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Volumn 1623, Issue 1, 2003, Pages 1-5

Oxidative stresses elevate the expression of cytochrome c peroxidase in Saccharomyces cerevisiae

Author keywords

Cytochrome c peroxidase; Hydrogen peroxide; Peroxynitrite; Reactive oxygen species; Saccharomyces cerevisiae

Indexed keywords

CYTOCHROME C PEROXIDASE; FUNGAL DNA; FUNGAL ENZYME; GENOMIC DNA; GLYCEROL; HYDROGEN PEROXIDE; LACTIC ACID; PEROXYNITRITE;

EID: 0042882611     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(03)00151-X     Document Type: Article
Times cited : (36)

References (26)
  • 2
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272:1997;20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 3
    • 0023487170 scopus 로고
    • Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium
    • Storz G., Christman M.F., Sies H., Ames B.N. Spontaneous mutagenesis and oxidative damage to DNA in Salmonella typhimurium. Proc. Natl. Acad. Sci. U. S. A. 84:1987;8917-8921.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 8917-8921
    • Storz, G.1    Christman, M.F.2    Sies, H.3    Ames, B.N.4
  • 5
    • 0030041567 scopus 로고    scopus 로고
    • The molecular defences against reactive oxygen species in yeast
    • Moradas-Ferreira P., Costa V., Piper P., Mager W. The molecular defences against reactive oxygen species in yeast. Mol. Microbiol. 19:1996;651-658.
    • (1996) Mol. Microbiol. , vol.19 , pp. 651-658
    • Moradas-Ferreira, P.1    Costa, V.2    Piper, P.3    Mager, W.4
  • 6
    • 0024266283 scopus 로고
    • Do mitochondrial DNA fragments promote cancer and aging?
    • Richter C. Do mitochondrial DNA fragments promote cancer and aging? FEBS Lett. 241:1988;1-5.
    • (1988) FEBS Lett. , vol.241 , pp. 1-5
    • Richter, C.1
  • 9
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequence of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 10
    • 0019862344 scopus 로고
    • A rapid boiling method for the preparation of bacterial plasmids
    • Holmes D.S., Quigley M. A rapid boiling method for the preparation of bacterial plasmids. Anal. Biochem. 114:1981;193-197.
    • (1981) Anal. Biochem. , vol.114 , pp. 193-197
    • Holmes, D.S.1    Quigley, M.2
  • 11
    • 0020121736 scopus 로고
    • A procedure for the large-scale isolation of highly purified plasmid DNA using alkaline extraction and binding to glass powder
    • Marko M.A., Chipperfield R., Birnboim H.C. A procedure for the large-scale isolation of highly purified plasmid DNA using alkaline extraction and binding to glass powder. Anal. Biochem. 121:1982;382-387.
    • (1982) Anal. Biochem. , vol.121 , pp. 382-387
    • Marko, M.A.1    Chipperfield, R.2    Birnboim, H.C.3
  • 12
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of E. coli
    • Hoffman C., Winston F. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of E. coli. Gene. 57:1987;267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.1    Winston, F.2
  • 14
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H., Fukuda Y., Murata K., Kimura K. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:1983;163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, K.4
  • 15
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R-factor DNA
    • Cohen S.N., Chang A.C.Y., Hsu L. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc. Natl. Acad. Sci. U. S. A. 69:1972;2110-2114.
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, L.3
  • 16
    • 0020645054 scopus 로고
    • One-step gene disruption in yeast
    • Rothstein R.J. One-step gene disruption in yeast. Methods Enzymol. 101:1983;202-211.
    • (1983) Methods Enzymol. , vol.101 , pp. 202-211
    • Rothstein, R.J.1
  • 17
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R.S., Hieter P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:1989;19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 18
    • 0023034916 scopus 로고
    • Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions
    • Myers A.M., Tzagoloff A., Kinney D.M., Lusty C.J. Yeast shuttle and integrative vectors with multiple cloning sites suitable for construction of lacZ fusions. Gene. 45:1986;299-310.
    • (1986) Gene , vol.45 , pp. 299-310
    • Myers, A.M.1    Tzagoloff, A.2    Kinney, D.M.3    Lusty, C.J.4
  • 19
    • 0020645053 scopus 로고
    • Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast
    • Rose M., Bostein D. Construction and use of gene fusions to lacZ (beta-galactosidase) that are expressed in yeast. Methods Enzymol. 101:1983;167-180.
    • (1983) Methods Enzymol. , vol.101 , pp. 167-180
    • Rose, M.1    Bostein, D.2
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0032583570 scopus 로고    scopus 로고
    • Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae
    • Grant C.M., Perrone G., Dawes I.W. Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 253:1998;893-898.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 893-898
    • Grant, C.M.1    Perrone, G.2    Dawes, I.W.3
  • 23
    • 0033578750 scopus 로고    scopus 로고
    • Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae
    • Inoue Y., Matsuda T., Sugiyama K., Izawa S., Kimura A. Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;27002-27009.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27002-27009
    • Inoue, Y.1    Matsuda, T.2    Sugiyama, K.3    Izawa, S.4    Kimura, A.5
  • 24
    • 0029042565 scopus 로고
    • Oxidative stress response in yeast: Effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae
    • Izawa S., Inoue Y., Kimura A. Oxidative stress response in yeast: effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae. FEBS Lett. 368:1995;73-76.
    • (1995) FEBS Lett. , vol.368 , pp. 73-76
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 26
    • 0029844594 scopus 로고    scopus 로고
    • Importance of catalase in the adaptive response to hydrogen peroxide: Analysis of acatalasemic Saccharomyces cerevisiae
    • Izawa S., Inoue Y., Kimura A. Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasemic Saccharomyces cerevisiae. Biochem. J. 320:1996;61-67.
    • (1996) Biochem. J. , vol.320 , pp. 61-67
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.