메뉴 건너뛰기




Volumn 27, Issue 2, 2008, Pages 303-314

Signal cross talks for sustained MAPK activation and cell migration: The potential role of reactive oxygen species

Author keywords

Cell migration; Integrin; MAPK activation; Protein kinase C; Reactive oxygen species; Receptor tyrosine kinase

Indexed keywords

INTEGRIN; MITOGEN ACTIVATED PROTEIN KINASE; PAXILLIN; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; SCAFFOLD PROTEIN;

EID: 43049124720     PISSN: 01677659     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10555-008-9112-4     Document Type: Review
Times cited : (145)

References (146)
  • 1
    • 33745297408 scopus 로고    scopus 로고
    • New signals from the invasive front (review)
    • 7092
    • Christofori, G. (2006). New signals from the invasive front (review). Nature, 441(7092), 444-450.
    • (2006) Nature , vol.441 , pp. 444-450
    • Christofori, G.1
  • 2
    • 0141988559 scopus 로고    scopus 로고
    • Molecular mechanisms of tumor invasion and metastasis: An integrated view
    • 7
    • Cairns, R. A., Khokha, R., & Hill, R. P. (2003). Molecular mechanisms of tumor invasion and metastasis: An integrated view. Current Molecular Medicine, 3(7), 659-671.
    • (2003) Current Molecular Medicine , vol.3 , pp. 659-671
    • Cairns, R.A.1    Khokha, R.2    Hill, R.P.3
  • 3
    • 33847736618 scopus 로고    scopus 로고
    • Tumor microenvironment promotes cancer progression, metastasis, and therapeutic resistance
    • 2
    • Sung, S. Y., Hsieh, C. L., Wu, D., Chung, L. W., & Johnstone, P. A. (2007). Tumor microenvironment promotes cancer progression, metastasis, and therapeutic resistance. Current Problems in Cancer, 31(2), 36-100.
    • (2007) Current Problems in Cancer , vol.31 , pp. 36-100
    • Sung, S.Y.1    Hsieh, C.L.2    Wu, D.3    Chung, L.W.4    Johnstone, P.A.5
  • 5
    • 19644395911 scopus 로고    scopus 로고
    • HGF/SF-Met signaling in tumor progression
    • 1
    • Gao, C. F., & Vande Woude, G. F. (2005). HGF/SF-Met signaling in tumor progression. Cell Research, 15(1), 49-51.
    • (2005) Cell Research , vol.15 , pp. 49-51
    • Gao, C.F.1    Vande Woude, G.F.2
  • 6
    • 33745515023 scopus 로고    scopus 로고
    • Tumour microenvironment: TGFbeta: the molecular Jekyll and Hyde of cancer
    • 7
    • Bierie, B., & Moses, H. L. (2006). Tumour microenvironment: TGFbeta: The molecular Jekyll and Hyde of cancer. Nature Reviews Cancer, 6(7), 506-520.
    • (2006) Nature Reviews Cancer , vol.6 , pp. 506-520
    • Bierie, B.1    Moses, H.L.2
  • 7
    • 0033604516 scopus 로고    scopus 로고
    • The role of the epidermal growth factor receptor family in mammary tumorigenesis and metastasis
    • 1
    • Kim, H., & Muller, W. J. (1999). The role of the epidermal growth factor receptor family in mammary tumorigenesis and metastasis. Experimental Cell Research, 253(1), 78-87.
    • (1999) Experimental Cell Research , vol.253 , pp. 78-87
    • Kim, H.1    Muller, W.J.2
  • 8
    • 23944524848 scopus 로고    scopus 로고
    • Wnts induce migration and invasion of myeloma plasma cells
    • 5
    • Qiang, Y. W., Walsh, K., Yao, L., Kedei, N., Blumberg, P. M., Rubin, J. S., et al. (2005). Wnts induce migration and invasion of myeloma plasma cells. Blood, 106(5), 1786-1793.
    • (2005) Blood , vol.106 , pp. 1786-1793
    • Qiang, Y.W.1    Walsh, K.2    Yao, L.3    Kedei, N.4    Blumberg, P.M.5    Rubin, J.S.6
  • 9
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • 5600
    • Johnson, G. L., & Lapadat, R. (2002). Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science, 298(5600), 1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 13
    • 23144455311 scopus 로고    scopus 로고
    • Prohibitin is required for Ras-induced Raf-MEK-ERK activation and epithelial cell migration
    • 8
    • Rajalingam, K., Wunder, C., Brinkmann, V., Churin, Y., Hekman, M., Sievers, C., et al. (2005). Prohibitin is required for Ras-induced Raf-MEK-ERK activation and epithelial cell migration. Nature Cell Biology, 7(8), 837-843.
    • (2005) Nature Cell Biology , vol.7 , pp. 837-843
    • Rajalingam, K.1    Wunder, C.2    Brinkmann, V.3    Churin, Y.4    Hekman, M.5    Sievers, C.6
  • 14
    • 16844376315 scopus 로고    scopus 로고
    • Oncogenic Ras in tumour progression and metastasis
    • 3
    • Giehl, K. (2005). Oncogenic Ras in tumour progression and metastasis. Biological Chemistry, 386(3), 193-205.
    • (2005) Biological Chemistry , vol.386 , pp. 193-205
    • Giehl, K.1
  • 15
    • 17644367566 scopus 로고    scopus 로고
    • H-Ras-specific activation of Rac-MKK3/6-p38 pathway: Its critical role in invasion and migration of breast epithelial cells
    • 15
    • Shin, I., Kim, S., Song, H., Kim, H. R., & Moon, A. (2005). H-Ras-specific activation of Rac-MKK3/6-p38 pathway: its critical role in invasion and migration of breast epithelial cells. Journal of Biological Chemistry, 280(15), 14675-14683.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 14675-14683
    • Shin, I.1    Kim, S.2    Song, H.3    Kim, H.R.4    Moon, A.5
  • 16
    • 3442876128 scopus 로고    scopus 로고
    • Activation of phosphatidylinositol 3-kinase and extracellular signal-regulated kinase is required for glial cell line-derived neurotrophic factor-induced migration and invasion of pancreatic carcinoma cells
    • 15
    • Veit, C., Genze, F., Menke, A., Hoeffert, S., Gress, T. M., Gierschik, P., et al. (2004). Activation of phosphatidylinositol 3-kinase and extracellular signal-regulated kinase is required for glial cell line-derived neurotrophic factor-induced migration and invasion of pancreatic carcinoma cells. Cancer Research, 64(15), 5291-5300.
    • (2004) Cancer Research , vol.64 , pp. 5291-5300
    • Veit, C.1    Genze, F.2    Menke, A.3    Hoeffert, S.4    Gress, T.M.5    Gierschik, P.6
  • 17
    • 0034744538 scopus 로고    scopus 로고
    • Induction of beta3-integrin gene expression by sustained activation of the Ras-regulated Raf-MEK-extracellular signal-regulated kinase signaling pathway
    • 9
    • Woods, D., Cherwinski, H., Venetsanakos, E., Bhat, A., Gysin, S., Humbert, M., et al. (2001). Induction of beta3-integrin gene expression by sustained activation of the Ras-regulated Raf-MEK-extracellular signal-regulated kinase signaling pathway. Molecular and Cellular Biology, 21(9), 3192-3205.
    • (2001) Molecular and Cellular Biology , vol.21 , pp. 3192-3205
    • Woods, D.1    Cherwinski, H.2    Venetsanakos, E.3    Bhat, A.4    Gysin, S.5    Humbert, M.6
  • 18
    • 34250761800 scopus 로고    scopus 로고
    • Signaling pathways involved in collagen-induced disruption of the E-cadherin complex during epithelial-mesenchymal transition
    • 1-3
    • Imamichi, Y., & Menke, A. (2007). Signaling pathways involved in collagen-induced disruption of the E-cadherin complex during epithelial-mesenchymal transition. Cells Tissues Organs, 185(1-3), 180-190.
    • (2007) Cells Tissues Organs , vol.185 , pp. 180-190
    • Imamichi, Y.1    Menke, A.2
  • 19
    • 34250729008 scopus 로고    scopus 로고
    • Epidermal growth factor receptor in cultured human retinal pigment epithelial cells
    • 4
    • Yan, F., Hui, Y. N., Li, Y. J., Guo, C. M., & Meng, H. (2007). Epidermal growth factor receptor in cultured human retinal pigment epithelial cells. Ophthalmologica, 221(4), 244-250.
    • (2007) Ophthalmologica , vol.221 , pp. 244-250
    • Yan, F.1    Hui, Y.N.2    Li, Y.J.3    Guo, C.M.4    Meng, H.5
  • 20
    • 0033553558 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates p38 mitogen-activated protein kinase through a Ras-dependent pathway that is important for actin reorganization and cell migration
    • 20
    • Matsumoto, T., Yokote, K., Tamura, K., Takemoto, M., Ueno, H., Saito, Y., et al. (1999). Platelet-derived growth factor activates p38 mitogen-activated protein kinase through a Ras-dependent pathway that is important for actin reorganization and cell migration. Journal of Biological Chemistry, 274(20), 13954-13960.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 13954-13960
    • Matsumoto, T.1    Yokote, K.2    Tamura, K.3    Takemoto, M.4    Ueno, H.5    Saito, Y.6
  • 22
    • 33751295132 scopus 로고    scopus 로고
    • Expression of Wnt-5a is correlated with aggressiveness of gastric cancer by stimulating cell migration and invasion
    • 21
    • Kurayoshi, M., Oue, N., Yamamoto, H., Kishida, M., Inoue, A., Asahara, T., et al. (2006). Expression of Wnt-5a is correlated with aggressiveness of gastric cancer by stimulating cell migration and invasion. Cancer Research, 66(21), 10439-10448.
    • (2006) Cancer Research , vol.66 , pp. 10439-10448
    • Kurayoshi, M.1    Oue, N.2    Yamamoto, H.3    Kishida, M.4    Inoue, A.5    Asahara, T.6
  • 23
    • 0037009371 scopus 로고    scopus 로고
    • Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling
    • 17
    • Abassi, Y. A., & Vuori, K. (2002). Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling. EMBO Journal, 21(17), 4571-4582.
    • (2002) EMBO Journal , vol.21 , pp. 4571-4582
    • Abassi, Y.A.1    Vuori, K.2
  • 25
    • 24344431570 scopus 로고    scopus 로고
    • A novel protein kinase C alpha-dependent signal to ERK1/2 activated by alphaVbeta3 integrin in osteoclasts and in Chinese hamster ovary (CHO) cells
    • Pt 15
    • Rucci, N., DiGiacinto, C., Orru, L., Millimaggi, D., Baron, R., & Teti, A. (2005). A novel protein kinase C alpha-dependent signal to ERK1/2 activated by alphaVbeta3 integrin in osteoclasts and in Chinese hamster ovary (CHO) cells. Journal of Cell Science, 118(Pt 15), 3263-3275.
    • (2005) Journal of Cell Science , vol.118 , pp. 3263-3275
    • Rucci, N.1    Digiacinto, C.2    Orru, L.3    Millimaggi, D.4    Baron, R.5    Teti, A.6
  • 26
    • 33748289487 scopus 로고    scopus 로고
    • Alpha1beta1-integrin engagement to distinct laminin-1 domains orchestrates spreading, migration and survival of neural crest cells through independent signaling pathways
    • Pt 15
    • Desban, N., Lissitzky, J. C., Rousselle, P., & Duband, J. L. (2006). alpha1beta1-integrin engagement to distinct laminin-1 domains orchestrates spreading, migration and survival of neural crest cells through independent signaling pathways. Journal of Cell Science, 119(Pt 15), 3206-3218.
    • (2006) Journal of Cell Science , vol.119 , pp. 3206-3218
    • Desban, N.1    Lissitzky, J.C.2    Rousselle, P.3    Duband, J.L.4
  • 27
    • 6344248651 scopus 로고    scopus 로고
    • PKC controls HGF-dependent c-Met traffic, signalling and cell migration
    • 19
    • Kermorgant, S., Zicha, D., & Parker, P. J. (2004). PKC controls HGF-dependent c-Met traffic, signalling and cell migration. EMBO Journal, 23(19), 3721-3734.
    • (2004) EMBO Journal , vol.23 , pp. 3721-3734
    • Kermorgant, S.1    Zicha, D.2    Parker, P.J.3
  • 28
    • 34249979835 scopus 로고    scopus 로고
    • Epidermal growth factor and transforming growth factor-beta1 enhance HK-2 cell migration through a synergistic increase of matrix metalloproteinase and sustained activation of ERK signaling pathway
    • 11
    • Tian, Y. C., Chen, Y. C., Chang, C. T., Hung, C. C., Wu, M. S., Phillips, A., et al. (2007). Epidermal growth factor and transforming growth factor-beta1 enhance HK-2 cell migration through a synergistic increase of matrix metalloproteinase and sustained activation of ERK signaling pathway. Experimental Cell Research, 313(11), 2367-2377.
    • (2007) Experimental Cell Research , vol.313 , pp. 2367-2377
    • Tian, Y.C.1    Chen, Y.C.2    Chang, C.T.3    Hung, C.C.4    Wu, M.S.5    Phillips, A.6
  • 29
    • 23444440323 scopus 로고    scopus 로고
    • A-Raf and Raf-1 work together to influence transient ERK phosphorylation and Gl/S cell cycle progression
    • 33
    • Mercer, K., Giblett, S., Oakden, A., Brown, J., Marais, R., & Pritchard, C. (2005). A-Raf and Raf-1 work together to influence transient ERK phosphorylation and Gl/S cell cycle progression. Oncogene, 24(33), 5207-5217.
    • (2005) Oncogene , vol.24 , pp. 5207-5217
    • Mercer, K.1    Giblett, S.2    Oakden, A.3    Brown, J.4    Marais, R.5    Pritchard, C.6
  • 30
    • 34748921018 scopus 로고    scopus 로고
    • Differential effect of FGF and PDGF on cell proliferation and migration in osteoblastic cells
    • 2
    • Kim, S. J., Kim, S. Y., Kwon, C. H., & Kim, Y. K. (2007). Differential effect of FGF and PDGF on cell proliferation and migration in osteoblastic cells. Growth Factors, 25(2), 77-86.
    • (2007) Growth Factors , vol.25 , pp. 77-86
    • Kim, S.J.1    Kim, S.Y.2    Kwon, C.H.3    Kim, Y.K.4
  • 31
    • 0033548181 scopus 로고    scopus 로고
    • Sustained activation of the mitogen-activated protein kinase pathway. a mechanism underlying receptor tyrosine kinase specificity for matrix metalloproteinase-9 induction and cell migration
    • 7
    • McCawley, L. J., Li, S., Wattenberg, E. V., & Hudson, L. G. (1999). Sustained activation of the mitogen-activated protein kinase pathway. A mechanism underlying receptor tyrosine kinase specificity for matrix metalloproteinase-9 induction and cell migration. Journal of Biological Chemistry, 274(7), 4347-4353.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 4347-4353
    • McCawley, L.J.1    Li, S.2    Wattenberg, E.V.3    Hudson, L.G.4
  • 32
    • 0035849787 scopus 로고    scopus 로고
    • Temporal and quantitative regulation of mitogen-activated protein kinase (MAPK) modulates cell motility and invasion
    • 31
    • Krueger, J. S., Keshamouni, V. G., Atanaskova, N., & Reddy, K. B. (2001). Temporal and quantitative regulation of mitogen-activated protein kinase (MAPK) modulates cell motility and invasion. Oncogene, 20(31), 4209-4218.
    • (2001) Oncogene , vol.20 , pp. 4209-4218
    • Krueger, J.S.1    Keshamouni, V.G.2    Atanaskova, N.3    Reddy, K.B.4
  • 33
    • 36249012382 scopus 로고    scopus 로고
    • EGF-receptor- mediated mammary epithelial cell migration is driven by sustained ERK signaling from autocrine stimulation
    • Pt 20
    • lin, E. J., Opresko, L. K., Wells, A., Wiley, H. S., & Lauffenburger, D. A. (2007). EGF-receptor- mediated mammary epithelial cell migration is driven by sustained ERK signaling from autocrine stimulation. Journal of Cell Science, 120(Pt 20), 3688-3699.
    • (2007) Journal of Cell Science , vol.120 , pp. 3688-3699
    • Lin, E.J.1    Opresko, L.K.2    Wells, A.3    Wiley, H.S.4    Lauffenburger, D.A.5
  • 34
    • 0036781973 scopus 로고    scopus 로고
    • A signaling pathway leading to metastasis is controlled by N-cadherin and the FGF receptor
    • 4
    • Suyama, K., Shapiro, I., Guttman, M., & Hazan, R. B. (2002). A signaling pathway leading to metastasis is controlled by N-cadherin and the FGF receptor. Cancer Cell, 2(4), 301-314.
    • (2002) Cancer Cell , vol.2 , pp. 301-314
    • Suyama, K.1    Shapiro, I.2    Guttman, M.3    Hazan, R.B.4
  • 35
    • 0032145417 scopus 로고    scopus 로고
    • Platelet-derived growth factor-BB, insulin-like growth factor-I, and phorbol ester activate different signaling pathways for stimulation of vascular smooth muscle cell migration
    • 2
    • Pukac, L., Huangpu, J., & Karnovsky, M. J. (1998). Platelet-derived growth factor-BB, insulin-like growth factor-I, and phorbol ester activate different signaling pathways for stimulation of vascular smooth muscle cell migration. Experimental Cell Research, 242(2), 548-560.
    • (1998) Experimental Cell Research , vol.242 , pp. 548-560
    • Pukac, L.1    Huangpu, J.2    Karnovsky, M.J.3
  • 36
    • 33750590656 scopus 로고    scopus 로고
    • Reactive oxygen species mediated sustained activation of protein kinase C alpha and extracellular signal-regulated kinase for migration of human hepatoma cell Hepg2
    • 10
    • Wu, W. S., Tsai, R. K., Chang, C. H., Wang, S., Wu, J. R., & Chang, Y. X. (2006). Reactive oxygen species mediated sustained activation of protein kinase C alpha and extracellular signal-regulated kinase for migration of human hepatoma cell Hepg2. Molecular Cancer Research, 4(10), 747-758.
    • (2006) Molecular Cancer Research , vol.4 , pp. 747-758
    • Wu, W.S.1    Tsai, R.K.2    Chang, C.H.3    Wang, S.4    Wu, J.R.5    Chang, Y.X.6
  • 37
    • 0037515655 scopus 로고    scopus 로고
    • Sustained induction of ERK, protein kinase B, and p70 S6 kinase regulates cell spreading and formation of F-actin microspikes upon ligation of integrins by galectin-8, a mammalian lectin
    • 16
    • Levy, Y., Ronen, D., Bershadsky, A. D., & Zick, Y. (2003). Sustained induction of ERK, protein kinase B, and p70 S6 kinase regulates cell spreading and formation of F-actin microspikes upon ligation of integrins by galectin-8, a mammalian lectin. Journal of Biological Chemistry, 278(16), 14533-14542.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 14533-14542
    • Levy, Y.1    Ronen, D.2    Bershadsky, A.D.3    Zick, Y.4
  • 39
    • 0034744538 scopus 로고    scopus 로고
    • Induction of beta3-integrin gene expression by sustained activation of the Ras-regulated Raf-MEK-extracellular signal-regulated kinase signaling pathway
    • 9
    • Woods, D., Cherwinski, H., Venetsanakos, E., Bhat, A., Gysin, S., Humbert, M., et al. (2001). Induction of beta3-integrin gene expression by sustained activation of the Ras-regulated Raf-MEK-extracellular signal-regulated kinase signaling pathway. Molecular and Cellular Biology, 21(9), 3192-3205.
    • (2001) Molecular and Cellular Biology , vol.21 , pp. 3192-3205
    • Woods, D.1    Cherwinski, H.2    Venetsanakos, E.3    Bhat, A.4    Gysin, S.5    Humbert, M.6
  • 40
    • 34547226194 scopus 로고    scopus 로고
    • Regulation of MAPKs by growth factors and receptor tyrosine kinases
    • 8
    • Katz, M., Amit, I., & Yarden, Y. (2007). Regulation of MAPKs by growth factors and receptor tyrosine kinases. Biochimica et Biophysica Acta, 1773(8), 1161-1176.
    • (2007) Biochimica et Biophysica Acta , vol.1773 , pp. 1161-1176
    • Katz, M.1    Amit, I.2    Yarden, Y.3
  • 41
    • 3142733866 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase (ERK)-dependent gene expression contributes to L1 cell adhesion molecule-dependent motility and invasion
    • 28
    • Silletti, S., Yebra, M., Perez, B., Cirulli, V., McMahon, M., & Montgomery, A. M. (2004). Extracellular signal-regulated kinase (ERK)-dependent gene expression contributes to L1 cell adhesion molecule-dependent motility and invasion. Journal of Biological Chemistry, 279(28), 28880-28888.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 28880-28888
    • Silletti, S.1    Yebra, M.2    Perez, B.3    Cirulli, V.4    McMahon, M.5    Montgomery, A.M.6
  • 42
    • 6344255031 scopus 로고    scopus 로고
    • Paxillin serves as an ERK-regulated scaffold for coordinating FAK and Rac activation in epithelial morphogenesis
    • 2
    • Ishibe, S., Joly, D., Liu, Z. X., & Cantley, L. G. (2004). Paxillin serves as an ERK-regulated scaffold for coordinating FAK and Rac activation in epithelial morphogenesis. Molecular Cell, 16(2), 257-267.
    • (2004) Molecular Cell , vol.16 , pp. 257-267
    • Ishibe, S.1    Joly, D.2    Liu, Z.X.3    Cantley, L.G.4
  • 43
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • 5430
    • Giancotti, F. G., & Ruoslahti, E. (1999). Integrin signaling. Science, 285(5430), 1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 44
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • 5
    • Mitra, S. K., & Schlaepfer, D. D. (2006). Integrin-regulated FAK-Src signaling in normal and cancer cells. Current Opinion in Cell Biology, 18(5), 516-523.
    • (2006) Current Opinion in Cell Biology , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 45
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • 2
    • Hood, J. D., & Cheresh, D. A. (2002). Role of integrins in cell invasion and migration. Nature Reviews. Cancer, 2(2), 91-100.
    • (2002) Nature Reviews. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 46
    • 33847063469 scopus 로고    scopus 로고
    • Redox signalling in anchorage-dependent cell growth
    • 4
    • Chiarugi, P., & Fiaschi, T. (2007). Redox signalling in anchorage-dependent cell growth. Cell Signal, 19(4), 672-682.
    • (2007) Cell Signal , vol.19 , pp. 672-682
    • Chiarugi, P.1    Fiaschi, T.2
  • 47
    • 33750887331 scopus 로고    scopus 로고
    • A functional RNAi screen for regulators of receptor tyrosine kinase and ERK signalling
    • 7116
    • Friedman, A., & Perrimon, N. (2006). A functional RNAi screen for regulators of receptor tyrosine kinase and ERK signalling. Nature, 444(7116), 230-234.
    • (2006) Nature , vol.444 , pp. 230-234
    • Friedman, A.1    Perrimon, N.2
  • 48
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti, F. G., & Tarone, G. (2003). Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annual Review of Cell and Developmental Biology, 19, 173-206.
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 49
    • 0034704174 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor beta and vascular endothelial growth factor receptor 2 bind to the beta 3 integrin through its extracellular domain
    • 51
    • Borges, E., Jan, Y., & Ruoslahti, E. (2000). Platelet-derived growth factor receptor beta and vascular endothelial growth factor receptor 2 bind to the beta 3 integrin through its extracellular domain. Journal of Biological Chemistry, 275(51), 39867-39873.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 39867-39873
    • Borges, E.1    Jan, Y.2    Ruoslahti, E.3
  • 50
    • 0034724667 scopus 로고    scopus 로고
    • Integrins regulate the linkage between upstream and downstream events in G protein-coupled receptor signaling to mitogen-activated protein kinase
    • 17
    • Short, S. M., Boyer, J. L., & Juliano, R. L. (2000). Integrins regulate the linkage between upstream and downstream events in G protein-coupled receptor signaling to mitogen-activated protein kinase. Journal of Biological Chemistry, 275(17), 12970-12977.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 12970-12977
    • Short, S.M.1    Boyer, J.L.2    Juliano, R.L.3
  • 51
    • 33746764457 scopus 로고    scopus 로고
    • Beta 4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis
    • 3
    • Guo, W., Pylayeva, Y., Pepe, A., Yoshioka, T., Muller, W. J., Inghirami, G., et al. (2006). Beta 4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis. Cell, 126(3), 489-502.
    • (2006) Cell , vol.126 , pp. 489-502
    • Guo, W.1    Pylayeva, Y.2    Pepe, A.3    Yoshioka, T.4    Muller, W.J.5    Inghirami, G.6
  • 52
    • 11244352382 scopus 로고    scopus 로고
    • Interaction between insulin-like growth factor-I receptor and alphaVbeta3 integrin linked signaling pathways: Cellular responses to changes in multiple signaling inputs
    • 1
    • Clemmons, D. R., & Maile, L. A. (2005). Interaction between insulin-like growth factor-I receptor and alphaVbeta3 integrin linked signaling pathways: cellular responses to changes in multiple signaling inputs. Molecular Endocrinology, 19(1), 1-11.
    • (2005) Molecular Endocrinology , vol.19 , pp. 1-11
    • Clemmons, D.R.1    Maile, L.A.2
  • 53
    • 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
    • 6 Pt 1
    • Miyamoto, S., Teramoto, H., Gutkind, J. S., & Yamada, K. M. (1996). Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. Journal of Cell Biology, 135(6 Pt 1), 1633-1642.
    • (1996) Journal of Cell Biology , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 54
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Pt 23
    • Turner, C. E. (2000). Paxillin interactions. Journal of Cell Science, 113(Pt 23), 4139-4140.
    • (2000) Journal of Cell Science , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 55
    • 33845669072 scopus 로고    scopus 로고
    • Integrin signaling in epithelial cells
    • 1
    • Gilcrease, M. Z. (2007). Integrin signaling in epithelial cells. Cancer Letters, 247(1), 1-25.
    • (2007) Cancer Letters , vol.247 , pp. 1-25
    • Gilcrease, M.Z.1
  • 56
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Pt 24
    • Li, F., Zhang, Y., & Wu, C. (1999). Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. Journal of Cell Science, 112(Pt 24), 4589-4599.
    • (1999) Journal of Cell Science , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 57
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • 12
    • Tu, Y., Li, F., & Wu, C. (1998). Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Molecular Biology of the Cell, 9(12), 3367-3382.
    • (1998) Molecular Biology of the Cell , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 58
    • 9644289575 scopus 로고    scopus 로고
    • Integrins: Versatile integrators of extracellular signals
    • 12
    • ffrench-Constant, C., & Colognato, H. (2004). Integrins: Versatile integrators of extracellular signals. Trends in Cell Biology, 14(12), 678-686.
    • (2004) Trends in Cell Biology , vol.14 , pp. 678-686
    • Ffrench-Constant, C.1    Colognato, H.2
  • 59
    • 33645359717 scopus 로고    scopus 로고
    • Crosstalk between hepatocyte growth factor and integrin signaling pathways
    • 2
    • Chan, P. C., Chen, S. Y., Chen, C. H., & Chen, H. C. (2006). Crosstalk between hepatocyte growth factor and integrin signaling pathways. Journal of Biomedical Science, 13(2), 215-223.
    • (2006) Journal of Biomedical Science , vol.13 , pp. 215-223
    • Chan, P.C.1    Chen, S.Y.2    Chen, C.H.3    Chen, H.C.4
  • 60
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • Playford, M. P., & Schaller, M. D. (2004). The interplay between Src and integrins in normal and tumor biology. Oncogene, 23, 7928-7946.
    • (2004) Oncogene , vol.23 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 61
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • 5
    • Mitra, S. K., & Schlaepfer, D. D. (2006). Integrin-regulated FAK-Src signaling in normal and cancer cells. Current Opinion in Cell Biology, 18(5), 516-523.
    • (2006) Current Opinion in Cell Biology , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 62
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Pt 1
    • Zaidel-Bar, R., Milo, R., Kam, Z., & Geiger, B. (2007). A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. Journal of Cell Science, 120(Pt 1), 137-148.
    • (2007) Journal of Cell Science , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 63
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: Adapting to change
    • 4
    • Brown, M. C., & Turner, C. E. (2004). Paxillin: adapting to change. Physiological Reviews, 84(4), 1315-1339.
    • (2004) Physiological Reviews , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 64
    • 5644238718 scopus 로고    scopus 로고
    • C-Src is involved in regulating signal transmission from PDGFbeta receptor-GPCR(s) complexes in mammalian cells
    • 2
    • Waters, C. M., Connell, M. C., Pyne, S., & Pyne, N. J. (2005). c-Src is involved in regulating signal transmission from PDGFbeta receptor-GPCR(s) complexes in mammalian cells. Cell Signal, 17(2), 263-277.
    • (2005) Cell Signal , vol.17 , pp. 263-277
    • Waters, C.M.1    Connell, M.C.2    Pyne, S.3    Pyne, N.J.4
  • 65
    • 34447517479 scopus 로고    scopus 로고
    • FAK signaling in neoplastic disorders: A linkage between inflammation and cancer
    • Mon, N. N., Ito, S., Senga, T., & Hamaguchi, M. (2006). FAK signaling in neoplastic disorders: a linkage between inflammation and cancer. Annals of the New York Academy of Sciences, 1086, 199-212.
    • (2006) Annals of the New York Academy of Sciences , vol.1086 , pp. 199-212
    • Mon, N.N.1    Ito, S.2    Senga, T.3    Hamaguchi, M.4
  • 66
    • 33845687683 scopus 로고    scopus 로고
    • RAFTK/Pyk2 regulates EGF-induced PC12 cell spreading and movement
    • 2
    • Park, S. Y., Li, H., & Avraham, S. (2007). RAFTK/Pyk2 regulates EGF-induced PC12 cell spreading and movement. Cell Signal, 19(2), 289-300.
    • (2007) Cell Signal , vol.19 , pp. 289-300
    • Park, S.Y.1    Li, H.2    Avraham, S.3
  • 67
    • 33746865874 scopus 로고    scopus 로고
    • Proepithelin promotes migration and invasion of 5637 bladder cancer cells through the activation of ERK1/2 and the formation of a paxillin/FAK/ERK complex
    • 14
    • Monami, G., Gonzalez, E. M., Hellman, M., Gomella, L. G., Baffa, R., Iozzo, R. V., et al. (2006). Proepithelin promotes migration and invasion of 5637 bladder cancer cells through the activation of ERK1/2 and the formation of a paxillin/FAK/ERK complex. Cancer Research, 66(14), 7103-7110.
    • (2006) Cancer Research , vol.66 , pp. 7103-7110
    • Monami, G.1    Gonzalez, E.M.2    Hellman, M.3    Gomella, L.G.4    Baffa, R.5    Iozzo, R.V.6
  • 68
    • 33745264885 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-1 mediates migration of human colorectal carcinoma cells by activation of Src family kinases
    • 11
    • Lesslie, D. P., Summy, J. M., Parikh, N. U., Fan, F., Trevino, J. G., Sawyer, T. K., et al. (2006). Vascular endothelial growth factor receptor-1 mediates migration of human colorectal carcinoma cells by activation of Src family kinases. British Journal of Cancer, 94(11), 1710-1717.
    • (2006) British Journal of Cancer , vol.94 , pp. 1710-1717
    • Lesslie, D.P.1    Summy, J.M.2    Parikh, N.U.3    Fan, F.4    Trevino, J.G.5    Sawyer, T.K.6
  • 69
    • 0344845048 scopus 로고    scopus 로고
    • Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis
    • 5
    • Ishibe, S., Joly, D., Zhu, X., & Cantley, L. G. (2003). Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Molecular Cell, 12(5), 1275-1285.
    • (2003) Molecular Cell , vol.12 , pp. 1275-1285
    • Ishibe, S.1    Joly, D.2    Zhu, X.3    Cantley, L.G.4
  • 70
    • 0031610579 scopus 로고    scopus 로고
    • PAK kinases are directly coupled to the PIX family of nucleotide exchange factors
    • 2
    • Manser, E., Loo, T. H., Koh, C. G., Zhao, Z. S., Chen, X. Q., Tan, L., et al. (1998). PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. Molecular Cell, 1(2), 183-192.
    • (1998) Molecular Cell , vol.1 , pp. 183-192
    • Manser, E.1    Loo, T.H.2    Koh, C.G.3    Zhao, Z.S.4    Chen, X.Q.5    Tan, L.6
  • 71
    • 0035833251 scopus 로고    scopus 로고
    • The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    • 1
    • West, K. A., Zhang, H., Brown, M. C., Nikolopoulos, S. N., Riedy, M. C., Horwitz, A. F., et al. (2001). The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). Journal of Cell Biology, 154(1), 161-176.
    • (2001) Journal of Cell Biology , vol.154 , pp. 161-176
    • West, K.A.1    Zhang, H.2    Brown, M.C.3    Nikolopoulos, S.N.4    Riedy, M.C.5    Horwitz, A.F.6
  • 72
    • 33646776346 scopus 로고    scopus 로고
    • Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics
    • 4
    • Nayal, A., Webb, D. J., Brown, C. M., Schaefer, E. M., Vicente-Manzanares, M., & Horwitz, A. R. (2006). Paxillin phosphorylation at Ser273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics. Journal of Cell Biology, 173(4), 587-589.
    • (2006) Journal of Cell Biology , vol.173 , pp. 587-589
    • Nayal, A.1    Webb, D.J.2    Brown, C.M.3    Schaefer, E.M.4    Vicente-Manzanares, M.5    Horwitz, A.R.6
  • 73
    • 0033577810 scopus 로고    scopus 로고
    • Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    • 4
    • Turner, C. E., Brown, M. C., Perrotta, J. A., Riedy, M. C., Nikolopoulos, S. N., McDonald, A. R., et al. (1999). Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. Journal of Cell Biology, 145(4), 851-863.
    • (1999) Journal of Cell Biology , vol.145 , pp. 851-863
    • Turner, C.E.1    Brown, M.C.2    Perrotta, J.A.3    Riedy, M.C.4    Nikolopoulos, S.N.5    McDonald, A.R.6
  • 74
    • 0037769892 scopus 로고    scopus 로고
    • Crk associates with a multimolecular paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of paxillin to focal contacts
    • 7
    • Lamorte, L., Rodrigues, S., Sangwan, V., Turner, C. E., & Park, M. (2003). Crk associates with a multimolecular paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of paxillin to focal contacts. Molecular Biology of the Cell, 14(7), 2818-2831.
    • (2003) Molecular Biology of the Cell , vol.14 , pp. 2818-2831
    • Lamorte, L.1    Rodrigues, S.2    Sangwan, V.3    Turner, C.E.4    Park, M.5
  • 75
    • 0033954773 scopus 로고    scopus 로고
    • The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo
    • 2
    • Shen, Y., Lyons, P., Cooley, M., Davidson, D., Veillette, A., Salgia, R., et al. (2000). The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo. Journal of Biological Chemistry, 275(2), 1405-1413.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 1405-1413
    • Shen, Y.1    Lyons, P.2    Cooley, M.3    Davidson, D.4    Veillette, A.5    Salgia, R.6
  • 77
    • 30544454785 scopus 로고    scopus 로고
    • Paxillin is essential for PTP-PEST-dependent regulation of cell spreading and motility: A role for paxillin kinase linker
    • Pt 24
    • Jamieson, J. S., Tumbarello, D. A., Hallé, M., Brown, M. C., Tremblay, M. L., & Turner, C. E. (2005). Paxillin is essential for PTP-PEST-dependent regulation of cell spreading and motility: a role for paxillin kinase linker. Journal of Cell Science, 118(Pt 24), 5835-5847.
    • (2005) Journal of Cell Science , vol.118 , pp. 5835-5847
    • Jamieson, J.S.1    Tumbarello, D.A.2    Hallé, M.3    Brown, M.C.4    Tremblay, M.L.5    Turner, C.E.6
  • 78
    • 33947603008 scopus 로고    scopus 로고
    • Protein kinase C and other diacylglycerol effectors in cancer
    • 4
    • Griner, E. M., & Kazanietz, M. G. (2007). Protein kinase C and other diacylglycerol effectors in cancer. Nature Reviews Cancer, 7(4), 281-294.
    • (2007) Nature Reviews Cancer , vol.7 , pp. 281-294
    • Griner, E.M.1    Kazanietz, M.G.2
  • 79
    • 33846117134 scopus 로고    scopus 로고
    • The signaling mechanism of ROS in tumor progression
    • 4
    • Wu, W. S. (2006). The signaling mechanism of ROS in tumor progression. Cancer and Metastasis Reviews, 25(4), 695-705.
    • (2006) Cancer and Metastasis Reviews , vol.25 , pp. 695-705
    • Wu, W.S.1
  • 80
    • 27644496163 scopus 로고    scopus 로고
    • Mobilization and activation of a signaling competent alpha6beta4integrin underlies its contribution to carcinoma progression
    • 3
    • Lipscomb, E. A., & Mercurio, A. M. (2005). Mobilization and activation of a signaling competent alpha6beta4integrin underlies its contribution to carcinoma progression. Cancer and Metastasis Reviews, 24(3), 413-423.
    • (2005) Cancer and Metastasis Reviews , vol.24 , pp. 413-423
    • Lipscomb, E.A.1    Mercurio, A.M.2
  • 82
    • 0033168515 scopus 로고    scopus 로고
    • Protein kinase C delta involvement in mammary tumor cell metastasis
    • 13
    • Kiley, S. C., Clark, K. J., Goodnough, M., Welch, D. R., & Jaken, S. (1999). Protein kinase C delta involvement in mammary tumor cell metastasis. Cancer Research, 59(13), 3230-3238.
    • (1999) Cancer Research , vol.59 , pp. 3230-3238
    • Kiley, S.C.1    Clark, K.J.2    Goodnough, M.3    Welch, D.R.4    Jaken, S.5
  • 83
    • 24944563309 scopus 로고    scopus 로고
    • Protein kinase C epsilon is a predictive biomarker of aggressive breast cancer and a validated target for RNA interference anticancer therapy
    • 18
    • Pan, Q., Bao, L. W., Kleer, C. G., Sabel, M. S., Griffith, K. A., Teknos, T. N., et al. (2005). Protein kinase C epsilon is a predictive biomarker of aggressive breast cancer and a validated target for RNA interference anticancer therapy. Cancer Research, 65(18), 8366-8371.
    • (2005) Cancer Research , vol.65 , pp. 8366-8371
    • Pan, Q.1    Bao, L.W.2    Kleer, C.G.3    Sabel, M.S.4    Griffith, K.A.5    Teknos, T.N.6
  • 84
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • 9
    • Gopalakrishna, R., & Jaken, S. (2000). Protein kinase C signaling and oxidative stress. Free Radical Biology & Medicine, 28(9), 1349-1361.
    • (2000) Free Radical Biology & Medicine , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 85
    • 0033226842 scopus 로고    scopus 로고
    • The role of protein kinase C and novel phorbol ester receptors in tumor cell invasion and metastasis (review)
    • 6
    • Gomez, D. E., Skilton, G., Alonso, D. F., & Kazanietz, M. G. (1999). The role of protein kinase C and novel phorbol ester receptors in tumor cell invasion and metastasis (review). Oncology Reports, 6(6), 1363-1370.
    • (1999) Oncology Reports , vol.6 , pp. 1363-1370
    • Gomez, D.E.1    Skilton, G.2    Alonso, D.F.3    Kazanietz, M.G.4
  • 86
    • 34548387882 scopus 로고    scopus 로고
    • Intracellular signaling molecules involved in vasoactive intestinal peptide-mediated wound healing in human bronchial epithelial cells
    • 9
    • Guan, C. X., Cui, Y. R., Zhang, M., Bai, H. B., Khunkhun, R., & Fang, X. (2007). Intracellular signaling molecules involved in vasoactive intestinal peptide-mediated wound healing in human bronchial epithelial cells. Peptides, 28(9), 1667-1673.
    • (2007) Peptides , vol.28 , pp. 1667-1673
    • Guan, C.X.1    Cui, Y.R.2    Zhang, M.3    Bai, H.B.4    Khunkhun, R.5    Fang, X.6
  • 87
    • 0037151034 scopus 로고    scopus 로고
    • Mechanism of 17-beta-estradiol-induced Erk1/2 activation in breast cancer cells. a role for HER2 and PKC-delta
    • 25
    • Keshamouni, V. G., Mattingly, R. R., & Reddy, K. B. (2002). Mechanism of 17-beta-estradiol-induced Erk1/2 activation in breast cancer cells. A role for HER2 AND PKC-delta. Journal of Biological Chemistry, 277(25), 22558-22565.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 22558-22565
    • Keshamouni, V.G.1    Mattingly, R.R.2    Reddy, K.B.3
  • 88
    • 0035504758 scopus 로고    scopus 로고
    • Differential activation of ERKs to focal adhesions by PKC epsilon is required for PMA-induced adhesion and migration of human glioma cells
    • 50
    • Besson, A., Davy, A., Robbins, S. M., & Yong, V. W. (2001). Differential activation of ERKs to focal adhesions by PKC epsilon is required for PMA-induced adhesion and migration of human glioma cells. Oncogene, 20(50), 7398-7407.
    • (2001) Oncogene , vol.20 , pp. 7398-7407
    • Besson, A.1    Davy, A.2    Robbins, S.M.3    Yong, V.W.4
  • 89
    • 0032145417 scopus 로고    scopus 로고
    • Platelet-derived growth factor-BB, insulin-like growth factor-I, and phorbol ester activate different signaling pathways for stimulation of vascular smooth muscle cell migration
    • 2
    • Pukac, L., Huangpu, J., & Karnovsky, M. J. (1998). Platelet-derived growth factor-BB, insulin-like growth factor-I, and phorbol ester activate different signaling pathways for stimulation of vascular smooth muscle cell migration. Experimental Cell Research, 242(2), 548-560.
    • (1998) Experimental Cell Research , vol.242 , pp. 548-560
    • Pukac, L.1    Huangpu, J.2    Karnovsky, M.J.3
  • 90
    • 0031768408 scopus 로고    scopus 로고
    • Integrin ligation and PKC activation are required for migration of colon carcinoma cells
    • Pt 20
    • Rigot, V., Lehmann, M., Andre, F., Daemi, N., Marvaldi, J., & Luis, J. (1998). Integrin ligation and PKC activation are required for migration of colon carcinoma cells. Journal of Cell Science, 111(Pt 20), 3119-3127.
    • (1998) Journal of Cell Science , vol.111 , pp. 3119-3127
    • Rigot, V.1    Lehmann, M.2    Andre, F.3    Daemi, N.4    Marvaldi, J.5    Luis, J.6
  • 91
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • 3
    • Larsson, C. (2006). Protein kinase C and the regulation of the actin cytoskeleton. Cellular Signalling, 18(3), 276-284.
    • (2006) Cellular Signalling , vol.18 , pp. 276-284
    • Larsson, C.1
  • 92
    • 0033527658 scopus 로고    scopus 로고
    • Integrin-mediated muscle cell spreading. the role of protein kinase C in outside-in and inside-out signaling and evidence of integrin cross-talk
    • 45
    • Disatnik, M. H., & Rando, T. A. (1999). Integrin-mediated muscle cell spreading. The role of protein kinase C in outside-in and inside-out signaling and evidence of integrin cross-talk. Journal of Biological Chemistry, 274(45), 32486-32492.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 32486-32492
    • Disatnik, M.H.1    Rando, T.A.2
  • 93
    • 2942628076 scopus 로고    scopus 로고
    • Protein kinase C-alpha phosphorylation of specific serines in the connecting segment of the beta 4 integrin regulates the dynamics of type II hemidesmosomes
    • 10
    • Rabinovitz, I., Tsomo, L., & Mercurio, A. M. (2004). Protein kinase C-alpha phosphorylation of specific serines in the connecting segment of the beta 4 integrin regulates the dynamics of type II hemidesmosomes. Molecular and Cellular Biology, 24(10), 4351-4360.
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 4351-4360
    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
  • 94
    • 18444412912 scopus 로고    scopus 로고
    • Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis
    • 16
    • Parsons, M., Keppler, M. D., Kline, A., Messent, A., Humphries, M. J., Gilchrist, R., et al. (2002). Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis. Molecular and Cellular Biology, 22(16), 5897-5911.
    • (2002) Molecular and Cellular Biology , vol.22 , pp. 5897-5911
    • Parsons, M.1    Keppler, M.D.2    Kline, A.3    Messent, A.4    Humphries, M.J.5    Gilchrist, R.6
  • 95
    • 38449123194 scopus 로고    scopus 로고
    • Src regulates phorbol 12-myristate 13-acetate-activated PKC-induced migration via Cas/Crk/Rac1 signaling pathway in glioblastoma cells
    • 4
    • Nomura, N., Nomura, M., Sugiyama, K., & Hamada, J. (2007). Src regulates phorbol 12-myristate 13-acetate-activated PKC-induced migration via Cas/Crk/Rac1 signaling pathway in glioblastoma cells. International Journal of Molecular Medicine, 20(4), 511-519.
    • (2007) International Journal of Molecular Medicine , vol.20 , pp. 511-519
    • Nomura, N.1    Nomura, M.2    Sugiyama, K.3    Hamada, J.4
  • 96
    • 33748044620 scopus 로고    scopus 로고
    • Integrin signaling and cell spreading mediated by phorbol 12-myristate 13-acetate treatment
    • 1
    • Lee, M. S., Kim, Y. B., Lee, S. Y., Kim, J. G., Kim, S. H., Ye, S. K., et al. (2006). Integrin signaling and cell spreading mediated by phorbol 12-myristate 13-acetate treatment. Journal of Cellular Biochemistry, 99(1), 88-95.
    • (2006) Journal of Cellular Biochemistry , vol.99 , pp. 88-95
    • Lee, M.S.1    Kim, Y.B.2    Lee, S.Y.3    Kim, J.G.4    Kim, S.H.5    Ye, S.K.6
  • 97
    • 0029976232 scopus 로고    scopus 로고
    • Integrin alpha v beta 5-dependent serine phosphorylation of paxillin in cultured human macrophages adherent to vitronectin
    • 18
    • De Nichilo, M. O., & Yamada, K. M. (1996). Integrin alpha v beta 5-dependent serine phosphorylation of paxillin in cultured human macrophages adherent to vitronectin. Journal of Biological Chemistry, 271(18), 11016-11022.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 11016-11022
    • De Nichilo, M.O.1    Yamada, K.M.2
  • 98
    • 34347230464 scopus 로고    scopus 로고
    • RACK1 regulates Src activity and modulates paxillin dynamics during cell migration
    • 12
    • Doan, A. T., & Huttenlocher, A. (2007). RACK1 regulates Src activity and modulates paxillin dynamics during cell migration. Experimental Cell Research, 313(12), 2667-2679.
    • (2007) Experimental Cell Research , vol.313 , pp. 2667-2679
    • Doan, A.T.1    Huttenlocher, A.2
  • 100
    • 0344827268 scopus 로고    scopus 로고
    • Oxidants in receptor tyrosine kinase signal transduction pathways
    • 6
    • Aslan, M., & Ozben, T. (2003). Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxidants & Redox Signalling, 5(6), 781-788.
    • (2003) Antioxidants & Redox Signalling , vol.5 , pp. 781-788
    • Aslan, M.1    Ozben, T.2
  • 101
    • 18144383207 scopus 로고    scopus 로고
    • PTPs versus PTKs: The redox side of the coin
    • 4
    • Chiarugi, P. (2005). PTPs versus PTKs: the redox side of the coin. Free Radical Research, 39(4), 353-364.
    • (2005) Free Radical Research , vol.39 , pp. 353-364
    • Chiarugi, P.1
  • 102
    • 33751522909 scopus 로고    scopus 로고
    • The redox regulation of thiol dependent signaling pathways in cancer
    • 34
    • Giles, G. I. (2006). The redox regulation of thiol dependent signaling pathways in cancer. Current Pharmaceutical Design, 12(34), 4427-4443.
    • (2006) Current Pharmaceutical Design , vol.12 , pp. 4427-4443
    • Giles, G.I.1
  • 103
    • 33845741242 scopus 로고    scopus 로고
    • The cellular basis for diverse responses to oxygen
    • 2
    • Chandel, N. S., & Budinger, G. R. (2007). The cellular basis for diverse responses to oxygen. Free Radical Biology & Medicine, 42(2), 165-174.
    • (2007) Free Radical Biology & Medicine , vol.42 , pp. 165-174
    • Chandel, N.S.1    Budinger, G.R.2
  • 104
    • 33751543500 scopus 로고    scopus 로고
    • Pro-oxidant milieu blunts scissors: Insight into tumor progression, drug resistance, and novel druggable targets
    • 34
    • Pervaiz, S. (2006). Pro-oxidant milieu blunts scissors: insight into tumor progression, drug resistance, and novel druggable targets. Current Pharmaceutical Design, 12(34), 4469-4477.
    • (2006) Current Pharmaceutical Design , vol.12 , pp. 4469-4477
    • Pervaiz, S.1
  • 105
    • 4744344023 scopus 로고    scopus 로고
    • Oxidative stress and thioredoxin-interacting protein promote intravasation of melanoma cells
    • 2
    • Cheng, G. C., Schulze, P. C., Lee, R. T., Sylvan, J., Zetter, B. R., & Huang, H. (2004). Oxidative stress and thioredoxin-interacting protein promote intravasation of melanoma cells. Experimental Cell Research, 300(2), 297-307.
    • (2004) Experimental Cell Research , vol.300 , pp. 297-307
    • Cheng, G.C.1    Schulze, P.C.2    Lee, R.T.3    Sylvan, J.4    Zetter, B.R.5    Huang, H.6
  • 106
    • 33745534837 scopus 로고    scopus 로고
    • Pro-metastatic signaling by c-Met through RAC-1 and reactive oxygen species (ROS)
    • 26
    • Ferraro, D., Corso, S., Fasano, E., Panieri, E., Santangelo, R., Borrello, S., et al. (2006). Pro-metastatic signaling by c-Met through RAC-1 and reactive oxygen species (ROS). Oncogene, 25(26), 3689-3698.
    • (2006) Oncogene , vol.25 , pp. 3689-3698
    • Ferraro, D.1    Corso, S.2    Fasano, E.3    Panieri, E.4    Santangelo, R.5    Borrello, S.6
  • 107
    • 33947602679 scopus 로고    scopus 로고
    • Differential modulation of AMPK signaling pathways by low or high levels of exogenous reactive oxygen species in colon cancer cells
    • Park, I. J., Hwang, J. T., Kim, Y. M., Ha, J., & Park, O. J. (2006). Differential modulation of AMPK signaling pathways by low or high levels of exogenous reactive oxygen species in colon cancer cells. Annals of the New York Academy of Sciences, 1091, 102-109.
    • (2006) Annals of the New York Academy of Sciences , vol.1091 , pp. 102-109
    • Park, I.J.1    Hwang, J.T.2    Kim, Y.M.3    Ha, J.4    Park, O.J.5
  • 110
    • 12444322028 scopus 로고    scopus 로고
    • Resveratrol inhibits hepatoma cell invasion by suppressing gene expression of hepatocyte growth factor via its reactive oxygen species-scavenging property
    • 5
    • Miura, D., Miura, Y., & Yagasaki, K. (2004). Resveratrol inhibits hepatoma cell invasion by suppressing gene expression of hepatocyte growth factor via its reactive oxygen species-scavenging property. Clinical & Experimental Metastasis, 21(5), 445-451.
    • (2004) Clinical & Experimental Metastasis , vol.21 , pp. 445-451
    • Miura, D.1    Miura, Y.2    Yagasaki, K.3
  • 111
  • 113
    • 0347711117 scopus 로고    scopus 로고
    • NADPH oxidases: Not just for leukocytes anymore!
    • 9
    • Bokoch, G. M., & Knaus, U. G. (2003). NADPH oxidases: not just for leukocytes anymore!. Trends in Biochemical Sciences, 28(9), 502-508.
    • (2003) Trends in Biochemical Sciences , vol.28 , pp. 502-508
    • Bokoch, G.M.1    Knaus, U.G.2
  • 114
    • 19644394554 scopus 로고    scopus 로고
    • Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
    • 7040
    • Choi, M. H., Lee, I. K., Kim, G. W., Kim, B. U., Han, Y. H., Yu, D. Y., et al. (2005). Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature, 435(7040), 347-353.
    • (2005) Nature , vol.435 , pp. 347-353
    • Choi, M.H.1    Lee, I.K.2    Kim, G.W.3    Kim, B.U.4    Han, Y.H.5    Yu, D.Y.6
  • 115
    • 0033531923 scopus 로고    scopus 로고
    • Involvement of oxidative stress in tumor cytotoxic activity of hepatocyte growth factor/scatter factor
    • 19
    • Arakaki, N., Kajihara, T., Arakaki, R., Ohnishi, T., Kazi, J. A., Nakashima, H., et al. (1999). Involvement of oxidative stress in tumor cytotoxic activity of hepatocyte growth factor/scatter factor. Journal of Biological Chemistry, 274(19), 13541-13546.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 13541-13546
    • Arakaki, N.1    Kajihara, T.2    Arakaki, R.3    Ohnishi, T.4    Kazi, J.A.5    Nakashima, H.6
  • 116
    • 0036479214 scopus 로고    scopus 로고
    • Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR
    • 5
    • Colavitti, R., Pani, G., Bedogni, B., Anzevino, R., Borrello, S., Waltenberger, J., et al. (2002). Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR. Journal of Biological Chemistry, 277(5), 3101-3108.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 3101-3108
    • Colavitti, R.1    Pani, G.2    Bedogni, B.3    Anzevino, R.4    Borrello, S.5    Waltenberger, J.6
  • 117
    • 0037157824 scopus 로고    scopus 로고
    • Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases
    • 2
    • Werner, E., & Werb, Z. (2002). Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases. Journal of Biological Chemistry, 158(2), 357-368.
    • (2002) Journal of Biological Chemistry , vol.158 , pp. 357-368
    • Werner, E.1    Werb, Z.2
  • 118
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • 5
    • Kamata, H., Honda, S., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005). Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell, 120(5), 649-661.
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 119
    • 33947126121 scopus 로고    scopus 로고
    • Cytotoxicity of TNFalpha is regulated by integrin-mediated matrix signaling
    • 5
    • Chen, C. C., Young, J. L., Monzon, R. I., Chen, N., Todorovic, V., & Lau, L. F. (2007). Cytotoxicity of TNFalpha is regulated by integrin-mediated matrix signaling. EMBO Journal, 26(5), 1257-1267.
    • (2007) EMBO Journal , vol.26 , pp. 1257-1267
    • Chen, C.C.1    Young, J.L.2    Monzon, R.I.3    Chen, N.4    Todorovic, V.5    Lau, L.F.6
  • 120
    • 0042734919 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of cell adhesion
    • 1
    • Chiarugi, P. (2003). Reactive oxygen species as mediators of cell adhesion. Italian Journal of Biochemistry, 52(1), 28-32.
    • (2003) Italian Journal of Biochemistry , vol.52 , pp. 28-32
    • Chiarugi, P.1
  • 121
    • 0037780966 scopus 로고    scopus 로고
    • Reactive oxygen species as essential mediators of cell adhesion: The oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion
    • 5
    • Chiarugi, P., Pani, G., Giannoni, E., Taddei, L., Colavitti, R., Raugei, G., et al. (2003). Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. Journal of Cell Biology, 161(5), 933-944.
    • (2003) Journal of Cell Biology , vol.161 , pp. 933-944
    • Chiarugi, P.1    Pani, G.2    Giannoni, E.3    Taddei, L.4    Colavitti, R.5    Raugei, G.6
  • 122
    • 19644394554 scopus 로고    scopus 로고
    • Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
    • 7040
    • Choi, M. H., Lee, I. K., Kim, G. W., Kim, B. U., Han, Y. H., Yu, D. Y., et al. (2005). Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature, 435(7040), 347-353.
    • (2005) Nature , vol.435 , pp. 347-353
    • Choi, M.H.1    Lee, I.K.2    Kim, G.W.3    Kim, B.U.4    Han, Y.H.5    Yu, D.Y.6
  • 123
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • 2
    • Meng, T. C., Fukada, T., & Tonks, N. K. (2002). Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Molecular Cell, 9(2), 387-399.
    • (2002) Molecular Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 124
    • 35649021332 scopus 로고    scopus 로고
    • NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases
    • 5
    • Lee, J. K., Edderkaoui, M., Truong, P., Ohno, I., Jang, K. T., Berti, A., et al. (2007). NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases. Gastroenterology, 133(5), 1637-1648.
    • (2007) Gastroenterology , vol.133 , pp. 1637-1648
    • Lee, J.K.1    Edderkaoui, M.2    Truong, P.3    Ohno, I.4    Jang, K.T.5    Berti, A.6
  • 125
    • 0032403050 scopus 로고    scopus 로고
    • Reactive oxygen species activate focal adhesion kinase, paxillin and p130cas tyrosine phosphorylation in endothelial cells
    • 9
    • Gozin, A., Franzini, E., Andrieu, V., Da Costa, L., Rollet-Labelle, E., & Pasquier, C. (1998). Reactive oxygen species activate focal adhesion kinase, paxillin and p130cas tyrosine phosphorylation in endothelial cells. Free Radical Biology & Medicine, 25(9), 1021-1032.
    • (1998) Free Radical Biology & Medicine , 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
  • 126
    • 0036954803 scopus 로고    scopus 로고
    • Novel role of gp91(phox) containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis
    • 12
    • Ushio-Fukai, M., Tang, Y., Fukai, T., Dikalov, S. I., Ma, Y., Fujimoto, M., et al. (2002). Novel role of gp91(phox) containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis. Circulation Research, 91(12), 1160-1167.
    • (2002) Circulation Research , vol.91 , pp. 1160-1167
    • Ushio-Fukai, M.1    Tang, Y.2    Fukai, T.3    Dikalov, S.I.4    Ma, Y.5    Fujimoto, M.6
  • 129
    • 0034112918 scopus 로고    scopus 로고
    • Molecular cloning of human Hic-5, a potential regulator involved in signal transduction and cellular senescence
    • 3
    • Zhang, J., Zhang, L. X., Meltzer, P. S., Barrett, J. C., & Trent, J. M. (2000). Molecular cloning of human Hic-5, a potential regulator involved in signal transduction and cellular senescence. Molecular Carcinogenesis, 27(3), 177-183.
    • (2000) Molecular Carcinogenesis , vol.27 , pp. 177-183
    • Zhang, J.1    Zhang, L.X.2    Meltzer, P.S.3    Barrett, J.C.4    Trent, J.M.5
  • 130
    • 0033577810 scopus 로고    scopus 로고
    • Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    • 4
    • Turner, C. E., Brown, M. C., Perrotta, J. A., Riedy, M. C., Nikolopoulos, S. N., McDonald, A. R., et al. (1999). Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. Journal of Cell Biology, 145(4), 851-863.
    • (1999) Journal of Cell Biology , vol.145 , pp. 851-863
    • Turner, C.E.1    Brown, M.C.2    Perrotta, J.A.3    Riedy, M.C.4    Nikolopoulos, S.N.5    McDonald, A.R.6
  • 131
    • 0031964904 scopus 로고    scopus 로고
    • Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions
    • 2
    • Matsuya, M., Sasaki, H., Aoto, H., Mitaka, T., Nagura, K., Ohba, T., et al. (1998). Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions. Journal of Biological Chemistry, 273(2), 1003-1014.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 1003-1014
    • Matsuya, M.1    Sasaki, H.2    Aoto, H.3    Mitaka, T.4    Nagura, K.5    Ohba, T.6
  • 132
    • 0033515444 scopus 로고    scopus 로고
    • Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain
    • 14
    • Nishiya, N., Iwabuchi, Y., Shibanuma, M., Côté, J. F., Tremblay, M. L., & Nose, K. (1999). Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain. Journal of Biological Chemistry, 274(14), 9847-9853.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 9847-9853
    • Nishiya, N.1    Iwabuchi, Y.2    Shibanuma, M.3    Côté, J.F.4    Tremblay, M.L.5    Nose, K.6
  • 133
    • 0037108204 scopus 로고    scopus 로고
    • Inhibition of PTPs by H(2)O(2) regulates the activation of distinct MAPK pathways
    • 8
    • Lee, K., & Esselman, W. J. (2002). Inhibition of PTPs by H(2)O(2) regulates the activation of distinct MAPK pathways. Free Radical Biology & Medicine, 33(8), 1121-1132.
    • (2002) Free Radical Biology & Medicine , vol.33 , pp. 1121-1132
    • Lee, K.1    Esselman, W.J.2
  • 134
    • 0035092997 scopus 로고    scopus 로고
    • Signaling events mediating the additive effects of oleic acid and angiotensin II on vascular smooth muscle cell migration
    • 2
    • Greene, E. L., Lu, G., Zhang, D., & Egan, B. M. (2001). Signaling events mediating the additive effects of oleic acid and angiotensin II on vascular smooth muscle cell migration. Hypertension, 37(2), 308-312.
    • (2001) Hypertension , vol.37 , pp. 308-312
    • Greene, E.L.1    Lu, G.2    Zhang, D.3    Egan, B.M.4
  • 135
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • 9
    • Gopalakrishna, R., & Jaken, S. (2000). Protein kinase C signaling and oxidative stress. Free Radical Biology & Medicine, 28(9), 1349-1361.
    • (2000) Free Radical Biology & Medicine , vol.28 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 137
    • 17144369501 scopus 로고    scopus 로고
    • Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions
    • 14
    • Lin, D., & Takemoto, D. J. (2005). Oxidative activation of protein kinase Cgamma through the C1 domain. Effects on gap junctions. Journal of Biological Chemistry, 280(14), 13682-13693.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 13682-13693
    • Lin, D.1    Takemoto, D.J.2
  • 138
    • 18144447696 scopus 로고    scopus 로고
    • Protein kinase C-dependent increase in reactive oxygen species (ROS) production in vascular tissues of diabetes: Role of vascular NAD(P)H oxidase
    • 8 Suppl 3
    • Inoguchi, T., Sonta, T., Tsubouchi, H., Etoh, T., Kakimoto, M., Sonoda, N., et al. (2003). Protein kinase C-dependent increase in reactive oxygen species (ROS) production in vascular tissues of diabetes: role of vascular NAD(P)H oxidase. Journal of the American Society of Nephrology, 14(8 Suppl 3), S227-232.
    • (2003) Journal of the American Society of Nephrology , vol.14 , pp. 227-232
    • Inoguchi, T.1    Sonta, T.2    Tsubouchi, H.3    Etoh, T.4    Kakimoto, M.5    Sonoda, N.6
  • 139
    • 0042867408 scopus 로고    scopus 로고
    • Reactive oxygen species-regulated signaling pathways in diabetic nephropathy
    • 8 Suppl 3
    • Lee, H. B., Yu, M. R., Yang, Y., Jiang, Z., & Ha, H. (2003). Reactive oxygen species-regulated signaling pathways in diabetic nephropathy. Journal of The American Society of Nephrology, 14(8 Suppl 3), S241-245.
    • (2003) Journal of the American Society of Nephrology , vol.14 , pp. 241-245
    • Lee, H.B.1    Yu, M.R.2    Yang, Y.3    Jiang, Z.4    Ha, H.5
  • 140
    • 33744913842 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase gamma signaling through protein kinase Czeta induces NADPH oxidase-mediated oxidant generation and NF-kappaB activation in endothelial cells
    • 23
    • Frey, R. S., Gao, X., Javaid, K., Siddiqui, S. S., Rahman, A., & Malik, A. B. (2006). Phosphatidylinositol 3-kinase gamma signaling through protein kinase Czeta induces NADPH oxidase-mediated oxidant generation and NF-kappaB activation in endothelial cells. Journal of Biological Chemistry, 281(23), 16128-16138.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 16128-16138
    • Frey, R.S.1    Gao, X.2    Javaid, K.3    Siddiqui, S.S.4    Rahman, A.5    Malik, A.B.6
  • 141
    • 32844463572 scopus 로고    scopus 로고
    • In high glucose protein kinase C-zeta activation is required for mesangial cell generation of reactive oxygen species
    • 6
    • Kwan, J., Wang, H., Munk, S., Xia, L., Goldberg, H. J., & Whiteside, C. I. (2005). In high glucose protein kinase C-zeta activation is required for mesangial cell generation of reactive oxygen species. Kidney International, 68(6), 2526-2541.
    • (2005) Kidney International , vol.68 , pp. 2526-2541
    • Kwan, J.1    Wang, H.2    Munk, S.3    Xia, L.4    Goldberg, H.J.5    Whiteside, C.I.6
  • 142
    • 33644866156 scopus 로고    scopus 로고
    • Mesangial cell NADPH oxidase upregulation in high glucose is protein kinase C dependent and required for collagen IV expression
    • 2
    • Xia, L., Wang, H., Goldberg, H. J., Munk, S., Fantus, I. G., & Whiteside, C. I. (2006). Mesangial cell NADPH oxidase upregulation in high glucose is protein kinase C dependent and required for collagen IV expression. American Journal of Physiology, Renal Physiology, 290(2), F345-356.
    • (2006) American Journal of Physiology, Renal Physiology , vol.290 , pp. 345-356
    • Xia, L.1    Wang, H.2    Goldberg, H.J.3    Munk, S.4    Fantus, I.G.5    Whiteside, C.I.6
  • 144
    • 1642463525 scopus 로고    scopus 로고
    • Reactive oxygen species amplify protein kinase C signaling in high glucose-induced fibronectin expression by human peritoneal mesothelial cells
    • 4
    • Lee, H. B., Yu, M. R., Song, J. S., & Ha, H. (2004). Reactive oxygen species amplify protein kinase C signaling in high glucose-induced fibronectin expression by human peritoneal mesothelial cells. Kidney International, 65(4), 1170-1179.
    • (2004) Kidney International , vol.65 , pp. 1170-1179
    • Lee, H.B.1    Yu, M.R.2    Song, J.S.3    Ha, H.4
  • 145
    • 33750510904 scopus 로고    scopus 로고
    • Mitogenic signalling and the p16INK4a-Rb pathway cooperate to enforce irreversible cellular senescence
    • 11
    • Takahashi, A., Ohtani, N., Yamakoshi, K., Iida, S., Tahara, H., Nakayama, K., et al. (2006). Mitogenic signalling and the p16INK4a-Rb pathway cooperate to enforce irreversible cellular senescence. Nature Cell Biology, 8(11), 1291-1297.
    • (2006) Nature Cell Biology , vol.8 , pp. 1291-1297
    • Takahashi, A.1    Ohtani, N.2    Yamakoshi, K.3    Iida, S.4    Tahara, H.5    Nakayama, K.6
  • 146
    • 0027360635 scopus 로고    scopus 로고
    • Protein kinase C alpha, delta, epsilon and zeta in C6 glioma cells. TPA induces translocation and down-regulation of conventional and new PKC isoforms but not atypical PKC zeta
    • 1-2
    • Chen, C. C. (1999). Protein kinase C alpha, delta, epsilon and zeta in C6 glioma cells. TPA induces translocation and down-regulation of conventional and new PKC isoforms but not atypical PKC zeta. FEBS Letters, 332(1-2), 169-173.
    • (1999) FEBS Letters , vol.332 , pp. 169-173
    • Chen, C.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.