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Volumn 899, Issue , 2000, Pages 69-87

Genetic responses to free radicals. Homeostasis and gene control

Author keywords

[No Author keywords available]

Indexed keywords

FREE RADICAL; HEME OXYGENASE; HYDROGEN PEROXIDE; IRON; MESSENGER RNA; NITRIC OXIDE; SULFUR; SUPEROXIDE;

EID: 0034082979     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2000.tb06177.x     Document Type: Conference Paper
Times cited : (48)

References (88)
  • 1
    • 0000797687 scopus 로고
    • The state of catalase in the respiring bacterial cells
    • 1. CHANCE, B. 1952. The state of catalase in the respiring bacterial cells. Science 116: 202-3
    • (1952) Science , vol.116 , pp. 202-203
    • Chance, B.1
  • 2
    • 70449538294 scopus 로고
    • An intermediate stage in the H2O2-induced synthesis of catalase in Rhodopseudomonas spheroides
    • 2. CLAYTON, R. K. 1960. An intermediate stage in the H2O2-induced synthesis of catalase in Rhodopseudomonas spheroides. J. Cell. Comp. Physiol. 55: 1-8.
    • (1960) J. Cell. Comp. Physiol. , vol.55 , pp. 1-8
    • Clayton, R.K.1
  • 3
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • 3. GONZÁLEZ-FLECHA, B. & B. DEMPLE. 1995. Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J. Biol. Chem. 270: 13681-13687.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13681-13687
    • González-Flecha, B.1    Demple, B.2
  • 4
    • 0031025115 scopus 로고    scopus 로고
    • Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli
    • 4. GONZÁLEZ-FLECHA, B. & B. DEMPLE. 1997. Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli. J. Bacteriol. 179: 382-388.
    • (1997) J. Bacteriol. , vol.179 , pp. 382-388
    • González-Flecha, B.1    Demple, B.2
  • 6
    • 0020529486 scopus 로고
    • Inducible repair of oxidative DNA damage in Escherichia coli
    • 6. DEMPLE, B. & J. HALBROOK. 1983. Inducible repair of oxidative DNA damage in Escherichia coli. Nature 304: 466-468.
    • (1983) Nature , vol.304 , pp. 466-468
    • Demple, B.1    Halbrook, J.2
  • 7
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: Direct activation by oxidation
    • 7. STORZ, G., L.A. TARTAGLIA & B.N. AMES. 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
  • 8
    • 0025721047 scopus 로고
    • Redox redux: The control of oxidative stress responses
    • 8. DEMPLE, B. & C.F. AMÁBILE-CUEVAS. 1991. Redox redux: the control of oxidative stress responses. Cell 67: 837-839.
    • (1991) Cell , vol.67 , pp. 837-839
    • Demple, B.1    Amábile-Cuevas, C.F.2
  • 9
    • 1842404770 scopus 로고    scopus 로고
    • Transcriptional regulation of the Escherichia coli oxyR gene as a function of cell growth
    • 9. GONZÁLEZ-FLECHA, B. & B. DEMPLE. 1997. Transcriptional regulation of the Escherichia coli oxyR gene as a function of cell growth. J. Bacteriol. 179: 6181-6186.
    • (1997) J. Bacteriol. , vol.179 , pp. 6181-6186
    • González-Flecha, B.1    Demple, B.2
  • 10
    • 0028787734 scopus 로고
    • Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: Intracellular levels of sigma 70 and sigma 38
    • 10. JISHAGE, D.E. & A. ISHIHAMA. 1995. Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: intracellular levels of sigma 70 and sigma 38. J. Bacteriol. 177: 6832-6835.
    • (1995) J. Bacteriol. , vol.177 , pp. 6832-6835
    • Jishage, D.E.1    Ishihama, A.2
  • 11
    • 0031459386 scopus 로고    scopus 로고
    • A small, stable RNA induced by oxidative stress: Role as a pleiotropic regulator and antimutator
    • 11. ALTUVIA, S., D. WEINSTEIN-FISCHER, A. ZHANG, L. POSTOW & G. STORZ. 1997. A small, stable RNA induced by oxidative stress: role as a pleiotropic regulator and antimutator. Cell 90:
    • (1997) Cell , vol.90
    • Altuvia, S.1    Weinstein-Fischer, D.2    Zhang, A.3    Postow, L.4    Storz, G.5
  • 12
    • 0344780826 scopus 로고    scopus 로고
    • Role of the oxyS gene in the regulation of intracellular hydrogen peroxide in Escherichia coli
    • 12. GONZÁLEZ-FLECHA, B. & B. DEMPLE. 1999. Role of the oxyS gene in the regulation of intracellular hydrogen peroxide in Escherichia coli. J. Bacteriol. 181: 3833-3836.
    • (1999) J. Bacteriol. , vol.181 , pp. 3833-3836
    • González-Flecha, B.1    Demple, B.2
  • 13
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen
    • 13. BOVERIS, A. & B. CHANCE. 1973. The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem. J. 134: 707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 14
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • 14. CHANCE, B., H. SIES & A. BOVERIS. 1979. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59: 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 15
    • 0002437327 scopus 로고
    • Production of superoxide anion and hydrogen peroxide in mitochondria
    • (Oberley, L. W., Ed.), II, CRC Press, Boca Raton, FL
    • 15. BOVERIS, A., & E. CADENAS. 1982. Production of superoxide anion and hydrogen peroxide in mitochondria. Superoxide Dismutase (Oberley, L. W., Ed.), II, CRC Press, Boca Raton, FL.
    • (1982) Superoxide Dismutase
    • Boveris, A.1    Cadenas, E.2
  • 16
    • 0027473685 scopus 로고
    • Time course and mechanism of oxidative stress and tissue damage in rat liver subjected to in vivo ischemia-reperfusion
    • 16. GONZÁLEZ-FLECHA, B., J.C. CUTRIN & A. BOVERIS. 1993. Time course and mechanism of oxidative stress and tissue damage in rat liver subjected to in vivo ischemia-reperfusion. J. Clin. Invest. 91: 456-464.
    • (1993) J. Clin. Invest. , vol.91 , pp. 456-464
    • González-Flecha, B.1    Cutrin, J.C.2    Boveris, A.3
  • 17
    • 0028915527 scopus 로고
    • Mitochondrial sites of hydrogen peroxide production in reperfused rat kidney cortex
    • 17. GONZÁLEZ-FLECHA, B. & A. BOVERIS. 1995. Mitochondrial sites of hydrogen peroxide production in reperfused rat kidney cortex. Biochim. Biophys. Acta 1243: 361-366.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 361-366
    • González-Flecha, B.1    Boveris, A.2
  • 18
    • 0027208005 scopus 로고
    • Hydrogen peroxide metabolism and oxidative stress in cortical, medullary and papillary zones of rat kidney
    • 18. GONZÁLEZ-FLECHA, B., P. EVELSON, N. STERIN-SPEZIALE & A. BOVERIS. 1993. Hydrogen peroxide metabolism and oxidative stress in cortical, medullary and papillary zones of rat kidney. Biochim. Biophys. Acta 1157: 155-161.
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 155-161
    • González-Flecha, B.1    Evelson, P.2    Sterin-Speziale, N.3    Boveris, A.4
  • 20
    • 0022627453 scopus 로고
    • Glucose metabolism in renal tubular function
    • 20. Ross, B.D., J. ESPINAL & P. SILVA. 1986. Glucose metabolism in renal tubular function. Kidney International 29: 54-67.
    • (1986) Kidney International , vol.29 , pp. 54-67
    • Ross, B.D.1    Espinal, J.2    Silva, P.3
  • 22
    • 0023906912 scopus 로고
    • The case for oxygen free radicals in the pathogenesis of ischemic acute renal failure
    • 22. CANAVESE, C., P. STRATTA & A. VERCELLONE. 1988. The case for oxygen free radicals in the pathogenesis of ischemic acute renal failure. Nephron 49: 9-15.
    • (1988) Nephron , vol.49 , pp. 9-15
    • Canavese, C.1    Stratta, P.2    Vercellone, A.3
  • 23
    • 0023774161 scopus 로고
    • Effects of oxygen free radical scavengers, xanthine oxidase inhibition and calcium entry-blockers on leakage of albumin after ischaemia. An experimental study in rabbit kidneys
    • 23. BRATELL, S., P. FOLMERZ, R. HANSSON, O. JONSSON, S. LUNDSTAM, S. PETTERSSON, B. RIPPE & T. SCHERSTEN. 1988. Effects of oxygen free radical scavengers, xanthine oxidase inhibition and calcium entry-blockers on leakage of albumin after ischaemia. An experimental study in rabbit kidneys. Acta Physiol. Scand. 134: 35-41.
    • (1988) Acta Physiol. Scand. , vol.134 , pp. 35-41
    • Bratell, S.1    Folmerz, P.2    Hansson, R.3    Jonsson, O.4    Lundstam, S.5    Pettersson, S.6    Rippe, B.7    Schersten, T.8
  • 26
    • 33745368131 scopus 로고    scopus 로고
    • Antioxidant enzyme expression in rat lungs during hyperoxia
    • 26. Ho, Y.S., M.S. DEY & J.D. CRAPO. 1996. Antioxidant enzyme expression in rat lungs during hyperoxia. Am. J. Physiol. 270: L810-L818.
    • (1996) Am. J. Physiol. , vol.270
    • Ho, Y.S.1    Dey, M.S.2    Crapo, J.D.3
  • 28
    • 0031055166 scopus 로고    scopus 로고
    • Dexamethasone differently modulates TNF-alpha- and IL-1beta-induced transcription of the hepatic Mn-superoxide dismutase gene
    • 28. ANTRAS-FERRY, J., K. MAHEO, F. MOREL, A. GUILLOUZO, P. CILLARD & J. CILLARD. 1997. Dexamethasone differently modulates TNF-alpha-and IL-1beta-induced transcription of the hepatic Mn-superoxide dismutase gene. FEBS Lett. 403: 100-104.
    • (1997) FEBS Lett. , vol.403 , pp. 100-104
    • Antras-Ferry, J.1    Maheo, K.2    Morel, F.3    Guillouzo, A.4    Cillard, P.5    Cillard, J.6
  • 29
    • 0030808843 scopus 로고    scopus 로고
    • Studies on hepatic injury and antioxidant enzyme activities in rat subcellular organelles following in vivo ischemia and reperfusion
    • 29. GUPTA, M., K. DOBASHI, E.L. GREENE, J.K. ORAK & I. SINGH. 1997. Studies on hepatic injury and antioxidant enzyme activities in rat subcellular organelles following in vivo ischemia and reperfusion. Mol. Cell. Biochem. 176: 337-347.
    • (1997) Mol. Cell. Biochem. , vol.176 , pp. 337-347
    • Gupta, M.1    Dobashi, K.2    Greene, E.L.3    Orak, J.K.4    Singh, I.5
  • 31
    • 0020644952 scopus 로고
    • Superoxide radical: An endogenous toxicant
    • 31. FRIDOVICH, I. 1983. Superoxide radical: an endogenous toxicant. Annu. Rev. Pharmacol. Toxico.l 23: 239-257.
    • (1983) Annu. Rev. Pharmacol. Toxico.l , vol.23 , pp. 239-257
    • Fridovich, I.1
  • 32
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: Redox cycling and lipid peroxidation
    • 32. KAPPUS, H. & H. SIES. 1981. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia 37: 1233-1241.
    • (1981) Experientia , vol.37 , pp. 1233-1241
    • Kappus, H.1    Sies, H.2
  • 33
    • 0030936964 scopus 로고    scopus 로고
    • Redox signal transduction: Mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form
    • 33. HIDALGO, E., H. DING & B. DEMPLE. 1997. Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form. Cell 88: 121-129.
    • (1997) Cell , vol.88 , pp. 121-129
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 34
    • 0029152251 scopus 로고
    • Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription
    • 34. HIDALGO, E., J.M. BOLLINGER, JR., T.M. BRADLEY, C.T. WALSH & B. DEMPLE. 1995. Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. J. Biol. Chem. 270: 20908-20914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20908-20914
    • Hidalgo, E.1    Bollinger J.M., Jr.2    Bradley, T.M.3    Walsh, C.T.4    Demple, B.5
  • 35
    • 0028929893 scopus 로고
    • Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli
    • 35. Wu, J., W.R. DUNHAM & B. WEISS. 1995. Overproduction and physical characterization of SoxR, a [2Fe-2S] protein that governs an oxidative response regulon in Escherichia coli. J. Biol. Chem. 270: 10323-10327.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10323-10327
    • Wu, J.1    Dunham, W.R.2    Weiss, B.3
  • 36
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • 36. DING, H., E. HIDALGO & B. DEMPLE. 1996. The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J. Biol. Chem. 271: 33173-33175.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 37
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • 37. GAUDU, P. & B. WEISS. 1996. SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc. Natl. Acad. Sci. USA 93: 10094-10098.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 39
    • 0028049068 scopus 로고
    • An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein
    • 39. HIDALGO, E. & B. DEMPLE. 1994. An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO Journal 13: 138-146.
    • (1994) EMBO Journal , vol.13 , pp. 138-146
    • Hidalgo, E.1    Demple, B.2
  • 40
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • 40. DING, H., E. HIDALGO & B. DEMPLE. 1996. The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J. Biol. Chem. 271: 33173-33175.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 41
    • 0031041391 scopus 로고    scopus 로고
    • Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor
    • 41. HIDALGO, E. & B. DEMPLE. 1997. Spacing of promoter elements regulates the basal expression of the soxS gene and converts SoxR from a transcriptional activator into a repressor. EMBO J. 16: 1056-1065.
    • (1997) EMBO J. , vol.16 , pp. 1056-1065
    • Hidalgo, E.1    Demple, B.2
  • 42
    • 0029796248 scopus 로고    scopus 로고
    • Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein
    • 42. DING, H. & B. DEMPLE. 1996. Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein. Proc. Natl. Acad. Sci. USA 93: 9449-9453.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9449-9453
    • Ding, H.1    Demple, B.2
  • 43
    • 0030844766 scopus 로고    scopus 로고
    • Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation
    • 43. BRADLEY, T.M., E. HIDALGO, V.S. LEAUTAUD, H. DING & B. DEMPLE. 1997. Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation. Nucleic Acids Res. 25: 1469-1475.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1469-1475
    • Bradley, T.M.1    Hidalgo, E.2    Leautaud, V.S.3    Ding, H.4    Demple, B.5
  • 44
    • 0029993477 scopus 로고    scopus 로고
    • Activation of SoxR-dependent transcription in vitro by noncatalytic or NifS-mediated assembly of [2Fe-2S] clusters into apo-SoxR
    • 44. HIDALGO, E. & B. DEMPLE. 1996. Activation of SoxR-dependent transcription in vitro by noncatalytic or NifS-mediated assembly of [2Fe-2S] clusters into apo-SoxR. J. Biol. Chem. 271: 7269-7272.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7269-7272
    • Hidalgo, E.1    Demple, B.2
  • 45
    • 0032497908 scopus 로고    scopus 로고
    • Thiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR
    • 45. DING, H. & B. DEMPLE. 1998. Thiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR. Biochemistry 37: 17280-17286.
    • (1998) Biochemistry , vol.37 , pp. 17280-17286
    • Ding, H.1    Demple, B.2
  • 46
    • 0030912902 scopus 로고    scopus 로고
    • Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
    • 46. HIDALGO, E., H. DING & B. DEMPLE. 1997. Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem Sci 22: 207-210.
    • (1997) Trends Biochem Sci , vol.22 , pp. 207-210
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 47
    • 0031048106 scopus 로고    scopus 로고
    • Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo
    • 47. GAUDU, P., N. MOON & B. WEISS. 1997. Regulation of the soxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo. J. Biol. Chem. 272: 5082-5086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5082-5086
    • Gaudu, P.1    Moon, N.2    Weiss, B.3
  • 48
    • 0030795788 scopus 로고    scopus 로고
    • In vivo kinetics of a redox-regulated transcriptional switch
    • 48. DING, H. & B. DEMPLE. 1997. In vivo kinetics of a redox-regulated transcriptional switch. Proc. Natl. Acad. Sci. USA 94: 8445-8449.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8445-8449
    • Ding, H.1    Demple, B.2
  • 49
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon
    • 49. LIOCHEV, S.I. & I. FRIDOVICH. 1992. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl. Acad. Sci. USA 89: 5892-5896.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 50
    • 0033021117 scopus 로고    scopus 로고
    • Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli
    • 50. KOBAYASHI, K. & S. TAGAWA. 1999. Isolation of reductase for SoxR that governs an oxidative response regulon from Escherichia coli. FEBS Lett. 451: 227-230.
    • (1999) FEBS Lett. , vol.451 , pp. 227-230
    • Kobayashi, K.1    Tagawa, S.2
  • 52
    • 0028924091 scopus 로고
    • Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein
    • 52. ARIZA, R.R., Z. LI, N. RINGSTAD & B. DEMPLE. 1995. Activation of multiple antibiotic resistance and binding of stress-inducible promoters by Escherichia coli Rob protein. J. Bacteriol. 177: 1655-1661.
    • (1995) J. Bacteriol. , vol.177 , pp. 1655-1661
    • Ariza, R.R.1    Li, Z.2    Ringstad, N.3    Demple, B.4
  • 53
    • 0029951890 scopus 로고    scopus 로고
    • Sequence specificity for DNA binding by Escherichia coli SoxS and Rob proteins
    • 53. LI, Z.Y. & B. DEMPLE. 1996. Sequence specificity for DNA binding by Escherichia coli SoxS and Rob proteins. Mol. Microbiol. 20: 937-945.
    • (1996) Mol. Microbiol. , vol.20 , pp. 937-945
    • Li, Z.Y.1    Demple, B.2
  • 54
    • 0025816912 scopus 로고
    • Molecular characterization of the soxRS genes of Escherichia coli: Two genes control a superoxide stress regulon
    • 54. AMÁBILE-CuEVAS, C.F. & B. DEMPLE. 1991. Molecular characterization of the soxRS genes of Escherichia coli: two genes control a superoxide stress regulon. Nucleic Acids Res. 19: 4479-4484.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4479-4484
    • Amábile-Cuevas, C.F.1    Demple, B.2
  • 55
    • 0025809949 scopus 로고
    • Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli
    • 55. Wu, J. & B. WEISS. 1991. Two divergently transcribed genes, soxR and soxS, control a superoxide response regulon of Escherichia coli. J. Bacteriol. 173: 2864-2871.
    • (1991) J. Bacteriol. , vol.173 , pp. 2864-2871
    • Wu, J.1    Weiss, B.2
  • 56
    • 0028358807 scopus 로고
    • SoxS, an activator of superoxide stress genes in Escherichia coli. Purification and interaction with DNA
    • 56. LI, Z. & B. DEMPLE. 1994. SoxS, an activator of superoxide stress genes in Escherichia coli. Purification and interaction with DNA. J. Biol. Chem. 269: 18371-18377.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18371-18377
    • Li, Z.1    Demple, B.2
  • 57
    • 0029671285 scopus 로고    scopus 로고
    • Ambidextrous transcriptional activation by SoxS: Requirement for the C-terminal domain of the RNA polymerase alpha subunit in a subset of the Escherichia coli superoxide-inducible genes
    • 57. JAIR, K.W., W.P. FAWCETT, N. FUJITA, A. ISHIHAMA & R.E.J. WOLF. 1996. Ambidextrous transcriptional activation by SoxS: requirement for the C-terminal domain of the RNA polymerase alpha subunit in a subset of the Escherichia coli superoxide-inducible genes. Mol. Microbiol. 19: 306-317.
    • (1996) Mol. Microbiol. , vol.19 , pp. 306-317
    • Jair, K.W.1    Fawcett, W.P.2    Fujita, N.3    Ishihama, A.4    Wolf, R.E.J.5
  • 58
    • 0028908084 scopus 로고
    • Genetic definition of the Escherichia coli zwf "soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide
    • 58. FAWCETT, W.P. & R.E. WOLF, JR. 1995. Genetic definition of the Escherichia coli zwf "soxbox," the DNA binding site for SoxS-mediated induction of glucose 6-phosphate dehydrogenase in response to superoxide. J. Bacteriol. 177: 1742-1750.
    • (1995) J. Bacteriol. , vol.177 , pp. 1742-1750
    • Fawcett, W.P.1    Wolf R.E., Jr.2
  • 59
    • 0031787969 scopus 로고    scopus 로고
    • Finding DNA regulatory motifs within unaligned noncoding sequences clustered by whole-genome mRNA quantitation
    • 59. ROTH, F.P., J.D. HUGHES, P.W. ESTEP & G.M. CHURCH. 1998. Finding DNA regulatory motifs within unaligned noncoding sequences clustered by whole-genome mRNA quantitation [see comments]. Natl. Biotechnol. 16: 939-945.
    • (1998) Natl. Biotechnol. , vol.16 , pp. 939-945
    • Roth, F.P.1    Hughes, J.D.2    Estep, P.W.3    Church, G.M.4
  • 60
    • 0025833517 scopus 로고
    • Activation of oxidative stress genes by mutations at the soxQ/cfxB/marA locus of Escherichia coli
    • 60. GREENBERG, J.T., J.H. CHOU, P.A. MONACH & B. DEMPLE. 1991. Activation of oxidative stress genes by mutations at the soxQ/cfxB/marA locus of Escherichia coli. J. Bacteriol. 173: 4433-4439.
    • (1991) J. Bacteriol. , vol.173 , pp. 4433-4439
    • Greenberg, J.T.1    Chou, J.H.2    Monach, P.A.3    Demple, B.4
  • 61
    • 0022930671 scopus 로고
    • - is a crucial intermediate in the high quantum yield luminescence of luminol
    • - is a crucial intermediate in the high quantum yield luminescence of luminol. J. Free Rad. Biol. Med. 2: 107-110.
    • (1986) J. Free Rad. Biol. Med. , vol.2 , pp. 107-110
    • Miller, E.K.1    Fridovich, I.2
  • 62
    • 0030055415 scopus 로고    scopus 로고
    • Regulation of the ribA gene encoding GTP cyclohydrolase II by the soxRS locus in Escherichia coli
    • 62. KOH, Y.S., J. CHOIH, J.H. LEE & J.H. ROE. 1996. Regulation of the ribA gene encoding GTP cyclohydrolase II by the soxRS locus in Escherichia coli. Mol. Gen. Genet. 251: 591-598.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 591-598
    • Koh, Y.S.1    Choih, J.2    Lee, J.H.3    Roe, J.H.4
  • 63
    • 0033616612 scopus 로고    scopus 로고
    • Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli
    • 63. LIOCHEV, S.I., A. HAUSLADEN & I. FRIDOVICH. 1999. Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. Proc. Natl. Acad. Sci. USA 96: 3537-3539.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3537-3539
    • Liochev, S.I.1    Hausladen, A.2    Fridovich, I.3
  • 64
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • 64. GREENBERG, J.T., P. MONACH, J.H. CHOU, P.D. JOSEPHY & B. DEMPLE. 1990. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl. Acad. Sci. USA 87: 6181-6185.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 65
    • 0027411681 scopus 로고
    • Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: Positive control of the micF antisense RNA by the soxRS locus
    • 65. CHOU, J.H., J.T. GREENBERG & B. DEMPLE. 1993. Posttranscriptional repression of Escherichia coli OmpF protein in response to redox stress: positive control of the micF antisense RNA by the soxRS locus. J. Bacteriol. 175: 1026-1031.
    • (1993) J. Bacteriol. , vol.175 , pp. 1026-1031
    • Chou, J.H.1    Greenberg, J.T.2    Demple, B.3
  • 67
    • 0029831354 scopus 로고    scopus 로고
    • Overlaps and parallels in the regulation of intrinsic multiple-antibiotic resistance in Escherichia coli
    • 67. MILLER, P.F. & M.C. SULAVIK. 1996. Overlaps and parallels in the regulation of intrinsic multiple-antibiotic resistance in Escherichia coli. Mol. Microbiol. 21: 441-448.
    • (1996) Mol. Microbiol. , vol.21 , pp. 441-448
    • Miller, P.F.1    Sulavik, M.C.2
  • 68
    • 0032439653 scopus 로고    scopus 로고
    • Oxidative stress responses of the yeast Saccharomyces cerevisiae
    • 68. AMIESON, D.J. 1998. Oxidative stress responses of the yeast Saccharomyces cerevisiae. Yeast 14: 1511-1527.
    • (1998) Yeast , vol.14 , pp. 1511-1527
    • Amieson, D.J.1
  • 69
    • 0031717526 scopus 로고    scopus 로고
    • Stress-activated signalling pathways in yeast
    • 69. TOONE, W.M. & N. JONES. 1998. Stress-activated signalling pathways in yeast. Genes Cells 3: 485-498.
    • (1998) Genes Cells , vol.3 , pp. 485-498
    • Toone, W.M.1    Jones, N.2
  • 70
    • 0027440762 scopus 로고
    • Nitric oxide synthase: Function and mechanism
    • 70. MARLETTA, M.A. 1993. Nitric oxide synthase: function and mechanism. Advances in Exp. Med. Biol. 338: 281-284.
    • (1993) Advances in Exp. Med. Biol. , vol.338 , pp. 281-284
    • Marletta, M.A.1
  • 71
    • 0029792562 scopus 로고    scopus 로고
    • Nitric oxide-cyclic GMP signal transduction system
    • 71. HOBBS, A.J. & L.J. IGNARRO. 1996. Nitric oxide-cyclic GMP signal transduction system. Methods in Enzymol. 269: 134-148.
    • (1996) Methods in Enzymol. , vol.269 , pp. 134-148
    • Hobbs, A.J.1    Ignarro, L.J.2
  • 74
    • 0027319211 scopus 로고
    • Potent intracellular oxidative stress exerted by the carcinogen 4-nitroquinoline-N-oxide
    • 74. NUNOSHIBA, T. & B. DEMPLE. 1993. Potent intracellular oxidative stress exerted by the carcinogen 4-nitroquinoline-N-oxide. Cancer Res. 53: 3250-3252.
    • (1993) Cancer Res. , vol.53 , pp. 3250-3252
    • Nunoshiba, T.1    Demple, B.2
  • 75
    • 0028960382 scopus 로고
    • Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages
    • 75. NUNOSHIBA, T., T. DEROJAS-WALKER, S.R. TANNENBAUM & B. DEMPLE. 1995. Roles of nitric oxide in inducible resistance of Escherichia coli to activated murine macrophages. Infection & Immunity 63: 794-798.
    • (1995) Infection & Immunity , vol.63 , pp. 794-798
    • Nunoshiba, T.1    Derojas-Walker, T.2    Tannenbaum, S.R.3    Demple, B.4
  • 78
    • 0032146141 scopus 로고    scopus 로고
    • Complex genetic response of human cells to sub-lethal levels of pure nitric oxide
    • 78. MARQUIS, J.C. & B. DEMPLE. 1998. Complex genetic response of human cells to sub-lethal levels of pure nitric oxide. Cancer Res 58: 3435-3440.
    • (1998) Cancer Res , vol.58 , pp. 3435-3440
    • Marquis, J.C.1    Demple, B.2
  • 79
    • 0030970287 scopus 로고    scopus 로고
    • Approaches to define pathways of redox regulation of a eukaryotic gene: The heme oxygenase 1 example
    • 79. TYRRELL, R.M. 1997. Approaches to define pathways of redox regulation of a eukaryotic gene: the heme oxygenase 1 example. Methods 11: 313-318.
    • (1997) Methods , vol.11 , pp. 313-318
    • Tyrrell, R.M.1
  • 80
    • 0027306121 scopus 로고
    • The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts
    • 80. ALESSI, D.R., C. SMYTHE & S.M. KEYSE. 1993. The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts. Oncogene 8: 2015-2020.
    • (1993) Oncogene , vol.8 , pp. 2015-2020
    • Alessi, D.R.1    Smythe, C.2    Keyse, S.M.3
  • 81
    • 0028929735 scopus 로고
    • Translational repressor activity is equivalent and is quantitatively predicted by in vitro RNA binding for two iron-responsive element-binding proteins, IRP1 and IRP2
    • 81. KIM, H.Y., R.D. KLAUSNER & T.A. ROUAULT. 1995. Translational repressor activity is equivalent and is quantitatively predicted by in vitro RNA binding for two iron-responsive element-binding proteins, IRP1 and IRP2. J. Biol. Chem. 270: 4983-4986.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4983-4986
    • Kim, H.Y.1    Klausner, R.D.2    Rouault, T.A.3
  • 83
    • 0023132858 scopus 로고
    • Bilirubin is an antioxidant of possible physiological importance
    • 83. STOCKER, R., Y. YAMAMOTO, A.F. MCDONAGH, A.N. GLAZER & B. N. AMES. 1987. Bilirubin is an antioxidant of possible physiological importance. Science 235: 1043-1046.
    • (1987) Science , vol.235 , pp. 1043-1046
    • Stocker, R.1    Yamamoto, Y.2    McDonagh, A.F.3    Glazer, A.N.4    Ames, B.N.5
  • 84
    • 0023813118 scopus 로고
    • Chemiluminescence enhancement by trypanocidal drugs and by inhibitors of antioxidant enzymes in Trypanosoma cruzi
    • 84. GIULIVI, C., J.F. TURRENS & A. BOVERIS. 1988. Chemiluminescence enhancement by trypanocidal drugs and by inhibitors of antioxidant enzymes in Trypanosoma cruzi. Mol. Biochem. Parasitol. 30: 243-251.
    • (1988) Mol. Biochem. Parasitol. , vol.30 , pp. 243-251
    • Giulivi, C.1    Turrens, J.F.2    Boveris, A.3
  • 85
    • 0025777585 scopus 로고
    • Superoxide anion and hydrogen peroxide metabolism in soybean embryonic axes during germination
    • 85. PUNTARULO, S., M. GALLEANO, R.A. SANCHEZ & A. BOVERIS. 1991. Superoxide anion and hydrogen peroxide metabolism in soybean embryonic axes during germination. Biochim. Biophys. Acta 1074: 277-283.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 277-283
    • Puntarulo, S.1    Galleano, M.2    Sanchez, R.A.3    Boveris, A.4
  • 86
    • 0015550886 scopus 로고
    • 2 generation in perfused rat liver and the reaction of catalase compound I and hydrogen donors
    • 2 generation in perfused rat liver and the reaction of catalase compound I and hydrogen donors. Arch. Biochem. Biophys. 154: 117-131.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 117-131
    • Oshino, N.1    Chance, B.2    Sies, H.3    Bucher, T.4
  • 88


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