메뉴 건너뛰기




Volumn 36, Issue 1, 2012, Pages 85-92

Cytosolic thioredoxin from Ruditapes philippinarum: Molecular cloning, characterization, expression and DNA protection activity of the recombinant protein

Author keywords

Bacterial challenge; Expressional analysis; MCO assay; Ruditapes philippinarum; Thioredoxin

Indexed keywords

DNA; RECOMBINANT PROTEIN; THIOREDOXIN;

EID: 80054955962     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2011.06.006     Document Type: Article
Times cited : (26)

References (60)
  • 1
    • 73449118619 scopus 로고    scopus 로고
    • Redox regulation of cell survival by the thioredoxin superfamily: an implication of redox gene therapy in the heart
    • Ahsan M.K., Lekli I., Ray D., Yodoi J., Das D.K. Redox regulation of cell survival by the thioredoxin superfamily: an implication of redox gene therapy in the heart. Antioxid. Redox Signal 2009, 11(11):2741-2758.
    • (2009) Antioxid. Redox Signal , vol.11 , Issue.11 , pp. 2741-2758
    • Ahsan, M.K.1    Lekli, I.2    Ray, D.3    Yodoi, J.4    Das, D.K.5
  • 2
    • 0030671351 scopus 로고    scopus 로고
    • Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60-asparagine mutant
    • Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., Montfort W.R. Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60-asparagine mutant. Biochemistry 1997, 36(46):13979-13988.
    • (1997) Biochemistry , vol.36 , Issue.46 , pp. 13979-13988
    • Andersen, J.F.1    Sanders, D.A.2    Gasdaska, J.R.3    Weichsel, A.4    Powis, G.5    Montfort, W.R.6
  • 4
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner E.S., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 2000, 267(20):6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , Issue.20 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 5
    • 33751178410 scopus 로고    scopus 로고
    • The thioredoxin system in cancer
    • Arner E.S., Holmgren A. The thioredoxin system in cancer. Semin. Cancer Biol. 2006, 16(6):420-426.
    • (2006) Semin. Cancer Biol. , vol.16 , Issue.6 , pp. 420-426
    • Arner, E.S.1    Holmgren, A.2
  • 6
    • 59349093202 scopus 로고    scopus 로고
    • Oxidative stress responses in bivalves (Scrobicularia plana, Cerastoderma edule) from the Oued Souss estuary (Morocco)
    • Bergayou H., Mouneyrac C., Pellerin J., Moukrim A. Oxidative stress responses in bivalves (Scrobicularia plana, Cerastoderma edule) from the Oued Souss estuary (Morocco). Ecotoxicol. Environ. Saf. 2009, 72(3):765-769.
    • (2009) Ecotoxicol. Environ. Saf. , vol.72 , Issue.3 , pp. 765-769
    • Bergayou, H.1    Mouneyrac, C.2    Pellerin, J.3    Moukrim, A.4
  • 7
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt C., Lillig C.H., Holmgren A. Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim. Biophys. Acta 2008, 1783(4):641-650.
    • (2008) Biochim. Biophys. Acta , vol.1783 , Issue.4 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 8
    • 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. 1976, 72248-72254.
    • (1976) Anal. Biochem. , pp. 72248-72254
    • Bradford, M.M.1
  • 9
    • 34247345795 scopus 로고    scopus 로고
    • Oxidative burst in hard clam (Mercenaria mercenaria) haemocytes
    • Bugge D.M., Hegaret H., Wikfors G.H., Allam B. Oxidative burst in hard clam (Mercenaria mercenaria) haemocytes. Fish Shellfish Immunol. 2007, 23(1):188-196.
    • (2007) Fish Shellfish Immunol. , vol.23 , Issue.1 , pp. 188-196
    • Bugge, D.M.1    Hegaret, H.2    Wikfors, G.H.3    Allam, B.4
  • 10
    • 0036012805 scopus 로고    scopus 로고
    • Generation of superoxide anion and SOD activity in haemocytes and muscle of American white shrimp (Litopenaeus vannamei) as a response to [beta]-glucan and sulphated polysaccharide
    • Campa-Córdova A.I., Hernández-Saavedra N.Y., De Philippis R., Ascencio F. Generation of superoxide anion and SOD activity in haemocytes and muscle of American white shrimp (Litopenaeus vannamei) as a response to [beta]-glucan and sulphated polysaccharide. Fish Shellfish Immunol. 2002, 12(4):353-366.
    • (2002) Fish Shellfish Immunol. , vol.12 , Issue.4 , pp. 353-366
    • Campa-Córdova, A.I.1    Hernández-Saavedra, N.Y.2    De Philippis, R.3    Ascencio, F.4
  • 11
    • 0037097751 scopus 로고    scopus 로고
    • Bacteria-hemocyte interactions and phagocytosis in marine bivalves
    • Canesi L., Gallo G., Gavioli M., Pruzzo C. Bacteria-hemocyte interactions and phagocytosis in marine bivalves. Microsc. Res. Tech. 2002, 57(6):469-476.
    • (2002) Microsc. Res. Tech. , vol.57 , Issue.6 , pp. 469-476
    • Canesi, L.1    Gallo, G.2    Gavioli, M.3    Pruzzo, C.4
  • 12
    • 0031206256 scopus 로고    scopus 로고
    • In vitrostudy of phagocytic ability ofMytilus galloprovincialisLmk. haemocytes
    • Carballal M.J., LÓPez C., Azevedo C., Villalba A. In vitrostudy of phagocytic ability ofMytilus galloprovincialisLmk. haemocytes. Fish Shellfish Immunol. 1997, 7(6):403-416.
    • (1997) Fish Shellfish Immunol. , vol.7 , Issue.6 , pp. 403-416
    • Carballal, M.J.1    López, C.2    Azevedo, C.3    Villalba, A.4
  • 13
    • 0037031939 scopus 로고    scopus 로고
    • Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells
    • Chen Y., Cai J., Murphy T.J., Jones D.P. Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. J. Biol. Chem. 2002, 277(36):33242-33248.
    • (2002) J. Biol. Chem. , vol.277 , Issue.36 , pp. 33242-33248
    • Chen, Y.1    Cai, J.2    Murphy, T.J.3    Jones, D.P.4
  • 14
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu M.L., Aw T.Y. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic. Biol. Med. 2010, 48(6):749-762.
    • (2010) Free Radic. Biol. Med. , vol.48 , Issue.6 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 15
    • 0037031899 scopus 로고    scopus 로고
    • Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death
    • Damdimopoulos A.E., Miranda-Vizuete A., Pelto-Huikko M., Gustafsson J.A., Spyrou G. Human mitochondrial thioredoxin. Involvement in mitochondrial membrane potential and cell death. J. Biol. Chem. 2002, 277(36):33249-33257.
    • (2002) J. Biol. Chem. , vol.277 , Issue.36 , pp. 33249-33257
    • Damdimopoulos, A.E.1    Miranda-Vizuete, A.2    Pelto-Huikko, M.3    Gustafsson, J.A.4    Spyrou, G.5
  • 16
    • 40049111243 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2 from disk abalone (Haliotis discus discus): molecular characterization, tissue expression and DNA protection activity of its recombinant protein
    • De Zoysa M., Pushpamali W.A., Whang I., Kim S.J., Lee J. Mitochondrial thioredoxin-2 from disk abalone (Haliotis discus discus): molecular characterization, tissue expression and DNA protection activity of its recombinant protein. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2008, 149(4):630-639.
    • (2008) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.149 , Issue.4 , pp. 630-639
    • De Zoysa, M.1    Pushpamali, W.A.2    Whang, I.3    Kim, S.J.4    Lee, J.5
  • 17
    • 50149095793 scopus 로고    scopus 로고
    • The Genome Sequencer FLX System-longer reads, more applications, straight forward bioinformatics and more complete data sets
    • Droege M., Hill B. The Genome Sequencer FLX System-longer reads, more applications, straight forward bioinformatics and more complete data sets. J. Biotechnol. 2008, 136(1-2):3-10.
    • (2008) J. Biotechnol. , vol.136 , Issue.1-2 , pp. 3-10
    • Droege, M.1    Hill, B.2
  • 18
    • 0032802807 scopus 로고    scopus 로고
    • Expression of thioredoxin and thioredoxin reductase in placentae of pregnant mice exposed to lipopolysaccharide
    • Ejima K., Koji T., Nanri H., Kashimura M., Ikeda M. Expression of thioredoxin and thioredoxin reductase in placentae of pregnant mice exposed to lipopolysaccharide. Placenta 1999, 20(7):561-566.
    • (1999) Placenta , vol.20 , Issue.7 , pp. 561-566
    • Ejima, K.1    Koji, T.2    Nanri, H.3    Kashimura, M.4    Ikeda, M.5
  • 19
    • 0242277285 scopus 로고    scopus 로고
    • The thioredoxin system-from science to clinic
    • Gromer S., Urig S., Becker K. The thioredoxin system-from science to clinic. Med. Res. Rev. 2004, 24(1):40-89.
    • (2004) Med. Res. Rev. , vol.24 , Issue.1 , pp. 40-89
    • Gromer, S.1    Urig, S.2    Becker, K.3
  • 20
    • 0024688488 scopus 로고
    • Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • Hendrick J.P., Hodges P.E., Rosenberg L.E. Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc. Natl. Acad. Sci. USA 1989, 86(11):4056-4060.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , Issue.11 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 25
    • 48749112811 scopus 로고    scopus 로고
    • Oxidative stress and thioredoxin system
    • Koharyova M., Kolarova M. Oxidative stress and thioredoxin system. Gen. Physiol. Biophys. 2008, 27(2):71-84.
    • (2008) Gen. Physiol. Biophys. , vol.27 , Issue.2 , pp. 71-84
    • Koharyova, M.1    Kolarova, M.2
  • 27
    • 0037634121 scopus 로고    scopus 로고
    • Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes
    • Kunchithapautham K., Padmavathi B., Narayanan R.B., Kaliraj P., Scott A.L. Thioredoxin from Brugia malayi: defining a 16-kilodalton class of thioredoxins from nematodes. Infect Immun. 2003, 71(7):4119-4126.
    • (2003) Infect Immun. , vol.71 , Issue.7 , pp. 4119-4126
    • Kunchithapautham, K.1    Padmavathi, B.2    Narayanan, R.B.3    Kaliraj, P.4    Scott, A.L.5
  • 29
    • 0038393110 scopus 로고    scopus 로고
    • Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii
    • Lemaire S.D., Collin V., Keryer E., Quesada A., Miginiac-Maslow M. Characterization of thioredoxin y, a new type of thioredoxin identified in the genome of Chlamydomonas reinhardtii. FEBS Lett. 2003, 543(1-3):87-92.
    • (2003) FEBS Lett. , vol.543 , Issue.1-3 , pp. 87-92
    • Lemaire, S.D.1    Collin, V.2    Keryer, E.3    Quesada, A.4    Miginiac-Maslow, M.5
  • 30
    • 61649088812 scopus 로고    scopus 로고
    • The role of antioxidants and antioxidant-related enzymes in protective responses to environmentally induced oxidative stress
    • Limon-Pacheco J., Gonsebatt M.E. The role of antioxidants and antioxidant-related enzymes in protective responses to environmentally induced oxidative stress. Mutat Res. 2009, 674(1-2):137-147.
    • (2009) Mutat Res. , vol.674 , Issue.1-2 , pp. 137-147
    • Limon-Pacheco, J.1    Gonsebatt, M.E.2
  • 31
    • 0346056673 scopus 로고    scopus 로고
    • Functional expression and characterization of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage
    • Li J., Zhang W.B., Loukas A., Lin R.Y., Ito A., Zhang L.H., Jones M., McManus D.P. Functional expression and characterization of Echinococcus granulosus thioredoxin peroxidase suggests a role in protection against oxidative damage. Gene 2004, 326157-326165.
    • (2004) Gene , pp. 326157-326165
    • Li, J.1    Zhang, W.B.2    Loukas, A.3    Lin, R.Y.4    Ito, A.5    Zhang, L.H.6    Jones, M.7    McManus, D.P.8
  • 32
    • 0027491032 scopus 로고
    • Chemical pathways of peptide degradation. V. Ascorbic acid promotes rather than inhibits the oxidation of methionine to methionine sulfoxide in small model peptides
    • Li S., Schoneich C., Wilson G.S., Borchardt R.T. Chemical pathways of peptide degradation. V. Ascorbic acid promotes rather than inhibits the oxidation of methionine to methionine sulfoxide in small model peptides. Pharm. Res. 1993, 10(11):1572-1579.
    • (1993) Pharm. Res. , vol.10 , Issue.11 , pp. 1572-1579
    • Li, S.1    Schoneich, C.2    Wilson, G.S.3    Borchardt, R.T.4
  • 33
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina C.V., Riggs P.D., Grandea A.G., Slatko B.E., Moran L.S., Tagliamonte J.A., McReynolds L.A., Guan C.D. An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene 1988, 74(2):365-373.
    • (1988) Gene , vol.74 , Issue.2 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Guan, C.D.8
  • 34
    • 85190484917 scopus 로고    scopus 로고
    • Leboulenger. The point about oxidative stress in molluscs. ISJ. 291-104.
    • Manduzio H, B.R., F Durand, C Galap, F Leboulenger. 2005. The point about oxidative stress in molluscs. ISJ. 291-104.
    • (2005)
    • Manduzio, H.B.R.F.1    Durand, C.2    Galap, F.3
  • 35
    • 0030722209 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a novel Escherichia coli thioredoxin
    • Miranda-Vizuete A., Damdimopoulos A.E., Gustafsson J., Spyrou G. Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. J. Biol. Chem. 1997, 272(49):30841-30847.
    • (1997) J. Biol. Chem. , vol.272 , Issue.49 , pp. 30841-30847
    • Miranda-Vizuete, A.1    Damdimopoulos, A.E.2    Gustafsson, J.3    Spyrou, G.4
  • 39
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J., Arner E.S. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic. Biol. Med. 2001, 31(11):1287-1312.
    • (2001) Free Radic. Biol. Med. , vol.31 , Issue.11 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 40
    • 33847374235 scopus 로고    scopus 로고
    • Redox regulation of cellular functions
    • Oktyabrsky O.N., Smirnova G.V. Redox regulation of cellular functions. Biochemistry (Mosc) 2007, 72(2):132-145.
    • (2007) Biochemistry (Mosc) , vol.72 , Issue.2 , pp. 132-145
    • Oktyabrsky, O.N.1    Smirnova, G.V.2
  • 43
    • 0026708475 scopus 로고
    • Generation of reactive oxygen metabolites by the haemocytes of the mussel Mytilus edulis
    • Pipe R.K. Generation of reactive oxygen metabolites by the haemocytes of the mussel Mytilus edulis. Dev. Comp. Immunol. 1992, 16(2-3):111-122.
    • (1992) Dev. Comp. Immunol. , vol.16 , Issue.2-3 , pp. 111-122
    • Pipe, R.K.1
  • 44
    • 71649112581 scopus 로고    scopus 로고
    • A thioredoxin response to the WSSV challenge on the Chinese white shrimp, Fenneropenaeus chinensis
    • Ren Q., Zhang R.R., Zhao X.F., Wang J.X. A thioredoxin response to the WSSV challenge on the Chinese white shrimp, Fenneropenaeus chinensis. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2010, 151(1):92-98.
    • (2010) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.151 , Issue.1 , pp. 92-98
    • Ren, Q.1    Zhang, R.R.2    Zhao, X.F.3    Wang, J.X.4
  • 45
    • 0034723199 scopus 로고    scopus 로고
    • Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli
    • Ritz D., Patel H., Doan B., Zheng M., Aslund F., Storz G., Beckwith J. Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. J. Biol. Chem. 2000, 275(4):2505-2512.
    • (2000) J. Biol. Chem. , vol.275 , Issue.4 , pp. 2505-2512
    • Ritz, D.1    Patel, H.2    Doan, B.3    Zheng, M.4    Aslund, F.5    Storz, G.6    Beckwith, J.7
  • 46
    • 0033106065 scopus 로고    scopus 로고
    • Defense mechanisms and disease prevention in farmed marine invertebrates
    • Roch P. Defense mechanisms and disease prevention in farmed marine invertebrates. Aquaculture 1999, 172(1-2):125-145.
    • (1999) Aquaculture , vol.172 , Issue.1-2 , pp. 125-145
    • Roch, P.1
  • 48
    • 0029645581 scopus 로고
    • Crystal structure of thioredoxin-2 from Anabaena
    • Saarinen M., Gleason F.K., Eklund H. Crystal structure of thioredoxin-2 from Anabaena. Structure 1995, 3(10):1097-1108.
    • (1995) Structure , vol.3 , Issue.10 , pp. 1097-1108
    • Saarinen, M.1    Gleason, F.K.2    Eklund, H.3
  • 49
    • 77957076445 scopus 로고    scopus 로고
    • Oxidative stress and bivalves: a proteomic approach
    • Sheehan D, B.M., 2008. Oxidative stress and bivalves: a proteomic approach. ISJ. 5. 110-123.
    • (2008) ISJ. , vol.5 , pp. 110-123
    • Sheehan, D.B.M.1
  • 51
    • 34250206320 scopus 로고    scopus 로고
    • A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins
    • Su D., Berndt C., Fomenko D.E., Holmgren A., Gladyshev V.N. A conserved cis-proline precludes metal binding by the active site thiolates in members of the thioredoxin family of proteins. Biochemistry 2007, 46(23):6903-6910.
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6903-6910
    • Su, D.1    Berndt, C.2    Fomenko, D.E.3    Holmgren, A.4    Gladyshev, V.N.5
  • 52
    • 33947174763 scopus 로고    scopus 로고
    • Thioredoxin-2 affects lifespan and oxidative stress in Drosophila
    • Svensson M.J., Larsson J. Thioredoxin-2 affects lifespan and oxidative stress in Drosophila. Hereditas 2007, 144(1):25-32.
    • (2007) Hereditas , vol.144 , Issue.1 , pp. 25-32
    • Svensson, M.J.1    Larsson, J.2
  • 53
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony methods
    • doi:10.1093/molbev/msr121
    • Tamura K, P.D., Peterson N, Stecher G, Nei M, and Kumar S. 2011. MEGA5: Molecular evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony methods. Mol Biol Evol. doi:10.1093/molbev/msr121.
    • (2011) Mol Biol Evol.
    • Tamura, K.P.D.1    Peterson, N.2    Stecher, G.3    Nei, M.4    Kumar, S.5
  • 54
    • 4444379924 scopus 로고    scopus 로고
    • Expression and purification of thioredoxin (TrxA) and thioredoxin reductase (TrxB) from Brevibacillus choshinensis
    • Tanaka R., Kosugi K., Mizukami M., Ishibashi M., Tokunaga H., Tokunaga M. Expression and purification of thioredoxin (TrxA) and thioredoxin reductase (TrxB) from Brevibacillus choshinensis. Protein Expr. Purif. 2004, 37(2):385-391.
    • (2004) Protein Expr. Purif. , vol.37 , Issue.2 , pp. 385-391
    • Tanaka, R.1    Kosugi, K.2    Mizukami, M.3    Ishibashi, M.4    Tokunaga, H.5    Tokunaga, M.6
  • 55
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22(22):4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 56
    • 5644268137 scopus 로고    scopus 로고
    • Defense mechanisms in farmed marine molluscs
    • Tiscar, P.G., Mosca, F. 2004. Defense mechanisms in farmed marine molluscs. Vet. Res. Commun. 28 Suppl 157-62.
    • (2004) Vet. Res. Commun. , vol.28 , Issue.SUPPL , pp. 157-162
    • Tiscar, P.G.1    Mosca, F.2
  • 58
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • Valko M., Rhodes C.J., Moncol J., Izakovic M., Mazur M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact. 2006, 160(1):1-40.
    • (2006) Chem Biol Interact. , vol.160 , Issue.1 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.