메뉴 건너뛰기




Volumn 106, Issue 2-3, 1999, Pages 93-106

Intracellular oxidation/reduction status in the regulation of transcription factors NF-κB and AP-1

Author keywords

AP 1; Intracellular oxidation reduction status; NF B; Transcription factors

Indexed keywords

1,10 PHENANTHROLINE; ACETYLCYSTEINE; ALPHA TOCOPHEROL; ANTIOXIDANT; AUROTHIOGLUCOSE; BUTYLATED HYDROXYANISOLE; CHELATING AGENT; CYSTEINE; DEFEROXAMINE; DIETHYLDITHIOCARBAMIC ACID; DISULFIRAM; GLUTATHIONE; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MERCAPTOETHANOL; NORDIHYDROGUAIARETIC ACID; PYRROLIDINE DITHIOCARBAMATE; REACTIVE OXYGEN METABOLITE; THIOCTIC ACID; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1;

EID: 0032998598     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4274(99)00024-7     Document Type: Review
Times cited : (254)

References (94)
  • 1
    • 0025782826 scopus 로고
    • Transcriptional regulation by Fos and Jun in vitro: Interaction among multiple activator and regulatory domains
    • Abate C., Luk D., Curran T. Transcriptional regulation by Fos and Jun in vitro: interaction among multiple activator and regulatory domains. Mol. Cell. Biol. 11:1991;3624-3632.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3624-3632
    • Abate, C.1    Luk, D.2    Curran, T.3
  • 2
    • 0025720735 scopus 로고
    • The role of Jun, Fos, and the AP-1 complex in cell-proliferation and transformation
    • Angel P., Karin M. The role of Jun, Fos, and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta. 1072:1991;129-157.
    • (1991) Biochim. Biophys. Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 3
    • 0029130938 scopus 로고
    • Oxidized LDL induces transcription factor activator protein-l but inhibits activation of nuclear factor-kappa B in human vascular smooth muscle cells
    • Ares M.P., Kallin B., Eriksson P., Nilsson J. Oxidized LDL induces transcription factor activator protein-l but inhibits activation of nuclear factor-kappa B in human vascular smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 15:1995;1584-1590.
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1584-1590
    • Ares, M.P.1    Kallin, B.2    Eriksson, P.3    Nilsson, J.4
  • 4
    • 0024294357 scopus 로고
    • Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor
    • Baeuerle P.A., Baltimore D. Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-κB transcription factor. Cell. 53:1988;211-217.
    • (1988) Cell , vol.53 , pp. 211-217
    • Baeuerle, P.A.1    Baltimore, D.2
  • 5
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: 10 years after
    • Baeuerle P.A., Baltimore D. NF-κB: 10 years after. Cell. 87:1996;13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 6
    • 0029874138 scopus 로고    scopus 로고
    • The NF-κB and I-κB proteins: New discoveries and insights
    • Baldwin A.S. The NF-κB and I-κB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:1996;649-681.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-681
    • Baldwin, A.S.1
  • 7
    • 0026783210 scopus 로고
    • I-κB interacts with the nuclear localization sequences of the subunits of NF-κB: A mechanism for cytoplasmic retention
    • Beg A.A., Ruben S.M., Scheinman R.I., Haskill S., Rosen C.A., Baldwin A.S. Jr. I-κB interacts with the nuclear localization sequences of the subunits of NF-κB: a mechanism for cytoplasmic retention. Genes Dev. 6:1992;1899-1913.
    • (1992) Genes Dev. , vol.6 , pp. 1899-1913
    • Beg, A.A.1    Ruben, S.M.2    Scheinman, R.I.3    Haskill, S.4    Rosen, C.A.5    Baldwin A.S., Jr.6
  • 8
    • 0032493369 scopus 로고    scopus 로고
    • Evidence for a role of NF-κB in the survival of hematopoietic cells mediated by interleukin-3 and the oncogenic TEL/platelet-derived growth factor receptor β-fusion protein
    • Besançon F., Atfi A., Gespach C., Cayre Y.E., Bourgeade M.F. Evidence for a role of NF-κB in the survival of hematopoietic cells mediated by interleukin-3 and the oncogenic TEL/platelet-derived growth factor receptor β-fusion protein. Proc. Natl. Acad. Sci. USA. 95:1998;8081-8086.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8081-8086
    • Besançon, F.1    Atfi, A.2    Gespach, C.3    Cayre, Y.E.4    Bourgeade, M.F.5
  • 10
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of I-κBα by a novel ubiquitination-dependent protein kinase activity
    • Chen Z.J., Parent L., Maniatis T. Site-specific phosphorylation of I-κBα by a novel ubiquitination-dependent protein kinase activity. Cell. 84:1996;853-862.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 11
    • 0023241823 scopus 로고
    • Multiple cis- And transacting elements mediate the transcriptional response to phorbol esters
    • Chiu R., Imagawa M., Imbra R.J., Bockoven J.R., Karin M. Multiple cis- and transacting elements mediate the transcriptional response to phorbol esters. Nature. 329:1987;648-651.
    • (1987) Nature , vol.329 , pp. 648-651
    • Chiu, R.1    Imagawa, M.2    Imbra, R.J.3    Bockoven, J.R.4    Karin, M.5
  • 12
    • 0029910072 scopus 로고    scopus 로고
    • Oxidative stress activates metal-responsive transcription factor-1 binding activity. Occupancy in vivo of metal response elements in the metallothionein-I gene promoter
    • Dalton T.P., Li Q., Bittel D., Liang L., Andrews G.K. Oxidative stress activates metal-responsive transcription factor-1 binding activity. Occupancy in vivo of metal response elements in the metallothionein-I gene promoter. J. Biol. Chem. 271:1996;26233-26241.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26233-26241
    • Dalton, T.P.1    Li, Q.2    Bittel, D.3    Liang, L.4    Andrews, G.K.5
  • 14
    • 0025721047 scopus 로고
    • Redux: The control of oxidative stress responses
    • Demple B., Amabile-Cuevas C.F. Redux: the control of oxidative stress responses. Cell. 67:1991;837-839.
    • (1991) Cell , vol.67 , pp. 837-839
    • Demple, B.1    Amabile-Cuevas, C.F.2
  • 15
    • 0027363407 scopus 로고
    • NF-κB activation by ultraviolet light not dependent on a nuclear signal
    • Devary Y., Rosette C., DiDonato J.A., Karin M. NF-κB activation by ultraviolet light not dependent on a nuclear signal. Science. 261:1993;1442-1445.
    • (1993) Science , vol.261 , pp. 1442-1445
    • Devary, Y.1    Rosette, C.2    DiDonato, J.A.3    Karin, M.4
  • 16
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible I-κB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato J.A., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., Karin M. Mapping of the inducible I-κB phosphorylation sites that signal its ubiquitination and degradation. Mol. Cell. Biol. 16:1996;1295-1304.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • Didonato, J.A.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 18
    • 0023832053 scopus 로고
    • The Fos complex and Fos-related antigens recognize sequence elements that contain AP-1 binding sites
    • Franza B.R. Jr., Rauscher III F.J., Josephs S.F., Curran T. The Fos complex and Fos-related antigens recognize sequence elements that contain AP-1 binding sites. Science. 239:1988;1150-1153.
    • (1988) Science , vol.239 , pp. 1150-1153
    • Franza B.R., Jr.1    Rauscher F.J. III2    Josephs, S.F.3    Curran, T.4
  • 19
    • 0027184023 scopus 로고
    • The candidate protooncogene bcl-3 encodes a transcriptional coactivator that activates through NF-κB p50 homodimers
    • Fujita T., Nolan G.P., Liou H.C., Scott M.L., Baltimore D. The candidate protooncogene bcl-3 encodes a transcriptional coactivator that activates through NF-κB p50 homodimers. Genes Dev. 7:1993;1354-1363.
    • (1993) Genes Dev. , vol.7 , pp. 1354-1363
    • Fujita, T.1    Nolan, G.P.2    Liou, H.C.3    Scott, M.L.4    Baltimore, D.5
  • 20
    • 0025352680 scopus 로고
    • Transcriptional activation and repression by Fos are independent functions: The C-terminus represses immediate-early gene expression via CArG elements
    • Gius D., Cao X., Rauscher F.J., Cohen D.R., Curran T., Sukhatme V.P. Transcriptional activation and repression by Fos are independent functions: the C-terminus represses immediate-early gene expression via CArG elements. Mol. Cell. Biol. 10:1990;4243-4255.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4243-4255
    • Gius, D.1    Cao, X.2    Rauscher, F.J.3    Cohen, D.R.4    Curran, T.5    Sukhatme, V.P.6
  • 22
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai T., Curran T. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc. Natl. Acad. Sci. USA. 88:1991;3720-3724.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 23
    • 84965889455 scopus 로고
    • Free radicals and antioxidant protection: Mechanisms and significance in toxicology and disease
    • Halliwell B., Gutteridge J.M. Free radicals and antioxidant protection: mechanisms and significance in toxicology and disease. Hum. Toxicol. 7:1988;7-13.
    • (1988) Hum. Toxicol. , vol.7 , pp. 7-13
    • Halliwell, B.1    Gutteridge, J.M.2
  • 24
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B., Gutteridge J.M. Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186:1990;1-85.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 25
    • 0028985335 scopus 로고
    • A-Lipoic acid increases intracellular glutathione in a human T-lymphocyte Jurkat cell line
    • Han D., Tritschler H.J., Packer L. a-Lipoic acid increases intracellular glutathione in a human T-lymphocyte Jurkat cell line. Biochem. Biophys. Res. Commun. 207:1995;258-264.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 258-264
    • Han, D.1    Tritschler, H.J.2    Packer, L.3
  • 26
    • 0023930518 scopus 로고
    • Kinetic studies on arachidonate 5-lipoxygenase from rat bosophilic leukemia cells
    • Haurand M., Flohe L. Kinetic studies on arachidonate 5-lipoxygenase from rat bosophilic leukemia cells. Biol. Chem. Hoppe Seyler. 369:1988;133-142.
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 133-142
    • Haurand, M.1    Flohe, L.2
  • 27
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor NF-κB: Involvement of a cellular reducing catalyst thioredoxin
    • Hayash T., Ueno Y., Okamoto T. Oxidoreductive regulation of nuclear factor NF-κB: involvement of a cellular reducing catalyst thioredoxin. J. Biol. Chem. 268:1993;11380-11388.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11380-11388
    • Hayash, T.1    Ueno, Y.2    Okamoto, T.3
  • 28
    • 0026523562 scopus 로고
    • Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit
    • Henkel T., Zabel U., van Zee K., Muller J.M., Fanning E., Baeuerle P.A. Intramolecular masking of the nuclear location signal and dimerization domain in the precursor for the p50 NF-κB subunit. Cell. 68:1992;1121-1133.
    • (1992) Cell , vol.68 , pp. 1121-1133
    • Henkel, T.1    Zabel, U.2    Van Zee, K.3    Muller, J.M.4    Fanning, E.5    Baeuerle, P.A.6
  • 29
    • 0027176524 scopus 로고
    • Rapid proteolysis of I-κBa is necessary for activation of transcription factor NF-κB
    • Henkel T., Machleidt T., Alkalay I., Dronke M., Ben-Neriah Y., Beauerle P.A. Rapid proteolysis of I-κBa is necessary for activation of transcription factor NF-κB. Nature. 365:1993;182-185.
    • (1993) Nature , vol.365 , pp. 182-185
    • Henkel, T.1    Machleidt, T.2    Alkalay, I.3    Dronke, M.4    Ben-Neriah, Y.5    Beauerle, P.A.6
  • 30
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals: Mechanisms and specificity
    • Hill C.S., Treisman R. Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell. 80:1995;199-211.
    • (1995) Cell , vol.80 , pp. 199-211
    • Hill, C.S.1    Treisman, R.2
  • 31
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc. Natl. Acad. Sci. USA. 94:1997;3633-3639.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3633-3639
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5    Yodoi, J.6
  • 32
    • 0026230108 scopus 로고
    • Response to adversity: Molecular control of gene activation following genotoxic stress
    • Holbrook N.J., Fornace A.J. Response to adversity: molecular control of gene activation following genotoxic stress. New Biologist. 3:1991;825-833.
    • (1991) New Biologist , vol.3 , pp. 825-833
    • Holbrook, N.J.1    Fornace, A.J.2
  • 33
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A.J., Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science. 257:1992;1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 34
    • 0023513624 scopus 로고
    • Regulation of glutathione levels in mouse spleen lymphocytes by transport of cysteine
    • Ishii T., Sugita Y., Bannai S. Regulation of glutathione levels in mouse spleen lymphocytes by transport of cysteine. J. Cell. Physiol. 133:1987;330-336.
    • (1987) J. Cell. Physiol. , vol.133 , pp. 330-336
    • Ishii, T.1    Sugita, Y.2    Bannai, S.3
  • 35
    • 0029328342 scopus 로고
    • Transcriptional control by protein phosphorylation: Signal transmission from cell surface to the nucleus
    • Karin M., Hunter T. Transcriptional control by protein phosphorylation: signal transmission from cell surface to the nucleus. Curr. Biol. 5:1995;747-757.
    • (1995) Curr. Biol. , vol.5 , pp. 747-757
    • Karin, M.1    Hunter, T.2
  • 36
    • 0026661584 scopus 로고
    • Control of transcription factors by signal transduction pathways: The beginning of the end
    • Karin M., Smeal T. Control of transcription factors by signal transduction pathways: the beginning of the end. Trends Biochem. Sci. 17:1992;418-422.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 418-422
    • Karin, M.1    Smeal, T.2
  • 37
    • 0028852684 scopus 로고
    • Transcription. Zen and the art of Fos and Jun
    • Kerppola T.K., Curran T. Transcription. Zen and the art of Fos and Jun. Nature. 373(6511):1995;199-200.
    • (1995) Nature , vol.373 , Issue.6511 , pp. 199-200
    • Kerppola, T.K.1    Curran, T.2
  • 40
    • 0028965108 scopus 로고
    • Mutational analysis of the redox-sensitive transcriptional regulator OxyR: Regions important for oxidation and transcriptional activation
    • Kullik I., Toledano M.B., Tartaglia L.A., Storz G. Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J. Bacteriol. 177:1995;1275-1284.
    • (1995) J. Bacteriol. , vol.177 , pp. 1275-1284
    • Kullik, I.1    Toledano, M.B.2    Tartaglia, L.A.3    Storz, G.4
  • 41
    • 0028930138 scopus 로고
    • Mutational analysis of the redox sensitive transcriptional regulator OxyR: Regions important for DNA binding and multimerization
    • Kullik I., Stevens J., Toledano M.B., Storz G. Mutational analysis of the redox sensitive transcriptional regulator OxyR: regions important for DNA binding and multimerization. J. Bacteriol. 177:1995;1285-1291.
    • (1995) J. Bacteriol. , vol.177 , pp. 1285-1291
    • Kullik, I.1    Stevens, J.2    Toledano, M.B.3    Storz, G.4
  • 42
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the I-κB kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee F.S., Hagler J., Chen Z.J., Maniatis T. Activation of the I-κB kinase complex by MEKK1, a kinase of the JNK pathway. Cell. 88:1997;213-222.
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.S.1    Hagler, J.2    Chen, Z.J.3    Maniatis, T.4
  • 43
    • 0027981492 scopus 로고
    • 2 and N-acetyl-L-cysteine regulate expression of c-Jun and c-Fos in lens systems
    • 2 and N-acetyl-L-cysteine regulate expression of c-Jun and c-Fos in lens systems. Exp. Eye Res. 59:1994;179-190.
    • (1994) Exp. Eye Res. , vol.59 , pp. 179-190
    • Li, W.C.1    Wang, G.M.2    Wang, R.R.3    Spector, A.4
  • 45
    • 0030055822 scopus 로고    scopus 로고
    • Selenium-mediated inhibition of transcription factor NF-κB and HIV-1 LTR promoter activity
    • Makropoulos V., Bruening T., Schulze-Osthoff K. Selenium-mediated inhibition of transcription factor NF-κB and HIV-1 LTR promoter activity. Arch. Toxicol. 70:1996;277-283.
    • (1996) Arch. Toxicol. , vol.70 , pp. 277-283
    • Makropoulos, V.1    Bruening, T.2    Schulze-Osthoff, K.3
  • 46
    • 0031865229 scopus 로고    scopus 로고
    • The C-Terminal domain of c-fos is required for activation of an AP-1 site specific for jun-fos heterodimers
    • McBride K., Nemer M. The C-Terminal domain of c-fos is required for activation of an AP-1 site specific for jun-fos heterodimers. Mol. Cell. Biol. 18:1998;5073-5081.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5073-5081
    • McBride, K.1    Nemer, M.2
  • 48
    • 0027269781 scopus 로고
    • 2 and antioxidants have opposite effects on activation of NF-κB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor
    • 2 and antioxidants have opposite effects on activation of NF-κB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J. 12:1993;2005-2015.
    • (1993) EMBO J. , vol.12 , pp. 2005-2015
    • Meyer, M.1    Schreck, R.2    Baeuerle, P.A.3
  • 49
    • 0028342913 scopus 로고
    • Regulation of the transcription factors NF-κB and AP-1 by redox changes
    • Meyer M., Pahl H.L., Bauerle P.A. Regulation of the transcription factors NF-κB and AP-1 by redox changes. Chem.-Biol. Interact. 91:1994;91-100.
    • (1994) Chem.-Biol. Interact. , vol.91 , pp. 91-100
    • Meyer, M.1    Pahl, H.L.2    Bauerle, P.A.3
  • 50
    • 0021688528 scopus 로고
    • Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action
    • Morris S.L., Walsh R.C., Hansen J.N. Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action. J. Biol. Chem. 259:1984;13590-13594.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13590-13594
    • Morris, S.L.1    Walsh, R.C.2    Hansen, J.N.3
  • 51
    • 0040204710 scopus 로고    scopus 로고
    • Study of the gene regulation by NF-κB and AP-1 in response to reactive oxygen intermediates
    • Muller J., Rupec R.A., Baeuerle P.A. Study of the gene regulation by NF-κB and AP-1 in response to reactive oxygen intermediates. Methods. 11:1997;301-312.
    • (1997) Methods , vol.11 , pp. 301-312
    • Muller, J.1    Rupec, R.A.2    Baeuerle, P.A.3
  • 52
    • 0030587928 scopus 로고    scopus 로고
    • Transcriptional up-regulation of intracellular adhesion molecule-1 in human endothelial cells by the antioxidant pyrrolidine dithiocarbamate involves the activation of activating protein-1
    • Munoz C., Castellanos M.C., Alfranca A., Vara A., Esteban M.A., Redondo J.M., de Landazuri M.O. Transcriptional up-regulation of intracellular adhesion molecule-1 in human endothelial cells by the antioxidant pyrrolidine dithiocarbamate involves the activation of activating protein-1. J. Immunol. 157:1996;3587-3597.
    • (1996) J. Immunol. , vol.157 , pp. 3587-3597
    • Munoz, C.1    Castellanos, M.C.2    Alfranca, A.3    Vara, A.4    Esteban, M.A.5    Redondo, J.M.6    De Landazuri, M.O.7
  • 53
    • 0027440247 scopus 로고
    • Activation by nitric oxide of anoxidative-stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba T., deRojas-Walker T., Wishnok J.S., Tannenbaum S.R., Demple B. Activation by nitric oxide of anoxidative-stress response that defends Escherichia coli against activated macrophages. Proc. Natl. Acad. Sci. USA. 90:1993;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
  • 54
    • 0028960382 scopus 로고
    • Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages
    • Nunoshiba T., DeRojas-Walker T., Tannenbaum S.R., Demple B. Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages. Infect. Immun. 63:1995;794-798.
    • (1995) Infect. Immun. , vol.63 , pp. 794-798
    • Nunoshiba, T.1    DeRojas-Walker, T.2    Tannenbaum, S.R.3    Demple, B.4
  • 56
    • 0027392874 scopus 로고
    • Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase activity in U937 leukaemic cells
    • Pulverer B.J., Hughes K., Franklin C.C., Kraft A.S., Leevers S.J., Woodgett J.R. Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase activity in U937 leukaemic cells. Oncogene. 8:1993;407-415.
    • (1993) Oncogene , vol.8 , pp. 407-415
    • Pulverer, B.J.1    Hughes, K.2    Franklin, C.C.3    Kraft, A.S.4    Leevers, S.J.5    Woodgett, J.R.6
  • 57
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse J., Cohen P., Trigon S., Morange M., Alonso-Llamazares A., Zamanillo D., Hunt T., Nebreda A. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell. 78:1994;1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso-Llamazares, A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.8
  • 58
    • 0028841622 scopus 로고
    • The genomic response of tumor cells to hypoxia and reoxygenation. Differential activation of transcription factors AP-1 and NF-kappa B
    • Rupic R., Baeuerle P.A. The genomic response of tumor cells to hypoxia and reoxygenation. Differential activation of transcription factors AP-1 and NF-kappa B. Eur. J. Biochem. 234:1995;632-640.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 632-640
    • Rupic, R.1    Baeuerle, P.A.2
  • 59
    • 0028344541 scopus 로고
    • Distinct effects of thioredoxin and other antioxidants on the activation of transcription factors NF-κB and AP-1
    • Schenk H., Klein M., Erdbrugger W., Droge W., Schulze-Osthoff K. Distinct effects of thioredoxin and other antioxidants on the activation of transcription factors NF-κB and AP-1. Proc. Natl. Acad. Sci. USA. 91:1994;1672-1676.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1672-1676
    • Schenk, H.1    Klein, M.2    Erdbrugger, W.3    Droge, W.4    Schulze-Osthoff, K.5
  • 60
    • 0029170274 scopus 로고
    • The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB
    • Schmidt K.N., Amstad P., Cerutti P., Baeuerle P.A. The roles of hydrogen peroxide and superoxide as messengers in the activation of transcription factor NF-κB. Chem. Biol. 2:1995;12-22.
    • (1995) Chem. Biol. , vol.2 , pp. 12-22
    • Schmidt, K.N.1    Amstad, P.2    Cerutti, P.3    Baeuerle, P.A.4
  • 61
    • 0028805786 scopus 로고
    • Induction of oxidative stress by okadaic acid is required for activation of NF-κB
    • Schmidt K.M., Traencker E.B., Meier B., Baeuerle P.A. Induction of oxidative stress by okadaic acid is required for activation of NF-κB. J. Biol. Chem. 270:1995;27136-27142.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27136-27142
    • Schmidt, K.M.1    Traencker, E.B.2    Meier, B.3    Baeuerle, P.A.4
  • 62
    • 0025739254 scopus 로고
    • Reactive oxygen species intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1
    • Schreck R., Rieber P., Baeuerle P.A. Reactive oxygen species intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10:1991;2247-2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1    Rieber, P.2    Baeuerle, P.A.3
  • 63
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • Schulze-Osthoff K., Bakker A.C., Vanhaesebroeck B., Beyaert R., Jocabs W.A., Fiers W. Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267:1992;5317-5323.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jocabs, W.A.5    Fiers, W.6
  • 64
    • 0029126754 scopus 로고
    • Redox signalling by transcription factors NF-κB and AP-1 in lymphocytes
    • Schulze-Osthoff K., Los M., Baeuerle P.A. Redox signalling by transcription factors NF-κB and AP-1 in lymphocytes. Biochem. Pharmacol. 50:1995;735-741.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 735-741
    • Schulze-Osthoff, K.1    Los, M.2    Baeuerle, P.A.3
  • 66
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequences
    • Sen R., Baltimore D. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell. 46:1986;705-716.
    • (1986) Cell , vol.46 , pp. 705-716
    • Sen, R.1    Baltimore, D.2
  • 67
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen C.K., Packer L. Antioxidant and redox regulation of gene transcription. FASEB J. 10:1996;709-720.
    • (1996) FASEB J. , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 68
    • 0028804551 scopus 로고
    • Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses
    • Sha W.C., Liou H.C., Tuomanen E.I., Baltimore D. Targeted disruption of the p50 subunit of NF-κB leads to multifocal defects in immune responses. Cell. 80:1995;321-330.
    • (1995) Cell , vol.80 , pp. 321-330
    • Sha, W.C.1    Liou, H.C.2    Tuomanen, E.I.3    Baltimore, D.4
  • 69
    • 0025987977 scopus 로고
    • Oxidative stress: From basic research to clinical application
    • Sies H. Oxidative stress: from basic research to clinical application. Am. J. Med. 91:1991;315-385.
    • (1991) Am. J. Med. , vol.91 , pp. 315-385
    • Sies, H.1
  • 70
    • 0025174861 scopus 로고
    • 2-resistant Chinese hamster fibroblasts
    • 2-resistant Chinese hamster fibroblasts. J. Cell. Physiol. 142:1990;255-260.
    • (1990) J. Cell. Physiol. , vol.142 , pp. 255-260
    • Spitz, D.R.1    Li, G.C.2
  • 72
    • 0028115871 scopus 로고
    • 2 stimulate mitogen-activated protein kinase activity in NIH3T3 cells through the formation of reactive oxygen intermediates
    • 2 stimulate mitogen-activated protein kinase activity in NIH3T3 cells through the formation of reactive oxygen intermediates. Cancer Res. 54:1994;12-15.
    • (1994) Cancer Res. , vol.54 , pp. 12-15
    • Stevenson, M.A.1    Pollock, S.S.2    Coleman, N.3    Calderwood, S.K.4
  • 74
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun Y., Oberley L.W. Redox regulation of transcriptional activators. Free Radic. Biol. Med. 21:1996;335-348.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 75
    • 0024281381 scopus 로고
    • A zinc finger-encoding gene coregulated with c-fos during growth and differentiation, and after cellular depolarization
    • Sukhatme V.P., Cao X.M., Chang L.C. et al. A zinc finger-encoding gene coregulated with c-fos during growth and differentiation, and after cellular depolarization. Cell. 53:1988;37-43.
    • (1988) Cell , vol.53 , pp. 37-43
    • Sukhatme, V.P.1    Cao, X.M.2    Chang, L.C.3
  • 76
    • 0027310696 scopus 로고
    • Inhibition of NF-κB activation by vitamin E derivatives
    • Suzuki Y.J., Packer L. Inhibition of NF-κB activation by vitamin E derivatives. Biochem. Biophys. Res. Commun. 193:1993;277-283.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 277-283
    • Suzuki, Y.J.1    Packer, L.2
  • 77
    • 0028023175 scopus 로고
    • Redox dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
    • Toledano B., Kullik I., Trinh F., Baird P.T., Schneider T.D., Storz G. Redox dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell. 78:1994;897-909.
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, B.1    Kullik, I.2    Trinh, F.3    Baird, P.T.4    Schneider, T.D.5    Storz, G.6
  • 78
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated from of I kappa B-alpha that is still bound to NF-kappa B
    • Traenckner E.B., Wilk S., Baeuerle P.A. A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated from of I kappa B-alpha that is still bound to NF-kappa B. EMBO J. 13:1994;5433-5441.
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.1    Wilk, S.2    Baeuerle, P.A.3
  • 79
    • 0028978032 scopus 로고
    • Phosphorylation of human I kappa B-alpha on serines 32/36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli
    • Traenckner E.B., Pahl H.L., Henkel T., Schmidt K.N., Wilk S., Baeuerle P.A. Phosphorylation of human I kappa B-alpha on serines 32/36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBO J. 14:1995;2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 80
    • 0028803402 scopus 로고
    • Journey to the surface of the cell: Fos regulation and the SRE
    • Treisman R. Journey to the surface of the cell: Fos regulation and the SRE. EMBO J. 14:1995;4905-4913.
    • (1995) EMBO J. , vol.14 , pp. 4905-4913
    • Treisman, R.1
  • 82
    • 0028596574 scopus 로고
    • A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress
    • Walker L.J., Craig R.B., Harris A.L., Hickson I.D. A role for the human DNA repair enzyme HAP1 in cellular protection against DNA damaging agents and hypoxic stress. Nucleic Acids Res. 22:1994;4884-4889.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4884-4889
    • Walker, L.J.1    Craig, R.B.2    Harris, A.L.3    Hickson, I.D.4
  • 85
    • 0028929893 scopus 로고
    • Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli
    • Wu J., Dunham W.R., Weiss B. Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli. J. Biol. Chem. 270:1995;10323-10327.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10323-10327
    • Wu, J.1    Dunham, W.R.2    Weiss, B.3
  • 86
    • 0026714672 scopus 로고
    • Redox activation of fos-jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G.G., Wang F., Pan Y.-C.E., Curran T. Redox activation of fos-jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11:1992;3323-3335.
    • (1992) EMBO J. , vol.11 , pp. 3323-3335
    • Xanthoudakis, S.1    Miao, G.G.2    Wang, F.3    Pan, Y.-C.E.4    Curran, T.5
  • 87
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis S., Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J. 11:1992;653-664.
    • (1992) EMBO J. , vol.11 , pp. 653-664
    • Xanthoudakis, S.1    Curran, T.2
  • 88
    • 0028058086 scopus 로고
    • The redox and DNA-repair activities of Ref-1 are encoded by non-overlapping domains
    • Xanthoudakis S., Miao G.G., Curran T. The redox and DNA-repair activities of Ref-1 are encoded by non-overlapping domains. Proc. Natl. Acad. Sci. USA. 91:1994;23-27.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 23-27
    • Xanthoudakis, S.1    Miao, G.G.2    Curran, T.3
  • 89
    • 0029759283 scopus 로고    scopus 로고
    • Redox regulation of AP-1: A link between transcription factor signaling and DNA repair
    • Xanthoudakis S., Curran T. Redox regulation of AP-1: a link between transcription factor signaling and DNA repair. Adv. Exp. Med. Biol. 387:1996;69-75.
    • (1996) Adv. Exp. Med. Biol. , vol.387 , pp. 69-75
    • Xanthoudakis, S.1    Curran, T.2
  • 90
    • 0030022244 scopus 로고    scopus 로고
    • The organization of the human GSTP1-1 gene promoter and its response to retinoic acid and cellular redox status
    • Xia C., Hu J., Ketterer B., Taylor J.B. The organization of the human GSTP1-1 gene promoter and its response to retinoic acid and cellular redox status. Biochem. J. 313:1996;155-161.
    • (1996) Biochem. J. , vol.313 , pp. 155-161
    • Xia, C.1    Hu, J.2    Ketterer, B.3    Taylor, J.B.4
  • 91
    • 0027936404 scopus 로고
    • Activation of AP-1 and of a nuclear redox factor, ref-1, in the response of HT29 colon cancer cells to hypoxia
    • Yao K.-S., Xanthoudakis S., Curran T., O'Dwyer P.J. Activation of AP-1 and of a nuclear redox factor, ref-1, in the response of HT29 colon cancer cells to hypoxia. Mol. Cell. Biol. 14:1994;5997-6003.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5997-6003
    • Yao, K.-S.1    Xanthoudakis, S.2    Curran, T.3    O'Dwyer, P.J.4
  • 92
    • 0025304791 scopus 로고
    • Purified human I-κB can rapidly dissociate the complex of the NF-B transcription factor with its cognate DNA
    • Zabel U., Baeuerle P.A. Purified human I-κB can rapidly dissociate the complex of the NF-B transcription factor with its cognate DNA. Cell. 61:1990;255-265.
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2
  • 93
    • 0030613551 scopus 로고    scopus 로고
    • The IB kinase complex (IKK) contains two kinase subunits IKK and IKKβ, necessary for IB phosphorylation and NF-B activation
    • Zandi E., Rothwarf D.M., Delhase M., Hayakawa M., Karin M. The IB kinase complex (IKK) contains two kinase subunits IKK and IKKβ, necessary for IB phosphorylation and NF-B activation. Cell. 91:1997;243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 94
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M., Aslund F., Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science. 279:1998;1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.