 scopus 로고
    • Identification of two SH3-binding motifs in the regulatory subunit of phosphatidylinositol 3-kinase
    • Kapeller, R. et al. (1994). Identification of two SH3-binding motifs in the regulatory subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 269, 1927-1933.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1927-1933
    • Kapeller, R.1
  • 47
    • 0027214258 scopus 로고
    • The v-Src SH3 domain binds phosphatidylinositol 3′-kinase
    • Liu, X., Marengere, L.E., Koch, C.A. and Pawson, T. (1994). The v-Src SH3 domain binds phosphatidylinositol 3′-kinase. Mol. Cell. Biol. 13, 5225-5232.
    • (1994) Mol. Cell. Biol. , vol.13 , pp. 5225-5232
    • Liu, X.1    Marengere, L.E.2    Koch, C.A.3    Pawson, T.4
  • 48
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and c-Src in a tyrosine phosphorylation-dependent manner
    • Sakai, R. et al. (1994). A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and c-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13, 3748-3756.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1
  • 49
    • 0025978644 scopus 로고
    • Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins
    • Matsuda, M., Mayer, B.J. and Hanafusa, H. (1991). Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins. Mol. Cell. Biol. 11, 1607-1613.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1607-1613
    • Matsuda, M.1    Mayer, B.J.2    Hanafusa, H.3
  • 50
    • 0028940658 scopus 로고
    • Adhesion-induced tyrosine phosphorylation of the p130 SRC substrate
    • Petch, L.A., Bockholt, S.M., Bouton, A., Parsons, J.T. and Burridge, K. (1995). Adhesion-induced tyrosine phosphorylation of the p130 SRC substrate. J. Cell. Sci. 108, 1371-1379.
    • (1995) J. Cell. Sci. , vol.108 , pp. 1371-1379
    • Petch, L.A.1    Bockholt, S.M.2    Bouton, A.3    Parsons, J.T.4    Burridge, K.5
  • 51
    • 0029034873 scopus 로고
    • Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs
    • Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs. J. Biol. Chem. 270, 15398-15402.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15398-15402
    • Nojima, Y.1
  • 53
    • 0029664531 scopus 로고    scopus 로고
    • cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol. Cell. Biol. 16, 2606-2613.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 57
    • 0028881018 scopus 로고
    • Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G
    • Gotoh, T. et al. (1995). Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G. Mol. Cell. Biol. 15, 6746-6753.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6746-6753
    • Gotoh, T.1
  • 58
    • 0028041168 scopus 로고
    • Cell polarity in yeast
    • Chant, J. (1994). Cell polarity in yeast. Trends Genet. 10, 328-333.
    • (1994) Trends Genet. , vol.10 , pp. 328-333
    • Chant, J.1
  • 59
    • 0028533592 scopus 로고
    • Tensin: A potential link between the cytoskeleton and signal transduction
    • Lo, S.H., Weisberg, E. and Chen, L.B. (1994). Tensin: a potential link between the cytoskeleton and signal transduction. BioEssays 16, 817-823.
    • (1994) BioEssays , vol.16 , pp. 817-823
    • Lo, S.H.1    Weisberg, E.2    Chen, L.B.3
  • 60
    • 0029562687 scopus 로고
    • Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn
    • Ishino, M., Ohba, T., Sasaki, H. and Sasaki, T. (1995). Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn. Oncogene 11, 2331-2338.
    • (1995) Oncogene , vol.11 , pp. 2331-2338
    • Ishino, M.1    Ohba, T.2    Sasaki, H.3    Sasaki, T.4
  • 62
    • 0029891787 scopus 로고    scopus 로고
    • Cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae
    • Cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 16, 3327-3337.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3327-3337
    • Law, S.F.1    Estojak, J.2    Wang, B.3    Mysliwiec, T.4    Kruh, G.5    Golemis, E.A.6
  • 63
    • 0028788937 scopus 로고
    • Budding yeast morphogenesis: Signalling, cytoskeleton and cell cycle
    • Kron, S.J. and Gow, N.A.R. (1995). Budding yeast morphogenesis: signalling, cytoskeleton and cell cycle. Curr. Opin. Cell Biol. 7, 845-855.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 845-855
    • Kron, S.J.1    Gow, N.A.R.2
  • 64
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • Hildebrand, J.D., Taylor, J.M. and Parsons, J.T. (1996). An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase. Mol. Cell. Biol. 16, 3169-3178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 65
    • 0028961293 scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia
    • Nobes, C.D. and Hall, A. (1995). Rho, Rac and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia. Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 66
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C.E., Glenney, J.R. and Burridge, K. (1990). Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111, 1059-1068.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney, J.R.2    Burridge, K.3
  • 67
    • 0027219262 scopus 로고
    • Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts
    • Birge, R.B. et al. (1993). Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol. Cell. Biol. 13, 4648-4656.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4648-4656
    • Birge, R.B.1
  • 68
    • 0028986116 scopus 로고
    • FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell. Biol. 15, 2635-2645.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 69
    • 0027293670 scopus 로고
    • Detection of Src homology 3-binding proteins, including paxillin, in normal and v-src-transformed Balb/c-3T3 cells
    • Weng, Z., Taylor, J.A., Turner, C.E., Brugge, J.S. and Seidel-Dugan, C. (1993). Detection of Src homology 3-binding proteins, including paxillin, in normal and v-src-transformed Balb/c-3T3 cells. J. Biol. Chem. 268, 14956-14963.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14956-14963
    • Weng, Z.1    Taylor, J.A.2    Turner, C.E.3    Brugge, J.S.4    Seidel-Dugan, C.5
  • 70
    • 0029166094 scopus 로고
    • Characterization of tyrosine phosphorylatin of paxillin in vitro by focal adhesion kinase
    • Bellis, S.L., Miller, J.T. and Turner, C.E. (1995). Characterization of tyrosine phosphorylatin of paxillin in vitro by focal adhesion kinase. J. Biol. Chem. 270, 17437-17441.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17437-17441
    • Bellis, S.L.1    Miller, J.T.2    Turner, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.