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Volumn 16, Issue 6, 1996, Pages 3169-3178

An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL CYCLE PROTEIN; COMPLEMENTARY DNA; FOCAL ADHESION KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; INTEGRIN; PROTEIN CDC42; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 0029955660     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.6.3169     Document Type: Article
Times cited : (307)

References (68)
  • 2
    • 0028236960 scopus 로고
    • FAK and protein kinase C-δ to focal adhesions
    • FAK and protein kinase C-δ to focal adhesions. J. Cell Sci. 107:2033-2045.
    • (1994) J. Cell Sci. , vol.107 , pp. 2033-2045
    • Barry, S.T.1    Critchley, D.R.2
  • 3
    • 0027170920 scopus 로고
    • SH3 domains direct cellular localization of signaling molecules
    • Bar-Sagi, D., D. Rotin, A. Batzer, V. Mandiyan, and J. Schlessinger. 1993 SH3 domains direct cellular localization of signaling molecules. Cell 74:83-92.
    • (1993) Cell , vol.74 , pp. 83-92
    • Bar-Sagi, D.1    Rotin, D.2    Batzer, A.3    Mandiyan, V.4    Schlessinger, J.5
  • 5
    • 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., J. E. Fajardo, C. Reichman, S. E. Shoelson, Z. Songyang, L. C. Cantley, and H. Hanafusa. 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    Fajardo, J.E.2    Reichman, C.3    Shoelson, S.E.4    Songyang, Z.5    Cantley, L.C.6    Hanafusa, H.7
  • 6
    • 0027227263 scopus 로고
    • Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin
    • Bockholt, S. M., and K. Burridge. 1993. Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J. Biol. Chem. 268:14565-14567.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14565-14567
    • Bockholt, S.M.1    Burridge, K.2
  • 7
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S., and F. McCormick. 1993. Proteins regulating Ras and its relatives. Nature (London) 366:643-654.
    • (1993) Nature (London) , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 8
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau, N., C. J. Sympson, Z. Werb, and M. Bissell. 1995. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 267:891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.4
  • 9
    • 0021219408 scopus 로고
    • src inactivate tyrosine protein kinase activity
    • src inactivate tyrosine protein kinase activity. Mol. Cell. Biol. 4:862-866.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 862-866
    • Bryant, D.1    Parsons, J.T.2
  • 10
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. E. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.E.5
  • 11
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893-903.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 12
    • 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. 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
  • 13
    • 0029153801 scopus 로고
    • Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation
    • Chang, J.-H., S. Gill, J. Settleman, and S. J. Parsons. 1995 c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation. J. Cell Biol. 130:355-368.
    • (1995) J. Cell Biol. , vol.130 , pp. 355-368
    • Chang, J.-H.1    Gill, S.2    Settleman, J.3    Parsons, S.J.4
  • 15
    • 0027938974 scopus 로고
    • Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
    • Chen, H.-C., and J.-L. Guan. 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
  • 16
    • 0028036684 scopus 로고
    • The small GTP-binding protein rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., A. Traynor-Kaplan, G. M. Bokoch, and M. A. Schwartz. 1994. The small GTP-binding protein rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 17
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways. the road taken
    • Clark, E. A., and J. S. Brugge. 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
  • 19
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, G. B., R. Ren, and D. Baltimore. 1995. Modular binding domains in signal transduction proteins. Cell 80:237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 20
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPk signaling pathway
    • Coso, O. A., M. Chiariello, J.-C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and J. S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPk signaling pathway. Cell 81:1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.-C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 21
  • 22
    • 0027752979 scopus 로고
    • A link between cyclin A expression and adhesion-dependent cell cycle progression
    • Guadagno, T. M., M. Ohtsubo, J. M. Roberts, and R. K. Assoian. 1993. A link between cyclin A expression and adhesion-dependent cell cycle progression. Science 262:1572-1575.
    • (1993) Science , vol.262 , pp. 1572-1575
    • Guadagno, T.M.1    Ohtsubo, M.2    Roberts, J.M.3    Assoian, R.K.4
  • 23
    • 0026759309 scopus 로고
    • FAK both by cellular adhesion and by oncogenic transformation
    • FAK both by cellular adhesion and by oncogenic transformation. Nature (London) 358:690-692.
    • (1992) Nature (London) , vol.358 , pp. 690-692
    • Guan, J.-L.1    Shalloway, D.2
  • 24
    • 0028951464 scopus 로고
    • Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85α with actin filaments and focal adhesion kinase
    • Guinebault, C., H. Payratre, C. Racaud-Sultan, H. Mazarguil, M. Breton, G. Mauco, M. Plantavid, and H. Chap. 1995. Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85α with actin filaments and focal adhesion kinase. J. Cell Biol. 129:831-842.
    • (1995) J. Cell Biol. , vol.129 , pp. 831-842
    • Guinebault, C.1    Payratre, H.2    Racaud-Sultan, C.3    Mazarguil, H.4    Breton, M.5    Mauco, G.6    Plantavid, M.7    Chap, H.8
  • 25
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. 1994. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10:31-54.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 26
    • 0026674919 scopus 로고
    • Focal adhesion protein tyrosine kinase phosphorylated in response to cell spreading on fibronectin
    • Hanks, S. K., M. B. Calalb, M. C. Harper, and S. K. Patel. 1992. Focal adhesion protein tyrosine kinase phosphorylated in response to cell spreading on fibronectin. Proc. Natl. Acad. Sci. USA 89:8487-8489.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8489
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 29
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein, binds to the carboxy terminal domain of focal adhesion kinase
    • Hildebrand, J. D., M. D. Schaller, and J. T. Parsons. 1995. Paxillin, a tyrosine phosphorylated focal adhesion-associated protein, binds to the carboxy 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
  • 30
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs, regulate transcriptional activation by SRF
    • Hill, S. H., J. Wyanne, and R. Treisman. 1995. The Rho family GTPases RhoA, Rac1, and CDC42Hs, regulate transcriptional activation by SRF. Cell 81:1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, S.H.1    Wyanne, J.2    Treisman, R.3
  • 31
    • 0023265819 scopus 로고
    • Adaptor plasmids simplify the insertion of foreign DNA into helper-independent retroviral vectors
    • Hughes, S. H., J. J. Greenhouse, C. J. Petropoulos, and P. Sutrave. 1987. Adaptor plasmids simplify the insertion of foreign DNA into helper-independent retroviral vectors. J. Virol. 61:3004-3012.
    • (1987) J. Virol. , vol.61 , pp. 3004-3012
    • Hughes, S.H.1    Greenhouse, J.J.2    Petropoulos, C.J.3    Sutrave, P.4
  • 32
    • 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
  • 33
    • 0024327617 scopus 로고
    • Association of type 3 protein kinase C with focal adhesions in rat embryo fibroblasts
    • Jaken, S., K. Leach, and T. Klauck. 1989. Association of type 3 protein kinase C with focal adhesions in rat embryo fibroblasts. J. Cell Biol. 109:697-704.
    • (1989) J. Cell Biol. , vol.109 , pp. 697-704
    • Jaken, S.1    Leach, K.2    Klauck, T.3
  • 34
    • 0023199043 scopus 로고
    • Inositol lipids dissociate gelsolin-actin complexes
    • Janmey, P. A., K. I. Ada, H. L. Yin, and T. P. Stossel. 1987. Inositol lipids dissociate gelsolin-actin complexes. J. Biol. Chem. 262:12228-12236.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12228-12236
    • Janmey, P.A.1    Ada, K.I.2    Yin, H.L.3    Stossel, T.P.4
  • 36
    • 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., K. B. Bibbins, J. R. Swedlow, M. Arnaud, D. O. Morgan, and H. E. Varmus. 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. 13:4747-4756.
    • (1994) EMBO J. , vol.13 , pp. 4747-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 37
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak, M. 1987. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:8125-8148.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 38
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibrohlasts
    • Kozma, R., S. Ahmed, A. Best, and L. Lim. 1995. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibrohlasts. Mol. Cell. Biol. 15:1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 0021919105 scopus 로고
    • Specific interactions between phosphatidylinositols-4.5-bisphosphate and profilactin
    • Lassing, I., and U. Lindberg. 1985. Specific interactions between phosphatidylinositols-4.5-bisphosphate and profilactin. Nature (London) 314:472-474.
    • (1985) Nature (London) , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 42
    • 0021683127 scopus 로고
    • Monoclonal antibodies specific for the carboxy terminus of simian virus 40 large T antigen
    • MacArthur, H., and G. Walter. 1984. Monoclonal antibodies specific for the carboxy terminus of simian virus 40 large T antigen. J. Virol. 52:483-491.
    • (1984) J. Virol. , vol.52 , pp. 483-491
    • MacArthur, H.1    Walter, G.2
  • 43
    • 0027235324 scopus 로고
    • A non-receptor tyrosine kinase that inhibits the GTPase activity of p21Cdc42
    • Manser, E., E. T. Leung, H. Salihuddin, L. Tan, and L. Lim. 1993. A non-receptor tyrosine kinase that inhibits the GTPase activity of p21Cdc42. Nature (London) 363:364-367.
    • (1993) Nature (London) , vol.363 , pp. 364-367
    • Manser, E.1    Leung, E.T.2    Salihuddin, H.3    Tan, L.4    Lim, L.5
  • 44
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., E. T. Leung, H. Salihuddin, Z. S. Zhao, and L. Lim. 1994. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature (London) 367:40-46.
    • (1994) Nature (London) , vol.367 , pp. 40-46
    • Manser, E.1    Leung, E.T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 45
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., A. Lin, F.-X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.-X.3    Abo, A.4    Karin, M.5
  • 46
    • 0028961293 scopus 로고
    • Rho, Rae, and Cdc42 GTPases regulate the assembly of multi-molecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rae, and Cdc42 GTPases regulate the assembly of multi-molecular 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
  • 48
    • 0028911031 scopus 로고
    • A novel type of myosin implicated in signaling by the rho family of GTPases
    • Reinhard, J., A. A. Scheel, D. Diekmann, A. Hall, C. Ruppert, and M. Bahler. 1995. A novel type of myosin implicated in signaling by the rho family of GTPases. EMBO J. 4:697-704.
    • (1995) EMBO J. , vol.4 , pp. 697-704
    • Reinhard, J.1    Scheel, A.A.2    Diekmann, D.3    Hall, A.4    Ruppert, C.5    Bahler, M.6
  • 49
    • 0024599702 scopus 로고
    • Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene
    • Reynolds, A. B., D. J. Roesel, S. B. Kanner, and J. T. Parsons. 1989. Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular src gene. Mol. Cell. Biol. 9:629-638.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 629-638
    • Reynolds, A.B.1    Roesel, D.J.2    Kanner, S.B.3    Parsons, J.T.4
  • 50
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson, A., and J. T. Parsons. 1995. Signal transduction through integrins: a central role for focal adhesion kinase? BioEssays 17:229-236.
    • (1995) BioEssays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 51
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 52
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: Requirement for a tyrosine kinase
    • Ridley, A. J., and A. Hall. 1994. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J. 13:2600-2610.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 53
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 54
    • 0027441940 scopus 로고
    • Rho family GTPase activating proteins p 190, her and rhoGAP show distinct specificities in vitro and in vivo
    • Ridley, A. J., A. J. Self, F. Kasmi, H. F. Paterson, A. Hall, C. J. Marshall, and C. Ellis. 1993. Rho family GTPase activating proteins p 190, her and rhoGAP show distinct specificities in vitro and in vivo. EMBO J. 12:5151-5160.
    • (1993) EMBO J. , vol.12 , pp. 5151-5160
    • Ridley, A.J.1    Self, A.J.2    Kasmi, F.3    Paterson, H.F.4    Hall, A.5    Marshall, C.J.6    Ellis, C.7
  • 55
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti, E., and J. C. Reed. 1994. Anchorage dependence, integrins, and apoptosis. Cell 77:477-478.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 59
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains
    • Schaller, M. D., C. A. Otey, J. D. Hildebrand, and J. T. Parsons. 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
  • 60
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associ-ated proteins
    • Schaller, M. D., and J. T. Parsons. 1994. Focal adhesion kinase and associ-ated proteins. Curr. Opin. Cell Biol. 6:705-710.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 61
    • 0028986116 scopus 로고
    • FAK-dependent phosphorylation of paxillin creates a high-affinity binding site for Crk
    • FAK-dependent 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
  • 62
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase
    • Schlaepfer, D. D., S. K. Hanks, T. Hunter, and P. van der Geer. 1994. Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase. Nature (London) 372:786-791.
    • (1994) Nature (London) , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 64
  • 65
    • 0024623870 scopus 로고
    • Molecular cloning of sequence-specific DNA binding proteins using recognition site probes
    • Singh, H., R. G. Clerc, and J. H. LeBowitz. 1989. Molecular cloning of sequence-specific DNA binding proteins using recognition site probes. Bio-Techniques 7:252-261.
    • (1989) Bio-Techniques , vol.7 , pp. 252-261
    • Singh, H.1    Clerc, R.G.2    Lebowitz, J.H.3
  • 67
    • 0024335963 scopus 로고
    • Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression
    • Werb, Z., P. M. Tremble, O. Behrendtsen, E. Crowley, and C. H. Damsky. 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    Behrendtsen, O.3    Crowley, E.4    Damsky, C.H.5
  • 68
    • 0025651999 scopus 로고
    • Cap39, a calcium ion- And polyphosphoinositide-regulated actin capping protein
    • Yu, F.-X., P. A. Johnston, T. C. Sudhof, and H. L. Yin. 1990. Cap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. Science 250:1413-1415.
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.-X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4


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