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Volumn 33, Issue 8, 2002, Pages 1061-1072

Hydrogen peroxide inhibits cell cycle progression by inhibition of the spreading of mitotic CHO cells

Author keywords

Cell cycle; DNA synthesis; Focal adhesions; Free radicals; Hydrogen peroxide; Reactive oxygen species; Signal transduction; Spreading; Stress fibers

Indexed keywords

CYCLIN A; CYCLIN D1; DNA; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 0037108007     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(02)00988-7     Document Type: Article
Times cited : (20)

References (73)
  • 3
    • 0028970609 scopus 로고
    • Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions
    • Albanese C., Johnson J., Watanabe G., Eklund N., Vu D., Arnold A., Pestell R.G. Transforming p21ras mutants and c-Ets-2 activate the cyclin D1 promoter through distinguishable regions. J. Biol. Chem. 270:1995;23589-23597.
    • (1995) J. Biol. Chem , vol.270 , pp. 23589-23597
    • Albanese, C.1    Johnson, J.2    Watanabe, G.3    Eklund, N.4    Vu, D.5    Arnold, A.6    Pestell, R.G.7
  • 5
    • 0029017456 scopus 로고
    • Ras transformation results in an elevated level of cyclin D1 and acceleration of G1 progression in NIH 3T3 cells
    • Liu J.J., Chao J.R., Jiang M.C., Ng S.Y., Yen J.J., Yang-Yen H.F. Ras transformation results in an elevated level of cyclin D1 and acceleration of G1 progression in NIH 3T3 cells. Mol. Cell Biol. 15:1995;3654-3663.
    • (1995) Mol. Cell Biol , vol.15 , pp. 3654-3663
    • Liu, J.J.1    Chao, J.R.2    Jiang, M.C.3    Ng, S.Y.4    Yen, J.J.5    Yang-Yen, H.F.6
  • 7
    • 0033618410 scopus 로고    scopus 로고
    • Multiple ras effector pathways contribute to G1 cell cycle progression
    • Gille H., Downward J. Multiple ras effector pathways contribute to G1 cell cycle progression. J. Biol. Chem. 274:1999;22033-22040.
    • (1999) J. Biol. Chem , vol.274 , pp. 22033-22040
    • Gille, H.1    Downward, J.2
  • 8
    • 0032491579 scopus 로고    scopus 로고
    • Cyclin D expression is controlled post-transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway
    • Muise-Helmericks R.C., Grimes H.L., Bellacosa A., Malstrom S.E., Tsichlis P.N., Rosen N. Cyclin D expression is controlled post-transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway. J. Biol. Chem. 273:1998;29864-29872.
    • (1998) J. Biol. Chem , vol.273 , pp. 29864-29872
    • Muise-Helmericks, R.C.1    Grimes, H.L.2    Bellacosa, A.3    Malstrom, S.E.4    Tsichlis, P.N.5    Rosen, N.6
  • 9
    • 0006224409 scopus 로고
    • Tumorigenicity of virus-transformed cells in nude mice is correlated specifically with anchorage-independent growth in vitro
    • Shin S.I., Freedman V.H., Risser R., Pollack R. Tumorigenicity of virus-transformed cells in nude mice is correlated specifically with anchorage-independent growth in vitro. Proc. Natl. Acad. Sci. USA. 72:1975;4435-4439.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4435-4439
    • Shin, S.I.1    Freedman, V.H.2    Risser, R.3    Pollack, R.4
  • 10
    • 0034660524 scopus 로고    scopus 로고
    • Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src
    • Fincham V.J., James M., Frame M.C., Winder S.J. Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src. Embo J. 19:2000;2911-2923.
    • (2000) Embo J , vol.19 , pp. 2911-2923
    • Fincham, V.J.1    James, M.2    Frame, M.C.3    Winder, S.J.4
  • 11
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks S.K., Calalb M.B., Harper M.C., Patel S.K. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA. 89:1992;8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 13
    • 0029664531 scopus 로고    scopus 로고
    • Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Vuori K., Hirai H., Aizawa S., Ruoslahti E. Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion a role for Src family kinases . Mol. Cell Biol. 16:1996;2606-2613.
    • (1996) Mol. Cell Biol , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 14
    • 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., Jones K.C., Hunter T. 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. 18:1998;2571-2585.
    • (1998) Mol. Cell Biol , vol.18 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 15
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen Q., Kinch M.S., Lin T.H., Burridge K., Juliano R.L. Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269:1994;26602-26605.
    • (1994) J. Biol. Chem , vol.269 , pp. 26602-26605
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.L.5
  • 16
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature. 372:1994;786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van der Geer, P.4
  • 18
    • 0028904784 scopus 로고
    • Integrin-dependent activation of MAP kinase: A link to shape-dependent cell proliferation
    • Zhu X., Assoian R.K. Integrin-dependent activation of MAP kinase a link to shape-dependent cell proliferation . Mol. Biol. Cell. 6:1995;273-282.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 273-282
    • Zhu, X.1    Assoian, R.K.2
  • 19
    • 17544364168 scopus 로고    scopus 로고
    • Ras activation is necessary for integrin-mediated activation of extracellular signal-regulated kinase 2 and cytosolic phospholipase A2 but not for cytoskeletal organization
    • Clark E.A., Hynes R.O. Ras activation is necessary for integrin-mediated activation of extracellular signal-regulated kinase 2 and cytosolic phospholipase A2 but not for cytoskeletal organization. J. Biol. Chem. 271:1996;14814-14818.
    • (1996) J. Biol. Chem , vol.271 , pp. 14814-14818
    • Clark, E.A.1    Hynes, R.O.2
  • 20
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto S., Teramoto H., Gutkind J.S., Yamada K.M. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation roles of integrin aggregation and occupancy of receptors . J. Cell Biol. 135:1996;1633-1642.
    • (1996) J. Cell Biol , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 21
    • 0029828456 scopus 로고    scopus 로고
    • Involvement of the small GTPase rho in integrin-mediated activation of mitogen-activated protein kinase
    • Renshaw M.W., Toksoz D., Schwartz M.A. Involvement of the small GTPase rho in integrin-mediated activation of mitogen-activated protein kinase. J. Biol. Chem. 271:1996;21691-21694.
    • (1996) J. Biol. Chem , vol.271 , pp. 21691-21694
    • Renshaw, M.W.1    Toksoz, D.2    Schwartz, M.A.3
  • 23
    • 0024724936 scopus 로고
    • 2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain
    • 2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain. Proc. Natl. Acad. Sci. USA. 86:1989;6758-6762.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6758-6762
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 24
    • 0029763774 scopus 로고    scopus 로고
    • Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases
    • Rao G.N. Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases. Oncogene. 13:1996;713-719.
    • (1996) Oncogene , vol.13 , pp. 713-719
    • Rao, G.N.1
  • 25
    • 0028843581 scopus 로고
    • Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor
    • Gamou S., Shimizu N. Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor. FEBS Lett. 357:1995;161-164.
    • (1995) FEBS Lett , vol.357 , pp. 161-164
    • Gamou, S.1    Shimizu, N.2
  • 26
    • 0028115871 scopus 로고
    • 2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates
    • 2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates. Cancer Res. 54:1994;12-15.
    • (1994) Cancer Res , vol.54 , pp. 12-15
    • Stevenson, M.A.1    Pollock, S.S.2    Coleman, C.N.3    Calderwood, S.K.4
  • 27
    • 0030575185 scopus 로고    scopus 로고
    • The phosphorylation state of MAP-kinases modulates the cytotoxic response of smooth muscle cells to hydrogen peroxide
    • Cantoni O., Boscoboinik D., Fiorani M., Stauble B., Azzi A. The phosphorylation state of MAP-kinases modulates the cytotoxic response of smooth muscle cells to hydrogen peroxide. FEBS Lett. 389:1996;285-288.
    • (1996) FEBS Lett , vol.389 , pp. 285-288
    • Cantoni, O.1    Boscoboinik, D.2    Fiorani, M.3    Stauble, B.4    Azzi, A.5
  • 28
    • 0000190627 scopus 로고    scopus 로고
    • Large-scale screening assay for the phosphorylation of mitogen-activated protein kinase in cells
    • de Wit R., Boonstra J., Verkleij A.J., Post J.A. Large-scale screening assay for the phosphorylation of mitogen-activated protein kinase in cells. J. Biomol. Screen. 3:1998;277-284.
    • (1998) J. Biomol. Screen , vol.3 , pp. 277-284
    • De Wit, R.1    Boonstra, J.2    Verkleij, A.J.3    Post, J.A.4
  • 30
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae Y.S., Kang S.W., Seo M.S., Baines I.C., Tekle E., Chock P.B., Rhee S.G. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272:1997;217-221.
    • (1997) J. Biol. Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5    Chock, P.B.6    Rhee, S.G.7
  • 32
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival application to proliferation and cytotoxicity assays . J. Immunol. Methods. 65:1983;55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 33
    • 0033614679 scopus 로고    scopus 로고
    • Both oxidative stress-dependent and -independent effects of amyloid β protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2, 5- diphenyltetrazolium bromide (MTT) reduction assay
    • Abe K., Saito H. Both oxidative stress-dependent and -independent effects of amyloid β protein are detected by 3-(4,5-dimethylthiazol-2-yl)-2, 5- diphenyltetrazolium bromide (MTT) reduction assay. Brain. Res. 830:1999;146-154.
    • (1999) Brain. Res , vol.830 , pp. 146-154
    • Abe, K.1    Saito, H.2
  • 35
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K., Fath K., Kelly T., Nuckolls G., Turner C. Focal adhesions transmembrane junctions between the 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
  • 36
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano R.L., Haskill S. Signal transduction from the extracellular matrix. J. Cell Biol. 120:1993;577-585.
    • (1993) J. Cell Biol , vol.120 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 38
    • 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., 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
  • 39
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg L., Earp H.S., Parsons J.T., Schaller M., Juliano R.L. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267:1992;23439-23442.
    • (1992) J. Biol. Chem , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 40
    • 0028331263 scopus 로고
    • Tyrosine kinase activity, cytoskeletal organization, and motility in human vascular endothelial cells
    • Romer L.H., McLean N., Turner C.E., Burridge K. Tyrosine kinase activity, cytoskeletal organization, and motility in human vascular endothelial cells. Mol. Biol. Cell. 5:1994;349-361.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 349-361
    • Romer, L.H.1    McLean, N.2    Turner, C.E.3    Burridge, K.4
  • 41
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller M.D., Hildebrand J.D., Shannon J.D., Fox J.W., Vines R.R., Parsons J.T. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol. Cell Biol. 14:1994;1680-1688.
    • (1994) Mol. Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 42
    • 0028986116 scopus 로고
    • Pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller M.D., Parsons J.T. pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell Biol. 15:1995;2635-2645.
    • (1995) Mol. Cell Biol , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 43
    • 0029856505 scopus 로고    scopus 로고
    • Signal transduction in cell-matrix interactions
    • Guan J.L., Chen H.C. Signal transduction in cell-matrix interactions. Int. Rev. Cytol. 168:1996;81-121.
    • (1996) Int. Rev. Cytol , vol.168 , pp. 81-121
    • Guan, J.L.1    Chen, H.C.2
  • 44
    • 0030898418 scopus 로고    scopus 로고
    • Src family protein tyrosine kinases: Cooperating with growth factor and adhesion signaling pathways
    • Parsons J.T., Parsons S.J. Src family protein tyrosine kinases cooperating with growth factor and adhesion signaling pathways . Curr. Opin. Cell Biol. 9:1997;187-192.
    • (1997) Curr. Opin. Cell Biol , vol.9 , pp. 187-192
    • Parsons, J.T.1    Parsons, S.J.2
  • 45
    • 0026778547 scopus 로고
    • Identification and properties of an atypical catalytic subunit (p34PSK- J3/cdk4) for mammalian D type G1 cyclins
    • Matsushime H., Ewen M.E., Strom D.K., Kato J.Y., Hanks S.K., Roussel M.F., Sherr C.J. Identification and properties of an atypical catalytic subunit (p34PSK- J3/cdk4) for mammalian D type G1 cyclins. Cell. 71:1992;323-334.
    • (1992) Cell , vol.71 , pp. 323-334
    • Matsushime, H.1    Ewen, M.E.2    Strom, D.K.3    Kato, J.Y.4    Hanks, S.K.5    Roussel, M.F.6    Sherr, C.J.7
  • 46
    • 0026459047 scopus 로고
    • D type cyclins associate with multiple protein kinases and the DNA replication and repair factor PCNA
    • Xiong Y., Zhang H., Beach D. D type cyclins associate with multiple protein kinases and the DNA replication and repair factor PCNA. Cell. 71:1992;505-514.
    • (1992) Cell , vol.71 , pp. 505-514
    • Xiong, Y.1    Zhang, H.2    Beach, D.3
  • 47
    • 0028039027 scopus 로고
    • CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1
    • Bates S., Bonetta L., MacAllan D., Parry D., Holder A., Dickson C., Peters G. CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1. Oncogene. 9:1994;71-79.
    • (1994) Oncogene , vol.9 , pp. 71-79
    • Bates, S.1    Bonetta, L.2    MacAllan, D.3    Parry, D.4    Holder, A.5    Dickson, C.6    Peters, G.7
  • 48
    • 0028181760 scopus 로고
    • Identification of G1 kinase activity for cdk6, a novel cyclin D partner
    • Meyerson M., Harlow E. Identification of G1 kinase activity for cdk6, a novel cyclin D partner. Mol. Cell Biol. 14:1994;2077-2086.
    • (1994) Mol. Cell Biol , vol.14 , pp. 2077-2086
    • Meyerson, M.1    Harlow, E.2
  • 50
    • 0026698263 scopus 로고
    • Association of human cyclin E with a periodic G1-S phase protein kinase
    • Dulic V., Lees E., Reed S.I. Association of human cyclin E with a periodic G1-S phase protein kinase. Science. 257:1992;1958-1961.
    • (1992) Science , vol.257 , pp. 1958-1961
    • Dulic, V.1    Lees, E.2    Reed, S.I.3
  • 51
    • 0027336491 scopus 로고
    • Mammalian G1 cyclins
    • Sherr C.J. Mammalian G1 cyclins. Cell. 73:1993;1059-1065.
    • (1993) Cell , vol.73 , pp. 1059-1065
    • Sherr, C.J.1
  • 52
    • 0026320075 scopus 로고
    • Cyclin A is required for the onset of DNA replication in mammalian fibroblasts
    • Girard F., Strausfeld U., Fernandez A., Lamb N.J. Cyclin A is required for the onset of DNA replication in mammalian fibroblasts. Cell. 67:1991;1169-1179.
    • (1991) Cell , vol.67 , pp. 1169-1179
    • Girard, F.1    Strausfeld, U.2    Fernandez, A.3    Lamb, N.J.4
  • 53
    • 0026583746 scopus 로고
    • Cyclin A is required at two points in the human cell cycle
    • Pagano M., Pepperkok R., Verde F., Ansorge W., Draetta G. Cyclin A is required at two points in the human cell cycle. Embo J. 11:1992;961-971.
    • (1992) Embo J , vol.11 , pp. 961-971
    • Pagano, M.1    Pepperkok, R.2    Verde, F.3    Ansorge, W.4    Draetta, G.5
  • 55
    • 77956860573 scopus 로고
    • Free radicals and cell proliferation
    • R.H. Burdon, & C. Rice-Evans. New York: Elsevier Science Inc
    • Burdon R.H. Free radicals and cell proliferation. Burdon R.H., Rice-Evans C., Free radical damaged and its control. 1994;155-185 Elsevier Science Inc, New York.
    • (1994) Free radical damaged and its control , pp. 155-185
    • Burdon, R.H.1
  • 56
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper G.E., McNamee H.P., Dike L.E., Bojanowski K., Ingber D.E. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell. 6:1995;1349-1365.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 57
    • 0030027049 scopus 로고    scopus 로고
    • Dependence of cyclin E-CDK2 kinase activity on cell anchorage
    • Fang F., Orend G., Watanabe N., Hunter T., Ruoslahti E. Dependence of cyclin E-CDK2 kinase activity on cell anchorage. Science. 271:1996;499-502.
    • (1996) Science , vol.271 , pp. 499-502
    • Fang, F.1    Orend, G.2    Watanabe, N.3    Hunter, T.4    Ruoslahti, E.5
  • 58
    • 0029876639 scopus 로고    scopus 로고
    • Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein
    • Zhu X., Ohtsubo M., Bohmer R.M., Roberts J.M., Assoian R.K. Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein. J. Cell Biol. 133:1996;391-403.
    • (1996) J. Cell Biol , vol.133 , pp. 391-403
    • Zhu, X.1    Ohtsubo, M.2    Bohmer, R.M.3    Roberts, J.M.4    Assoian, R.K.5
  • 59
    • 0031022256 scopus 로고    scopus 로고
    • Anchorage-dependent cell cycle progression
    • Assoian R.K. Anchorage-dependent cell cycle progression. J. Cell Biol. 136:1997;1-4.
    • (1997) J. Cell Biol , vol.136 , pp. 1-4
    • Assoian, R.K.1
  • 60
    • 0025880916 scopus 로고
    • G1/S control of anchorage-independent growth in the fibroblast cell cycle
    • Guadagno T.M., Assoian R.K. G1/S control of anchorage-independent growth in the fibroblast cell cycle. J. Cell Biol. 115:1991;1419-1425.
    • (1991) J. Cell Biol , vol.115 , pp. 1419-1425
    • Guadagno, T.M.1    Assoian, R.K.2
  • 62
    • 0032403050 scopus 로고    scopus 로고
    • Reactive oxygen species activate focal adhesion kinase, paxillin and p130cas tyrosine phosphorylation in endothelial cells
    • Gozin A., Franzini E., Andrieu V., Da Costa L., Rollet-Labelle E., Pasquier C. Reactive oxygen species activate focal adhesion kinase, paxillin and p130cas tyrosine phosphorylation in endothelial cells. Free Radic. Biol. Med. 25:1998;1021-1032.
    • (1998) Free Radic. Biol. Med , vol.25 , pp. 1021-1032
    • Gozin, A.1    Franzini, E.2    Andrieu, V.3    Da Costa, L.4    Rollet-Labelle, E.5    Pasquier, C.6
  • 63
    • 0032790741 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates tyrosine phosphorylation of focal adhesion kinase in vascular endothelial cells
    • Vepa S., Scribner W.M., Parinandi N.L., English D., Garcia J.G., Natarajan V. Hydrogen peroxide stimulates tyrosine phosphorylation of focal adhesion kinase in vascular endothelial cells. Am. J. Physiol. 277:1999;L150-L158.
    • (1999) Am. J. Physiol , vol.277
    • Vepa, S.1    Scribner, W.M.2    Parinandi, N.L.3    English, D.4    Garcia, J.G.5    Natarajan, V.6
  • 65
    • 0028972851 scopus 로고
    • 2-treated actin: Assembly and polymer interactions with cross-linking proteins
    • 2-treated actin assembly and polymer interactions with cross-linking proteins . Biophys. J. 69:1995;2710-2719.
    • (1995) Biophys. J , vol.69 , pp. 2710-2719
    • DalleDonne, I.1    Milzani, A.2    Colombo, R.3
  • 67
    • 0027135637 scopus 로고
    • Cellularly generated active oxygen species and HeLa cell proliferation
    • Burdon R.H., Gill V. Cellularly generated active oxygen species and HeLa cell proliferation. Free Radic. Res. Commun. 19:1993;203-213.
    • (1993) Free Radic. Res. Commun , vol.19 , pp. 203-213
    • Burdon, R.H.1    Gill, V.2
  • 68
    • 0028918334 scopus 로고
    • Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
    • Burdon R.H. Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic. Biol. Med. 18:1995;775-794.
    • (1995) Free Radic. Biol. Med , vol.18 , pp. 775-794
    • Burdon, R.H.1
  • 70
    • 0029032770 scopus 로고
    • Antioxidant enzyme levels as a function of growth state in cell culture
    • Oberley T.D., Schultz J.L., Li N., Oberley L.W. Antioxidant enzyme levels as a function of growth state in cell culture. Free Radic. Biol. Med. 19:1995;53-65.
    • (1995) Free Radic. Biol. Med , vol.19 , pp. 53-65
    • Oberley, T.D.1    Schultz, J.L.2    Li, N.3    Oberley, L.W.4
  • 71
    • 0027135244 scopus 로고
    • Neutrophil signal transduction and activation of the respiratory burst
    • Thelen M., Dewald B., Baggiolini M. Neutrophil signal transduction and activation of the respiratory burst. Physiol. Rev. 73:1993;797-821.
    • (1993) Physiol. Rev , vol.73 , pp. 797-821
    • Thelen, M.1    Dewald, B.2    Baggiolini, M.3
  • 72
    • 0025992764 scopus 로고
    • The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects
    • Morel F., Doussiere J., Vignais P.V. The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects. Eur. J. Biochem. 201:1991;523-546.
    • (1991) Eur. J. Biochem , vol.201 , pp. 523-546
    • Morel, F.1    Doussiere, J.2    Vignais, P.V.3
  • 73
    • 0028198653 scopus 로고
    • Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins
    • Bokoch G.M. Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins. Curr. Opin. Cell Biol. 6:1994;212-218.
    • (1994) Curr. Opin. Cell Biol , vol.6 , pp. 212-218
    • Bokoch, G.M.1


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