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Volumn 3, Issue C, 1996, Pages 133-158

The cytoskeleton and neoplastic transformation

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EID: 77957121117     PISSN: 18746020     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6020(96)80007-3     Document Type: Review
Times cited : (2)

References (137)
  • 1
    • 0026639826 scopus 로고
    • Signal transduction and the actin cytoskeleton: The role of MARKS and profilin
    • Adarem A. Signal transduction and the actin cytoskeleton: The role of MARKS and profilin. Trends. Bioch. Sci. 17 (1992) 438-443
    • (1992) Trends. Bioch. Sci. , vol.17 , pp. 438-443
    • Adarem, A.1
  • 3
    • 0017646305 scopus 로고
    • Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein
    • Ali I.U., Mautner V., Lanza R., and Hynes R.O. Restoration of normal morphology, adhesion and cytoskeleton in transformed cells by addition of a transformation-sensitive surface protein. Cell 11 (1977) 115-126
    • (1977) Cell , vol.11 , pp. 115-126
    • Ali, I.U.1    Mautner, V.2    Lanza, R.3    Hynes, R.O.4
  • 4
  • 5
    • 0021915158 scopus 로고
    • Increased phosphorylation of tyrosine in vinculin does not occur upon transformation by some avian sarcoma viruses
    • Antler A.M., Greenberg M.E., Edelman G.M., and Hanafusa H. Increased phosphorylation of tyrosine in vinculin does not occur upon transformation by some avian sarcoma viruses. Mol. Cell. Biol. 5 (1985) 263-267
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 263-267
    • Antler, A.M.1    Greenberg, M.E.2    Edelman, G.M.3    Hanafusa, H.4
  • 7
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cell transformed with a temperature-sensitive v-SRC gene
    • Behrens J., Vakaet L., Friis R., Winterhager E., Van Roy F., Mareel M.M., and Birchmeier W. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cell transformed with a temperature-sensitive v-SRC gene. J. Cell Biol. 120 (1993) 757-766
    • (1993) J. Cell Biol. , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 8
    • 0020081847 scopus 로고
    • On the dynamics of the microfilament system in HeLa cells
    • Blikstad I., and Carlsson L. On the dynamics of the microfilament system in HeLa cells. J. Cell Biol. 93 (1982) 122-128
    • (1982) J. Cell Biol. , vol.93 , pp. 122-128
    • Blikstad, I.1    Carlsson, L.2
  • 9
    • 0027232605 scopus 로고
    • Emerging concepts in the ras superfamily of GTP-binding proteins
    • Bokoch G.M., and Der C.J. Emerging concepts in the ras superfamily of GTP-binding proteins. FASEB J. 7 (1993) 750-759
    • (1993) FASEB J. , vol.7 , pp. 750-759
    • Bokoch, G.M.1    Der, C.J.2
  • 10
    • 0019472077 scopus 로고
    • Early changes in the distribution and organisation of micro-filament proteins during cell transformation
    • Boschek C.B., Jockusch B.M., Friis R.R., Back R., Gandemann E., and Bauer H. Early changes in the distribution and organisation of micro-filament proteins during cell transformation. Cell 24 (1981) 175-184
    • (1981) Cell , vol.24 , pp. 175-184
    • Boschek, C.B.1    Jockusch, B.M.2    Friis, R.R.3    Back, R.4    Gandemann, E.5    Bauer, H.6
  • 11
    • 0025181618 scopus 로고
    • Disintegration of adhesion plaques in chick embryo fibroblasts upon Rous sarcoma virus transformation: Different dissociation rates for talin and vinculin
    • Brands R., De Boer A., Feltkamp C.A., and Roos E. Disintegration of adhesion plaques in chick embryo fibroblasts upon Rous sarcoma virus transformation: Different dissociation rates for talin and vinculin. Exptl. Cell Res. 186 (1990) 138-148
    • (1990) Exptl. Cell Res. , vol.186 , pp. 138-148
    • Brands, R.1    De Boer, A.2    Feltkamp, C.A.3    Roos, E.4
  • 12
    • 0018956423 scopus 로고
    • Variations in cell form and cytoskeleton in human breast carcinoma cells in vitro
    • Brinkley B.R., Beall P., Wible L., Mace M., Turner D., and Cailleau R. Variations in cell form and cytoskeleton in human breast carcinoma cells in vitro. Cancer Res. 40 (1980) 3118-3129
    • (1980) Cancer Res. , vol.40 , pp. 3118-3129
    • Brinkley, B.R.1    Beall, P.2    Wible, L.3    Mace, M.4    Turner, D.5    Cailleau, R.6
  • 13
    • 0041023111 scopus 로고
    • Sequence of events in the transformation process in cells infected with a temperature-sensitive transformation mutant of Moloney murine sarcoma virus
    • Brown R.L., Horn J.P., Wible L., Arlinghaus R.B., and Brinkley B.R. Sequence of events in the transformation process in cells infected with a temperature-sensitive transformation mutant of Moloney murine sarcoma virus. Proc. Natl. Acad. Sci. USA 78 (1981) 5593-5597
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5593-5597
    • Brown, R.L.1    Horn, J.P.2    Wible, L.3    Arlinghaus, R.B.4    Brinkley, B.R.5
  • 15
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein and Sos nucleotide exchange factor
    • Buday L., and Downward J. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein and Sos nucleotide exchange factor. Cell 73 (1993) 611-620
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 16
    • 0019307674 scopus 로고
    • Association of the src gene product of Rous sarcoma virus with cytoskeletal structures of chick embryo fibroblasts
    • Burr J.G., Dreyfuss G., Penman S., and Buchanan J.M. Association of the src gene product of Rous sarcoma virus with cytoskeletal structures of chick embryo fibroblasts. Proc. Natl. Acad. Sci. USA 77 (1981) 3484-3488
    • (1981) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3484-3488
    • Burr, J.G.1    Dreyfuss, G.2    Penman, S.3    Buchanan, J.M.4
  • 17
    • 0023027454 scopus 로고
    • Substrate adhesions in normal and transformed fibroblasts: Organization and regulation of cytoskeletal, membrane and extracellular matrix components at focal contacts
    • Burridge K. Substrate adhesions in normal and transformed fibroblasts: Organization and regulation of cytoskeletal, membrane and extracellular matrix components at focal contacts. Cancer Rev. 4 (1986) 18-78
    • (1986) Cancer Rev. , vol.4 , pp. 18-78
    • Burridge, K.1
  • 18
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques
    • Burridge K., and Connell L. A new protein of adhesion plaques. J. Cell Biol. 97 (1983) 359-367
    • (1983) J. Cell Biol. , vol.97 , pp. 359-367
    • Burridge, K.1    Connell, L.2
  • 19
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between extracellular matrix and the cytoskeleton
    • Burridge K., Fath K., Kelly T., Nuckolls G., and Turner C. Focal adhesions: Transmembrane junctions between extracellular matrix and the cytoskeleton. Ann. Rev. Cell Biol. 4 (1988) 487-525
    • (1988) Ann. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 20
    • 0021214312 scopus 로고
    • An interaction between vinculin and talin
    • Burridge K., and Mangeat P. An interaction between vinculin and talin. Nature 308 (1984) 744-746
    • (1984) Nature , vol.308 , pp. 744-746
    • Burridge, K.1    Mangeat, P.2
  • 21
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • Burridge K., Turner C.E., and Romer L.H. Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly. J. Cell Biol. 119 (1992) 893-903
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 22
    • 0022982333 scopus 로고
    • Regulation of fibronectin receptor distribution by transformation, exogenous fibronectin and synthetic peptides
    • Chen W.-T., Wang J., Hasegawa T., Yamada S.S., and Yamada K.M. Regulation of fibronectin receptor distribution by transformation, exogenous fibronectin and synthetic peptides. J. Cell Biol. 103 (1986) 1649-1661
    • (1986) J. Cell Biol. , vol.103 , pp. 1649-1661
    • Chen, W.-T.1    Wang, J.2    Hasegawa, T.3    Yamada, S.S.4    Yamada, K.M.5
  • 23
    • 0023868707 scopus 로고
    • The growth cone cytoskeleton. Glycoprotein association, calmodulin binding, and tyrosine/serine phosphorylation of tubulin
    • Cheng N., and Sayhoun N. The growth cone cytoskeleton. Glycoprotein association, calmodulin binding, and tyrosine/serine phosphorylation of tubulin. J. Biol. Chem. 8 (1988) 3935-3942
    • (1988) J. Biol. Chem. , vol.8 , pp. 3935-3942
    • Cheng, N.1    Sayhoun, N.2
  • 24
    • 0027340192 scopus 로고
    • c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets
    • c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol. Cell. Biol. 13 (1993) 1863-1871
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1863-1871
    • Clark, E.A.1    Brugge, J.S.2
  • 25
    • 0021400799 scopus 로고
    • detection of phosphotyrosine-containing proteins in the detergent-insoluble fraction of RSV-transformed fibroblasts by azobenzophosphanate antibodies
    • Comoglio P.M., Direnzo M.F., Tarone G., Giancotti F.G., Naldini L., and Marchisio P.C. detection of phosphotyrosine-containing proteins in the detergent-insoluble fraction of RSV-transformed fibroblasts by azobenzophosphanate antibodies. EMBO J. 3 (1984) 483-489
    • (1984) EMBO J. , vol.3 , pp. 483-489
    • Comoglio, P.M.1    Direnzo, M.F.2    Tarone, G.3    Giancotti, F.G.4    Naldini, L.5    Marchisio, P.C.6
  • 26
    • 0020998090 scopus 로고
    • Regulation of cell growth and transformation by the tyrosine-specific protein kinases: The search for important cellular substrate proteins
    • Cooper J.A., and Hunter T. Regulation of cell growth and transformation by the tyrosine-specific protein kinases: The search for important cellular substrate proteins. Curr. Top. Microbiol. Immunol. 107 (1983) 125-162
    • (1983) Curr. Top. Microbiol. Immunol. , vol.107 , pp. 125-162
    • Cooper, J.A.1    Hunter, T.2
  • 29
    • 0025261843 scopus 로고
    • Phosphorylation of connexin-43 gap junction protein in uninfected and RSV-transformed mammalian fibroblasts
    • Crow D.S., Beyer E.C., Paul D.L., Kobe S.S., and Lau A.F. Phosphorylation of connexin-43 gap junction protein in uninfected and RSV-transformed mammalian fibroblasts. Mol. Cell. Biol. 10 (1990) 1754-1780
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1754-1780
    • Crow, D.S.1    Beyer, E.C.2    Paul, D.L.3    Kobe, S.S.4    Lau, A.F.5
  • 31
    • 0025605786 scopus 로고
    • Immunolocalisation of the cellular src protein in interphase and mitotic NIH c-src overexpressor cells
    • David-Pfeuty T., and Nouvian-Dooghe Y. Immunolocalisation of the cellular src protein in interphase and mitotic NIH c-src overexpressor cells. J. Cell Biol. 111 (1990) 3097-3116
    • (1990) J. Cell Biol. , vol.111 , pp. 3097-3116
    • David-Pfeuty, T.1    Nouvian-Dooghe, Y.2
  • 32
    • 0019294081 scopus 로고
    • Altered distributions of the cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus
    • David-Pfeuty T., and Singer S.J. Altered distributions of the cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 77 (1980) 6687-6691
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 6687-6691
    • David-Pfeuty, T.1    Singer, S.J.2
  • 33
    • 0023085011 scopus 로고
    • Phosphorylation of talin at tyrosine in Rous sarcoma virus transformed cells
    • Declue J.E., and Martin G.S. Phosphorylation of talin at tyrosine in Rous sarcoma virus transformed cells. Mol. Cell. Biol. 7 (1987) 371-378
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 371-378
    • Declue, J.E.1    Martin, G.S.2
  • 34
    • 0025082999 scopus 로고
    • Tyrosine-specific phosphorylation of gpIIIa in platelet membranes
    • Elmore M.A., Anand R., Horvath A.R., and Kellie S. Tyrosine-specific phosphorylation of gpIIIa in platelet membranes. FEBS Letts. 269 (1990) 283-287
    • (1990) FEBS Letts. , vol.269 , pp. 283-287
    • Elmore, M.A.1    Anand, R.2    Horvath, A.R.3    Kellie, S.4
  • 35
    • 0025196249 scopus 로고
    • v-src association with the cytoskeleton induces actin reorganization without affecting polymerization status
    • v-src association with the cytoskeleton induces actin reorganization without affecting polymerization status. Eur. J. Cell Biol. 52 (1990) 47-59
    • (1990) Eur. J. Cell Biol. , vol.52 , pp. 47-59
    • Felice, G.R.1    Eason, P.2    Nermut, M.V.3    Kellie, S.4
  • 36
    • 0021719520 scopus 로고
    • Microinjection of the oncogenic form of the human H-ras (T24) protein results in rapid proliferation of quiescent cells
    • Feramisco J.R., Kamata T., Gross M., Rosenberg M., and Sweet R.W. Microinjection of the oncogenic form of the human H-ras (T24) protein results in rapid proliferation of quiescent cells. Cell 38 (1984) 109-117
    • (1984) Cell , vol.38 , pp. 109-117
    • Feramisco, J.R.1    Kamata, T.2    Gross, M.3    Rosenberg, M.4    Sweet, R.W.5
  • 37
    • 3142588838 scopus 로고
    • Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets
    • Ferrell J.E., and Martin G.S. Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets. Proc. Natl. Acad. Sci. USA 86 (1989) 2234-2238
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2234-2238
    • Ferrell, J.E.1    Martin, G.S.2
  • 40
    • 0021265128 scopus 로고
    • Actin cytoskeletal reorganisation loss in benign-to-malignant tumor transitions in cultured human colonic cells
    • Friedman E., Verderame M., Winawer S., and Pollack R. Actin cytoskeletal reorganisation loss in benign-to-malignant tumor transitions in cultured human colonic cells. Cancer Res. 44 (1984) 3040-3050
    • (1984) Cancer Res. , vol.44 , pp. 3040-3050
    • Friedman, E.1    Verderame, M.2    Winawer, S.3    Pollack, R.4
  • 41
    • 0344496523 scopus 로고
    • Phosphorylation of tyrosine residues of calmodulin in Rous sarcoma virus transformed cells
    • Fukami Y., Nakamura T., Nakayama A., and Karehisa T. Phosphorylation of tyrosine residues of calmodulin in Rous sarcoma virus transformed cells. Proc. Natl. Acad. Sci. USA 83 (1986) 4190-4193
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4190-4193
    • Fukami, Y.1    Nakamura, T.2    Nakayama, A.3    Karehisa, T.4
  • 42
    • 0027229556 scopus 로고
    • GRB2 mediates the EGF-dependent activation of guanine nucleotide exchange on ras
    • Gale W.N., Kaplan D., Lowenstein E.J., Schlessinger J., and Bar-Sagi D. GRB2 mediates the EGF-dependent activation of guanine nucleotide exchange on ras. Nature 363 (1993) 88-92
    • (1993) Nature , vol.363 , pp. 88-92
    • Gale, W.N.1    Kaplan, D.2    Lowenstein, E.J.3    Schlessinger, J.4    Bar-Sagi, D.5
  • 43
    • 0024728927 scopus 로고
    • Ultrastructure and gold immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells
    • Gavazzi I., Nermut M.V., and Marchisio P.C. Ultrastructure and gold immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells. J. Cell Sci. 94 (1989) 85-99
    • (1989) J. Cell Sci. , vol.94 , pp. 85-99
    • Gavazzi, I.1    Nermut, M.V.2    Marchisio, P.C.3
  • 44
    • 0022441416 scopus 로고
    • A 135,000 molecular weight plasma membrane glycoprotein involved in fibronectin-mediated cell adhesion
    • Giancotti F.G., Comoglio P.M., and Tarone G. A 135,000 molecular weight plasma membrane glycoprotein involved in fibronectin-mediated cell adhesion. Exp. Cell Res. 163 (1986) 47-62
    • (1986) Exp. Cell Res. , vol.163 , pp. 47-62
    • Giancotti, F.G.1    Comoglio, P.M.2    Tarone, G.3
  • 45
    • 0025214421 scopus 로고
    • 1 fibronectin receptor suppresses the transformed phenotype of chinese hamster ovary cells
    • 1 fibronectin receptor suppresses the transformed phenotype of chinese hamster ovary cells. Cell 69 (1990) 849-859
    • (1990) Cell , vol.69 , pp. 849-859
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 47
    • 0024382542 scopus 로고
    • Novel tyrosine kinase substrates from Rous sarcoma virus transformed cells are present in the membrane skeleton
    • Glenney J.R., and Zokas L. Novel tyrosine kinase substrates from Rous sarcoma virus transformed cells are present in the membrane skeleton. J. Cell Biol. 108 (1989) 2401-2408
    • (1989) J. Cell Biol. , vol.108 , pp. 2401-2408
    • Glenney, J.R.1    Zokas, L.2
  • 49
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • Guan J.-L., Trevithick J.E., and Hynes R.O. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Reg. 2 (1991) 951-964
    • (1991) Cell Reg. , vol.2 , pp. 951-964
    • Guan, J.-L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 50
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan J.-L., and Shalloway D. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358 (1992) 690-692
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.-L.1    Shalloway, D.2
  • 51
    • 0027242121 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal reorganisation in platelets are triggered by interaction of integrin receptors with their immobilized ligands
    • Haimovich B., Lipfert L., Brugge J.S., and Shattil S. Tyrosine phosphorylation and cytoskeletal reorganisation in platelets are triggered by interaction of integrin receptors with their immobilized ligands. J. Biol. Chem. 268 (1993) 15868-15877
    • (1993) J. Biol. Chem. , vol.268 , pp. 15868-15877
    • Haimovich, B.1    Lipfert, L.2    Brugge, J.S.3    Shattil, S.4
  • 52
    • 0023317189 scopus 로고
    • src with triton X-100-resistant cellular structure correlates with morphological transformation
    • src with triton X-100-resistant cellular structure correlates with morphological transformation. Proc. Natl. Acad. Sci. USA 84 (1987) 2312-2316
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2312-2316
    • Hamaguchi, M.1    Hanafusa, H.2
  • 53
    • 0024588383 scopus 로고
    • v-src kinase in the plasma membrane matrix fraction
    • v-src kinase in the plasma membrane matrix fraction. Oncogene Res. 4 (1989) 29-37
    • (1989) Oncogene Res. , vol.4 , pp. 29-37
    • Hamaguchi, M.1    Hanafusa, H.2
  • 55
    • 0020590357 scopus 로고
    • Levels of filamentous and globular actin in Chinese Hamster ovary cells throughout the cell cycle
    • Heacock C.S., and Bambourg S.R. Levels of filamentous and globular actin in Chinese Hamster ovary cells throughout the cell cycle. Expl. Cell Res. 147 (1983) 240-246
    • (1983) Expl. Cell Res. , vol.147 , pp. 240-246
    • Heacock, C.S.1    Bambourg, S.R.2
  • 56
    • 0025010018 scopus 로고
    • Mutations in src homology 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells
    • Hiraj J., and Varmus H.E. Mutations in src homology 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells. Proc. Natl. Acad. Sci. USA 87 (1990) 8592-8596
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8592-8596
    • Hiraj, J.1    Varmus, H.E.2
  • 57
    • 0012148048 scopus 로고
    • Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases
    • Hirst R., Horwitz A., Buck C., and Rohrschneider L. Phosphorylation of the fibronectin receptor complex in cells transformed by oncogenes that encode tyrosine kinases. Proc. Natl. Acad. Sci. USA 83 (1986) 6470-6474
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6470-6474
    • Hirst, R.1    Horwitz, A.2    Buck, C.3    Rohrschneider, L.4
  • 58
    • 0025031614 scopus 로고
    • Differential tyrosine-specific phosphorylation of integrin in Rous sarcoma virus transformed cells with differing transformed phenotype
    • Horvath A.R., Elmore M.A., and Kellie S. Differential tyrosine-specific phosphorylation of integrin in Rous sarcoma virus transformed cells with differing transformed phenotype. Oncogene 5 (1990) 1349-1357
    • (1990) Oncogene , vol.5 , pp. 1349-1357
    • Horvath, A.R.1    Elmore, M.A.2    Kellie, S.3
  • 59
    • 0025134750 scopus 로고
    • Regulation of integrin mobility and cytoskeletal association in normal and RSV-transformed chick embryo fibroblasts
    • Horvath A.R., and Kellie S. Regulation of integrin mobility and cytoskeletal association in normal and RSV-transformed chick embryo fibroblasts. J. Cell Sci. 97 (1990) 307-315
    • (1990) J. Cell Sci. , vol.97 , pp. 307-315
    • Horvath, A.R.1    Kellie, S.2
  • 60
    • 0026597050 scopus 로고
    • c-src to the cytoskeleton during platelet aggregation
    • c-src to the cytoskeleton during platelet aggregation. EMBO J. 11 (1992) 855-861
    • (1992) EMBO J. , vol.11 , pp. 855-861
    • Horvath, A.R.1    Muszbek, L.2    Kellie, S.3
  • 61
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage
    • Horwitz A., Duggan K., Buck C., Beckerle M.C., and Burridge K. Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage. Nature 320 (1986) 531-533
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 63
    • 0027621036 scopus 로고
    • Dynamic aspects of adhesion receptor function-integrins both twist and shout
    • Humphries M.J., Mould A.P., and Tuckwell D.S. Dynamic aspects of adhesion receptor function-integrins both twist and shout. BioEssays 15 (1993) 391-397
    • (1993) BioEssays , vol.15 , pp. 391-397
    • Humphries, M.J.1    Mould, A.P.2    Tuckwell, D.S.3
  • 64
    • 0017156231 scopus 로고
    • Cell surface protein and malignant transformation
    • Hynes R.O. Cell surface protein and malignant transformation. Biochim. Biophys. Acta 458 (1976) 73-107
    • (1976) Biochim. Biophys. Acta , vol.458 , pp. 73-107
    • Hynes, R.O.1
  • 65
    • 0022185833 scopus 로고
    • Reduced microfilament organization in adenovirus type 5-infected rat embryo cells: A function of early region la
    • Jackson P., and Bellett A.J.D. Reduced microfilament organization in adenovirus type 5-infected rat embryo cells: A function of early region la. J. Virol. 55 (1985) 644-650
    • (1985) J. Virol. , vol.55 , pp. 644-650
    • Jackson, P.1    Bellett, A.J.D.2
  • 67
    • 0023515851 scopus 로고
    • Cell transformation by the viral src gene
    • Jove J.A., and Hanafusa H. Cell transformation by the viral src gene. Ann. Rev. Cell Biol. 3 (1987) 31-56
    • (1987) Ann. Rev. Cell Biol. , vol.3 , pp. 31-56
    • Jove, J.A.1    Hanafusa, H.2
  • 68
    • 0022519437 scopus 로고
    • Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known peptide substrates without inducing transformation
    • Kamps M.P., Buss J.E., and Sefton B.M. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known peptide substrates without inducing transformation. Cell 45 (1986) 105-112
    • (1986) Cell , vol.45 , pp. 105-112
    • Kamps, M.P.1    Buss, J.E.2    Sefton, B.M.3
  • 69
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine phosphorylted protein substrates of oncogene-encoded tyrosine kinases
    • Kanner S.B., Reynolds A.B., Vines R.R., and Parsons T.J. Monoclonal antibodies to individual tyrosine phosphorylted protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl. Acad. Sci. USA 87 (1990) 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, T.J.4
  • 70
    • 0025138727 scopus 로고
    • The src protein contains multiple domains for specific attachment to membranes
    • Kaplan J.M., Varmus H.E., and Bishop J.M. The src protein contains multiple domains for specific attachment to membranes. Mol. Cell. Biol. 10 (1990) 1000-1009
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1000-1009
    • Kaplan, J.M.1    Varmus, H.E.2    Bishop, J.M.3
  • 72
    • 0023673239 scopus 로고
    • Cellular transformation, tyrosine kinase oncogenes and the cellular adhesion plaque
    • Kellie S. Cellular transformation, tyrosine kinase oncogenes and the cellular adhesion plaque. BioEssays 8 (1988) 25-30
    • (1988) BioEssays , vol.8 , pp. 25-30
    • Kellie, S.1
  • 73
    • 0022178995 scopus 로고
    • Interaction of tumour promoters with epithelial cells in culture
    • Kellie S., Holme T.C., and Bissell M.J. Interaction of tumour promoters with epithelial cells in culture. Exp. Cell Res. 160 (1985) 259-274
    • (1985) Exp. Cell Res. , vol.160 , pp. 259-274
    • Kellie, S.1    Holme, T.C.2    Bissell, M.J.3
  • 75
    • 0022735710 scopus 로고
    • Comparison of the relative importance of tyrosine-specific vinculin phosphorylation and the loss of surface-associated fibronectin in the morphology of cells transformed by Rous sarcoma virus
    • Kellie S., Patel B., Wigglesworth N.M., Mitchell A., Critchley D.R., and Wyke J.A. Comparison of the relative importance of tyrosine-specific vinculin phosphorylation and the loss of surface-associated fibronectin in the morphology of cells transformed by Rous sarcoma virus. J. Cell Sci. 82 (1986) 129-142
    • (1986) J. Cell Sci. , vol.82 , pp. 129-142
    • Kellie, S.1    Patel, B.2    Wigglesworth, N.M.3    Mitchell, A.4    Critchley, D.R.5    Wyke, J.A.6
  • 77
    • 0021288579 scopus 로고
    • src proteins of recovered avian sarcoma viruses interact with adhesion plaques as peripheral membrane proteins: Effect on cell transformation
    • src proteins of recovered avian sarcoma viruses interact with adhesion plaques as peripheral membrane proteins: Effect on cell transformation. Mol. Cell. Biol. 4 (1983) 454-467
    • (1983) Mol. Cell. Biol. , vol.4 , pp. 454-467
    • Kreuger, J.G.1    Garber, E.A.2    Chin, S.S.3    Hanafusa, H.4    Goldberg, A.5
  • 78
    • 0023854786 scopus 로고
    • Evidence that the phosphatidylinositol cycle is linked to cell motility
    • Lassing I., and Lindberg U. Evidence that the phosphatidylinositol cycle is linked to cell motility. Exp. Cell Res. 174 (1988) 1-15
    • (1988) Exp. Cell Res. , vol.174 , pp. 1-15
    • Lassing, I.1    Lindberg, U.2
  • 79
    • 0019921987 scopus 로고
    • Reorganisation of cytoskeletal and contractile elements during transition of human monocytes into adherent macrophages
    • Lehto V.P., Hori T., Vartio T., Badley R.A., and Virtanen I. Reorganisation of cytoskeletal and contractile elements during transition of human monocytes into adherent macrophages. Lab. Invest. 47 (1982) 391-399
    • (1982) Lab. Invest. , vol.47 , pp. 391-399
    • Lehto, V.P.1    Hori, T.2    Vartio, T.3    Badley, R.A.4    Virtanen, I.5
  • 81
    • 0027358716 scopus 로고
    • Profilin as a mediator of membrane-cytoskeleton communication
    • Machesky L.M., and Pollard T.D. Profilin as a mediator of membrane-cytoskeleton communication. Trends in Cell Biology 3 (1993) 381-385
    • (1993) Trends in Cell Biology , vol.3 , pp. 381-385
    • Machesky, L.M.1    Pollard, T.D.2
  • 83
    • 0021723422 scopus 로고
    • Cell-substratum interaction of cultured avian osteoclasts is mediated by specific adhesion structures
    • Marchisio P.C., Cirilo D., Naldini L., Primavera M.V., and Teti A. Cell-substratum interaction of cultured avian osteoclasts is mediated by specific adhesion structures. J. Cell Biol. 99 (1984) 1696-1705
    • (1984) J. Cell Biol. , vol.99 , pp. 1696-1705
    • Marchisio, P.C.1    Cirilo, D.2    Naldini, L.3    Primavera, M.V.4    Teti, A.5
  • 84
    • 0023123876 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions
    • Marchisio P.C., Cirillo D., Teti A., Zambonin-Zallone A., and Tarone G. Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions. Exp. Cell Res. 169 (1987) 202-214
    • (1987) Exp. Cell Res. , vol.169 , pp. 202-214
    • Marchisio, P.C.1    Cirillo, D.2    Teti, A.3    Zambonin-Zallone, A.4    Tarone, G.5
  • 85
    • 0026742310 scopus 로고
    • Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
    • Matsuyoshi N., Hamaguchi M., Taniguchi S., Nagafuchi A., Tsukita S., and Takeichi M. Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol. 118 (1992) 703-714
    • (1992) J. Cell Biol. , vol.118 , pp. 703-714
    • Matsuyoshi, N.1    Hamaguchi, M.2    Taniguchi, S.3    Nagafuchi, A.4    Tsukita, S.5    Takeichi, M.6
  • 87
    • 0019121161 scopus 로고
    • Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells
    • Morris A., and Tannenbaum J. Cytochalasin D does not produce net depolymerization of actin filaments in HEp-2 cells. Nature 287 (1980) 637-639
    • (1980) Nature , vol.287 , pp. 637-639
    • Morris, A.1    Tannenbaum, J.2
  • 88
    • 0024803852 scopus 로고
    • Dynamic cytoskeleton-integrin associations induced by cell binding to immoblised fibronectin
    • Mueller S.C., Kelly T., Dai M.Z., Dai H.N., and Chen W.T. Dynamic cytoskeleton-integrin associations induced by cell binding to immoblised fibronectin. J. Cell Biol. 109 (1989) 3455-3464
    • (1989) J. Cell Biol. , vol.109 , pp. 3455-3464
    • Mueller, S.C.1    Kelly, T.2    Dai, M.Z.3    Dai, H.N.4    Chen, W.T.5
  • 89
    • 0020080525 scopus 로고
    • Phosphorylation of a 36,000 Mr cellular protein in cells infected with partial transformation mutants of Rous sarcoma virus
    • Nakamura K.D., and Weber M.J. Phosphorylation of a 36,000 Mr cellular protein in cells infected with partial transformation mutants of Rous sarcoma virus. Mol. Cell. Biol. 2 (1982) 147-153
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 147-153
    • Nakamura, K.D.1    Weber, M.J.2
  • 91
    • 77957164177 scopus 로고
    • Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide
    • Nigg E.A., Sefton B.A., Hunter T., Walter G., and Singer S.J. Immunofluorescent localization of the transforming protein of Rous sarcoma virus with antibodies against a synthetic src peptide. Proc. Natl. Acad. Sci. USA 79 (1986) 5939-5942
    • (1986) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5939-5942
    • Nigg, E.A.1    Sefton, B.A.2    Hunter, T.3    Walter, G.4    Singer, S.J.5
  • 92
    • 0025313592 scopus 로고
    • Functional studies of the domains of talin
    • Nuckolls G.H., Turner C.E., and Burridge K. Functional studies of the domains of talin. J. Cell Biol. 110 (1990) 1635-1644
    • (1990) J. Cell Biol. , vol.110 , pp. 1635-1644
    • Nuckolls, G.H.1    Turner, C.E.2    Burridge, K.3
  • 93
    • 0017751285 scopus 로고
    • Mechanism of the decrease in the major cell surface protein of chick embryo fibroblasts after transformation
    • Olden K., and Yamada K.M. Mechanism of the decrease in the major cell surface protein of chick embryo fibroblasts after transformation. Cell 11 (1977) 957-969
    • (1977) Cell , vol.11 , pp. 957-969
    • Olden, K.1    Yamada, K.M.2
  • 95
    • 0027570012 scopus 로고
    • The assembly of signalling complexes by receptor tyrosine kinases
    • Panayotou G., and Waterfield M.W. The assembly of signalling complexes by receptor tyrosine kinases. BioEssays 15 (1993) 171-177
    • (1993) BioEssays , vol.15 , pp. 171-177
    • Panayotou, G.1    Waterfield, M.W.2
  • 97
    • 2542553245 scopus 로고
    • Talin is phosphorylated on tyrosine in chicken embryo fibroblasts transformed by Rous sarcoma virus
    • Pasquale E.B., Maher P.A., and Singer S.J. Talin is phosphorylated on tyrosine in chicken embryo fibroblasts transformed by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 83 (1986) 5507-5511
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5507-5511
    • Pasquale, E.B.1    Maher, P.A.2    Singer, S.J.3
  • 100
    • 0024534377 scopus 로고
    • Changes in integrin receptors in oncogenically transformed cells
    • Plantefaber L.C., and Hynes R.O. Changes in integrin receptors in oncogenically transformed cells. Cell 56 (1989) 281-290
    • (1989) Cell , vol.56 , pp. 281-290
    • Plantefaber, L.C.1    Hynes, R.O.2
  • 101
    • 0016760813 scopus 로고
    • Patterns of organisation of actin and myosin in normal and transformed cells
    • Pollack R., Osborn M., and Weber K. Patterns of organisation of actin and myosin in normal and transformed cells. Proc. Natl. Acad. Sci. USA 72 (1975) 994-998
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 994-998
    • Pollack, R.1    Osborn, M.2    Weber, K.3
  • 102
    • 0019945690 scopus 로고
    • Growth control and cell spreading: Differential response in preneoplastic and in metastatic cell variants
    • Raz A., and Ben-Ze'ev A. Growth control and cell spreading: Differential response in preneoplastic and in metastatic cell variants. Int. J. Cancer 29 (1982) 711-715
    • (1982) Int. J. Cancer , vol.29 , pp. 711-715
    • Raz, A.1    Ben-Ze'ev, A.2
  • 103
    • 0026924396 scopus 로고
    • Localization of the viral and cellular src kinases to perinuclear vesicles in fibroblasts
    • Redmond T., Brott B.K., Jove R., and Welsh M.J. Localization of the viral and cellular src kinases to perinuclear vesicles in fibroblasts. Cell Growth Differ. 3 (1992) 567-576
    • (1992) Cell Growth Differ. , vol.3 , pp. 567-576
    • Redmond, T.1    Brott, B.K.2    Jove, R.3    Welsh, M.J.4
  • 105
    • 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 Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70 (1992) 389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 106
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., and Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70 (1992) 401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 109
    • 0346481004 scopus 로고
    • Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product
    • Rohrschneider L.R. Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc. Natl. Acad. Sci. USA 77 (1980) 3514-3518
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3514-3518
    • Rohrschneider, L.R.1
  • 110
    • 0022240158 scopus 로고
    • Regulation of cellular morphology by Rous sarcoma virus src gene: Analysis of fusiform mutants
    • Rohrschneider L., and Reynolds S. Regulation of cellular morphology by Rous sarcoma virus src gene: Analysis of fusiform mutants. Mol. Cell. Biol. 5 (1985) 3097-3107
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3097-3107
    • Rohrschneider, L.1    Reynolds, S.2
  • 111
    • 0020646480 scopus 로고
    • v-src localization in cells infected with partial transformation mutants of Rous sarcoma virus
    • v-src localization in cells infected with partial transformation mutants of Rous sarcoma virus. Mol. Cell. Biol. 3 (1983) 731-746
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 731-746
    • Rohrshneider, L.1    Rosok, M.J.2
  • 113
    • 0020674105 scopus 로고
    • Increased phosphorylation of vinculin on tyrosine does not occur during the release of stress fibers before mitosis in normal cells
    • Rosok M.J., and Rohrschneider L. Increased phosphorylation of vinculin on tyrosine does not occur during the release of stress fibers before mitosis in normal cells. Mol. Cell. Biol. 3 (1983) 475-479
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 475-479
    • Rosok, M.J.1    Rohrschneider, L.2
  • 114
    • 0017888284 scopus 로고
    • Actin content and organisation in normal and transformed cells in culture
    • Rubin R.W., Warren R.H., Lukemann R.S., and Clements A. Actin content and organisation in normal and transformed cells in culture. J. Cell Biol. 78 (1978) 28-35
    • (1978) J. Cell Biol. , vol.78 , pp. 28-35
    • Rubin, R.W.1    Warren, R.H.2    Lukemann, R.S.3    Clements, A.4
  • 116
    • 0019468487 scopus 로고
    • Vinculin: A cytoskeletal target of the transforming protein of Rous sarcoma virus
    • Sefton B.M., Hunter T., Ball E.H., and Singer S.J. Vinculin: A cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell 24 (1981) 165-174
    • (1981) Cell , vol.24 , pp. 165-174
    • Sefton, B.M.1    Hunter, T.2    Ball, E.H.3    Singer, S.J.4
  • 117
    • 0026572318 scopus 로고
    • Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-src
    • Seidel-Dugan C., Meyer B.E., Thomas S.M., and Brugge J.S. Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-src. Mol. Cell. Biol. 21 (1992) 1835-1845
    • (1992) Mol. Cell. Biol. , vol.21 , pp. 1835-1845
    • Seidel-Dugan, C.1    Meyer, B.E.2    Thomas, S.M.3    Brugge, J.S.4
  • 118
    • 0023259015 scopus 로고
    • Alpha-actinin-containing structures in transformed cells are highly dynamic structures
    • Stickel S.K., and Wang Y. Alpha-actinin-containing structures in transformed cells are highly dynamic structures. J. Cell Biol. 104 (1987) 1521-1526
    • (1987) J. Cell Biol. , vol.104 , pp. 1521-1526
    • Stickel, S.K.1    Wang, Y.2
  • 119
    • 0022448135 scopus 로고
    • v-src proteins expressed by two distinct temperature-sensitive mutants of Rous sarcoma virus
    • v-src proteins expressed by two distinct temperature-sensitive mutants of Rous sarcoma virus. J. Virol. 58 (1986) 876-883
    • (1986) J. Virol. , vol.58 , pp. 876-883
    • Stoker, A.1    Kellie, S.2    Wyke, J.A.3
  • 120
    • 0024457508 scopus 로고
    • From signal to pseudopod. How cells control cytoplasmic actin assembly
    • Stossel P.T. From signal to pseudopod. How cells control cytoplasmic actin assembly. J. Biol. Chem. 264 (1989) 18261-18264
    • (1989) J. Biol. Chem. , vol.264 , pp. 18261-18264
    • Stossel, P.T.1
  • 121
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel P.T. On the crawling of animal cells. Science 260 (1993) 1086-1094
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, P.T.1
  • 123
    • 0024506601 scopus 로고
    • Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts
    • Tapley P., Horwitz A., Buck C., Duggan K., and Rohrschneider L. Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts. Oncogene 4 (1989) 325-333
    • (1989) Oncogene , vol.4 , pp. 325-333
    • Tapley, P.1    Horwitz, A.2    Buck, C.3    Duggan, K.4    Rohrschneider, L.5
  • 124
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podsomes
    • Tarone G., Cirillo D., Giancotti F.G., Comoglio P.M., and Marchisio P.C. Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podsomes. Exp. Cell Res. 159 (1985) 141-157
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 125
    • 0019797603 scopus 로고
    • Interaction of serum and cell spreading affects the growth of neoplastic and non-neoplastic fibroblasts
    • Tucker R.W., Butterfield C.E., and Folkman J. Interaction of serum and cell spreading affects the growth of neoplastic and non-neoplastic fibroblasts. J. Supramol. Struct. 15 (1981) 29-40
    • (1981) J. Supramol. Struct. , vol.15 , pp. 29-40
    • Tucker, R.W.1    Butterfield, C.E.2    Folkman, J.3
  • 126
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner C.E., Glenney J.R., and Burridge K. Paxillin: A new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111 (1990) 1059-1068
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney, J.R.2    Burridge, K.3
  • 128
    • 0026114963 scopus 로고
    • Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed chick lens cells
    • Volberg T., Geiger B., Dror R., and Zick Y. Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed chick lens cells. Cell Reg. 2 (1991) 105-120
    • (1991) Cell Reg. , vol.2 , pp. 105-120
    • Volberg, T.1    Geiger, B.2    Dror, R.3    Zick, Y.4
  • 129
    • 0026529501 scopus 로고
    • The effect of tyrosine-specific phosphorylation on the assembly of adherens-type junctions
    • Volberg T., Zick Y., Dror R., Sananay I., Gilon C., Levitski A., and Geiger B. The effect of tyrosine-specific phosphorylation on the assembly of adherens-type junctions. EMBO J. 11 (1992) 1733-1742
    • (1992) EMBO J. , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3    Sananay, I.4    Gilon, C.5    Levitski, A.6    Geiger, B.7
  • 130
    • 0026526146 scopus 로고
    • Mutations in the SH3 domain of the src oncogen which decrease association of phosphatidylinositol 3′-kinase activity with pp60v-src and alter cellular morphology
    • Wages D.S., Keefer J., Rall T.B., and Weber M.J. Mutations in the SH3 domain of the src oncogen which decrease association of phosphatidylinositol 3′-kinase activity with pp60v-src and alter cellular morphology. J. Virol. 66 (1992) 1866-1874
    • (1992) J. Virol. , vol.66 , pp. 1866-1874
    • Wages, D.S.1    Keefer, J.2    Rall, T.B.3    Weber, M.J.4
  • 131
    • 0017139523 scopus 로고
    • Changes in microfilament organisation and surface topography upon transformation of chick embryo fibroblasts with Rous sarcoma virus
    • Wang E.A., and Goldberg R. Changes in microfilament organisation and surface topography upon transformation of chick embryo fibroblasts with Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 73 (1976) 4065-4069
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4065-4069
    • Wang, E.A.1    Goldberg, R.2
  • 132
    • 0016640950 scopus 로고
    • Decrease in membrane-associated actin of fibroblasts after transformation by Rous sarcoma virus
    • Wickus G., Gruenstein E., Robbins P.W., and Rich A. Decrease in membrane-associated actin of fibroblasts after transformation by Rous sarcoma virus. Proc. Natl. Acad. Sci. USA 72 (1975) 746-749
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 746-749
    • Wickus, G.1    Gruenstein, E.2    Robbins, P.W.3    Rich, A.4
  • 133
    • 0020966073 scopus 로고
    • Transformation-sensitive isoactin in passaged chick embryo fibroblasts transformed by Rous sarcoma virus
    • Witt D.P., Brown D.P., and Gordon J. Transformation-sensitive isoactin in passaged chick embryo fibroblasts transformed by Rous sarcoma virus. J. Cell Biol. 96 (1983) 1766-1771
    • (1983) J. Cell Biol. , vol.96 , pp. 1766-1771
    • Witt, D.P.1    Brown, D.P.2    Gordon, J.3
  • 134
    • 0027419589 scopus 로고
    • c-src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • c-src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120 (1993) 1417-1426
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 135
    • 0023126096 scopus 로고
    • Genetic analysis of the form and function of the viral src gene
    • Wyke J.A., and Stoker A. Genetic analysis of the form and function of the viral src gene. Biochim. Biophys. Acta 907 (1987) 47-70
    • (1987) Biochim. Biophys. Acta , vol.907 , pp. 47-70
    • Wyke, J.A.1    Stoker, A.2
  • 136
    • 1842389885 scopus 로고
    • Cell surface protein partially restores morphology, adhesiveness and contact inhibition of movement to transformed fibroblasts
    • Yamada K.M., Yamada S.S., and Pastan I. Cell surface protein partially restores morphology, adhesiveness and contact inhibition of movement to transformed fibroblasts. Proc. Natl. Acad. Sci. 73 (1976) 1217-1221
    • (1976) Proc. Natl. Acad. Sci. , vol.73 , pp. 1217-1221
    • Yamada, K.M.1    Yamada, S.S.2    Pastan, I.3
  • 137
    • 0023942517 scopus 로고
    • Growth factor receptor tyrosine kinases
    • Yarden Y., and Ullrich A. Growth factor receptor tyrosine kinases. Ann. Rev. Biochem. 57 (1988) 443-478
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 443-478
    • Yarden, Y.1    Ullrich, A.2


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