메뉴 건너뛰기




Volumn 12, Issue 21, 1998, Pages 3431-3441

Bacterial senescence: Stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon

Author keywords

Disulfide bonds; DnaK; OxyR; Protein carbonylation; RpoS; Stationary phase

Indexed keywords

SUPEROXIDE DISMUTASE;

EID: 0032213238     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.21.3431     Document Type: Article
Times cited : (196)

References (60)
  • 1
    • 0028177036 scopus 로고
    • Effects of starvation for exogenous carbon on functional mRNA stability and rate of peptide chain elongation in Escherichia coli
    • Albertson, N.H. and T. Nyström. 1994. Effects of starvation for exogenous carbon on functional mRNA stability and rate of peptide chain elongation in Escherichia coli. FEMS Microbiol. Lett. 117: 181-187.
    • (1994) FEMS Microbiol. Lett. , vol.117 , pp. 181-187
    • Albertson, N.H.1    Nyström, T.2
  • 2
    • 0027083350 scopus 로고
    • A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli
    • Almiron, M., A.J. Link, D. Furlong, and R. Kolter. 1992. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli. Genes & Dev. 6: 2646-2654.
    • (1992) Genes & Dev. , vol.6 , pp. 2646-2654
    • Almiron, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 3
    • 0024514390 scopus 로고
    • Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions
    • Amici, A., R.L. Levine, L. Tsai, and E.R. Stadtman. 1989. Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. J. Biol. Chem. 264: 3341-3346.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3341-3346
    • Amici, A.1    Levine, R.L.2    Tsai, L.3    Stadtman, E.R.4
  • 4
    • 0028812869 scopus 로고
    • Role of rpoS in the regulation of glutathione oxidoreductase (gor) in Escherichia coli
    • Becker-Hapak, M. and A. Eisenstark. 1995. Role of rpoS in the regulation of glutathione oxidoreductase (gor) in Escherichia coli. FEMS Microbiol. Lett. 134: 39-44.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 39-44
    • Becker-Hapak, M.1    Eisenstark, A.2
  • 5
    • 0029160991 scopus 로고
    • A superoxide dismutase mimic protects sodA sodB Escherichia coli against aerobic heating and stationary-phase death
    • Benov, L. and I. Fridovich. 1995. A superoxide dismutase mimic protects sodA sodB Escherichia coli against aerobic heating and stationary-phase death. Arch. Biochem. Biophys. 322: 291-294.
    • (1995) Arch. Biochem. Biophys. , vol.322 , pp. 291-294
    • Benov, L.1    Fridovich, I.2
  • 6
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, B.S. and E.R. Stadtman. 1997. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272: 20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 7
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau, B. 1993. Regulation of the Escherichia coli heat-shock response. Mol. Microbiol. 9: 671-680.
    • (1993) Mol. Microbiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 8
    • 0021930684 scopus 로고
    • Positive control of a regulon for defense against oxidative stress and some heat shock proteins in Salmonella typhimurium
    • Christman, M.F., R.W. Morgan, F.S. Jacobson, and B.N. Ames. 1985. Positive control of a regulon for defense against oxidative stress and some heat shock proteins in Salmonella typhimurium. Cell 41: 753-762.
    • (1985) Cell , vol.41 , pp. 753-762
    • Christman, M.F.1    Morgan, R.W.2    Jacobson, F.S.3    Ames, B.N.4
  • 9
    • 0021039796 scopus 로고
    • Photochemical formation of hydrogen peroxide in surface and ground waters exposed to sunlight
    • Cooper, W.J. and R.G. Zika. 1983. Photochemical formation of hydrogen peroxide in surface and ground waters exposed to sunlight. Science 220: 711-712.
    • (1983) Science , vol.220 , pp. 711-712
    • Cooper, W.J.1    Zika, R.G.2
  • 10
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals
    • Davies, K.J.A. 1987. Protein damage and degradation by oxygen radicals. J. Biol. Chem. 262: 9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 11
    • 0020529486 scopus 로고
    • Inducible repair of oxidative damage in Escherichia coli
    • Demple, B. and J. Halbrook. 1983. Inducible repair of oxidative damage in Escherichia coli. Nature 304: 466-468.
    • (1983) Nature , vol.304 , pp. 466-468
    • Demple, B.1    Halbrook, J.2
  • 13
    • 0023030789 scopus 로고
    • Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase
    • Farber, J.M. and R.L. Levine. 1986. Sequence of a peptide susceptible to mixed-function oxidation. Probable cation binding site in glutamine synthetase. J. Biol. Chem. 261: 4574-4578.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4574-4578
    • Farber, J.M.1    Levine, R.L.2
  • 14
    • 0018263443 scopus 로고
    • The biology of oxygen radicals. the superoxide radical is an agent of oxygen toxicity: Superoxide dismutases provide an important defense
    • Fridovich, I. 1978. The biology of oxygen radicals. The superoxide radical is an agent of oxygen toxicity: Superoxide dismutases provide an important defense. Science 201: 875-880.
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 15
    • 0344710499 scopus 로고
    • Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and aging
    • Fucci, L., C.N. Oliver, M.J. Coon, and E.R. Stadtman. 1983. Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and aging. Proc. Natl Acad. Sci. 80: 1521-1525.
    • (1983) Proc. Natl Acad. Sci. , vol.80 , pp. 1521-1525
    • Fucci, L.1    Oliver, C.N.2    Coon, M.J.3    Stadtman, E.R.4
  • 16
    • 0022344755 scopus 로고
    • Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes
    • Goff, S.A. and A.L. Goldberg. 1985. Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes. Cell 41: 587-595.
    • (1985) Cell , vol.41 , pp. 587-595
    • Goff, S.A.1    Goldberg, A.L.2
  • 17
    • 0029018721 scopus 로고
    • Metabolic source of hydrogen peroxide in aerobically growing Escherichia coli
    • Gonzalez-Flecha, B. and B. Demple. 1995. Metabolic source of hydrogen peroxide in aerobically growing Escherichia coli. J. Biol. Chem. 270: 13681-13687.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13681-13687
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 18
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg, J.T., P. Monach, J.H. Chou, P.D. Josephy, and B. Demple. 1990. Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc. Natl. Acad. Sci. 87: 6181-6185.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 19
    • 0001241680 scopus 로고    scopus 로고
    • Function and regulation of the heat shock proteins
    • (ed. F.C. Neidhardt), ASM Press, Washington, D.C.
    • Gross, C.A. 1996. Function and regulation of the heat shock proteins. In Escherichia coli and Salmonella: Cellular and molecular biology (ed. F.C. Neidhardt), pp. 1382-1399. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 1382-1399
    • Gross, C.A.1
  • 20
    • 84908739973 scopus 로고
    • Superoxide dismutase, catalase and glutathione peroxidase: Solutions to the problems of living with oxygen
    • Halliwell, B. 1974. Superoxide dismutase, catalase and glutathione peroxidase: Solutions to the problems of living with oxygen. New Phytol. 73: 1075-1086.
    • (1974) New Phytol. , vol.73 , pp. 1075-1086
    • Halliwell, B.1
  • 21
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell, B. and J.M.C. Gutteridge. 1984. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219: 1-14.
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 22
    • 0027509821 scopus 로고
    • Survival of hunger and stress: The role of rpoS in early stationary phase gene regulation in E. coli
    • Hengge-Aronis, R. 1993. Survival of hunger and stress: The role of rpoS in early stationary phase gene regulation in E. coli. Cell 72: 165-168.
    • (1993) Cell , vol.72 , pp. 165-168
    • Hengge-Aronis, R.1
  • 23
    • 0022492626 scopus 로고
    • Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiology
    • Ito, K., Y. Akiyama, T. Yura, and K. Shiba. 1986. Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiology. J. Bacteriol. 167: 201-204.
    • (1986) J. Bacteriol. , vol.167 , pp. 201-204
    • Ito, K.1    Akiyama, Y.2    Yura, T.3    Shiba, K.4
  • 25
    • 0026035207 scopus 로고
    • Role of RpoH, a heat shock regulator protein, in Escherichia coli carbon starvation protein synthesis and survival
    • Jenkins, D.E., E.A. Auger, and A. Matin. 1991. Role of RpoH, a heat shock regulator protein, in Escherichia coli carbon starvation protein synthesis and survival. J. Bacteriol. 173: 1992-1996.
    • (1991) J. Bacteriol. , vol.173 , pp. 1992-1996
    • Jenkins, D.E.1    Auger, E.A.2    Matin, A.3
  • 26
    • 0027383520 scopus 로고
    • The stationary phase of the bacterial life cycle
    • Kolter, R., D.A. Siegele, and A. Tormo. 1993. The stationary phase of the bacterial life cycle. Annu. Rev. Microbiol. 47: 855-874.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 855-874
    • Kolter, R.1    Siegele, D.A.2    Tormo, A.3
  • 27
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary phase gene expression in Escherichia coli
    • Lange, R. and R. Hengge-Aronis. 1991. Identification of a central regulator of stationary phase gene expression in Escherichia coli. Mol. Microbiol. 5: 49-59.
    • (1991) Mol. Microbiol. , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 28
    • 0021100174 scopus 로고
    • Oxidative modification of glutamine synthetase
    • Levine, R.L. 1983. Oxidative modification of glutamine synthetase. J. Biol. Chem. 258: 11823-11827.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11823-11827
    • Levine, R.L.1
  • 29
    • 0030449173 scopus 로고    scopus 로고
    • Methionine residues as endogenous antioxidants in proteins. Proc
    • Levine, R.L., L. Mosoni, B.S. Berlett, and E.R. Stadtman. 1996. Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. 93: 15036-15040.
    • (1996) Natl. Acad. Sci. , vol.93 , pp. 15036-15040
    • Levine, R.L.1    Mosoni, L.2    Berlett, B.S.3    Stadtman, E.R.4
  • 30
    • 0026661893 scopus 로고
    • A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance
    • Li, C. and S. Clarke. 1992. A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance. Proc. Natl. Acad. Sci. 89: 9885-9889.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 9885-9889
    • Li, C.1    Clarke, S.2
  • 31
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez, A. and R. Kolter. 1997. Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J. Bacteriol. 179: 5188-5194.
    • (1997) J. Bacteriol. , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 32
    • 0025785253 scopus 로고
    • The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli
    • McCann, M.P., J.P. Kidwell, and A. Matin. 1991. The putative sigma factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli. J. Bacteriol. 173: 4188-4194.
    • (1991) J. Bacteriol. , vol.173 , pp. 4188-4194
    • McCann, M.P.1    Kidwell, J.P.2    Matin, A.3
  • 33
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • Miller, J. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 34
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
    • Moskovitz, J., M.A. Rahman, J. Strassman, S.O. Yancey, S.R. Kushner, N. Brot, and H. Weissbach. 1995. Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage. J. Bacteriol. 177: 502-507.
    • (1995) J. Bacteriol. , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6    Weissbach, H.7
  • 35
    • 0014010845 scopus 로고
    • The release of enzymes by osmotic shock from Escherichia coli in exponential phase
    • Nossal, N.G. and L.A. Heppel. 1966. The release of enzymes by osmotic shock from Escherichia coli in exponential phase. J. Biol. Chem. 241: 3055-3062.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3055-3062
    • Nossal, N.G.1    Heppel, L.A.2
  • 36
    • 0028335964 scopus 로고
    • The glucose starvation stimulon of Escherichia coli: Induced and repressed synthesis of enzymes of central metabolic pathways and the role of acetyl phosphate in gene expression and starvation survival
    • Nyström, T. 1994. The glucose starvation stimulon of Escherichia coli: Induced and repressed synthesis of enzymes of central metabolic pathways and the role of acetyl phosphate in gene expression and starvation survival. Mol. Microbiol. 12: 833-843.
    • (1994) Mol. Microbiol. , vol.12 , pp. 833-843
    • Nyström, T.1
  • 37
    • 0029560549 scopus 로고
    • The glucose-starvation stimulon of Escherichia coli: Role of integration host factor in starvation survival and growth-phase-dependent proteins synthesis
    • _. 1995. The glucose-starvation stimulon of Escherichia coli: Role of integration host factor in starvation survival and growth-phase-dependent proteins synthesis. J. Bacteriol. 177: 5707-5710.
    • (1995) J. Bacteriol. , vol.177 , pp. 5707-5710
  • 38
    • 0026526320 scopus 로고
    • Cloning, mapping and nucleotide sequencing of a gene encoding a universal stress protein in Escherichia coli
    • Nyström, T. and F.C. Neidhardt. 1992. Cloning, mapping and nucleotide sequencing of a gene encoding a universal stress protein in Escherichia coli. Mol. Microbiol. 6: 3187-3198.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3187-3198
    • Nyström, T.1    Neidhardt, F.C.2
  • 39
    • 0030035132 scopus 로고    scopus 로고
    • Bacterial defense against aging: Role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis
    • Nyström, T., C. Larsson, and L. Gustafsson. 1996. Bacterial defense against aging: Role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. EMBO J. 15: 3219-3228.
    • (1996) EMBO J. , vol.15 , pp. 3219-3228
    • Nyström, T.1    Larsson, C.2    Gustafsson, L.3
  • 40
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrel, P.H. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrel, P.H.1
  • 41
    • 0024709959 scopus 로고
    • Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation
    • Parsell, D.A. and R.T. Sauer. 1989. Induction of a heat shock-like response by unfolded protein in Escherichia coli: Dependence on protein level not protein degradation. Genes & Dev. 3: 1226-1232.
    • (1989) Genes & Dev. , vol.3 , pp. 1226-1232
    • Parsell, D.A.1    Sauer, R.T.2
  • 43
    • 0023108239 scopus 로고
    • Fate of superoxide in coastal sea water
    • Petasne, R.G. and R.G. Zika. 1987. Fate of superoxide in coastal sea water. Nature 325: 516-518.
    • (1987) Nature , vol.325 , pp. 516-518
    • Petasne, R.G.1    Zika, R.G.2
  • 44
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz, W.A., F. Åslund, A. Holmgren, and J. Beckwith. 1997. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272: 15661-15667.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Åslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 45
    • 0021702095 scopus 로고
    • Role of protein synthesis in the survival of carbon-starved Escherichia coli K-12
    • Reeve, C.A., A.T. Bockman, and A. Matin. 1984. Role of protein synthesis in the survival of carbon-starved Escherichia coli K-12. J. Bacteriol. 160: 1041-1046.
    • (1984) J. Bacteriol. , vol.160 , pp. 1041-1046
    • Reeve, C.A.1    Bockman, A.T.2    Matin, A.3
  • 46
    • 0025305991 scopus 로고
    • Metal-catalysed oxidation of Escherichia coli glutamine synthetase: Correlation of structural and functional changes
    • Rivett, A.J. and R.L. Levine. 1990. Metal-catalysed oxidation of Escherichia coli glutamine synthetase: Correlation of structural and functional changes. Arch. Biochem. Biophys. 278: 26-34.
    • (1990) Arch. Biochem. Biophys. , vol.278 , pp. 26-34
    • Rivett, A.J.1    Levine, R.L.2
  • 48
    • 0024603522 scopus 로고
    • Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product
    • Sak, B.D., A. Eisenstark, and D. Touati. 1989. Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product. Proc. Natl. Acad. Sci. 86: 3271-3275.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 3271-3275
    • Sak, B.D.1    Eisenstark, A.2    Touati, D.3
  • 50
    • 0025633154 scopus 로고
    • Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation
    • Spence, J., A. Cegielska, and C. Georgopoulos. 1990. Role of Escherichia coli heat shock proteins DnaK and HtpG (C62.5) in response to nutritional deprivation. J. Bacteriol. 172: 7157-7166.
    • (1990) J. Bacteriol. , vol.172 , pp. 7157-7166
    • Spence, J.1    Cegielska, A.2    Georgopoulos, C.3
  • 51
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman, E.R. 1992. Protein oxidation and aging. Science 257: 1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 52
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit, J., E. Cabiscol, and J. Ros. 1998. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273: 3027-3032.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 53
    • 0025369726 scopus 로고
    • soxR, a locus governing a superoxide response regulon in Escherichia coli K-12
    • Tsaneva, I.R. and B. Weiss. 1990. soxR, a locus governing a superoxide response regulon in Escherichia coli K-12. J. Bacteriol. 172: 4197-4205.
    • (1990) J. Bacteriol. , vol.172 , pp. 4197-4205
    • Tsaneva, I.R.1    Weiss, B.2
  • 55
    • 0025328743 scopus 로고
    • Ribosomes as sensors of heat and cold shock in Escherichia coli
    • VanBogelen, R.A. and F.C. Neidhardt. 1990. Ribosomes as sensors of heat and cold shock in Escherichia coli. Proc. Natl. Acad. Sci. 87: 5589-5593.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 5589-5593
    • Vanbogelen, R.A.1    Neidhardt, F.C.2
  • 56
    • 0025648952 scopus 로고
    • Gene-protein database of Escherichia coli K-12: Edition 3
    • VanBogelen, R.A., M.E. Hutton, and F.C. Neidhardt. 1990. Gene-protein database of Escherichia coli K-12: Edition 3. Electrophoresis 11: 1131-1166.
    • (1990) Electrophoresis , vol.11 , pp. 1131-1166
    • VanBogelen, R.A.1    Hutton, M.E.2    Neidhardt, F.C.3
  • 57
    • 0026074553 scopus 로고
    • Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII
    • Von Ossowski, I., M.R. Melvey, P.A. Leco, A. Borys, and P.C. Loewen. 1991. Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J. Bacteriol. 173: 514-520.
    • (1991) J. Bacteriol. , vol.173 , pp. 514-520
    • Von Ossowski, I.1    Melvey, M.R.2    Leco, P.A.3    Borys, A.4    Loewen, P.C.5
  • 58
    • 0028109191 scopus 로고
    • Superoxide dismutase, aging, and degenerative disease
    • Warner, H.R. 1994. Superoxide dismutase, aging, and degenerative disease. Free Radicals Biol. Med. 17: 249-258.
    • (1994) Free Radicals Biol. Med. , vol.17 , pp. 249-258
    • Warner, H.R.1
  • 59
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan, L.J., R.L. Levine, and R.S. Sohal. 1997. Oxidative damage during aging targets mitochondrial aconitase. Proc. Natl. Acad. Sci. 94: 11168-11172.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 11168-11172
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 60
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., F. Åslund, and G. Storz. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Åslund, F.2    Storz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.