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Volumn 735, Issue 1-2, 2012, Pages 1-11

Intervention of glutathione in pre-mutagenic catechol-mediated DNA damage in the presence of copper(II) ions

Author keywords

Catechol pro oxidant; DAPI fluorescent probe; DNA hairpin molecular beacon; DNA melting determination; Glutathione antioxidant; Reactive oxygen species

Indexed keywords

8 HYDROXYGUANINE; ADENINE; CATECHOL; COPPER ION; CYTOSINE; DOUBLE STRANDED DNA; FLUORESCENT DYE; GLUTATHIONE; GUANOSINE; OLIGONUCLEOTIDE; REACTIVE OXYGEN METABOLITE; SEMIQUINONE; THYMIDINE;

EID: 84863008635     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2012.05.005     Document Type: Article
Times cited : (42)

References (81)
  • 2
    • 78149407246 scopus 로고    scopus 로고
    • Oxidative stress in diabetes mellitus
    • Moussa S.A. Oxidative stress in diabetes mellitus. Romanian J Biophys 2008, 18:225-236.
    • (2008) Romanian J Biophys , vol.18 , pp. 225-236
    • Moussa, S.A.1
  • 3
    • 0347753692 scopus 로고    scopus 로고
    • Oxidative stress as a therapeutic target in diabetes: revisiting the controversy
    • Wiernsperger N.F. Oxidative stress as a therapeutic target in diabetes: revisiting the controversy. Diabetes Metab 2003, 29:579-585.
    • (2003) Diabetes Metab , vol.29 , pp. 579-585
    • Wiernsperger, N.F.1
  • 7
    • 43949102806 scopus 로고    scopus 로고
    • Oxidative stress and coronary heart disease
    • Tardif J.-C. Oxidative stress and coronary heart disease. Cardiol. Rounds 2003, 7.
    • (2003) Cardiol. Rounds , vol.7
    • Tardif, J.-C.1
  • 8
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W.R. Oxidative stress hypothesis in Alzheimer's disease. Free Radic. Biol. Med. 1997, 23:134-147.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 10
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Yves C. Oxidative stress and Alzheimer disease. Am. J. Clin. Nutr. 2000, 71:621S-629S.
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Yves, C.1
  • 11
    • 70449113626 scopus 로고    scopus 로고
    • Oxidative stress and Parkinson's disease: electrochemical behavior of hydrogen peroxide in aqueous sodium chloride
    • Krishnan C.V., Garnett M., Chu B. Oxidative stress and Parkinson's disease: electrochemical behavior of hydrogen peroxide in aqueous sodium chloride. Int. J. Electrochem. Sci. 2008, 3:1348-1363.
    • (2008) Int. J. Electrochem. Sci. , vol.3 , pp. 1348-1363
    • Krishnan, C.V.1    Garnett, M.2    Chu, B.3
  • 13
    • 30344475717 scopus 로고    scopus 로고
    • Free radicals and oxidative stress in neurodegenerative diseases: relevance of dietary antioxidants
    • Singh R.P., Sharad S., Kapur S. Free radicals and oxidative stress in neurodegenerative diseases: relevance of dietary antioxidants. JIACM 2004, 5:218-225.
    • (2004) JIACM , vol.5 , pp. 218-225
    • Singh, R.P.1    Sharad, S.2    Kapur, S.3
  • 14
    • 0035172345 scopus 로고    scopus 로고
    • Oxidative stress in chronic rental failure
    • Galle J. Oxidative stress in chronic rental failure. Nephrol. Dial. Transplant. 2001, 16:2135-2137.
    • (2001) Nephrol. Dial. Transplant. , vol.16 , pp. 2135-2137
    • Galle, J.1
  • 16
    • 33846331650 scopus 로고    scopus 로고
    • Oxidative stress and cancer: have we moved forward?
    • Halliwell B. Oxidative stress and cancer: have we moved forward?. Biochem. J. 2007, 401:1-11.
    • (2007) Biochem. J. , vol.401 , pp. 1-11
    • Halliwell, B.1
  • 17
    • 20444370621 scopus 로고    scopus 로고
    • Oxidative stress: a novel strategy in cancer treatment
    • Tandon V.R., Sharma S., Mahajan A., Bardi G.H. Oxidative stress: a novel strategy in cancer treatment. JK Sci. 2005, 7:1-3.
    • (2005) JK Sci. , vol.7 , pp. 1-3
    • Tandon, V.R.1    Sharma, S.2    Mahajan, A.3    Bardi, G.H.4
  • 18
    • 80051723535 scopus 로고    scopus 로고
    • The identification of protein biomarkers for oxidative stress in Down syndrome
    • Perluigi M., Butterfield D.A. The identification of protein biomarkers for oxidative stress in Down syndrome. Expert Rev. Proteomics 2011, 8:427-429.
    • (2011) Expert Rev. Proteomics , vol.8 , pp. 427-429
    • Perluigi, M.1    Butterfield, D.A.2
  • 19
    • 33847349325 scopus 로고    scopus 로고
    • Oxidative stress: a bridge between Down's syndrome and Alzheimer's disease
    • Zana M., Janka Z., Kalman J. Oxidative stress: a bridge between Down's syndrome and Alzheimer's disease. Neurobiol. Aging 2007, 28:648-676.
    • (2007) Neurobiol. Aging , vol.28 , pp. 648-676
    • Zana, M.1    Janka, Z.2    Kalman, J.3
  • 20
    • 15244348759 scopus 로고    scopus 로고
    • Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism
    • James S.J., Cutler P., Melnyk S., Jernigan S., Janak L., Gaylor D.W., Neubrander J.A. Metabolic biomarkers of increased oxidative stress and impaired methylation capacity in children with autism. Am. J. Clin. Nutr. 2004, 80:1611-1617.
    • (2004) Am. J. Clin. Nutr. , vol.80 , pp. 1611-1617
    • James, S.J.1    Cutler, P.2    Melnyk, S.3    Jernigan, S.4    Janak, L.5    Gaylor, D.W.6    Neubrander, J.A.7
  • 22
    • 25144482448 scopus 로고    scopus 로고
    • Novel mechanisms of natural antioxidant compounds in biological systems: involvement of glutathione and glutathione-related enzymes
    • Masella R., Di Benedetto R., Vari R., Filesi C., Giovannini C. Novel mechanisms of natural antioxidant compounds in biological systems: involvement of glutathione and glutathione-related enzymes. J. Nutr. Biochem. 2005, 16:577-586.
    • (2005) J. Nutr. Biochem. , vol.16 , pp. 577-586
    • Masella, R.1    Di Benedetto, R.2    Vari, R.3    Filesi, C.4    Giovannini, C.5
  • 23
    • 0036867895 scopus 로고    scopus 로고
    • Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions and methods for their quantification
    • Kohen R., Nyska A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions and methods for their quantification. Toxicol. Pathol. 2002, 30:620-650.
    • (2002) Toxicol. Pathol. , vol.30 , pp. 620-650
    • Kohen, R.1    Nyska, A.2
  • 24
    • 84862982929 scopus 로고    scopus 로고
    • Detection of oxidative stress biomarkers using functional gold nanoparticles
    • Springer Sci. Publ., New York, E. Matijevic (Ed.)
    • Hepel M., Stobiecka M. Detection of oxidative stress biomarkers using functional gold nanoparticles. Fine Particles in Medicine and Pharmacy 2012, 241-291. Springer Sci. Publ., New York. E. Matijevic (Ed.).
    • (2012) Fine Particles in Medicine and Pharmacy , pp. 241-291
    • Hepel, M.1    Stobiecka, M.2
  • 25
    • 3042812485 scopus 로고    scopus 로고
    • Nanogravimetric study of templated copper deposition in ion-channels of self-assembled glutathione films on gold piezoelectrodes
    • Hepel M., Tewksbury E. Nanogravimetric study of templated copper deposition in ion-channels of self-assembled glutathione films on gold piezoelectrodes. Electrochim. Acta 2004, 49:3827-3840.
    • (2004) Electrochim. Acta , vol.49 , pp. 3827-3840
    • Hepel, M.1    Tewksbury, E.2
  • 26
    • 77955332430 scopus 로고    scopus 로고
    • Resonance elastic light scattering (RELS) spectroscopy of fast non-Langmuirian ligand-exchange in glutathione-induced gold nanoparticle assembly
    • Stobiecka M., Coopersmith K., Hepel M. Resonance elastic light scattering (RELS) spectroscopy of fast non-Langmuirian ligand-exchange in glutathione-induced gold nanoparticle assembly. J. Colloid Interface Sci. 2010, 350:168-177.
    • (2010) J. Colloid Interface Sci. , vol.350 , pp. 168-177
    • Stobiecka, M.1    Coopersmith, K.2    Hepel, M.3
  • 29
    • 0035211211 scopus 로고    scopus 로고
    • Chemical properties of catechols and their molecular modes of toxic action in cells, from microorganisms to mammals
    • Schweigert N., Zehnder A.J.B., Eggen R.I.L. Chemical properties of catechols and their molecular modes of toxic action in cells, from microorganisms to mammals. Environ. Microbiol. 2001, 3:81-91.
    • (2001) Environ. Microbiol. , vol.3 , pp. 81-91
    • Schweigert, N.1    Zehnder, A.J.B.2    Eggen, R.I.L.3
  • 31
    • 84872497435 scopus 로고    scopus 로고
    • Note
    • No P7896 Pyrocatechol, in: MSDS effective: 2.16.2006.
  • 37
    • 0023100690 scopus 로고
    • Formation of glutathione-conjugated semiquinones by the reaction of quinones with glutathione: an ESR study
    • Takahashi N., Schreiber J., Fischer V., Mason R.P. Formation of glutathione-conjugated semiquinones by the reaction of quinones with glutathione: an ESR study. Arch. Biochem. Biophys. Res. Commun. 1987, 252:41-48.
    • (1987) Arch. Biochem. Biophys. Res. Commun. , vol.252 , pp. 41-48
    • Takahashi, N.1    Schreiber, J.2    Fischer, V.3    Mason, R.P.4
  • 38
    • 0031041078 scopus 로고    scopus 로고
    • Human class Mu glutathione transferases, in particular isoenzyme M2-2, catalyze detoxication of the dopamine metabolite aminochromel
    • Segura-Aguilar J., Baez S., Widersten M., Welch C.J., Mannervik B. Human class Mu glutathione transferases, in particular isoenzyme M2-2, catalyze detoxication of the dopamine metabolite aminochromel. J. Biol. Chem. 1997, 272:5727-5731.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5727-5731
    • Segura-Aguilar, J.1    Baez, S.2    Widersten, M.3    Welch, C.J.4    Mannervik, B.5
  • 39
    • 48649105157 scopus 로고    scopus 로고
    • Predicting how polyphenol antioxidants prevent DNA damage by binding to iron
    • Perron N.R., Hodges J.N., Jenkins M., Brumaghim J.L. Predicting how polyphenol antioxidants prevent DNA damage by binding to iron. Inorg. Chem. 2008, 47:6153-6161.
    • (2008) Inorg. Chem. , vol.47 , pp. 6153-6161
    • Perron, N.R.1    Hodges, J.N.2    Jenkins, M.3    Brumaghim, J.L.4
  • 40
    • 0032581569 scopus 로고    scopus 로고
    • Distinct mechanisms of site-specific DNA damage induced by endogenous reductants in the presence of iron(III) and copper(II)
    • Oikawa S., Kawanishi S. Distinct mechanisms of site-specific DNA damage induced by endogenous reductants in the presence of iron(III) and copper(II). Biochim. Biophys. Acta 1998, 1399:19-30.
    • (1998) Biochim. Biophys. Acta , vol.1399 , pp. 19-30
    • Oikawa, S.1    Kawanishi, S.2
  • 42
    • 3543050047 scopus 로고    scopus 로고
    • Phenol and catechol induce prehemolytic and hemolytic changes in human erythrocytes
    • Bukowska B., Kowalska S. Phenol and catechol induce prehemolytic and hemolytic changes in human erythrocytes. Toxycol. Lett. 2004, 152:73-84.
    • (2004) Toxycol. Lett. , vol.152 , pp. 73-84
    • Bukowska, B.1    Kowalska, S.2
  • 43
    • 13444270668 scopus 로고    scopus 로고
    • Early administration of entacapone prevents levodopa-induced motor fluctuations in hemiparkinsonian rats
    • Marin C., Aguilar E., Bonastre M., Tolosa E., Obeso J.A. Early administration of entacapone prevents levodopa-induced motor fluctuations in hemiparkinsonian rats. Exp. Neurol. 2005, 192:184-193.
    • (2005) Exp. Neurol. , vol.192 , pp. 184-193
    • Marin, C.1    Aguilar, E.2    Bonastre, M.3    Tolosa, E.4    Obeso, J.A.5
  • 44
    • 0003165544 scopus 로고    scopus 로고
    • Antioxidants: carcinogenic and chemopreventive properties
    • Elsevier Sci., Amsterdam
    • Ito N., Hirose M., Imaida K. Antioxidants: carcinogenic and chemopreventive properties. Encyclopedia of Cancer 1997, Elsevier Sci., Amsterdam, pp. 89-101.
    • (1997) Encyclopedia of Cancer , pp. 89-101
    • Ito, N.1    Hirose, M.2    Imaida, K.3
  • 45
    • 66249145446 scopus 로고    scopus 로고
    • Involvement of DNA conformational change induced by rearrangement of copper-coordination geometry in oxidative DNA damages caused by copper and dopamine
    • Ando M., Ueda K., Makino R., Nishino Y., Nishida H., Toda C., Okamoto Y., Kojima N. Involvement of DNA conformational change induced by rearrangement of copper-coordination geometry in oxidative DNA damages caused by copper and dopamine. J. Health Sci. 2009, 55:319-323.
    • (2009) J. Health Sci. , vol.55 , pp. 319-323
    • Ando, M.1    Ueda, K.2    Makino, R.3    Nishino, Y.4    Nishida, H.5    Toda, C.6    Okamoto, Y.7    Kojima, N.8
  • 51
    • 0024458564 scopus 로고
    • Hydroxyl free radical is not the main active species in site-specific DNA damage induced by copper(II) in and hydrogen peroxide
    • Yamamoto K., Kawanishi S. Hydroxyl free radical is not the main active species in site-specific DNA damage induced by copper(II) in and hydrogen peroxide. J. Biol. Chem. 1989, 264:15435-15440.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15435-15440
    • Yamamoto, K.1    Kawanishi, S.2
  • 52
    • 34547686141 scopus 로고    scopus 로고
    • Quantitative determination of DNA-ligand binding using fluorescence spectroscopy
    • Healy E.F. Quantitative determination of DNA-ligand binding using fluorescence spectroscopy. J. Chem. Educ. 2007, 84:1304-1307.
    • (2007) J. Chem. Educ. , vol.84 , pp. 1304-1307
    • Healy, E.F.1
  • 53
    • 0027535529 scopus 로고
    • Binding of 4',6-diamidino-2-phenylindole (DAPI) to AT regions of DNA: evidence for an allosteric conformational change
    • Eriksson S., Kim S.K., Kubista M., Norden B. Binding of 4',6-diamidino-2-phenylindole (DAPI) to AT regions of DNA: evidence for an allosteric conformational change. Biochemistry 1993, 32:2987-2998.
    • (1993) Biochemistry , vol.32 , pp. 2987-2998
    • Eriksson, S.1    Kim, S.K.2    Kubista, M.3    Norden, B.4
  • 55
    • 0024371196 scopus 로고
    • Binding of 4',6-diamidino-2-phenylindole (DAPI) to GC and mixed sequences in DNA: intercalation of a classical groove-binding molecule
    • Wilson W.D., Tanious F.A., Barton H.J., Strekowski L., Boykin D.W. Binding of 4',6-diamidino-2-phenylindole (DAPI) to GC and mixed sequences in DNA: intercalation of a classical groove-binding molecule. JACS 1989, 111:5008-5010.
    • (1989) JACS , vol.111 , pp. 5008-5010
    • Wilson, W.D.1    Tanious, F.A.2    Barton, H.J.3    Strekowski, L.4    Boykin, D.W.5
  • 57
    • 0025022218 scopus 로고
    • A fluorescence study of the binding of Hoest 33258 and DAPI to halogenated DNAs
    • Härd T., Fan P., Kearns D.R. A fluorescence study of the binding of Hoest 33258 and DAPI to halogenated DNAs. Photochem. Photobiol. 1990, 51:77-86.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 77-86
    • Härd, T.1    Fan, P.2    Kearns, D.R.3
  • 58
    • 0141447366 scopus 로고    scopus 로고
    • DNA binding properties of DAPI (4',6-diamino-2-phenylindole) analogs having an imidazole ring or a tetrahydropyrimidine ring: groove-binding and intercalation
    • Kubota Y., Kubota K., Tani S. DNA binding properties of DAPI (4',6-diamino-2-phenylindole) analogs having an imidazole ring or a tetrahydropyrimidine ring: groove-binding and intercalation. Nucl. Acids Symp. Ser. 2000, 44:53-54.
    • (2000) Nucl. Acids Symp. Ser. , vol.44 , pp. 53-54
    • Kubota, Y.1    Kubota, K.2    Tani, S.3
  • 59
    • 0036630078 scopus 로고    scopus 로고
    • DAPI binding to the DNA minor groove: a continuum solvent analysis
    • Pineda De Castro L.F., Zacharias M. DAPI binding to the DNA minor groove: a continuum solvent analysis. J. Mol. Recogn. 2002, 15:209-220.
    • (2002) J. Mol. Recogn. , vol.15 , pp. 209-220
    • Pineda De Castro, L.F.1    Zacharias, M.2
  • 60
    • 38949127619 scopus 로고    scopus 로고
    • Dynamics in the DNA recognition by DAPI: exploration of the various binding modes
    • Banerjee D., Pal S.K. Dynamics in the DNA recognition by DAPI: exploration of the various binding modes. J. Phys. Chem. B 2008, 112:1016-1021.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 1016-1021
    • Banerjee, D.1    Pal, S.K.2
  • 61
    • 0029731421 scopus 로고    scopus 로고
    • DNA melting investigated by differential scanning calorimetry and Raman spectroscopy
    • Duguid J.G., Bloomfield V.A., Benevides J.M., Thomas G.J. DNA melting investigated by differential scanning calorimetry and Raman spectroscopy. Biophys. J. 1996, 71:3350-3360.
    • (1996) Biophys. J. , vol.71 , pp. 3350-3360
    • Duguid, J.G.1    Bloomfield, V.A.2    Benevides, J.M.3    Thomas, G.J.4
  • 62
    • 0034897760 scopus 로고    scopus 로고
    • Site specificity and mechanism of oxidative DNA damage induced by carcinogenic catechol
    • Oikawa S., Hirosawa I., Hirakawa K., Kawanishi S. Site specificity and mechanism of oxidative DNA damage induced by carcinogenic catechol. Carcinogenesis 2001, 22:1239-1245.
    • (2001) Carcinogenesis , vol.22 , pp. 1239-1245
    • Oikawa, S.1    Hirosawa, I.2    Hirakawa, K.3    Kawanishi, S.4
  • 63
    • 17644400526 scopus 로고    scopus 로고
    • Sequence-specific DNA damage by reactive oxygen species: implications for carcinogenesis and aging
    • Oikawa S. Sequence-specific DNA damage by reactive oxygen species: implications for carcinogenesis and aging. Environ. Health Prev. Med. 2005, 10:65-71.
    • (2005) Environ. Health Prev. Med. , vol.10 , pp. 65-71
    • Oikawa, S.1
  • 64
    • 0036569113 scopus 로고    scopus 로고
    • N-acetylcysteine in acute cardiology: 10 years later
    • Sochman J. N-acetylcysteine in acute cardiology: 10 years later. J. Am. Coll. Cardiol. 2002, 39:1422-1428.
    • (2002) J. Am. Coll. Cardiol. , vol.39 , pp. 1422-1428
    • Sochman, J.1
  • 65
    • 70349333095 scopus 로고    scopus 로고
    • Detection of DNA damage induced by hydroquinone and catechol using an electrochemical DNA biosensor
    • Wang C., Zhao J., Zhang D., Yang Z. Detection of DNA damage induced by hydroquinone and catechol using an electrochemical DNA biosensor. Aust. J. Chem. 2009, 62:1181-1184.
    • (2009) Aust. J. Chem. , vol.62 , pp. 1181-1184
    • Wang, C.1    Zhao, J.2    Zhang, D.3    Yang, Z.4
  • 66
    • 3543016133 scopus 로고    scopus 로고
    • Electrochemical study of quercetin-DNA interactions. Part II. In situ sensing with DNA biosensors
    • Brett A.M.O., Diculescu V.C. Electrochemical study of quercetin-DNA interactions. Part II. In situ sensing with DNA biosensors. Biochemistry 2004, 64:143-150.
    • (2004) Biochemistry , vol.64 , pp. 143-150
    • Brett, A.M.O.1    Diculescu, V.C.2
  • 68
    • 65949108217 scopus 로고    scopus 로고
    • Mechanistic and kinetic aspects of the formation of guanidinohydantoin and spiro iminohydantoin under acid conditions
    • Ye Y., Munk B.H., Muller J.G., Cogbill A., Burrows C.J., Schlegel H.B. Mechanistic and kinetic aspects of the formation of guanidinohydantoin and spiro iminohydantoin under acid conditions. Chem. Res. Toxicol. 2009, 22:526-535.
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 526-535
    • Ye, Y.1    Munk, B.H.2    Muller, J.G.3    Cogbill, A.4    Burrows, C.J.5    Schlegel, H.B.6
  • 69
    • 3543069474 scopus 로고    scopus 로고
    • Spermine participates in oxidative damage of guanosine and 8-oxoguanosine leading to deoxyribosylurea formation
    • Hosford M.E., Muller J.G., Burrows C.J. Spermine participates in oxidative damage of guanosine and 8-oxoguanosine leading to deoxyribosylurea formation. J. Am. Chem. Soc. 2004, 126:9540-9541.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9540-9541
    • Hosford, M.E.1    Muller, J.G.2    Burrows, C.J.3
  • 71
    • 0018648449 scopus 로고
    • Copper(I) complexes with penicillamine and glutathione
    • Osterberg R., Ligaarden R., Persson D. Copper(I) complexes with penicillamine and glutathione. J. Inorg. Biochem. 1979, 10:341-355.
    • (1979) J. Inorg. Biochem. , vol.10 , pp. 341-355
    • Osterberg, R.1    Ligaarden, R.2    Persson, D.3
  • 72
    • 70350140918 scopus 로고    scopus 로고
    • Investigating the antioxidant properties of oxo-sulfur compounds on metal-mediated DNA damage
    • Ramoutar R., Brumaghim J.L. Investigating the antioxidant properties of oxo-sulfur compounds on metal-mediated DNA damage. Main Group Chem. 2007, 6:143-153.
    • (2007) Main Group Chem. , vol.6 , pp. 143-153
    • Ramoutar, R.1    Brumaghim, J.L.2
  • 73
    • 34247117979 scopus 로고    scopus 로고
    • Stability of metal-glutathione complexes during oxidation by hydrogen peroxide and Cu(II)-catalysis
    • Hsu-Kim H. Stability of metal-glutathione complexes during oxidation by hydrogen peroxide and Cu(II)-catalysis. Environ. Sci. Technol. 2007, 41:2338-2342.
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 2338-2342
    • Hsu-Kim, H.1
  • 74
    • 55349118470 scopus 로고    scopus 로고
    • Metal specificity in DNA damage prevention by sulfur antioxidants
    • Battin E.E., Brumaghim J.L. Metal specificity in DNA damage prevention by sulfur antioxidants. J. Inorg. Biochem. 2008, 102:2036-2042.
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 2036-2042
    • Battin, E.E.1    Brumaghim, J.L.2
  • 75
    • 0016827580 scopus 로고
    • Estimation of life times and diffusion distances of radicals involved in X-ray-induced DNA strand breaks or killing of mammalian cells
    • Roots R., Okada S. Estimation of life times and diffusion distances of radicals involved in X-ray-induced DNA strand breaks or killing of mammalian cells. Radiat. Res. 1975, 64:306-320.
    • (1975) Radiat. Res. , vol.64 , pp. 306-320
    • Roots, R.1    Okada, S.2
  • 77
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 2001, 30:1191-1212.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 78
    • 15244348061 scopus 로고    scopus 로고
    • Regulation of apoptosis by glutathione redox state in PC12 cells exposed simultaneously to iron and ascorbic acid
    • Hiroi M., Ogihara T., Hirano K., Hasegawa M., Morinobu T., Tamai H., Niki E. Regulation of apoptosis by glutathione redox state in PC12 cells exposed simultaneously to iron and ascorbic acid. Free Radic. Biol. Med. 2005, 38:1057-1072.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1057-1072
    • Hiroi, M.1    Ogihara, T.2    Hirano, K.3    Hasegawa, M.4    Morinobu, T.5    Tamai, H.6    Niki, E.7
  • 79
    • 1842479866 scopus 로고    scopus 로고
    • Electrochemical oxidation of catechols in the presence of acetylacetone
    • Nematollahi D., Rafiee M. Electrochemical oxidation of catechols in the presence of acetylacetone. J. Electroanal. Chem. 2004, 566:31-37.
    • (2004) J. Electroanal. Chem. , vol.566 , pp. 31-37
    • Nematollahi, D.1    Rafiee, M.2
  • 80
    • 31644432580 scopus 로고    scopus 로고
    • The central role of metal coordination in selenium antioxidant activity
    • Battin E.E., Perron N.R., Brumaghim J.L. The central role of metal coordination in selenium antioxidant activity. Inorg. Chem. 2006, 45:499-501.
    • (2006) Inorg. Chem. , vol.45 , pp. 499-501
    • Battin, E.E.1    Perron, N.R.2    Brumaghim, J.L.3
  • 81
    • 0002810701 scopus 로고
    • Copper(II)-catalyzed oxidation of catechol by molecular oxygen in aqueous solution
    • Balla J., Kiss T., Jameson R.F. Copper(II)-catalyzed oxidation of catechol by molecular oxygen in aqueous solution. Inorg. Chem. 1992, 31:58-62.
    • (1992) Inorg. Chem. , vol.31 , pp. 58-62
    • Balla, J.1    Kiss, T.2    Jameson, R.F.3


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