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Volumn 11, Issue 2, 1997, Pages 118-124

An essential role for free radicals and derived species in signal transduction

Author keywords

intracellular messenger; PDGF; reactive nitrogen species; reactive oxygen species; specificity regulation

Indexed keywords

CYTOKINE; FREE RADICAL; GLUTATHIONE; GROWTH FACTOR; LIGAND; NITROGEN DERIVATIVE; REACTIVE OXYGEN METABOLITE; SCAVENGER; TRANSCRIPTION FACTOR;

EID: 0031036917     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.2.9039953     Document Type: Review
Times cited : (829)

References (90)
  • 1
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan, C. (1992) Nitric oxide as a secretory product of mammalian cells. FASEB J. 6, 3051-3064
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 2
    • 0025977048 scopus 로고
    • Signal transduction mechanisms involving nitric oxide
    • Ignarro, L. J. (1991) Signal transduction mechanisms involving nitric oxide. Biochem. Pharm. 41, 485-490
    • (1991) Biochem. Pharm. , vol.41 , pp. 485-490
    • Ignarro, L.J.1
  • 5
    • 0029862899 scopus 로고    scopus 로고
    • Nitric oxide amplifies interleukin-1-induced cyclooxygenase-2 expression in rat mesangial cells
    • Tetsuka, T., Daphona-Iken, D., Miller, B. W., Guang, Z., Baier, L. D., and Morrison, A. R. (1996) Nitric oxide amplifies interleukin-1-induced cyclooxygenase-2 expression in rat mesangial cells. J. Clin. Invest. 97, 2051-2056
    • (1996) J. Clin. Invest. , vol.97 , pp. 2051-2056
    • Tetsuka, T.1    Daphona-Iken, D.2    Miller, B.W.3    Guang, Z.4    Baier, L.D.5    Morrison, A.R.6
  • 6
    • 0028942661 scopus 로고
    • Involvement of reactive oxygen intermediates in cyclooxygenase-2 expression induced by interleukin-1, tumor necrosis factor-α, and lipopolysaccharide
    • Feng, L., Xia, Y., Garcia, G. E., Hwang, D., and Wilson, C. B. (1995) Involvement of reactive oxygen intermediates in cyclooxygenase-2 expression induced by interleukin-1, tumor necrosis factor-α, and lipopolysaccharide. J. Clin. Invest. 95, 1669-1675
    • (1995) J. Clin. Invest. , vol.95 , pp. 1669-1675
    • Feng, L.1    Xia, Y.2    Garcia, G.E.3    Hwang, D.4    Wilson, C.B.5
  • 7
    • 0030044265 scopus 로고    scopus 로고
    • A redox-based mechanism for induction of interleukin-1 production by nitric oxide in a human colonic epithelial cell line (HT29-CL.16E)
    • Vallette, G., Jarry, A., Branka, J.-E., and Laboisse, C. L. (1996) A redox-based mechanism for induction of interleukin-1 production by nitric oxide in a human colonic epithelial cell line (HT29-CL.16E). Biochem. J. 313, 35-38
    • (1996) Biochem. J. , vol.313 , pp. 35-38
    • Vallette, G.1    Jarry, A.2    Branka, J.-E.3    Laboisse, C.L.4
  • 8
    • 0029977979 scopus 로고    scopus 로고
    • Regulation of macrophage inflammatory protein-1 mRNA by oxidative stress
    • Shi, M. M., Godleski, J. J., and Paulauskis, J. D. (1996) Regulation of macrophage inflammatory protein-1 mRNA by oxidative stress. J. Biol. Chem. 271, 5878-5883
    • (1996) J. Biol. Chem. , vol.271 , pp. 5878-5883
    • Shi, M.M.1    Godleski, J.J.2    Paulauskis, J.D.3
  • 9
    • 0029921173 scopus 로고    scopus 로고
    • Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants
    • Buck, M., and Chojkier, M. (1996) Muscle wasting and dedifferentiation induced by oxidative stress in a murine model of cachexia is prevented by inhibitors of nitric oxide synthesis and antioxidants. EMBO J. 15, 1753-1765
    • (1996) EMBO J. , vol.15 , pp. 1753-1765
    • Buck, M.1    Chojkier, M.2
  • 10
    • 0029997906 scopus 로고    scopus 로고
    • Nitric oxide attenuates vascular smooth muscle cell activation by IFN-γ
    • Shin, W. S., Hong, Y.-H., Peng, B.-H., DeCaterina, R., Libby, P., and Liao, J. K. (1996) Nitric oxide attenuates vascular smooth muscle cell activation by IFN-γ. J. Biol. Chem. 271, 11317-11324
    • (1996) J. Biol. Chem. , vol.271 , pp. 11317-11324
    • Shin, W.S.1    Hong, Y.-H.2    Peng, B.-H.3    DeCaterina, R.4    Libby, P.5    Liao, J.K.6
  • 11
    • 0029610424 scopus 로고
    • Intracellular reactive oxygen species as apparent modulators of heat shock protein 27 structural organization and phosphorylation in basal and tumor necrosis factor α-treated T47D human carcinoma cells
    • Mehlen, P., Kretz-Remy, C., Biolay, J., fastan, P., Mirault, M.-E., and Arrigo, A.-P. (1995) Intracellular reactive oxygen species as apparent modulators of heat shock protein 27 structural organization and phosphorylation in basal and tumor necrosis factor α-treated T47D human carcinoma cells. Biochem. J. 312, 367-375
    • (1995) Biochem. J. , vol.312 , pp. 367-375
    • Mehlen, P.1    Kretz-Remy, C.2    Biolay, J.3    Fastan, P.4    Mirault, M.-E.5    Arrigo, A.-P.6
  • 12
    • 0029898072 scopus 로고    scopus 로고
    • 2α by human monocytes. Discriminate production by reactive oxygen species and prostaglandin endoperoxide synthase-2
    • 2α by human monocytes. Discriminate production by reactive oxygen species and prostaglandin endoperoxide synthase-2. J. Biol. Chem. 271, 8919-8924
    • (1996) J. Biol. Chem. , vol.271 , pp. 8919-8924
    • Pratico, D.1    Fitzgerald, G.A.2
  • 13
    • 0028806450 scopus 로고
    • Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway
    • Chen, Q., Olashaw, N., and Wu, J. (1995) Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway. J. Biol. Chem. 270, 28499-28502
    • (1995) J. Biol. Chem. , vol.270 , pp. 28499-28502
    • Chen, Q.1    Olashaw, N.2    Wu, J.3
  • 14
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the cJun activation domain
    • Derijard, B., Hibi, M., Wu, I. H., Barrett, T., Su, B., Deng, T., Karin, M., and Davis, R. J. (1994) JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the cJun activation domain. Cell 76, 1025-1037
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 16
    • 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, 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
  • 17
    • 0028006744 scopus 로고
    • Activation of the mitogen activated protein kinase signaling pathway in neutrophils. Role of oxidants
    • Fialkow, L., Chan, C. K., Rotin, D., Grinstein, S., and Downey, G. P. (1994) Activation of the mitogen activated protein kinase signaling pathway in neutrophils. Role of oxidants. J. Biol. Chem. 269, 31234-31242
    • (1994) J. Biol. Chem. , vol.269 , pp. 31234-31242
    • Fialkow, L.1    Chan, C.K.2    Rotin, D.3    Grinstein, S.4    Downey, G.P.5
  • 18
    • 0029807306 scopus 로고    scopus 로고
    • Differential activation of MAP kinases by nitric oxide-related species
    • Lander, H. M., Jacovina, A. T., Davis, R. J., and Tauras, J. M. (1996) Differential activation of MAP kinases by nitric oxide-related species. J. Biol. Chem. 271, 19705-19709
    • (1996) J. Biol. Chem. , vol.271 , pp. 19705-19709
    • Lander, H.M.1    Jacovina, A.T.2    Davis, R.J.3    Tauras, J.M.4
  • 19
    • 0028854165 scopus 로고
    • Nitric oxide stimulates tyrosine phophorylation in murine fibroblasts in the absence and presence of epidermal-derived growth factor
    • Peranovich, T. M. S., Dasilva, A. M., Fries, D. M., Stern, A., and Monteiro, H. P. (1995) Nitric oxide stimulates tyrosine phophorylation in murine fibroblasts in the absence and presence of epidermal-derived growth factor. Biochem. J. 305, 613-619
    • (1995) Biochem. J. , vol.305 , pp. 613-619
    • Peranovich, T.M.S.1    Dasilva, A.M.2    Fries, D.M.3    Stern, A.4    Monteiro, H.P.5
  • 20
    • 0025825989 scopus 로고
    • Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum
    • Bauskin, A. R., Alkalay, I., and Ben-Neriah, Y. (1991) Redox regulation of a protein tyrosine kinase in the endoplasmic reticulum. Cell 66, 685-696
    • (1991) Cell , vol.66 , pp. 685-696
    • Bauskin, A.R.1    Alkalay, I.2    Ben-Neriah, Y.3
  • 22
    • 0026488222 scopus 로고
    • Nitric oxide mediates norepinephrine-induced prostaglandin E2 release from the hypothalamus
    • Rettori, V., Gimeno, M., Lyson, K., and McCann, S. M. (1992) Nitric oxide mediates norepinephrine-induced prostaglandin E2 release from the hypothalamus. Proc. Natl Acad. Sci. USA 89, 11543-11546
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11543-11546
    • Rettori, V.1    Gimeno, M.2    Lyson, K.3    McCann, S.M.4
  • 23
    • 0026059929 scopus 로고
    • Oxygen radicals induce human endothelial cells to express GMP-140 and bind neutrophils
    • Patel, K. D., Zimmerman, G. A., Prescott, S. M., McEver, R. P., and McIntyre, T. M. (1991) Oxygen radicals induce human endothelial cells to express GMP-140 and bind neutrophils. J. Cell Biol. 112, 749-759
    • (1991) J. Cell Biol. , vol.112 , pp. 749-759
    • Patel, K.D.1    Zimmerman, G.A.2    Prescott, S.M.3    McEver, R.P.4    McIntyre, T.M.5
  • 24
    • 0027301258 scopus 로고
    • Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor α and IgG
    • Satriano, J. A., Shuldiner, M., Hora, K., Xing, Y., Shan, Z., and Schlondorff, D. (1993) Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor α and IgG. J. Clin. Invest. 92, 1564-1571
    • (1993) J. Clin. Invest. , vol.92 , pp. 1564-1571
    • Satriano, J.A.1    Shuldiner, M.2    Hora, K.3    Xing, Y.4    Shan, Z.5    Schlondorff, D.6
  • 25
    • 0024461627 scopus 로고
    • Translocation and enhancement of phosphotransferase activity of protein kinase C following exposure in mouse epidermal cells to oxidants
    • Larsson, R., and Cerutti, P. (1989) Translocation and enhancement of phosphotransferase activity of protein kinase C following exposure in mouse epidermal cells to oxidants. Cancer Res. 49, 5627-5632
    • (1989) Cancer Res. , vol.49 , pp. 5627-5632
    • Larsson, R.1    Cerutti, P.2
  • 26
    • 0028129243 scopus 로고
    • Oxygen-derived radicals stimulate renin release of isolated juxtaglomerular cells
    • Galle, J., Herzog, C., Schollmeyer, P., and Wanner, C. (1994) Oxygen-derived radicals stimulate renin release of isolated juxtaglomerular cells. FEBS Lett. 351, 314-316
    • (1994) FEBS Lett. , vol.351 , pp. 314-316
    • Galle, J.1    Herzog, C.2    Schollmeyer, P.3    Wanner, C.4
  • 27
    • 0026555238 scopus 로고
    • Decreased renin release and constant kallikrein secretion after injection of L-NAME in isolated perfused rat kidney
    • Gardes, J., Poux, J. M., Gonzalez, M. F., Alhenc-Gelas, F., and Menard, J. (1992) Decreased renin release and constant kallikrein secretion after injection of L-NAME in isolated perfused rat kidney. Life Sci. 50, 987-993
    • (1992) Life Sci. , vol.50 , pp. 987-993
    • Gardes, J.1    Poux, J.M.2    Gonzalez, M.F.3    Alhenc-Gelas, F.4    Menard, J.5
  • 28
    • 0028015832 scopus 로고
    • Production of hydrogen peroxide by transforming growth factor-beta 1 and its involvement in induction of egr-1 in mouse osteoblastic cells
    • Ohba, M., Shibanuma, M., Kuroki, T., and Nose, K. (1994) Production of hydrogen peroxide by transforming growth factor-beta 1 and its involvement in induction of egr-1 in mouse osteoblastic cells. J. Cell Biol. 126, 1079-1088
    • (1994) J. Cell Biol. , vol.126 , pp. 1079-1088
    • Ohba, M.1    Shibanuma, M.2    Kuroki, T.3    Nose, K.4
  • 29
    • 0030030918 scopus 로고    scopus 로고
    • Thioredoxin as a potent costimulus of cytokine expression
    • Schenk, H., Vogt, M., Dröge, W., and Schulze-Osthoff, K. (1996) Thioredoxin as a potent costimulus of cytokine expression. J. Immunol. 156, 765-771
    • (1996) J. Immunol. , vol.156 , pp. 765-771
    • Schenk, H.1    Vogt, M.2    Dröge, W.3    Schulze-Osthoff, K.4
  • 32
    • 0022978272 scopus 로고
    • Effect of antioxidants on primary alloantigen-induced T cell activation and proliferation
    • Chaudhri, G., Clark, I. A., Hunt, N. H., Cowden, W. B., and Ceredig, R. (1986) Effect of antioxidants on primary alloantigen-induced T cell activation and proliferation. J. Immunol. 137, 2646-2652
    • (1986) J. Immunol. , vol.137 , pp. 2646-2652
    • Chaudhri, G.1    Clark, I.A.2    Hunt, N.H.3    Cowden, W.B.4    Ceredig, R.5
  • 34
    • 0029020218 scopus 로고
    • Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes
    • Lo, Y. Y., and Cruz, T. F. (1995) Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J. Biol. Chem. 270, 11727-11730
    • (1995) J. Biol. Chem. , vol.270 , pp. 11727-11730
    • Lo, Y.Y.1    Cruz, T.F.2
  • 35
    • 0028172409 scopus 로고
    • Adenosine A3 receptors regulate serotonin transport via nitric oxide and cGMP
    • Miller, K. J., and Hoffman, B. J. (1994) Adenosine A3 receptors regulate serotonin transport via nitric oxide and cGMP. J. Biol. Chem. 269, 27351-27356
    • (1994) J. Biol. Chem. , vol.269 , pp. 27351-27356
    • Miller, K.J.1    Hoffman, B.J.2
  • 36
    • 0028168591 scopus 로고
    • Mechanisms of prostaglandin E2 release and increase in PGH2/PGE2 isomerase activity by PDGF: Involvement of nitric oxide
    • Kelner, M. J., and Uglik, S. F. (1994) Mechanisms of prostaglandin E2 release and increase in PGH2/PGE2 isomerase activity by PDGF: involvement of nitric oxide. Arch. Biochem. Biophys. 312, 240-243
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 240-243
    • Kelner, M.J.1    Uglik, S.F.2
  • 37
  • 38
    • 0027403306 scopus 로고
    • A one hour pulse with IL-1 beta induces formation of nitric oxide and inhibits insulin secretion by rat islets of Langerhans: Evidence fora a tyrosine kinase signaling mechanism
    • Corbett, J. A., Sweetland, M. A., Lancaster, J. R., Jr., and McDaniel, M. I., (1993) A one hour pulse with IL-1 beta induces formation of nitric oxide and inhibits insulin secretion by rat islets of Langerhans: evidence fora a tyrosine kinase signaling mechanism. FASEB J. 7, 369-374
    • (1993) FASEB J. , vol.7 , pp. 369-374
    • Corbett, J.A.1    Sweetland, M.A.2    Lancaster Jr., J.R.3    McDaniel, M.I.4
  • 39
    • 0028032263 scopus 로고
    • Thiol reducing reagents inhibit the heat shock response. Involvement of a redox mechanism in the heat shock signal transduction pathway
    • Huang, L. E., Zhang, H., Bae, S. W., and Liu, A. Y. (1994) Thiol reducing reagents inhibit the heat shock response. Involvement of a redox mechanism in the heat shock signal transduction pathway. J. Biol. Chem. 269, 30718-30725
    • (1994) J. Biol. Chem. , vol.269 , pp. 30718-30725
    • Huang, L.E.1    Zhang, H.2    Bae, S.W.3    Liu, A.Y.4
  • 40
    • 0027510941 scopus 로고
    • Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/interleukin-1 signal transduction
    • Guy, G. R., Cairns, J., Ng, S. B., and Tan, Y. H. (1993) Inactivation of a redox-sensitive protein phosphatase during the early events of tumor necrosis factor/interleukin-1 signal transduction. J. Biol. Chem. 268, 2141-2148
    • (1993) J. Biol. Chem. , vol.268 , pp. 2141-2148
    • Guy, G.R.1    Cairns, J.2    Ng, S.B.3    Tan, Y.H.4
  • 41
    • 0029394936 scopus 로고
    • Hydrogen peroxide and the proliferation of BHK-21 cells
    • Burdon, R. H., Alliangana, D., and Gill, V. (1995) Hydrogen peroxide and the proliferation of BHK-21 cells, Free Rad. Res. 23, 471-486
    • (1995) Free Rad. Res. , vol.23 , pp. 471-486
    • Burdon, R.H.1    Alliangana, D.2    Gill, V.3
  • 42
    • 0027485027 scopus 로고
    • Role of nitric oxide in the control of leutinizing hormone-releasing hormone release in vivo and in vitro
    • Rettori, V., Belova, N., Dees, W. L., Nyberg, L. L., Gimeno, M., and McCann, S. M. (1993) Role of nitric oxide in the control of leutinizing hormone-releasing hormone release in vivo and in vitro. Proc. Natl. Acad. Sci. USA 90, 10130-10134
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10130-10134
    • Rettori, V.1    Belova, N.2    Dees, W.L.3    Nyberg, L.L.4    Gimeno, M.5    McCann, S.M.6
  • 43
    • 0028220671 scopus 로고
    • Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle cells
    • Bolotina, V. M., Najibi, S., Placino, J. J., Pagano, P. J., and Cohen, R. A. (1994) Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle cells. Nature (London) 368, 850-853
    • (1994) Nature (London) , vol.368 , pp. 850-853
    • Bolotina, V.M.1    Najibi, S.2    Placino, J.J.3    Pagano, P.J.4    Cohen, R.A.5
  • 44
    • 0027524161 scopus 로고
    • +-channel activation in response to low doses of γ-irradiation involves reactive oxygen intermediates in nonexcitatory cells
    • +-channel activation in response to low doses of γ-irradiation involves reactive oxygen intermediates in nonexcitatory cells. Proc. Natl. Acad. Sci. USA 90, 908-912
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 908-912
    • Kuo, S.S.1    Saad, A.H.2    Koong, A.L.3    Hahn, G.M.4    Giaccia, A.J.5
  • 45
    • 0029010464 scopus 로고
    • Activation of CFTR chloride current by nitric oxide in human T lymphocytes
    • Dong, Y. J., Chao, A. C., Kouyama, K., Hsu, Y. P., Bocian, R. C., Moss, R. B., and Gardner, P. (1995) Activation of CFTR chloride current by nitric oxide in human T lymphocytes. EMBO J. 14, 2700-2707
    • (1995) EMBO J. , vol.14 , pp. 2700-2707
    • Dong, Y.J.1    Chao, A.C.2    Kouyama, K.3    Hsu, Y.P.4    Bocian, R.C.5    Moss, R.B.6    Gardner, P.7
  • 46
    • 0028027127 scopus 로고
    • A GTP-binding protein inhibits a gastric housekeeping chloride channel via intracellular production of superoxide
    • Sakai, H., and Takeguchi, N. (1994) A GTP-binding protein inhibits a gastric housekeeping chloride channel via intracellular production of superoxide. J. Biol. Chem. 269, 23426-23430
    • (1994) J. Biol. Chem. , vol.269 , pp. 23426-23430
    • Sakai, H.1    Takeguchi, N.2
  • 47
    • 0028896285 scopus 로고
    • Nitric oxide donor SIN-1 inhibits mammalian cardiac calcium current through cGMP-dependent protein kinase
    • Wahler, G. M., and Dollinger, S. J. (1995) Nitric oxide donor SIN-1 inhibits mammalian cardiac calcium current through cGMP-dependent protein kinase. Am J. Physiol. 268, C45-C54
    • (1995) Am J. Physiol. , vol.268
    • Wahler, G.M.1    Dollinger, S.J.2
  • 48
    • 0028567151 scopus 로고
    • Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls
    • Liu, G., and Pessah, I. N. (1994) Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls. J. Biol. Chem. 269, 33028-33034
    • (1994) J. Biol. Chem. , vol.269 , pp. 33028-33034
    • Liu, G.1    Pessah, I.N.2
  • 50
    • 0027301897 scopus 로고
    • Biosynthesis of nitric oxide activates iron regulatory factor in macrophages
    • Drapier, J. C., Hirling, H., Wietzerbin, J., Kaldy, P., and Kuhn, L. L. (1993) Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J. 12, 3643-3649
    • (1993) EMBO J. , vol.12 , pp. 3643-3649
    • Drapier, J.C.1    Hirling, H.2    Wietzerbin, J.3    Kaldy, P.4    Kuhn, L.L.5
  • 51
    • 0025077481 scopus 로고
    • Redox regulation of fus and jun DNA-binding activity in vitro
    • Abate, C., Patel, L., Rauscher, F. J., and Curran, T. (1990) Redox regulation of fus and jun DNA-binding activity in vitro. Science 249, 1157-1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.3    Curran, T.4
  • 52
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in presence of iron
    • Fenton, H. J. H. (1894) Oxidation of tartaric acid in presence of iron. J. Chem. Soc. 65, 899-910
    • (1894) J. Chem. Soc. , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 53
    • 0027190721 scopus 로고
    • Activation of human peripheral blood mononuclear cells by nitric oxide generating compounds
    • Lander, H. M., Sehajpal, P., Levine, D.M., and Novogrodsky, A. (1993) Activation of human peripheral blood mononuclear cells by nitric oxide generating compounds. J. Immunol. 150, 1509-1516
    • (1993) J. Immunol. , vol.150 , pp. 1509-1516
    • Lander, H.M.1    Sehajpal, P.2    Levine, D.M.3    Novogrodsky, A.4
  • 54
    • 0029123437 scopus 로고
    • Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1
    • Wang, G. L., Jiang, B. H., and Semenza, G. L. (1995) Effect of altered redox states on expression and DNA-binding activity of hypoxia-inducible factor 1. Biochem. Biophys. Res. Commun. 212, 550-556
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 550-556
    • Wang, G.L.1    Jiang, B.H.2    Semenza, G.L.3
  • 55
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • Storz, G., Tartaglia, L. A., and Ames, B. N. (1990) Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248, 189-194
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 56
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • Hausladen, A., Privalle, C. T., keng, T., DeAngelo, J., and Stamler, J. S. (1996) Nitrosative stress: activation of the transcription factor OxyR. Cell 86, 719-729
    • (1996) Cell , vol.86 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    Deangelo, J.4    Stamler, J.S.5
  • 57
    • 0030052038 scopus 로고    scopus 로고
    • Isolation of an oxidant-sensitive FNR protein of e coli: Interaction at activator and repressor sites of FNR-controlled genes
    • Melville, S. B., and Gunsalus, R. P. (1996) Isolation of an oxidant-sensitive FNR protein of E coli: interaction at activator and repressor sites of FNR-controlled genes. Proc. Natl. Acad. Sci. USA 93, 1226-1231
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1226-1231
    • Melville, S.B.1    Gunsalus, R.P.2
  • 58
    • 0027208296 scopus 로고
    • Amplification of calcium-induced gene transcription by nitric oxide in neuronal cells
    • Peunova, N., and Enikolopov, G. (1993) Amplification of calcium-induced gene transcription by nitric oxide in neuronal cells. Nature (London) 364, 450-453
    • (1993) Nature (London) , vol.364 , pp. 450-453
    • Peunova, N.1    Enikolopov, G.2
  • 59
    • 0028998576 scopus 로고
    • The DNA binding activity and the dimerization ability of the thyroid transcription factor I are redox regulated
    • Arnone, M. I., Zannini, M., and DiLauro, R. (1995) The DNA binding activity and the dimerization ability of the thyroid transcription factor I are redox regulated. J. Biol. Chem. 270, 12048-12055
    • (1995) J. Biol. Chem. , vol.270 , pp. 12048-12055
    • Arnone, M.I.1    Zannini, M.2    DiLauro, R.3
  • 60
    • 0028139041 scopus 로고
    • Identification of a conserved oxidation-sensitive cysteine residue in the NF1 family of DNA-binding proteins
    • Bandyopadhyay, S., and Gromostajski, R. M. (1994) Identification of a conserved oxidation-sensitive cysteine residue in the NF1 family of DNA-binding proteins. J. Biol. Chem. 269, 29949-29955
    • (1994) J. Biol. Chem. , vol.269 , pp. 29949-29955
    • Bandyopadhyay, S.1    Gromostajski, R.M.2
  • 61
    • 0026473086 scopus 로고
    • The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-senstitive manner
    • Pognonec, P., Kato, H., and Roeder, R. G. (1992) The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-senstitive manner. J. Biol. Chem. 267, 24563-24567
    • (1992) J. Biol. Chem. , vol.267 , pp. 24563-24567
    • Pognonec, P.1    Kato, H.2    Roeder, R.G.3
  • 62
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • Hainaut, P., and Milner, J. (1993) Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res. 53, 4469-4473
    • (1993) Cancer Res. , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 63
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative stress response that defends e coli against activated macrophages
    • Nunoshiba, T., deRojas-Walker, T., Wishnok, J. S., Tannenbaum, S. R., and Demple, B. (1993) Activation by nitric oxide of an oxidative stress response that defends E coli against activated macrophages. Proc. Natl. Acad. Sci. USA 90, 9993-9997
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    Derojas-Walker, T.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 64
    • 0028844540 scopus 로고
    • Stimulation of immediate early gene expression in striatal neurons by nitric oxide
    • Morris, B. J. (1995) Stimulation of immediate early gene expression in striatal neurons by nitric oxide. J. Biol. Chem. 270, 24740-24744
    • (1995) J. Biol. Chem. , vol.270 , pp. 24740-24744
    • Morris, B.J.1
  • 65
    • 0029057806 scopus 로고
    • Nitric oxide-dependent parasympathetic signaling is due to activation of constitutive endothelial (Type III) nitric oxide synthase in cardiac myocytes
    • Balligand, J. L., Kobzik, L., Han, X., Kaye, D. M., Beihasen, L., O'Hara, D. S., Kelly, R. A., Smith, T. W., and Michel, T. (1995) Nitric oxide-dependent parasympathetic signaling is due to activation of constitutive endothelial (Type III) nitric oxide synthase in cardiac myocytes. J. Biol. Chem. 270, 14582-14586
    • (1995) J. Biol. Chem. , vol.270 , pp. 14582-14586
    • Balligand, J.L.1    Kobzik, L.2    Han, X.3    Kaye, D.M.4    Beihasen, L.5    O'Hara, D.S.6    Kelly, R.A.7    Smith, T.W.8    Michel, T.9
  • 66
    • 0028580097 scopus 로고
    • Resetting the biological clock: Mediation of nocturnal circadian shifts by glutamate and NO
    • Ding, J. M., Chen, D., Weber, E. T., Faiman, L. E., Rea, M. A., and Gillette, M. U. (1994) Resetting the biological clock: mediation of nocturnal circadian shifts by glutamate and NO. Science 266, 1713-1717
    • (1994) Science , vol.266 , pp. 1713-1717
    • Ding, J.M.1    Chen, D.2    Weber, E.T.3    Faiman, L.E.4    Rea, M.A.5    Gillette, M.U.6
  • 67
    • 0028059563 scopus 로고
    • Nitric oxide mediates the formation of synaptic connections in developing and regenerating olfactory receptor neurons
    • Roskams, A. J., Bredt, D. S., Danson, T. M., and Ronnett, G. V. (1994) Nitric oxide mediates the formation of synaptic connections in developing and regenerating olfactory receptor neurons. Neuron 13, 289-299
    • (1994) Neuron , vol.13 , pp. 289-299
    • Roskams, A.J.1    Bredt, D.S.2    Danson, T.M.3    Ronnett, G.V.4
  • 68
    • 0027267817 scopus 로고
    • Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus
    • Zhuo, M., Small, S. A., Kandel, E. R., and Hawkins, R. D. (1993) Nitric oxide and carbon monoxide produce activity-dependent long-term synaptic enhancement in hippocampus. Science 260, 1946-1950
    • (1993) Science , vol.260 , pp. 1946-1950
    • Zhuo, M.1    Small, S.A.2    Kandel, E.R.3    Hawkins, R.D.4
  • 69
    • 0027194540 scopus 로고
    • A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
    • Lipton, S. A., Choi, Y. B., Pan, Z. H., Lei, S. Z., Chen, H. S., Sucher, N. J., Loscalzo, J., Singel, D. J., and Stamler, J. S. (1993) A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature (London) 364, 626-632
    • (1993) Nature (London) , vol.364 , pp. 626-632
    • Lipton, S.A.1    Choi, Y.B.2    Pan, Z.H.3    Lei, S.Z.4    Chen, H.S.5    Sucher, N.J.6    Loscalzo, J.7    Singel, D.J.8    Stamler, J.S.9
  • 71
    • 0030175826 scopus 로고    scopus 로고
    • Nitric oxide modulates synaptic vesicle docking/fusion reactions
    • Meffert, M. K., Calakos, N. C., Scheller, R. H., and Schulman, H. (1996) Nitric oxide modulates synaptic vesicle docking/fusion reactions. Neuron 16, 1229-1236
    • (1996) Neuron , vol.16 , pp. 1229-1236
    • Meffert, M.K.1    Calakos, N.C.2    Scheller, R.H.3    Schulman, H.4
  • 72
    • 0024378999 scopus 로고
    • Nitric oxide mediates glutamate-induced enhancement of cGMP levels in the cerebellum
    • Bredt, D. S., and Snyder, S. H. (1989) Nitric oxide mediates glutamate-induced enhancement of cGMP levels in the cerebellum. Proc. Natl. Acad. Sci. USA 86, 9030-9033
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9030-9033
    • Bredt, D.S.1    Snyder, S.H.2
  • 73
    • 0029417023 scopus 로고
    • Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro
    • Busciglio, J., and Yankner, B. A. (1995) Apoptosis and increased generation of reactive oxygen species in Down's syndrome neurons in vitro. Nature (London) 378, 776-779
    • (1995) Nature (London) , vol.378 , pp. 776-779
    • Busciglio, J.1    Yankner, B.A.2
  • 74
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Buttke, T. M., and Sandstrom, P. A. (1994) Oxidative stress as a mediator of apoptosis. Immunol. Today 15, 7-10
    • (1994) Immunol. Today , vol.15 , pp. 7-10
    • Buttke, T.M.1    Sandstrom, P.A.2
  • 75
    • 0029873387 scopus 로고    scopus 로고
    • Reactive oxygen species and programmed cell death
    • Jacobson, M. D. (1996) Reactive oxygen species and programmed cell death. Trends Biochem. Sci. 21, 83-86
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 83-86
    • Jacobson, M.D.1
  • 76
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Stamler, J. S. (1994) Redox signaling: Nitrosylation and related target interactions of nitric oxide. Cell 78, 931-936
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 77
    • 0028365310 scopus 로고
    • Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells
    • Griendling, K. K., Minieri, C. A., Ollerenshaw, J. D., and Alexander, R. W. (1994) Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ. Res. 74, 1141-1148
    • (1994) Circ. Res. , vol.74 , pp. 1141-1148
    • Griendling, K.K.1    Minieri, C.A.2    Ollerenshaw, J.D.3    Alexander, R.W.4
  • 78
    • 0029417335 scopus 로고
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor 1
    • 2-generating NADH oxidase in human lung fibroblasts by transforming growth factor 1. J. Biol. Chem. 270, 30334-30338
    • (1995) J. Biol. Chem. , vol.270 , pp. 30334-30338
    • Thannickal, V.J.1    Fanburg, B.L.2
  • 79
    • 0027274617 scopus 로고
    • Regulation of tyrosine phosphorylation in neutrophils by the NADPH oxidase. Role of reactive oxygen intermediates
    • Fialkow, L., Chan, C. K., Grinstein, S., and Downey, G. P. (1993) Regulation of tyrosine phosphorylation in neutrophils by the NADPH oxidase. Role of reactive oxygen intermediates. J. Biol. Chem. 268, 17131-17137
    • (1993) J. Biol. Chem. , vol.268 , pp. 17131-17137
    • Fialkow, L.1    Chan, C.K.2    Grinstein, S.3    Downey, G.P.4
  • 80
    • 0028270719 scopus 로고
    • Regulation of biosynthesis of nitric oxide
    • Nathan, C., and Xie, Q.-W. (1994) Regulation of biosynthesis of nitric oxide. J. Biol. Chem. 269, 13725-13728
    • (1994) J. Biol. Chem. , vol.269 , pp. 13725-13728
    • Nathan, C.1    Xie, Q.-W.2
  • 81
    • 25744468688 scopus 로고
    • Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins
    • Bokoch, G. M. (1994) Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins. FASEB J. 7, 750-759
    • (1994) FASEB J. , vol.7 , pp. 750-759
    • Bokoch, G.M.1
  • 84
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen, C. K., and Packer, L. P. (1996) Antioxidant and redox regulation of gene transcription. FASEB J. 10, 709-720
    • (1996) FASEB J. , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.P.2
  • 85
    • 0029163992 scopus 로고
    • Nitric oxide enhances prostaglandin-H synthase-1 activity by a heme-independent mechanism: Evidence implicating nitrosothiols
    • Hajjar, D. P., Lander, H. M., Pearce, S. F. A., Upmacis, R. K., and Pomerantz, K. B. (1995) Nitric oxide enhances prostaglandin-H synthase-1 activity by a heme-independent mechanism: evidence implicating nitrosothiols. J. Am. Chem. Soc. 117, 3340-3346
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3340-3346
    • Hajjar, D.P.1    Lander, H.M.2    Pearce, S.F.A.3    Upmacis, R.K.4    Pomerantz, K.B.5
  • 86
    • 0029005691 scopus 로고
    • Inhibition of ribonucleotide reductase by nitric oxide derived from thionitrites: Reversible modifications of both subunits
    • Roy, B., Lepoivre, M., Henry, Y., and Fontecave, M. (1995) Inhibition of ribonucleotide reductase by nitric oxide derived from thionitrites: reversible modifications of both subunits. Biochemistry 34, 5411-54418
    • (1995) Biochemistry , vol.34 , pp. 5411-54418
    • Roy, B.1    Lepoivre, M.2    Henry, Y.3    Fontecave, M.4
  • 88
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used second messengers in the activation of the NF-κB transcription factor and HIV-1
    • Schreck, R., Rieber, P., and Baeuerle, P. A. (1991) Reactive oxygen intermediates as apparently widely used second messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10, 2247-2258
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 90
    • 0028199634 scopus 로고
    • Tetrachlorodecaoxygen, a wound healing agent, produces vascular relaxation through hemoglobin-dependent inactivation of serotonin and norepinephrine
    • Wolin, M. S., Kleber, E., Mohazzab-H., K. M., and Elstner, E. F. (1994) Tetrachlorodecaoxygen, a wound healing agent, produces vascular relaxation through hemoglobin-dependent inactivation of serotonin and norepinephrine. J. Cardiovasc. Pharm. 23, 664-668
    • (1994) J. Cardiovasc. Pharm. , vol.23 , pp. 664-668
    • Wolin, M.S.1    Kleber, E.2    Mohazzab-H, K.M.3    Elstner, E.F.4


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