메뉴 건너뛰기




Volumn 8, Issue 1, 2003, Pages 51-56

Thermosensitive phenotype of Escherichia coli mutant lacking NADP+-dependent isocitrate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; ISOCITRATE DEHYDROGENASE (NADP); REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0037275811     PISSN: 13510002     EISSN: None     Source Type: Journal    
DOI: 10.1179/135100003125001251     Document Type: Review
Times cited : (11)

References (43)
  • 1
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. The heat-shock response. Annu Rev Biochem 1986; 55: 1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 3
    • 0021227190 scopus 로고
    • AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress
    • Bochner BR, Lee PC, Wilson SW, Cutler CW, Ames BN. AppppA and related adenylylated nucleotides are synthesized as a consequence of oxidation stress. Cell 1984; 37: 225-232.
    • (1984) Cell , vol.37 , pp. 225-232
    • Bochner, B.R.1    Lee, P.C.2    Wilson, S.W.3    Cutler, C.W.4    Ames, B.N.5
  • 4
    • 0018841837 scopus 로고
    • Transition series metals and sulfhydryl reagents induce the synthesis of four proteins in eukaryotic cells
    • Levinson W, Oppermann H, Jackson J. Transition series metals and sulfhydryl reagents induce the synthesis of four proteins in eukaryotic cells. Biochim Biophys Acta 1980; 606: 170-180.
    • (1980) Biochim. Biophys. Acta , vol.606 , pp. 170-180
    • Levinson, W.1    Oppermann, H.2    Jackson, J.3
  • 5
    • 0018382014 scopus 로고
    • The induction of gene activity in Drosophila by heat shock
    • Ashburner M, Bonner JJ. The induction of gene activity in Drosophila by heat shock. Cell 1979; 17: 241-254.
    • (1979) Cell , vol.17 , pp. 241-254
    • Ashburner, M.1    Bonner, J.J.2
  • 6
    • 0013294002 scopus 로고
    • An oxygen effect for gamma-radiation induction of radiation resistance in yeast
    • Mitchel REJ, Morrison DP. An oxygen effect for gamma-radiation induction of radiation resistance in yeast. Radiat Res 1983; 90: 284-291.
    • (1983) Radiat. Res. , vol.90 , pp. 284-291
    • Mitchel, R.E.J.1    Morrison, D.P.2
  • 7
    • 0020508747 scopus 로고
    • Dietary carcinogens and anticarcinogens. Oxygen radicals and degenerative diseases
    • Ames BN. Dietary carcinogens and anticarcinogens. Oxygen radicals and degenerative diseases. Science 1983; 221: 1256-1264.
    • (1983) Science , vol.221 , pp. 1256-1264
    • Ames, B.N.1
  • 8
    • 0021066303 scopus 로고
    • The possible role of the superoxide ion in the induction of heat-shock and specific proteins in aerobic Drosophila cells during return to normoxia after a period of anaerobiosis
    • Ropp M, Courgeon AM, Calrayrac R, Best-Belpomme M. The possible role of the superoxide ion in the induction of heat-shock and specific proteins in aerobic Drosophila cells during return to normoxia after a period of anaerobiosis. Can J Biochem Cell Biol 1983; 61: 456-461.
    • (1983) Can. J. Biochem. Cell Biol. , vol.61 , pp. 456-461
    • Ropp, M.1    Courgeon, A.M.2    Calrayrac, R.3    Best-Belpomme, M.4
  • 9
    • 0011488224 scopus 로고
    • Induction of glucose-regulated proteins during anaerobic exposure and of heat-shock proteins after reoxygenation
    • Sciandra JJ, Subjeck JR, Hughes CS. Induction of glucose-regulated proteins during anaerobic exposure and of heat-shock proteins after reoxygenation. Proc Natl Acad Sci USA 1984; 81: 4843-4847.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4843-4847
    • Sciandra, J.J.1    Subjeck, J.R.2    Hughes, C.S.3
  • 10
    • 0021837809 scopus 로고
    • Synthesis of heat shock proteins in rat liver after ischemia and hyperthermia
    • Cairo G, Bardella L, Schiaffonati L, Bernelli-Zazzera A. Synthesis of heat shock proteins in rat liver after ischemia and hyperthermia. Hepatology 1985; 5: 357-361.
    • (1985) Hepatology , vol.5 , pp. 357-361
    • Cairo, G.1    Bardella, L.2    Schiaffonati, L.3    Bernelli-Zazzera, A.4
  • 11
    • 0021846801 scopus 로고
    • Superoxide dismutase levels in Chinese hamster ovary cells and ovarian carcinoma cells after hyperthermia or exposure to cycloheximide
    • Loven DP, Leeper DB, Oberley LW. Superoxide dismutase levels in Chinese hamster ovary cells and ovarian carcinoma cells after hyperthermia or exposure to cycloheximide. Cancer Res 1985; 45: 3029-3033.
    • (1985) Cancer Res. , vol.45 , pp. 3029-3033
    • Loven, D.P.1    Leeper, D.B.2    Oberley, L.W.3
  • 12
    • 0004976475 scopus 로고
    • Induction of superoxide dismutase in Escherichia coli by heat shock
    • Privalle CT, Fridovich I. Induction of superoxide dismutase in Escherichia coli by heat shock. Proc Natl Acad Sci USA 1987; 84: 2723-2726.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2723-2726
    • Privalle, C.T.1    Fridovich, I.2
  • 13
    • 0021964203 scopus 로고
    • Pro-oxidant states and tumor promotion
    • Cerutti PA. Pro-oxidant states and tumor promotion. Science 1985; 227: 375-380.
    • (1985) Science , vol.227 , pp. 375-380
    • Cerutti, P.A.1
  • 16
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969; 224: 6049-6055.
    • (1969) J. Biol. Chem. , vol.224 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 17
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H, Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979; 59: 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 19
    • 0018397107 scopus 로고
    • Phosphorylation of isocitrate dehydrogenase of Escherichia coli
    • Garnak M, Reeves HC. Phosphorylation of isocitrate dehydrogenase of Escherichia coli. Science 1979; 203: 1111-1112.
    • (1979) Science , vol.203 , pp. 1111-1112
    • Garnak, M.1    Reeves, H.C.2
  • 20
    • 0021448708 scopus 로고
    • Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308
    • Nimmo GA, Borthwick AC, Holms WH, Nimmo HG. Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308. Eur J Biochem 1984; 141: 401-408.
    • (1984) Eur. J. Biochem. , vol.141 , pp. 401-408
    • Nimmo, G.A.1    Borthwick, A.C.2    Holms, W.H.3    Nimmo, H.G.4
  • 21
    • 0022212761 scopus 로고
    • Compensatory phosphorylation of isocitrate dehydrogenase. A mechanism for adaptation to the intracellular environment
    • LaPorte DC, Thorsness PE, Koshland Jr DE. Compensatory phosphorylation of isocitrate dehydrogenase. A mechanism for adaptation to the intracellular environment. J Biol Chem 1985; 260: 10563-10568.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10563-10568
    • LaPorte, D.C.1    Thorsness, P.E.2    Koshland D.E., Jr.3
  • 22
    • 0020644952 scopus 로고
    • Superoxide radical: An endogenous toxicant
    • Fridovich I. Superoxide radical: an endogenous toxicant. Annu Rev Pharmacol Toxicol 1983; 23: 239-257.
    • (1983) Annu. Rev. Pharmacol. Toxicol. , vol.23 , pp. 239-257
    • Fridovich, I.1
  • 23
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers Jr RF, Sizer IW. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 1952; 195: 33-140.
    • (1952) J. Biol. Chem. , vol.195 , pp. 33-140
    • Beers R.F., Jr.1    Sizer, I.W.2
  • 24
    • 0016272750 scopus 로고
    • Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase
    • Marklund SL, Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 1974; 47: 469-474.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 469-474
    • Marklund, S.L.1    Marklund, G.2
  • 25
    • 0014478046 scopus 로고
    • The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates
    • Pinto RE, Bartley W. The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates. J Biochem (Tokyo) 1969; 112: 109-115.
    • (1969) J. Biochem. (Tokyo) , vol.112 , pp. 109-115
    • Pinto, R.E.1    Bartley, W.2
  • 26
    • 0023852943 scopus 로고
    • Epidermal growth factor rapidly activates the hexose monophosphate shunt in kidney cells
    • Stanton RC, Seifter JL. Epidermal growth factor rapidly activates the hexose monophosphate shunt in kidney cells. Am J Physiol 1988; 254: C267-C271.
    • (1988) Am. J. Physiol. , vol.254
    • Stanton, R.C.1    Seifter, J.L.2
  • 27
    • 0026632930 scopus 로고
    • Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein
    • Jiang ZY, Hunt JV, Wolff SP. Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein. Anal Biochem 1992; 202: 384-389.
    • (1992) Anal. Biochem. , vol.202 , pp. 384-389
    • Jiang, Z.Y.1    Hunt, J.V.2    Wolff, S.P.3
  • 28
    • 0025102226 scopus 로고
    • Determination of carbonyl content in oxidatively modified proteins
    • Levine RL, Garland D, Oliver CN et al. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 1990; 186: 464-478.
    • (1990) Methods Enzymol. , vol.186 , pp. 464-478
    • Levine, R.L.1    Garland, D.2    Oliver, C.N.3
  • 30
    • 0025862421 scopus 로고
    • Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae
    • Wieser R, Adam G, Wagner A et al. Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae. J Biol Chem 1991; 266: 12406-12411.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12406-12411
    • Wieser, R.1    Adam, G.2    Wagner, A.3
  • 33
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae HZ, Chung SJ, Rhee SG. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 1994; 269: 27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 34
    • 0028283815 scopus 로고
    • Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin
    • Kim SJ, Park J-W, Choi WK, Kim IH, Kim K. Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin. Biochem Biophys Res Commun 1994; 201: 8-15.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 8-15
    • Kim, S.J.1    Park, J.-W.2    Choi, W.K.3    Kim, I.H.4    Kim, K.5
  • 35
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methionine sulfoxide residues in proteins
    • Brot N, Weissbach H. Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch Biochem Biophys 1983; 223: 271-281.
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 36
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A 'housekeeping' enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress
    • Kletzien RK, Harris PKW, Foellmi LA. Glucose-6-phosphate dehydrogenase: a 'housekeeping' enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress. FASEB J 1994; 8: 174-181.
    • (1994) FASEB J. , vol.8 , pp. 174-181
    • Kletzien, R.K.1    Harris, P.K.W.2    Foellmi, L.A.3
  • 37
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi PP, Sonati F, Rivi R, Mason P, Grosveld F, Luzzatto L. Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J 1995; 14: 5209-5215.
    • (1995) EMBO J. , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzzatto, L.6
  • 38
    • 0014621744 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver
    • Veech RL, Eggleston LV, Krebs HA. The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem J 1969; 115: 609-619.
    • (1969) Biochem. J. , vol.115 , pp. 609-619
    • Veech, R.L.1    Eggleston, L.V.2    Krebs, H.A.3
  • 41
    • 0020490598 scopus 로고
    • Superoxide radical inhibits catalase
    • Kono Y, Fridovich I. Superoxide radical inhibits catalase. J Biol Chem 1982; 257: 5751-5754.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5751-5754
    • Kono, Y.1    Fridovich, I.2
  • 42
    • 0025057048 scopus 로고
    • Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals
    • Pigeolet E, Corbisier P, Houbion A et al. Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals. Mech Age 1990; 51: 283-297.
    • (1990) Mech. Age , vol.51 , pp. 283-297
    • Pigeolet, E.1    Corbisier, P.2    Houbion, A.3
  • 43
    • 0027970488 scopus 로고
    • Susceptibility of glutathione peroxidase and glutathione reductase to oxidative damage and the protective effect of spin trapping agents
    • Tabatabaie T, Floyd RA. Susceptibility of glutathione peroxidase and glutathione reductase to oxidative damage and the protective effect of spin trapping agents. Arch Biochem Biophys 1994; 314: 112-119.
    • (1994) Arch. Biochem. Biophys. , vol.314 , pp. 112-119
    • Tabatabaie, T.1    Floyd, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.