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Volumn , Issue , 2008, Pages 25-46

Integrin Signaling Through Focal Adhesion Kinase

Author keywords

Cell junctions; Cell matrix junctions; FAK activity regulation; FAK signaling pathways; Focal adhesion kinase (FAK); Integrin signalling; Regulation of cellular functions; Structure of FAK

Indexed keywords


EID: 39149130455     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527622092.ch2     Document Type: Chapter
Times cited : (2)

References (156)
  • 1
    • 0019779921 scopus 로고
    • Extracellular matrix
    • Hay, E.D., Extracellular matrix. J. Cell Biol. 1981, 91 (3 Pt. 2), 205s-223s.
    • (1981) J. Cell Biol. , vol.91 , Issue.3 PT. 2
    • Hay, E.D.1
  • 2
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano, R.L. and S. Haskill, Signal transduction from the extracellular matrix. J. Cell Biol. 1993, 120, 577-585.
    • (1993) J. Cell Biol. , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 3
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: the road taken
    • Clark, E.A. and J.S. Brugge, Integrins and signal transduction pathways: the road taken. Science 1995, 268, 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 4
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes, R.O., Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110 (6), 673-687.
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 5
    • 0023666065 scopus 로고
    • Integrins: a family of cell surface receptors
    • Hynes, R.O., Integrins: a family of cell surface receptors. Cell 1987, 48, 549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 6
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O., Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992, 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 7
    • 0031022256 scopus 로고    scopus 로고
    • Anchorage-dependent cell cycle progression
    • Assoian, R.K., Anchorage-dependent cell cycle progression. J. Cell Biol. 1997, 136, 14.
    • (1997) J. Cell Biol. , vol.136 , pp. 14
    • Assoian, R.K.1
  • 8
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: a physically integrated molecular process
    • Lauffenburger, D.A. and A.F. Horwitz, Cell migration: a physically integrated molecular process. Cell 1996, 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 9
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti, E. and J.C. Reed, Anchorage dependence, integrins, and apoptosis. Cell 1994, 77, 477-478.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 10
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan, J.L. and D. Shalloway, Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 1992, 358, 690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 11
    • 0025946283 scopus 로고
    • Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins
    • Kornberg, L.J., et al., Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins. Proc. Natl. Acad. Sci. USA 1991, 88, 8392-8396.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1
  • 12
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • Guan, J.L., J.E. Trevithick, and R.O. Hynes, Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Regul. 1991, 2, 951-964.
    • (1991) Cell Regul. , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 13
    • 0026612521 scopus 로고
    • Pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions
    • Schaller, M.D., et al., pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc. Natl. Acad. Sci. USA 1992, 89, 5192-5196.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5192-5196
    • Schaller, M.D.1
  • 14
    • 0142141199 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility
    • Hanks, S.K., et al., Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front. Biosci. 2003, 8, 982-996.
    • (2003) Front. Biosci. , vol.8 , pp. 982-996
    • Hanks, S.K.1
  • 15
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: the first ten years
    • Parsons, J.T., Focal adhesion kinase: the first ten years. J. Cell Sci. 2003, 116 (Pt. 8), 1409-1416.
    • (2003) J. Cell Sci. , vol.116 , Issue.PT. 8 , pp. 1409-1416
    • Parsons, J.T.1
  • 16
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S.K., et al., Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 1992, 89, 8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1
  • 17
    • 0027448821 scopus 로고
    • Expression of focal adhesion kinase gene and invasive cancer
    • Weiner, T.M., et al., Expression of focal adhesion kinase gene and invasive cancer. Lancet 1993, 342, 1024-1025.
    • (1993) Lancet , vol.342 , pp. 1024-1025
    • Weiner, T.M.1
  • 18
    • 0029153296 scopus 로고
    • Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis
    • Hens, M.D. and D.W. DeSimone, Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis. Dev. Biol. 1995, 170, 274-288.
    • (1995) Dev. Biol. , vol.170 , pp. 274-288
    • Hens, M.D.1    DeSimone, D.W.2
  • 19
    • 0029120211 scopus 로고
    • Cloning of a Xenopus laevis cDNA encoding focal adhesion kinase (FAK) and expression during early development
    • Zhang, X., C.V. Wright, and S.K. Hanks, Cloning of a Xenopus laevis cDNA encoding focal adhesion kinase (FAK) and expression during early development. Gene 1995, 160, 219-222.
    • (1995) Gene , vol.160 , pp. 219-222
    • Zhang, X.1    Wright, C.V.2    Hanks, S.K.3
  • 20
    • 0028986116 scopus 로고
    • Pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller, M.D. and J.T. Parsons, pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell. Biol. 1995, 15, 2635-2645.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 21
    • 0033772308 scopus 로고    scopus 로고
    • FAK integrates growth-factor and integrin signals to promote cell migration
    • Sieg, D.J., et al., FAK integrates growth-factor and integrin signals to promote cell migration. Nat. Cell Biol. 2000, 2, 249-256.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 249-256
    • Sieg, D.J.1
  • 22
    • 2942596543 scopus 로고    scopus 로고
    • FERM domain interaction promotes FAK signaling
    • Dunty, J.M., et al., FERM domain interaction promotes FAK signaling. Mol. Cell. Biol. 2004, 24, 5353-5368.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5353-5368
    • Dunty, J.M.1
  • 23
    • 0036860545 scopus 로고    scopus 로고
    • Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation
    • Sun, C.X., V.A. Robb, and D.H. Gutmann, Protein 4.1 tumor suppressors: getting a FERM grip on growth regulation. J. Cell Sci. 2002, 115 (Pt. 21), 3991-4000.
    • (2002) J. Cell Sci. , vol.115 , Issue.PT. 21 , pp. 3991-4000
    • Sun, C.X.1    Robb, V.A.2    Gutmann, D.H.3
  • 24
    • 0035003136 scopus 로고    scopus 로고
    • Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain
    • Chen, R., et al., Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain. Nat. Cell Biol. 2001, 3, 439-444.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 439-444
    • Chen, R.1
  • 25
    • 0035813119 scopus 로고    scopus 로고
    • Ezrin interacts with focal adhesion kinase and induces its activation independently of cell-matrix adhesion
    • Poullet, P., et al., Ezrin interacts with focal adhesion kinase and induces its activation independently of cell-matrix adhesion. J. Biol. Chem. 2001, 276, 37686-37691.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37686-37691
    • Poullet, P.1
  • 26
    • 0242495710 scopus 로고    scopus 로고
    • Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction
    • Cooper, L.A., T.L. Shen, and J.L. Guan, Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction. Mol. Cell. Biol. 2003, 23, 8030-8041.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8030-8041
    • Cooper, L.A.1    Shen, T.L.2    Guan, J.L.3
  • 27
    • 0037969627 scopus 로고    scopus 로고
    • Signaling between focal adhesion kinase and trio
    • Medley, Q.G., et al., Signaling between focal adhesion kinase and trio. J. Biol. Chem. 2003, 278, 13265-13270.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13265-13270
    • Medley, Q.G.1
  • 28
    • 0036839636 scopus 로고    scopus 로고
    • Alternative splicing controls the mechanisms of FAK autophosphorylation
    • Toutant, M., et al., Alternative splicing controls the mechanisms of FAK autophosphorylation. Mol. Cell. Biol. 2002, 22, 7731-7743.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7731-7743
    • Toutant, M.1
  • 29
    • 0346220294 scopus 로고    scopus 로고
    • PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation
    • Kadare, G., et al., PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation. J. Biol. Chem. 2003, 278, 47434-47440.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47434-47440
    • Kadare, G.1
  • 30
    • 0347356250 scopus 로고    scopus 로고
    • Nuclear import of N-terminal FAK by activation of the FcepsilonRI receptor in RBL-2H3 cells
    • Jones, G. and G. Stewart, Nuclear import of N-terminal FAK by activation of the FcepsilonRI receptor in RBL-2H3 cells. Biochem. Biophys. Res. Commun. 2004, 314, 39-45.
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 39-45
    • Jones, G.1    Stewart, G.2
  • 31
    • 0038070109 scopus 로고    scopus 로고
    • FAK induces expression of Prx1 to promote tenascin-C-dependent fibroblast migration
    • McKean, D.M., et al., FAK induces expression of Prx1 to promote tenascin-C-dependent fibroblast migration. J. Cell Biol. 2003, 161, 393-402.
    • (2003) J. Cell Biol. , vol.161 , pp. 393-402
    • McKean, D.M.1
  • 32
    • 0038433306 scopus 로고    scopus 로고
    • Identification of transcription factor KLF8 as a downstream target of focal adhesion kinase in its regulation of cyclin D1 and cell cycle progression
    • Zhao, J., et al., Identification of transcription factor KLF8 as a downstream target of focal adhesion kinase in its regulation of cyclin D1 and cell cycle progression. Mol. Cell 2003, 11, 1503-1515.
    • (2003) Mol. Cell , vol.11 , pp. 1503-1515
    • Zhao, J.1
  • 33
    • 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., T.R. Polte, and S.K. Hanks, Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 1995, 15, 954-963.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 34
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto-and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • Owen, J.D., et al., Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto-and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. Mol. Cell. Biol. 1999, 19, 4806-4818.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4806-4818
    • Owen, J.D.1
  • 35
    • 3042717667 scopus 로고    scopus 로고
    • Regulation of integrin-mediated cellular responses through assembly of a CAS/Crk scaffold
    • Chodniewicz, D. and R.L. Klemke, Regulation of integrin-mediated cellular responses through assembly of a CAS/Crk scaffold. Biochim. Biophys. Acta 2004, 1692, 63-76.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 63-76
    • Chodniewicz, D.1    Klemke, R.L.2
  • 36
    • 0042090404 scopus 로고    scopus 로고
    • Direct interaction of focal adhesion kinase with p190RhoGEF
    • Zhai, J., et al., Direct interaction of focal adhesion kinase with p190RhoGEF. J. Biol. Chem. 2003, 278, 24865-24873.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24865-24873
    • Zhai, J.1
  • 37
    • 0035137373 scopus 로고    scopus 로고
    • Selective expression of an endogenous inhibitor of FAK regulates proliferation and migration of vascular smooth muscle cells
    • Taylor, J.M., et al., Selective expression of an endogenous inhibitor of FAK regulates proliferation and migration of vascular smooth muscle cells. Mol. Cell. Biol. 2001, 21, 1565-1572.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1565-1572
    • Taylor, J.M.1
  • 38
    • 0027439594 scopus 로고
    • Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK
    • Schaller, M.D., C.A. Borgman, and J.T. Parsons, Autonomous expression of a noncatalytic domain of the focal adhesion-associated protein tyrosine kinase pp125FAK. Mol. Cell. Biol. 1993, 13, 785-791.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 785-791
    • Schaller, M.D.1    Borgman, C.A.2    Parsons, J.T.3
  • 39
    • 0032784060 scopus 로고    scopus 로고
    • Regulated expression of focal adhesion kinase-related nonkinase, the autonomously expressed C-terminal domain of focal adhesion kinase
    • Nolan, K., J. Lacoste, and J.T. Parsons, Regulated expression of focal adhesion kinase-related nonkinase, the autonomously expressed C-terminal domain of focal adhesion kinase. Mol. Cell. Biol. 1999, 19, 6120-6129.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6120-6129
    • Nolan, K.1    Lacoste, J.2    Parsons, J.T.3
  • 40
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation
    • Gilmore, A.P. and L.H. Romer, Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation. Mol. Biol. Cell 1996, 7, 1209-1224.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 41
    • 0029971297 scopus 로고    scopus 로고
    • A mechanism for regulation of the adhesion-associated protein tyrosine kinase pp125FAK
    • Richardson, A. and T. Parsons, A mechanism for regulation of the adhesion-associated protein tyrosine kinase pp125FAK. Nature 1996, 380, 538-540.
    • (1996) Nature , vol.380 , pp. 538-540
    • Richardson, A.1    Parsons, T.2
  • 42
    • 0033555070 scopus 로고    scopus 로고
    • Focal adhesion kinase in integrin-mediated signaling
    • Cary, L.A. and J.L. Guan, Focal adhesion kinase in integrin-mediated signaling. Front. Biosci. 1999, 4, D102-D113.
    • (1999) Front. Biosci. , vol.4
    • Cary, L.A.1    Guan, J.L.2
  • 43
    • 0028343192 scopus 로고
    • Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras
    • Akiyama, S.K., et al., Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras. J. Biol. Chem. 1994, 269, 15961-15964.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15961-15964
    • Akiyama, S.K.1
  • 44
    • 0029587579 scopus 로고
    • Integrin signaling: roles for the cytoplasmic tails of alpha IIb beta 3 in the tyrosine phosphorylation of pp125FAK
    • Leong, L., et al., Integrin signaling: roles for the cytoplasmic tails of alpha IIb beta 3 in the tyrosine phosphorylation of pp125FAK. J. Cell Sci. 1995, 108 (Pt. 12), 3817-3825.
    • (1995) J. Cell Sci. , vol.108 , Issue.PT. 12 , pp. 3817-3825
    • Leong, L.1
  • 45
    • 0028238346 scopus 로고
    • Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain
    • Lukashev, M.E., D. Sheppard, and R. Pytela, Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed beta 1 integrin cytoplasmic domain. J. Biol. Chem. 1994, 269, 18311-18314.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18311-18314
    • Lukashev, M.E.1    Sheppard, D.2    Pytela, R.3
  • 46
    • 0027227263 scopus 로고
    • Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin
    • Bockholt, S.M. and K. Burridge, Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J. Biol. Chem. 1993, 268, 14565-14567.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14565-14567
    • Bockholt, S.M.1    Burridge, K.2
  • 47
    • 0026497659 scopus 로고
    • Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets
    • Lipfert, L., et al., Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J. Cell Biol. 1992, 119, 905-912.
    • (1992) J. Cell Biol. , vol.119 , pp. 905-912
    • Lipfert, L.1
  • 48
    • 0031921101 scopus 로고    scopus 로고
    • Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: summation of both c-Src-and focal adhesion kinase-initiated tyrosine phosphorylation events
    • Schlaepfer, D.D., K.C. Jones, and T. Hunter, Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: summation of both c-Src-and focal adhesion kinase-initiated tyrosine phosphorylation events. Mol. Cell. Biol. 1998, 18, 2571-2585.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 49
    • 0028236960 scopus 로고
    • The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions
    • Barry, S.T. and D.R. Critchley, The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions. J. Cell Sci. 1994, 107 (Pt. 7), 2033-2045.
    • (1994) J. Cell Sci. , vol.107 , Issue.PT. 7 , pp. 2033-2045
    • Barry, S.T.1    Critchley, D.R.2
  • 50
    • 0029892628 scopus 로고    scopus 로고
    • Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin
    • Flinn, H.M. and A.J. Ridley, Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin. J. Cell Sci. 1996, 109 (Pt. 5), 1133-1141.
    • (1996) J. Cell Sci. , vol.109 , Issue.PT. 5 , pp. 1133-1141
    • Flinn, H.M.1    Ridley, A.J.2
  • 51
    • 0028944227 scopus 로고
    • Guanosine 5 ′-3-O-(thio)triphosphate stimulates tyrosine phosphorylation of p125FAK and paxillin in permeabilized Swiss 3T3 cells
    • Seckl, M.J., et al., Guanosine 5 ′-3-O-(thio)triphosphate stimulates tyrosine phosphorylation of p125FAK and paxillin in permeabilized Swiss 3T3 cells. Role of p21rho. J. Biol. Chem. 1995, 270, 6984-6990.
    • (1995) Role of p21rho. J. Biol. Chem. , vol.270 , pp. 6984-6990
    • Seckl, M.J.1
  • 52
    • 0030968768 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate stimulates rho-mediated tyrosine phosphorylation of focal adhesion kinase and paxillin in Swiss 3T3 fibroblasts
    • Wang, F., et al., Sphingosine 1-phosphate stimulates rho-mediated tyrosine phosphorylation of focal adhesion kinase and paxillin in Swiss 3T3 fibroblasts. Biochem. J. 1997, 324 (Pt. 2), 481-488.
    • (1997) Biochem. J. , vol.324 , Issue.PT. 2 , pp. 481-488
    • Wang, F.1
  • 53
    • 0842281489 scopus 로고    scopus 로고
    • Multiple connections link FAK to cell motility and invasion
    • Schlaepfer, D.D. and S.K. Mitra, Multiple connections link FAK to cell motility and invasion. Curr. Opin. Genet. Dev. 2004, 14, 92-101.
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 92-101
    • Schlaepfer, D.D.1    Mitra, S.K.2
  • 54
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller, M.D. and J.T. Parsons, Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol. 1994, 6, 705-710.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 55
    • 0032500744 scopus 로고    scopus 로고
    • Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation
    • Maa, M.C. and T.H. Leu, Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation. Biochem. Biophys. Res. Commun. 1998, 251, 344-349.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 344-349
    • Maa, M.C.1    Leu, T.H.2
  • 56
    • 3142779450 scopus 로고    scopus 로고
    • Phosphorylation of focal adhesion kinase at tyrosine 861 is crucial for Ras transformation of fibroblasts
    • Lim, Y., et al., Phosphorylation of focal adhesion kinase at tyrosine 861 is crucial for Ras transformation of fibroblasts. J. Biol. Chem. 2004, 279, 29060-29065.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29060-29065
    • Lim, Y.1
  • 57
    • 0036544562 scopus 로고    scopus 로고
    • Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling
    • Eliceiri, B.P., et al., Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling. J. Cell Biol. 2002, 157, 149-160.
    • (2002) J. Cell Biol. , vol.157 , pp. 149-160
    • Eliceiri, B.P.1
  • 58
    • 0035837360 scopus 로고    scopus 로고
    • Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration: analysis of specific phosphorylation events using site-directed antibodies
    • Nakamura, K., et al., Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration: analysis of specific phosphorylation events using site-directed antibodies. Oncogene 2001, 20, 2626-2635.
    • (2001) Oncogene , vol.20 , pp. 2626-2635
    • Nakamura, K.1
  • 59
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen, Q., et al., Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 1994, 269, 26602-26605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.1
  • 60
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D.D., et al., Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994, 372, 786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1
  • 61
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: integrating signals from front to back
    • Ridley, A.J., et al., Cell migration: integrating signals from front to back. Science 2003, 302, 1704-1709.
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 62
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • Hayashi, I., K. Vuori, and R.C. Liddington, The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat. Struct. Biol. 2002, 9, 101-106.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 63
    • 0041706118 scopus 로고    scopus 로고
    • Targeting membrane-localized focal adhesion kinase to focal adhesions: roles of tyrosine phosphorylation and SRC family kinases
    • Katz, B.Z., et al., Targeting membrane-localized focal adhesion kinase to focal adhesions: roles of tyrosine phosphorylation and SRC family kinases. J. Biol. Chem. 2003, 278, 29115-29120.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29115-29120
    • Katz, B.Z.1
  • 64
    • 0036197382 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase
    • Liu, G., C.D. Guibao, and J. Zheng, Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase. Mol. Cell. Biol. 2002, 22, 2751-2760.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2751-2760
    • Liu, G.1    Guibao, C.D.2    Zheng, J.3
  • 65
    • 2342649951 scopus 로고    scopus 로고
    • The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation
    • Prutzman, K.C., et al., The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation. Structure 2004, 12, 881-891.
    • (2004) Structure , vol.12 , pp. 881-891
    • Prutzman, K.C.1
  • 66
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner, C.E., Paxillin and focal adhesion signalling. Nat. Cell Biol. 2000, 2, E231-E236.
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 67
    • 13944282937 scopus 로고    scopus 로고
    • Identification of Src-specific phosphorylation site on focal adhesion kinase: dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior
    • Brunton, V.G., et al., Identification of Src-specific phosphorylation site on focal adhesion kinase: dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior. Cancer Res. 2005, 65, 1335-1342.
    • (2005) Cancer Res. , vol.65 , pp. 1335-1342
    • Brunton, V.G.1
  • 68
    • 27444431517 scopus 로고    scopus 로고
    • Regulation of FAK Ser-722 phosphorylation and kinase activity by GSK3 and PP1 during cell spreading and migration
    • Bianchi, M., et al., Regulation of FAK Ser-722 phosphorylation and kinase activity by GSK3 and PP1 during cell spreading and migration. Biochem. J. 2005, 391 (Pt. 2), 359-370.
    • (2005) Biochem. J. , vol.391 , Issue.PT. 2 , pp. 359-370
    • Bianchi, M.1
  • 69
    • 0042329506 scopus 로고    scopus 로고
    • Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration
    • Xie, Z., et al., Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration. Cell 2003, 114, 469-482.
    • (2003) Cell , vol.114 , pp. 469-482
    • Xie, Z.1
  • 70
    • 0035176458 scopus 로고    scopus 로고
    • Serine phosphorylation of focal adhesion kinase in interphase and mitosis: a possible role in modulating binding to p130(Cas)
    • Ma, A., et al., Serine phosphorylation of focal adhesion kinase in interphase and mitosis: a possible role in modulating binding to p130(Cas). Mol. Biol. Cell 2001, 12, 1-12.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1-12
    • Ma, A.1
  • 71
    • 0033601745 scopus 로고    scopus 로고
    • Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK
    • Yamakita, Y., et al., Dissociation of FAK/p130(CAS)/c-Src complex during mitosis: role of mitosis-specific serine phosphorylation of FAK. J. Cell Biol. 1999, 144, 315-324.
    • (1999) J. Cell Biol. , vol.144 , pp. 315-324
    • Yamakita, Y.1
  • 72
    • 0036734653 scopus 로고    scopus 로고
    • Regulation of focal adhesion kinase by a novel protein inhibitor FIP200
    • Abbi, S., et al., Regulation of focal adhesion kinase by a novel protein inhibitor FIP200. Mol. Biol. Cell 2002, 13, 3178-3191.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3178-3191
    • Abbi, S.1
  • 73
    • 0141865509 scopus 로고    scopus 로고
    • Negative regulation of FAK signaling by SOCS proteins
    • Liu, E., J.F. Cote, and K. Vuori, Negative regulation of FAK signaling by SOCS proteins. EMBO J. 2003, 22, 5036-5046
    • (2003) EMBO J. , vol.22 , pp. 5036-5046
    • Liu, E.1    Cote, J.F.2    Vuori, K.3
  • 74
    • 0141865507 scopus 로고    scopus 로고
    • Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2
    • von Wichert, G., et al., Force-dependent integrin-cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2. EMBO J. 2003, 22, 5023-5035.
    • (2003) EMBO J. , vol.22 , pp. 5023-5035
    • Von Wichert, G.1
  • 75
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu, D.H., et al., Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem. 1998, 273, 21125-21131.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21125-21131
    • Yu, D.H.1
  • 76
    • 0037421205 scopus 로고    scopus 로고
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng, L., et al., PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 2003, 160, 137-146.
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1
  • 77
    • 0039441744 scopus 로고    scopus 로고
    • Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility
    • Manes, S., et al., Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility. Mol. Cell. Biol. 1999, 19, 3125-3135.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3125-3135
    • Manes, S.1
  • 78
    • 0033785409 scopus 로고    scopus 로고
    • Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation
    • Miao, H., et al., Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat. Cell Biol. 2000, 2, 62-69.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 62-69
    • Miao, H.1
  • 79
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • Tamura, M., et al., Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science 1998, 280, 1614-1617.
    • (1998) Science , vol.280 , pp. 1614-1617
    • Tamura, M.1
  • 80
    • 0033556443 scopus 로고    scopus 로고
    • Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: differential involvement of focal adhesion kinase and p130Cas
    • Tamura, M., et al., Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: differential involvement of focal adhesion kinase and p130Cas. Cancer Res. 1999, 59, 442-449.
    • (1999) Cancer Res. , vol.59 , pp. 442-449
    • Tamura, M.1
  • 81
    • 0033575287 scopus 로고    scopus 로고
    • PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway
    • Tamura, M., et al., PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway. J. Biol. Chem. 1999, 274, 20693-20703.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20693-20703
    • Tamura, M.1
  • 82
    • 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., J.F. Chang, and J.L. Guan, Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J. Cell Sci. 1996, 109 (Pt. 7), 1787-1794.
    • (1996) J. Cell Sci. , vol.109 , Issue.PT. 7 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.L.3
  • 83
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic, D., et al., Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 1995, 377, 539-544.
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1
  • 84
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
    • Webb, D.J., et al., FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat. Cell Biol. 2004, 6, 154-161.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 154-161
    • Webb, D.J.1
  • 85
    • 0028988989 scopus 로고
    • V-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts
    • Fincham, V.J., J.A. Wyke, and M.C. Frame, v-Src-induced degradation of focal adhesion kinase during morphological transformation of chicken embryo fibroblasts. Oncogene 1995, 10, 2247-2252.
    • (1995) Oncogene , vol.10 , pp. 2247-2252
    • Fincham, V.J.1    Wyke, J.A.2    Frame, M.C.3
  • 86
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X.D., et al., Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 2000, 113 (Pt. 20), 3673-3678.
    • (2000) J. Cell Sci. , vol.113 , Issue.PT. 20 , pp. 3673-3678
    • Ren, X.D.1
  • 87
    • 4043077024 scopus 로고    scopus 로고
    • Isoform specific function of calpain 2 in regulating membrane protrusion
    • Franco, S., B. Perrin, and A. Huttenlocher, Isoform specific function of calpain 2 in regulating membrane protrusion. Exp. Cell Res. 2004, 299, 179-187.
    • (2004) Exp. Cell Res. , vol.299 , pp. 179-187
    • Franco, S.1    Perrin, B.2    Huttenlocher, A.3
  • 88
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X.D., W.B. Kiosses, and M.A. Schwartz, Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 1999, 18, 578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 89
    • 0032513047 scopus 로고    scopus 로고
    • Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin
    • Shen, Y., et al., Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin. J. Biol. Chem. 1998, 273, 6474-6481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6474-6481
    • Shen, Y.1
  • 90
    • 1542289014 scopus 로고    scopus 로고
    • NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model
    • Gao, G., et al., NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model. J. Biol. Chem. 2004, 279, 8441-8451.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8441-8451
    • Gao, G.1
  • 91
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions
    • Hildebrand, J.D., M.D. Schaller, and J.T. Parsons, Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions. J. Cell Biol. 1993, 123, 993-1005.
    • (1993) J. Cell Biol. , vol.123 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 92
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
    • Sieg, D.J., C.R. Hauck, and D.D. Schlaepfer, Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration. J. Cell Sci. 1999, 112 (Pt. 16), 2677-2691.
    • (1999) J. Cell Sci. , vol.112 , Issue.PT. 16 , pp. 2677-2691
    • Sieg, D.J.1    Hauck, C.R.2    Schlaepfer, D.D.3
  • 93
    • 0030694182 scopus 로고    scopus 로고
    • Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation
    • Richardson, A., et al., Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation. Mol. Cell. Biol. 1997, 17, 6906-6914.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6906-6914
    • Richardson, A.1
  • 94
    • 0028331263 scopus 로고
    • Tyrosine kinase activity, cytoskeletal organization, and motility in human vascular endothelial cells
    • Romer, L.H., et al., Tyrosine kinase activity, cytoskeletal organization, and motility in human vascular endothelial cells. Mol. Biol. Cell 1994, 5, 349-361.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 349-361
    • Romer, L.H.1
  • 95
    • 14844327984 scopus 로고    scopus 로고
    • P27Kip1 and cyclin D1 are necessary for focal adhesion kinase regulation of cell cycle progression in glioblastoma cells propagated in vitro and in vivo in the scid mouse brain
    • Ding, Q., et al., p27Kip1 and cyclin D1 are necessary for focal adhesion kinase regulation of cell cycle progression in glioblastoma cells propagated in vitro and in vivo in the scid mouse brain. J. Biol. Chem. 2005, 280, 6802-6815.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6802-6815
    • Ding, Q.1
  • 96
    • 0035476836 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells
    • Hauck, C.R., et al., Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells. Cancer Res. 2001, 61, 7079-7090.
    • (2001) Cancer Res. , vol.61 , pp. 7079-7090
    • Hauck, C.R.1
  • 97
    • 33645022769 scopus 로고    scopus 로고
    • HEF1 is a necessary and specific downstream effector of FAK that promotes the migration of glioblastoma cells
    • Natarajan, M., et al., HEF1 is a necessary and specific downstream effector of FAK that promotes the migration of glioblastoma cells. Oncogene 2006, 25, 1721-1732.
    • (2006) Oncogene , vol.25 , pp. 1721-1732
    • Natarajan, M.1
  • 98
    • 0034532347 scopus 로고    scopus 로고
    • P125 focal adhesion kinase promotes malignant astrocytoma cell proliferation in vivo
    • Wang, D., et al., p125 focal adhesion kinase promotes malignant astrocytoma cell proliferation in vivo. J. Cell Sci. 2000, 113 (Pt. 23), 4221-4230.
    • (2000) J. Cell Sci. , vol.113 , Issue.PT. 23 , pp. 4221-4230
    • Wang, D.1
  • 99
    • 0034677772 scopus 로고    scopus 로고
    • Involvement of focal adhesion kinase in hepatocyte growth factor-induced scatter of Madin-Darby canine kidney cells
    • Lai, J.F., et al., Involvement of focal adhesion kinase in hepatocyte growth factor-induced scatter of Madin-Darby canine kidney cells. J. Biol. Chem. 2000, 275, 7474-7480.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7474-7480
    • Lai, J.F.1
  • 100
    • 0034705424 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator stimulates the Ras/Extracellular signal-regulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc. Rapid dissociation of GRB2/Sps-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells
    • Nguyen, D.H., et al., Urokinase-type plasminogen activator stimulates the Ras/Extracellular signal-regulated kinase (ERK) signaling pathway and MCF-7 cell migration by a mechanism that requires focal adhesion kinase, Src, and Shc. Rapid dissociation of GRB2/Sps-Shc complex is associated with the transient phosphorylation of ERK in urokinase-treated cells. J. Biol. Chem. 2000, 275, 19382-19388.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19382-19388
    • Nguyen, D.H.1
  • 101
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke, R.L., et al., CAS/Crk coupling serves as a "molecular switch" for induction of cell migration. J. Cell Biol. 1998, 140, 961-972.
    • (1998) J. Cell Biol. , vol.140 , pp. 961-972
    • Klemke, R.L.1
  • 102
    • 0032509565 scopus 로고    scopus 로고
    • Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration
    • Cary, L.A., et al., Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration. J. Cell Biol. 1998, 140, 211-221.
    • (1998) J. Cell Biol. , vol.140 , pp. 211-221
    • Cary, L.A.1
  • 103
    • 0032472411 scopus 로고    scopus 로고
    • The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility
    • Fincham, V.J. and M.C. Frame, The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility. EMBO J. 1998, 17, 81-92.
    • (1998) EMBO J. , vol.17 , pp. 81-92
    • Fincham, V.J.1    Frame, M.C.2
  • 104
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer, R.A., et al., Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 1999, 18, 2459-2471.
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1
  • 105
    • 0032825266 scopus 로고    scopus 로고
    • Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells
    • Cheresh, D.A., J. Leng, and R.L. Klemke, Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells. J. Cell Biol. 1999, 146, 1107-1116.
    • (1999) J. Cell Biol. , vol.146 , pp. 1107-1116
    • Cheresh, D.A.1    Leng, J.2    Klemke, R.L.3
  • 106
    • 0034599542 scopus 로고    scopus 로고
    • Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix
    • Cho, S.Y. and R.L. Klemke, Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix. J. Cell Biol. 2000, 149, 223-236.
    • (2000) J. Cell Biol. , vol.149 , pp. 223-236
    • Cho, S.Y.1    Klemke, R.L.2
  • 107
    • 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., Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol. Cell. Biol. 1993, 13, 4648-4656.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4648-4656
    • Birge, R.B.1
  • 108
    • 0034610997 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells
    • Petit, V., et al., Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells. J. Cell Biol. 2000, 148, 957-970.
    • (2000) J. Cell Biol. , vol.148 , pp. 957-970
    • Petit, V.1
  • 109
    • 0033617357 scopus 로고    scopus 로고
    • Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration
    • Reiske, H.R., et al., Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration. J. Biol. Chem. 1999, 274, 12361-12366.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12361-12366
    • Reiske, H.R.1
  • 110
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the alpha6beta4 integrin promotes carcinoma invasion
    • Shaw, L.M., et al., Activation of phosphoinositide 3-OH kinase by the alpha6beta4 integrin promotes carcinoma invasion. Cell 1997, 91, 949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1
  • 111
    • 0028055272 scopus 로고
    • Regulation of chemotaxis by the platelet-derived growth factor receptor-beta
    • Kundra, V., et al., Regulation of chemotaxis by the platelet-derived growth factor receptor-beta. Nature 1994, 367, 474-476.
    • (1994) Nature , vol.367 , pp. 474-476
    • Kundra, V.1
  • 112
    • 0033529825 scopus 로고    scopus 로고
    • Focal adhesion kinase promotes phospholipase C-gamma1 activity
    • Zhang, X., et al., Focal adhesion kinase promotes phospholipase C-gamma1 activity. Proc. Natl. Acad. Sci. USA 1999, 96, 9021-9026.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9021-9026
    • Zhang, X.1
  • 113
    • 2542490290 scopus 로고    scopus 로고
    • Grb7 in intracellular signaling and its role in cell regulation
    • Shen, T.L. and J.L. Guan, Grb7 in intracellular signaling and its role in cell regulation. Front. Biosci. 2004, 9, 192-200.
    • (2004) Front. Biosci. , vol.9 , pp. 192-200
    • Shen, T.L.1    Guan, J.L.2
  • 114
    • 0031128420 scopus 로고    scopus 로고
    • C. elegans cell migration gene mig-10 shares similarities with a family of SH2 domain proteins and acts cell nonautonomously in excretory canal development
    • Manser, J., C. Roonprapunt, and B. Margolis, C. elegans cell migration gene mig-10 shares similarities with a family of SH2 domain proteins and acts cell nonautonomously in excretory canal development. Dev. Biol. 1997, 184, 150-164.
    • (1997) Dev. Biol. , vol.184 , pp. 150-164
    • Manser, J.1    Roonprapunt, C.2    Margolis, B.3
  • 115
    • 0000226650 scopus 로고    scopus 로고
    • Association of focal adhesion kinase with Grb7 and its role in cell migration
    • Han, D.C. and J.L. Guan, Association of focal adhesion kinase with Grb7 and its role in cell migration. J. Biol. Chem. 1999, 274, 24425-24430.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24425-24430
    • Han, D.C.1    Guan, J.L.2
  • 116
    • 0034666146 scopus 로고    scopus 로고
    • Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration
    • Han, D.C., T.L. Shen, and J.L. Guan, Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration. J. Biol. Chem. 2000, 275, 28911-28917.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28911-28917
    • Han, D.C.1    Shen, T.L.2    Guan, J.L.3
  • 117
    • 0037072731 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells
    • Chen, B.H., et al., Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells. J. Biol. Chem. 2002, 277, 33857-33863.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.H.1
  • 118
    • 0037416174 scopus 로고    scopus 로고
    • Differential regulation of cell motility and invasion by FAK
    • Hsia, D.A., et al., Differential regulation of cell motility and invasion by FAK. J. Cell Biol. 2003, 160, 753-767.
    • (2003) J. Cell Biol. , vol.160 , pp. 753-767
    • Hsia, D.A.1
  • 119
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer, D.D., S.K. Mitra, and D. Ilic, Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 2004, 1692, 77-102.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 120
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • Hildebrand, J.D., J.M. Taylor, and J.T. Parsons, An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase. Mol. Cell. Biol. 1996, 16, 3169-3178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 121
    • 0035985220 scopus 로고    scopus 로고
    • The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly
    • Liu, Y., et al., The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly. Mol. Biol. Cell 2002, 13, 2147-2156.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2147-2156
    • Liu, Y.1
  • 122
    • 1542304700 scopus 로고    scopus 로고
    • Focal adhesion kinase regulation of N-WASP subcellular localization and function
    • Wu, X., et al., Focal adhesion kinase regulation of N-WASP subcellular localization and function. J. Biol. Chem. 2004, 279, 9565-9576.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9565-9576
    • Wu, X.1
  • 123
    • 0037066778 scopus 로고    scopus 로고
    • V-Src SH3-enhanced interaction with focal adhesion kinase at beta 1 integrin-containing invadopodia promotes cell invasion
    • Hauck, C.R., et al., v-Src SH3-enhanced interaction with focal adhesion kinase at beta 1 integrin-containing invadopodia promotes cell invasion. J. Biol. Chem. 2002, 277, 12487-12490.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12487-12490
    • Hauck, C.R.1
  • 124
    • 0029039421 scopus 로고
    • Overexpression of the focal adhesion kinase (p125FAK) in invasive human tumors
    • Owens, L.V., et al., Overexpression of the focal adhesion kinase (p125FAK) in invasive human tumors. Cancer Res. 1995, 55, 2752-2755.
    • (1995) Cancer Res. , vol.55 , pp. 2752-2755
    • Owens, L.V.1
  • 125
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes
    • Cance, W.G., et al., Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes. Clin. Cancer Res. 2000, 6, 2417-2423.
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2417-2423
    • Cance, W.G.1
  • 126
    • 0031657454 scopus 로고    scopus 로고
    • Focal adhesion kinase and its potential involvement in tumor invasion and metastasis
    • Kornberg, L.J., Focal adhesion kinase and its potential involvement in tumor invasion and metastasis. Head Neck 1998, 20, 745-752.
    • (1998) Head Neck , vol.20 , pp. 745-752
    • Kornberg, L.J.1
  • 127
    • 0037011055 scopus 로고    scopus 로고
    • FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth
    • Hauck, C.R., et al., FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth. EMBO J. 2002, 21, 6289-6302.
    • (2002) EMBO J. , vol.21 , pp. 6289-6302
    • Hauck, C.R.1
  • 128
    • 0032031062 scopus 로고    scopus 로고
    • Both focal adhesion kinase and c-Ras are required for the enhanced matrix metalloproteinase 9 secretion by fibronectin in ovarian cancer cells
    • Shibata, K., et al., Both focal adhesion kinase and c-Ras are required for the enhanced matrix metalloproteinase 9 secretion by fibronectin in ovarian cancer cells. Cancer Res. 1998, 58, 900-903.
    • (1998) Cancer Res. , vol.58 , pp. 900-903
    • Shibata, K.1
  • 129
    • 22944438407 scopus 로고    scopus 로고
    • FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation
    • Wu, X., et al., FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation. Dev. Cell 2005, 9, 185-196.
    • (2005) Dev. Cell , vol.9 , pp. 185-196
    • Wu, X.1
  • 130
    • 0036570080 scopus 로고    scopus 로고
    • Increased Src activity disrupts cadherin/catenin-mediated homotypic adhesion in human colon cancer and transformed rodent cells
    • Irby, R.B. and T.J. Yeatman, Increased Src activity disrupts cadherin/catenin-mediated homotypic adhesion in human colon cancer and transformed rodent cells. Cancer Res. 2002, 62, 2669-2674.
    • (2002) Cancer Res. , vol.62 , pp. 2669-2674
    • Irby, R.B.1    Yeatman, T.J.2
  • 131
    • 0036048217 scopus 로고    scopus 로고
    • Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling
    • Avizienyte, E., et al., Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling. Nat. Cell Biol. 2002, 4, 632-638.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 632-638
    • Avizienyte, E.1
  • 132
    • 0035408594 scopus 로고    scopus 로고
    • Plasma membrane-associated pY397FAK is a marker of cytotrophoblast invasion in vivo and in vitro
    • Ilic, D., et al., Plasma membrane-associated pY397FAK is a marker of cytotrophoblast invasion in vivo and in vitro. Am. J. Pathol. 2001, 159, 93-108.
    • (2001) Am. J. Pathol. , vol.159 , pp. 93-108
    • Ilic, D.1
  • 133
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch, S.M., et al., Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 1996, 134, 793-799.
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1
  • 134
    • 0027967292 scopus 로고
    • A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK
    • Chan, P.Y., et al., A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK. J. Biol. Chem. 1994, 269, 20567-20574.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20567-20574
    • Chan, P.Y.1
  • 135
    • 0030300180 scopus 로고    scopus 로고
    • Inhibition of pp125FAK in cultured fibroblasts results in apoptosis
    • Hungerford, J.E., et al., Inhibition of pp125FAK in cultured fibroblasts results in apoptosis. J. Cell Biol. 1996, 135, 1383-1390.
    • (1996) J. Cell Biol. , vol.135 , pp. 1383-1390
    • Hungerford, J.E.1
  • 136
    • 0029848157 scopus 로고    scopus 로고
    • Attenuation of the expression of the focal adhesion kinase induces apoptosis in tumor cells
    • Xu, L.H., et al., Attenuation of the expression of the focal adhesion kinase induces apoptosis in tumor cells. Cell Growth Differ. 1996, 7, 413-418.
    • (1996) Cell Growth Differ. , vol.7 , pp. 413-418
    • Xu, L.H.1
  • 137
    • 0032547796 scopus 로고    scopus 로고
    • Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis
    • Ilic, D., et al., Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis. J. Cell Biol. 1998, 143, 547-560.
    • (1998) J. Cell Biol. , vol.143 , pp. 547-560
    • Ilic, D.1
  • 138
    • 0033578641 scopus 로고    scopus 로고
    • Suppression of ultraviolet irradiation-induced apoptosis by overexpression of focal adhesion kinase in Madin-Darby canine kidney cells
    • Chan, P.C., et al., Suppression of ultraviolet irradiation-induced apoptosis by overexpression of focal adhesion kinase in Madin-Darby canine kidney cells. J. Biol. Chem. 1999, 274, 26901-26906.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26901-26906
    • Chan, P.C.1
  • 139
    • 0034717285 scopus 로고    scopus 로고
    • Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60
    • Sonoda, Y., et al., Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60. J. Biol. Chem. 2000, 275, 16309-16315.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16309-16315
    • Sonoda, Y.1
  • 140
    • 0036081178 scopus 로고    scopus 로고
    • FAK blunts adenosine-homocysteine-induced endothelial cell apoptosis: requirement for PI 3-kinase
    • Bellas, R.E., et al., FAK blunts adenosine-homocysteine-induced endothelial cell apoptosis: requirement for PI 3-kinase. Am. J. Physiol. Lung Cell. Mol. Physiol. 2002, 282, L1135-L1142.
    • (2002) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.282
    • Bellas, R.E.1
  • 141
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • Vivanco, I. and C.L. Sawyers, The phosphatidylinositol 3-Kinase AKT pathway in human cancer. Nat. Rev. Cancer 2002, 2, 489-501.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 142
    • 0034194714 scopus 로고    scopus 로고
    • Matrix survival signaling: from fibronectin via focal adhesion kinase to c-Jun NH(2)-terminal kinase
    • Almeida, E.A., et al., Matrix survival signaling: from fibronectin via focal adhesion kinase to c-Jun NH(2)-terminal kinase. J. Cell Biol. 2000, 149, 741-754.
    • (2000) J. Cell Biol. , vol.149 , pp. 741-754
    • Almeida, E.A.1
  • 143
    • 2942531163 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses apoptosis by binding to the death domain of receptor-interacting protein
    • Kurenova, E., et al., Focal adhesion kinase suppresses apoptosis by binding to the death domain of receptor-interacting protein. Mol. Cell. Biol. 2004, 24, 4361-4371.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4361-4371
    • Kurenova, E.1
  • 144
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Deveraux, Q.L. and J.C. Reed, IAP family proteins-suppressors of apoptosis. Genes Dev. 1999, 13, 239-252.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 145
    • 0032576547 scopus 로고    scopus 로고
    • Regulation of the cell cycle by focal adhesion kinase
    • Zhao, J.H., H. Reiske, and J.L. Guan, Regulation of the cell cycle by focal adhesion kinase. J. Cell Biol. 1998, 143, 1997-2008.
    • (1998) J. Cell Biol. , vol.143 , pp. 1997-2008
    • Zhao, J.H.1    Reiske, H.2    Guan, J.L.3
  • 146
    • 0035661624 scopus 로고    scopus 로고
    • Transcriptional activation of cyclin D1 promoter by FAK contributes to cell cycle progression
    • Zhao, J., R. Pestell, and J.L. Guan, Transcriptional activation of cyclin D1 promoter by FAK contributes to cell cycle progression. Mol. Biol. Cell 2001, 12, 4066-4077.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4066-4077
    • Zhao, J.1    Pestell, R.2    Guan, J.L.3
  • 147
    • 4444250590 scopus 로고    scopus 로고
    • Focal adhesion kinase (FAK)-dependent regulation of S-phase kinase-associated protein-2 (Skp-2) stability. A novel mechanism regulating smooth muscle cell proliferation
    • Bond, M., G.B. Sala-Newby, and A.C. Newby, Focal adhesion kinase (FAK)-dependent regulation of S-phase kinase-associated protein-2 (Skp-2) stability. A novel mechanism regulating smooth muscle cell proliferation. J. Biol. Chem. 2004, 279, 37304-37310.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37304-37310
    • Bond, M.1    Sala-Newby, G.B.2    Newby, A.C.3
  • 148
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano, A.C., et al., SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat. Cell Biol. 1999, 1, 193-199.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 193-199
    • Carrano, A.C.1
  • 149
    • 0033174070 scopus 로고    scopus 로고
    • P45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells
    • Sutterluty, H., et al., p45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells. Nat. Cell Biol. 1999, 1, 207-214.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 207-214
    • Sutterluty, H.1
  • 150
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta, Y., et al., Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 1995, 11, 1989-1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1
  • 151
    • 0028924161 scopus 로고
    • Focal adhesion kinase is not essential for in vitro and in vivo differentiation of ES cells
    • Ilic, D., et al., Focal adhesion kinase is not essential for in vitro and in vivo differentiation of ES cells. Biochem. Biophys. Res. Commun. 1995, 209, 300-309.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 300-309
    • Ilic, D.1
  • 152
    • 31044436891 scopus 로고    scopus 로고
    • Inactivation of focal adhesion kinase in cardiomyocytes promotes eccentric cardiac hypertrophy and fibrosis in mice
    • Peng, X., et al., Inactivation of focal adhesion kinase in cardiomyocytes promotes eccentric cardiac hypertrophy and fibrosis in mice. J. Clin. Invest. 2006, 116, 217-227.
    • (2006) J. Clin. Invest. , vol.116 , pp. 217-227
    • Peng, X.1
  • 153
    • 33748741079 scopus 로고    scopus 로고
    • Myocyte-restricted focal adhesion kinase deletion attenuates pressure overload-induced hypertrophy
    • DiMichele, L.A., et al., Myocyte-restricted focal adhesion kinase deletion attenuates pressure overload-induced hypertrophy. Circ. Res. 2006, 99, 636-645.
    • (2006) Circ. Res. , vol.99 , pp. 636-645
    • DiMichele, L.A.1
  • 154
    • 22344434300 scopus 로고    scopus 로고
    • Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis
    • Shen, T.L., et al., Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis. J. Cell Biol. 2005, 169, 941-952.
    • (2005) J. Cell Biol. , vol.169 , pp. 941-952
    • Shen, T.L.1
  • 155
    • 0345550397 scopus 로고    scopus 로고
    • FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies
    • Beggs, H.E., et al., FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies. Neuron 2003, 40, 501-514.
    • (2003) Neuron , vol.40 , pp. 501-514
    • Beggs, H.E.1
  • 156
    • 33244478048 scopus 로고    scopus 로고
    • Hair cycle and wound healing in mice with a keratinocyte-restricted deletion of FAK
    • Essayem, S., et al., Hair cycle and wound healing in mice with a keratinocyte-restricted deletion of FAK. Oncogene 2006, 25, 1081-1089.
    • (2006) Oncogene , vol.25 , pp. 1081-1089
    • Essayem, S.1


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