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Volumn 205, Issue 1, 2004, Pages 69-79

Investigation of intracellular signalling events mediating the mechanism of action of 7-hydroxycoumarin and 6-nitro-7-hdroxycoumarin in human renal cells

Author keywords

6 Nitro 7 hydroxycoumarin; In vitro; Mitogen activated protein kinase; Renal cell carcinoma

Indexed keywords

6 NITRO 7 HYDROXYCOUMARIN; COUMARIN DERIVATIVE; DNA TOPOISOMERASE; GLYCOPROTEIN P; MELPHALAN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; STRESS ACTIVATED PROTEIN KINASE; UMBELLIFERONE; UNCLASSIFIED DRUG; VINBLASTINE;

EID: 1242293659     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.canlet.2003.09.024     Document Type: Article
Times cited : (39)

References (61)
  • 2
    • 0025663358 scopus 로고
    • The pharmacology, metabolism, analysis and applications of coumarin and coumarin related compounds
    • Egan D.A., O'Kennedy R., Moran E., Thornes R.D. The pharmacology, metabolism, analysis and applications of coumarin and coumarin related compounds. Drug. Metab. Rev. 22:(5):1990;503-529.
    • (1990) Drug. Metab. Rev. , vol.22 , Issue.5 , pp. 503-529
    • Egan, D.A.1    O'Kennedy, R.2    Moran, E.3    Thornes, R.D.4
  • 3
    • 0030936401 scopus 로고    scopus 로고
    • Structure-cytotoxicity relationships of a series of natural and semi-synthetic simple coumarins as assessed in two human tumour cell lines
    • Kolodziej H., Kayser O., Woerdenbag H.J., Van Ulden W., Pras N. Structure-cytotoxicity relationships of a series of natural and semi-synthetic simple coumarins as assessed in two human tumour cell lines. Naturforshung. 52:1997;240-244.
    • (1997) Naturforshung , vol.52 , pp. 240-244
    • Kolodziej, H.1    Kayser, O.2    Woerdenbag, H.J.3    Van Ulden, W.4    Pras, N.5
  • 5
    • 0034771727 scopus 로고    scopus 로고
    • Study of the in vitro potential of natural and synthetic coumarin derivatives, using human normal and neoplastic skin cell lines
    • Finn G.J., Creaven B., Egan D. Study of the in vitro potential of natural and synthetic coumarin derivatives, using human normal and neoplastic skin cell lines. Melanoma Res. 11:2001;461-467.
    • (2001) Melanoma Res. , vol.11 , pp. 461-467
    • Finn, G.J.1    Creaven, B.2    Egan, D.3
  • 7
    • 0030176193 scopus 로고    scopus 로고
    • Pharmacological and biochemical actions of simple coumarins: Natural products with therapeutic potential
    • Hoult J.R.S., Paya M. Pharmacological and biochemical actions of simple coumarins: natural products with therapeutic potential. Gen. Pharmac. 27:(4):1996;713-722.
    • (1996) Gen. Pharmac. , vol.27 , Issue.4 , pp. 713-722
    • Hoult, J.R.S.1    Paya, M.2
  • 8
    • 0032749584 scopus 로고    scopus 로고
    • Umbelliferone analogues and their potential to inhibit benzo(a)pyrene and hydrogen peroxide induced mutations
    • Pillai S.P., Menon S.R., Mitscher L.A., Pillai C.A., Shankel D.A. Umbelliferone analogues and their potential to inhibit benzo(a)pyrene and hydrogen peroxide induced mutations. J. Nat. Prod. 62:1999;1358-1362.
    • (1999) J. Nat. Prod. , vol.62 , pp. 1358-1362
    • Pillai, S.P.1    Menon, S.R.2    Mitscher, L.A.3    Pillai, C.A.4    Shankel, D.A.5
  • 9
    • 0021798643 scopus 로고
    • Inhibition of the formation of 5-hydroxy-6, 8, 11, 14-eicosatetraenoic acid from arachidonic acid in polymorphonuclear leukocytes by various coumarins
    • Kimura Y., Okuda H., Arichi S., Baba K., Kozawa M. Inhibition of the formation of 5-hydroxy-6, 8, 11, 14-eicosatetraenoic acid from arachidonic acid in polymorphonuclear leukocytes by various coumarins. Biochim. Biophys. Acta. 834:1985;224-229.
    • (1985) Biochim. Biophys. Acta. , vol.834 , pp. 224-229
    • Kimura, Y.1    Okuda, H.2    Arichi, S.3    Baba, K.4    Kozawa, M.5
  • 10
    • 0032486081 scopus 로고    scopus 로고
    • Inhibitors of lipoxygenase metabolism exert synergistic effects with retinoic acid on differentiation of human leukaemia HL-60 cells
    • Hoffmanova J., Kozubik A., Dusek L., Pachernik J. Inhibitors of lipoxygenase metabolism exert synergistic effects with retinoic acid on differentiation of human leukaemia HL-60 cells. Eur. J. Pharmacol. 350:1998;273-284.
    • (1998) Eur. J. Pharmacol. , vol.350 , pp. 273-284
    • Hoffmanova, J.1    Kozubik, A.2    Dusek, L.3    Pachernik, J.4
  • 11
    • 0027186702 scopus 로고
    • Evaluation of the anti-tumour activity of coumarin in prostrate cancer models
    • Maucher A., Kager M., von Angerer E. Evaluation of the anti-tumour activity of coumarin in prostrate cancer models. J. Clin. Res. Clin. Oncol. 119:1993;150-154.
    • (1993) J. Clin. Res. Clin. Oncol. , vol.119 , pp. 150-154
    • Maucher, A.1    Kager, M.2    Von Angerer, E.3
  • 12
    • 0028149620 scopus 로고
    • Screening of potential chemo-preventive agents using biochemical markers of carcinogenesis
    • Sharma S., Stutzman D., Kellof J.G., Steele V.E. Screening of potential chemo-preventive agents using biochemical markers of carcinogenesis. Cancer Res. 54:1994;5848-5855.
    • (1994) Cancer Res. , vol.54 , pp. 5848-5855
    • Sharma, S.1    Stutzman, D.2    Kellof, J.G.3    Steele, V.E.4
  • 13
    • 0030763338 scopus 로고    scopus 로고
    • Studies on the cytostatic and cytotoxic effects and mode of action of 8-nitro-7-hydroxycoumarin
    • Egan D., James P., Cooke D., O'Kennedy R. Studies on the cytostatic and cytotoxic effects and mode of action of 8-nitro-7-hydroxycoumarin. Cancer Lett. 118:1997;201-211.
    • (1997) Cancer Lett. , vol.118 , pp. 201-211
    • Egan, D.1    James, P.2    Cooke, D.3    O'Kennedy, R.4
  • 14
    • 0032562434 scopus 로고    scopus 로고
    • Regulation of rat glutathione S-transferase A5 by cancer chemo-preventative agents: Mechanisms of inducible resistance to aflatoxin B1
    • Hayes J.D., Pulford D.J., Ellis E.M., McLeod R., James R.F.L., Seidegard J., et al. Regulation of rat glutathione S-transferase A5 by cancer chemo-preventative agents: mechanisms of inducible resistance to aflatoxin B1. Chemico-Biological Inter. 111-112:1998;51-67.
    • (1998) Chemico-Biological Inter. , vol.111-112 , pp. 51-67
    • Hayes, J.D.1    Pulford, D.J.2    Ellis, E.M.3    McLeod, R.4    James, R.F.L.5    Seidegard, J.6
  • 15
    • 0024493947 scopus 로고
    • Effects of coumarin (1,2-benzopyrone) and cimetidine on peripheral blood lymphocytes, natural killer cells and monocytes in patients with advanced malignancies
    • Marshall E.M., Riley L.K., Rhoades J., Eichnorm T., Jennings C.D., Cibule M., Thompson J. Effects of coumarin (1,2-benzopyrone) and cimetidine on peripheral blood lymphocytes, natural killer cells and monocytes in patients with advanced malignancies. J. Biol. Response Mod. 8:(1):1989;62-69.
    • (1989) J. Biol. Response Mod. , vol.8 , Issue.1 , pp. 62-69
    • Marshall, E.M.1    Riley, L.K.2    Rhoades, J.3    Eichnorm, T.4    Jennings, C.D.5    Cibule, M.6    Thompson, J.7
  • 16
    • 0023212047 scopus 로고
    • Treatment of metastatic renal cell carcinoma with coumarin (1,2-benzopyrone) and cimetadine: A pilot study
    • Marshall E.M., Mendleson L., Butler K., Riley L., Cantress J., Wiseman C., et al. Treatment of metastatic renal cell carcinoma with coumarin (1,2-benzopyrone) and cimetadine: a pilot study. J. Clin. Oncol. 5:(6):1987;862-866.
    • (1987) J. Clin. Oncol. , vol.5 , Issue.6 , pp. 862-866
    • Marshall, E.M.1    Mendleson, L.2    Butler, K.3    Riley, L.4    Cantress, J.5    Wiseman, C.6
  • 18
    • 0009508452 scopus 로고
    • Treatment of advanced renal cell carcinoma (RCC) with coumarin and cimetidine: Long-term follow-up of patients treated on a phase I trial
    • Marshall M.E., Ryles M., Butler K., Weiss L. Treatment of advanced renal cell carcinoma (RCC) with coumarin and cimetidine: long-term follow-up of patients treated on a phase I trial. J. Cancer Res. Clin. Oncol. 120:1994;535-538.
    • (1994) J. Cancer Res. Clin. Oncol. , vol.120 , pp. 535-538
    • Marshall, M.E.1    Ryles, M.2    Butler, K.3    Weiss, L.4
  • 20
    • 0002582409 scopus 로고
    • Effects of coumarin on human tumour cell growth and cell cycle analysis in vitro
    • Conley D., Marshall M.E. Effects of coumarin on human tumour cell growth and cell cycle analysis in vitro. Proc. Am. Assoc. Cancer Res. 28:1987;63.
    • (1987) Proc. Am. Assoc. Cancer Res. , vol.28 , pp. 63
    • Conley, D.1    Marshall, M.E.2
  • 22
    • 0037044111 scopus 로고    scopus 로고
    • In vitro cytotoxic potential and mechanism of action of selected coumarins, using human renal cell lines
    • Finn G.J., Kenealy E., Creaven B.S., Egan D.A. In vitro cytotoxic potential and mechanism of action of selected coumarins, using human renal cell lines. Cancer Lett. 183:2002;61-68.
    • (2002) Cancer Lett. , vol.183 , pp. 61-68
    • Finn, G.J.1    Kenealy, E.2    Creaven, B.S.3    Egan, D.A.4
  • 25
    • 0034634596 scopus 로고    scopus 로고
    • Ceramide directly activates protein kinase C to regulate a stress-activated protein kinase signalling complex
    • Bourbon N.A., Yun J., Kester M. Ceramide directly activates protein kinase C to regulate a stress-activated protein kinase signalling complex. J. Biol. Chem. 275:(45):2000;35617-35623.
    • (2000) J. Biol. Chem. , vol.275 , Issue.45 , pp. 35617-35623
    • Bourbon, N.A.1    Yun, J.2    Kester, M.3
  • 26
    • 0028846891 scopus 로고
    • Mitogen-activated protein kinase pathway and AP-1 are activated during cAMP-induced melanogenesis in B-16 melanoma cells
    • Englaro W., Rezzonic R., Durand-clement M., Lallemand D., Ortonne J.P., Bollotti R. Mitogen-activated protein kinase pathway and AP-1 are activated during cAMP-induced melanogenesis in B-16 melanoma cells. J. Biol. Chem. 270:(41):1995;24315-24320.
    • (1995) J. Biol. Chem. , vol.270 , Issue.41 , pp. 24315-24320
    • Englaro, W.1    Rezzonic, R.2    Durand-Clement, M.3    Lallemand, D.4    Ortonne, J.P.5    Bollotti, R.6
  • 27
    • 0034617367 scopus 로고    scopus 로고
    • The involvement of P38 mitogen-activated protein kinase in the alpha-melanocyte stimulating hormone induced melanogenic and anti-proliferative effects in B16 murine melanoma cells
    • Smalley K., Eisen T. The involvement of P38 mitogen-activated protein kinase in the alpha-melanocyte stimulating hormone induced melanogenic and anti-proliferative effects in B16 murine melanoma cells. Fed. Eur. Biochem. Soc. Lett. 476:2000;198-202.
    • (2000) Fed. Eur. Biochem. Soc. Lett. , vol.476 , pp. 198-202
    • Smalley, K.1    Eisen, T.2
  • 28
    • 0028920049 scopus 로고
    • Mitogenic and melanogenic stimulation of normal human melanocytes by melantrophic peptides
    • Malek Z., Swope V., Suzuki I., Akali C., Harriger M.D., Boyces S.T., et al. Mitogenic and melanogenic stimulation of normal human melanocytes by melantrophic peptides. Proc. Natl Acad. Sci. USA. 92:1995;1789-1793.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1789-1793
    • Malek, Z.1    Swope, V.2    Suzuki, I.3    Akali, C.4    Harriger, M.D.5    Boyces, S.T.6
  • 29
    • 0029775645 scopus 로고
    • Inhibition of the phosphatidylinositol 3-kinase/p70s6-kinase pathway induces B16 melanoma cell differentiation
    • Busca R., Berlotto J., Ballotti R. Inhibition of the phosphatidylinositol 3-kinase/p70s6-kinase pathway induces B16 melanoma cell differentiation. J. Biol. Chem. 271:(50):1976;31824-31830.
    • (1976) J. Biol. Chem. , vol.271 , Issue.50 , pp. 31824-31830
    • Busca, R.1    Berlotto, J.2    Ballotti, R.3
  • 30
    • 0032540355 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase pathway triggers B16 melanoma cell differentiation
    • Englaro W., Berlotto C., Busca R., Brunet A., Pages G., Ortonne J., Ballotti R. Inhibition of the mitogen-activated protein kinase pathway triggers B16 melanoma cell differentiation. J. Biol. Chem. 273:(16):1998;9966-9970.
    • (1998) J. Biol. Chem. , vol.273 , Issue.16 , pp. 9966-9970
    • Englaro, W.1    Berlotto, C.2    Busca, R.3    Brunet, A.4    Pages, G.5    Ortonne, J.6    Ballotti, R.7
  • 31
    • 0033548233 scopus 로고    scopus 로고
    • Stress activated protein kinase, p38 and a rapamycin sensitive pathway are required for C2C12 myogenesis
    • Cuenda A., Cohen P. Stress activated protein kinase, p38 and a rapamycin sensitive pathway are required for C2C12 myogenesis. J. Biol. Chem. 274:1999;4341-4346.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4341-4346
    • Cuenda, A.1    Cohen, P.2
  • 32
    • 0033544862 scopus 로고    scopus 로고
    • Constitutively active mitogen-activated protein kinase kinase 6 or salicylate induces 3T3 L1 adipogenesis
    • Engelman J.A. Constitutively active mitogen-activated protein kinase kinase 6 or salicylate induces 3T3 L1 adipogenesis. J. Biol. Chem. 274:1999;35630-35638.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35630-35638
    • Engelman, J.A.1
  • 33
    • 0033216770 scopus 로고    scopus 로고
    • Signalling pathways mediating melanogenesis
    • Park H.E., Gilchrest B.A. Signalling pathways mediating melanogenesis. Cell. Mol. Biol. 45:(7):1999;919-930.
    • (1999) Cell. Mol. Biol. , vol.45 , Issue.7 , pp. 919-930
    • Park, H.E.1    Gilchrest, B.A.2
  • 34
    • 0034213138 scopus 로고    scopus 로고
    • P38 MAP kinases: Beyond the stress responses
    • Nebreda A.R. p38 MAP kinases: beyond the stress responses. Trends Biochem. Sci. 25:2000;257-260.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 257-260
    • Nebreda, A.R.1
  • 35
    • 0035212589 scopus 로고    scopus 로고
    • The ups and downs of MEK kinase interactions
    • Hagemann C., Blank J. The ups and downs of MEK kinase interactions. Cell. Signal. 13:2001;863-875.
    • (2001) Cell. Signal. , vol.13 , pp. 863-875
    • Hagemann, C.1    Blank, J.2
  • 36
    • 0033605366 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase c-jun terminal kinase and p38 kinase in calphostin c induced apoptosis requires caspase-3 -like proteases but is dispensable for cell death
    • Ozaki I., Tani E., Ikemoto H., Kitagawa H., Fujikawa H. Activation of stress-activated protein kinase c-jun terminal kinase and p38 kinase in calphostin c induced apoptosis requires caspase-3 -like proteases but is dispensable for cell death. J. Biol. Chem. 7:(9):1999;5310-5317.
    • (1999) J. Biol. Chem. , vol.7 , Issue.9 , pp. 5310-5317
    • Ozaki, I.1    Tani, E.2    Ikemoto, H.3    Kitagawa, H.4    Fujikawa, H.5
  • 37
    • 0033708421 scopus 로고    scopus 로고
    • Modulation of mitogen-activated protein kinases and phosphorylation of Bcl-2 by vinblastine represent persistent forms of normal fluctuations at G2M
    • Fan M., Du L., Stone A.A., Gilbert K., Chambers T.C. Modulation of mitogen-activated protein kinases and phosphorylation of Bcl-2 by vinblastine represent persistent forms of normal fluctuations at G2M. Cancer Res. 60:2000;6403-6407.
    • (2000) Cancer Res. , vol.60 , pp. 6403-6407
    • Fan, M.1    Du, L.2    Stone, A.A.3    Gilbert, K.4    Chambers, T.C.5
  • 38
    • 0034671527 scopus 로고    scopus 로고
    • MEK inhibition enhances paclitaxel-induced tumor apoptosis
    • MacKeigan J.P., Collins T.S., Ting J.P.Y. MEK inhibition enhances paclitaxel-induced tumor apoptosis. J. Biol. Chem. 275:(50):2000;38953-38956.
    • (2000) J. Biol. Chem. , vol.275 , Issue.50 , pp. 38953-38956
    • MacKeigan, J.P.1    Collins, T.S.2    Ting, J.P.Y.3
  • 39
    • 0034907636 scopus 로고    scopus 로고
    • Pharmacologic interruption of the mitogen-activated extracellular- regulated kinase/mitogen-activated protein kinase signal pathway: Potential role in promoting cytotoxic drug action
    • Dent P., Grant S. Pharmacologic interruption of the mitogen-activated extracellular-regulated kinase/mitogen-activated protein kinase signal pathway: potential role in promoting cytotoxic drug action. Clin. Cancer Res. 7:2001;775-783.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 775-783
    • Dent, P.1    Grant, S.2
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0027360206 scopus 로고
    • Biochemical characterisation of elasamicin and other coumarin-related antitumor agents as potent inhibitors of human topoisomerase II
    • Lorico A., Long B.H. Biochemical characterisation of elasamicin and other coumarin-related antitumor agents as potent inhibitors of human topoisomerase II. Eur. J. Cancer. 29A:(14):1993;1985-1993.
    • (1993) Eur. J. Cancer , vol.29 , Issue.14 , pp. 1985-1993
    • Lorico, A.1    Long, B.H.2
  • 42
    • 0021878218 scopus 로고
    • Augmentation of adriamycin, melphalan, and cisplatin cytotoxicity in drug-resistant and -sensitive human ovarian carcinoma cell lines by buthionine sulfoximine mediated glutathione depletion
    • Hamilton C., Winker M., Louie K., Batist G., Behrens B., Tsuruo T., et al. Augmentation of adriamycin, melphalan, and cisplatin cytotoxicity in drug-resistant and -sensitive human ovarian carcinoma cell lines by buthionine sulfoximine mediated glutathione depletion. Biochem. Pharm. 34:1985;2583-2586.
    • (1985) Biochem. Pharm. , vol.34 , pp. 2583-2586
    • Hamilton, C.1    Winker, M.2    Louie, K.3    Batist, G.4    Behrens, B.5    Tsuruo, T.6
  • 43
    • 0037044111 scopus 로고    scopus 로고
    • In vitro cytotoxic potential and mechanism of action of selected coumarins, using human renal cell lines
    • Finn G., Creaven B., Egan D. In vitro cytotoxic potential and mechanism of action of selected coumarins, using human renal cell lines. Cancer Lett. 183:2002;61-68.
    • (2002) Cancer Lett. , vol.183 , pp. 61-68
    • Finn, G.1    Creaven, B.2    Egan, D.3
  • 44
    • 0023130372 scopus 로고
    • Evaluation of a tetrazolium-based colorimetric assay: Assessment of chemosensitivity testing
    • Carmichael J., DeGraff G., Gazdar A., Minna J., Mitchell J. Evaluation of a tetrazolium-based colorimetric assay: assessment of chemosensitivity testing. Cancer Res. 47:1987;936-942.
    • (1987) Cancer Res. , vol.47 , pp. 936-942
    • Carmichael, J.1    Degraff, G.2    Gazdar, A.3    Minna, J.4    Mitchell, J.5
  • 45
    • 0026202059 scopus 로고
    • Strategies for the purification of P-glycoprotein from multi-drug resistant Chinese ovary cells
    • Doige C.A., Sharom F.J. Strategies for the purification of P-glycoprotein from multi-drug resistant Chinese ovary cells. Protein Exp. Purific. 2:1991;256-265.
    • (1991) Protein Exp. Purific. , vol.2 , pp. 256-265
    • Doige, C.A.1    Sharom, F.J.2
  • 46
    • 0031900740 scopus 로고    scopus 로고
    • Signal transduction through MAP kinase cascades
    • Lewis T.S., Shapiro P., Ahn N.G. Signal transduction through MAP kinase cascades. Adv. Cancer Res. 74:1998;49-139.
    • (1998) Adv. Cancer Res. , vol.74 , pp. 49-139
    • Lewis, T.S.1    Shapiro, P.2    Ahn, N.G.3
  • 47
    • 0035866406 scopus 로고    scopus 로고
    • Inhibition of extracellular signal-regulated kinase (ERK) mediates cell cycle phase independent apoptosis in vinblastine-treated Ml-1 cells
    • Stadheim T.A., Xiao H., Eastmann A. Inhibition of extracellular signal-regulated kinase (ERK) mediates cell cycle phase independent apoptosis in vinblastine-treated Ml-1 cells. Cancer Res. 61:2001;1533-1540.
    • (2001) Cancer Res. , vol.61 , pp. 1533-1540
    • Stadheim, T.A.1    Xiao, H.2    Eastmann, A.3
  • 49
    • 0029080247 scopus 로고
    • Constitutive activation of mitogen-activated protein (MAP) kinases in human renal cell carcinoma
    • Oka H., Chatani Y., Hoshino R., Ogawa O., Kakehi Y., Terachi T., et al. Constitutive activation of mitogen-activated protein (MAP) kinases in human renal cell carcinoma. Cancer Res. 55:1995;4182-4187.
    • (1995) Cancer Res. , vol.55 , pp. 4182-4187
    • Oka, H.1    Chatani, Y.2    Hoshino, R.3    Ogawa, O.4    Kakehi, Y.5    Terachi, T.6
  • 50
    • 0033605366 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase c-jun terminal kinase and p38 kinase in calphostin c induced apoptosis requires caspase-3 -like proteases but is dispensable for cell death
    • Ozaki I., Tani E., Ikemoto H., Kitagawa H., Fujikawa H. Activation of stress-activated protein kinase c-jun terminal kinase and p38 kinase in calphostin c induced apoptosis requires caspase-3 -like proteases but is dispensable for cell death. J. Biol. Chem. 7:(9):1999;5310-5317.
    • (1999) J. Biol. Chem. , vol.7 , Issue.9 , pp. 5310-5317
    • Ozaki, I.1    Tani, E.2    Ikemoto, H.3    Kitagawa, H.4    Fujikawa, H.5
  • 51
    • 85030892149 scopus 로고    scopus 로고
    • Daphnetin induced differentiation of human renal carcinoma cells and its mediation by p38 mitogen-activated protein kinase
    • (in press)
    • Finn G.J., Creaven B.S., Egan D.A. Daphnetin induced differentiation of human renal carcinoma cells and its mediation by p38 mitogen-activated protein kinase. Biochem. Pharm. 2003;. (in press).
    • (2003) Biochem. Pharm.
    • Finn, G.J.1    Creaven, B.S.2    Egan, D.A.3
  • 53
    • 0025245508 scopus 로고
    • Evidence for a common mechanism of action of antitumour and antibacterial agents that inhibit type II topoisomerases
    • Huff A., Kreuzer K.N. Evidence for a common mechanism of action of antitumour and antibacterial agents that inhibit type II topoisomerases. J. Biol. Chem. 265:1990;20496-20505.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20496-20505
    • Huff, A.1    Kreuzer, K.N.2
  • 55
    • 0032504157 scopus 로고    scopus 로고
    • Merbarone inhibits the catalytic activity of human topoisomerase II by blocking DNA cleavage
    • Fortune J.M., Osheroff N. Merbarone inhibits the catalytic activity of human topoisomerase II by blocking DNA cleavage. J. Biol. Chem. 273:(28):1998;17643-17650.
    • (1998) J. Biol. Chem. , vol.273 , Issue.28 , pp. 17643-17650
    • Fortune, J.M.1    Osheroff, N.2
  • 57
    • 0034923502 scopus 로고    scopus 로고
    • DNA topoisomerases: Structure, function and mechanism
    • Champoux J.J. DNA topoisomerases: structure, function and mechanism. Annu. Rev. Biochem. 70:2001;369-413.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 369-413
    • Champoux, J.J.1
  • 58
    • 18644369699 scopus 로고    scopus 로고
    • Caspase activation in etoposide-treated fibroblasts is correlated to ERK phosphorylation and both events are blocked by polyamine depletion
    • Stefanelli C., Tantini B., Fattori M., Stanic I., Pignatti C., Clo G., et al. Caspase activation in etoposide-treated fibroblasts is correlated to ERK phosphorylation and both events are blocked by polyamine depletion. Fed. Eur. Biochem. Soc. Lett. 527:2002;223-228.
    • (2002) Fed. Eur. Biochem. Soc. Lett. , vol.527 , pp. 223-228
    • Stefanelli, C.1    Tantini, B.2    Fattori, M.3    Stanic, I.4    Pignatti, C.5    Clo, G.6
  • 61
    • 0344827168 scopus 로고    scopus 로고
    • Modulation of mitogen-activated protein kinases by 6-nitro-7- hydroxycoumarin, mediates apoptosis in renal carcinoma cells
    • (in press)
    • Finn G.J., Creaven B.S., Egan D.A. Modulation of mitogen-activated protein kinases by 6-nitro-7-hydroxycoumarin, mediates apoptosis in renal carcinoma cells. Eur. J. Pharm. 2003;. (in press).
    • (2003) Eur. J. Pharm.
    • Finn, G.J.1    Creaven, B.S.2    Egan, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.