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Volumn 31, Issue 1, 2011, Pages 65-76

Superoxide dismutase: An industrial perspective

Author keywords

antioxidant; industrial production; orgotein; oxidative stress; SOD

Indexed keywords

ANTIOXIDANT; ANTIOXIDANT ENZYME; ENZYME ENGINEERING; ENZYME TECHNOLOGY; INDUSTRIAL ENZYMES; INDUSTRIAL PRODUCTION; ORGOTEIN; OTHER APPLICATIONS; PROCESS OPTIMIZATION; PRODUCTION PROCESS; SCALE-UP; SOD; SUPER OXIDE DISMUTASE; SUPEROXIDE DISMUTASES; THERAPEUTIC APPLICATION;

EID: 79951833588     PISSN: 07388551     EISSN: 15497801     Source Type: Journal    
DOI: 10.3109/07388551.2010.490937     Document Type: Review
Times cited : (86)

References (107)
  • 1
    • 4444291348 scopus 로고    scopus 로고
    • Coexpression of yeast copper chaperone (yCCS) and CuZn-superoxide dismutases in Escherichia coli yields protein with high copper contents
    • DOI 10.1016/j.pep.2004.06.006, PII S1046592804001913
    • Ahl IM, Lindberg MJ, Tibell LAE. 2004. Coexpression of yeast copper chaperone (yCCS) and CuZn-superoxide dismutases in Escherichia coli yields protein with high copper contents. Protein Expr Purif 37: 311-319. (Pubitemid 39187967)
    • (2004) Protein Expression and Purification , vol.37 , Issue.2 , pp. 311-319
    • Ahl, I.-M.1    Lindberg, M.J.2    Tibell, L.A.E.3
  • 2
    • 77952050772 scopus 로고    scopus 로고
    • Simultaneous expression of choline oxidase, superoxide dismutase and ascorbate peroxidase in potato plant chloroplasts provides synergistically enhanced protection against various abiotic stresses
    • Ahmad R, Kim YH, Kim MD, Kwon SY, Cho K, Lee HS, Kwak SS. 2010. Simultaneous expression of choline oxidase, superoxide dismutase and ascorbate peroxidase in potato plant chloroplasts provides synergistically enhanced protection against various abiotic stresses. Physiol Plant 138: 520-533.
    • (2010) Physiol Plant , vol.138 , pp. 520-533
    • Ahmad, R.1    Kim, Y.H.2    Kim, M.D.3    Kwon, S.Y.4    Cho, K.5    Lee, H.S.6    Kwak, S.S.7
  • 3
    • 77249155990 scopus 로고    scopus 로고
    • Resistance to ciprofoxacin by enhancement of antioxidant defenses in bioflm and planktonic Proteus mirabilis
    • Aiassa V, Barnes AI, Albesa I. 2010. Resistance to ciprofoxacin by enhancement of antioxidant defenses in bioflm and planktonic Proteus mirabilis. Biochem Biophys Res Commun 393: 84-88.
    • (2010) Biochem Biophys Res Commun , vol.393 , pp. 84-88
    • Aiassa, V.1    Barnes, A.I.2    Albesa, I.3
  • 4
    • 77955311185 scopus 로고    scopus 로고
    • Oxidative stress during aging of the yeast in a stationary culture and its attenuation by antioxidants
    • Alina O, Bartosz G, Biliski T. 2010. Oxidative stress during aging of the yeast in a stationary culture and its attenuation by antioxidants. Cell Biol. Int. 34: 731-734.
    • (2010) Cell Biol. Int. , vol.34 , pp. 731-734
    • Alina, O.1    Bartosz, G.2    Biliski, T.3
  • 7
    • 40749155816 scopus 로고    scopus 로고
    • Effect of heat-generated product from uronic acids on the physiological activities of microbial cells and its application
    • DOI 10.1016/j.biortech.2007.08.036, PII S0960852407006906
    • Aoyagi H, Ishii H, Ugwu CU, Tanaka H. 2008. Efect of heat-generated product from uronic acids on the physiological activities of microbial cells and its application. Bioresour Technol 99: 4534-4538. (Pubitemid 351380802)
    • (2008) Bioresource Technology , vol.99 , Issue.10 , pp. 4534-4538
    • Aoyagi, H.1    Ishii, H.2    Ugwu, C.U.3    Tanaka, H.4
  • 10
    • 0023815254 scopus 로고
    • Efcient production of active human manganese superoxide dismutase in Escherichia coli
    • Beck Y, Bartfeld D, Yavin Z, Levanon A, Gorecki M, Hartman JR. 1988. Efcient production of active human manganese superoxide dismutase in Escherichia coli. Biotechnology 6: 930-935.
    • (1988) Biotechnology , vol.6 , pp. 930-935
    • Beck, Y.1    Bartfeld, D.2    Yavin, Z.3    Levanon, A.4    Gorecki, M.5    Hartman, J.R.6
  • 11
    • 0030038769 scopus 로고    scopus 로고
    • Purification and characterization of the Cu,Zn SOD from Escherichia coli
    • DOI 10.1016/0891-5849(95)02217-1
    • Benov LT, Beyer WF, Jr, Stevens RD, Fridovich I. 1996. Purifcation and characterization of the Cu,Zn SOD from Escherichia coli. Free Radic Biol Med 21: 117-121. (Pubitemid 26235222)
    • (1996) Free Radical Biology and Medicine , vol.21 , Issue.1 , pp. 117-121
    • Benov, L.T.1    Beyer Jr., W.F.2    Stevens, R.D.3    Fridovich, I.4
  • 17
    • 0034711245 scopus 로고    scopus 로고
    • Tobacco nectarin I. Purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of floral reproductive tissues
    • DOI 10.1074/jbc.M006461200
    • Carter C, Tornburg RW. 2000. Tobacco nectarin I. Purifcation and characterization as a germin-like, manganese superoxide dismutase implicated in the defense of foral reproductive tissues. J Biol Chem 275: 36726-36733. (Pubitemid 32002079)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 36726-36733
    • Carter, C.1    Thornburg, R.W.2
  • 18
    • 33751238512 scopus 로고    scopus 로고
    • Production and characterization of human extracellular superoxide dismutase in the methylotrophic yeast Pichia pastoris
    • Chen HL, Yen CC, Tsai TC, Yu CH, Liou YJ, Lai YW, Wang ML, Chen CM. 2006. Production and characterization of human extracellular superoxide dismutase in the methylotrophic yeast Pichia pastoris. J Agric Food Chem 54: 8041-8047.
    • (2006) J Agric Food Chem , vol.54 , pp. 8041-8047
    • Chen, H.L.1    Yen, C.C.2    Tsai, T.C.3    Yu, C.H.4    Liou, Y.J.5    Lai, Y.W.6    Wang, M.L.7    Chen, C.M.8
  • 20
    • 33750058553 scopus 로고    scopus 로고
    • Engineering and characterization of human manganese superoxide dismutase mutants with high activity and low product inhibition
    • DOI 10.1111/j.1742-4658.2006.05484.x
    • Chockalingam K, Luba J, Nick HS, Silverman DN, Zhao H. 2006. Engineering and characterization of human manganese superoxide dismutase mutants with high activity and low product inhibition. FEBS J 273: 4853-4861. (Pubitemid 44583510)
    • (2006) FEBS Journal , vol.273 , Issue.21 , pp. 4853-4861
    • Chockalingam, K.1    Luba, J.2    Nick, H.S.3    Silverman, D.N.4    Zhao, H.5
  • 27
    • 0028791398 scopus 로고
    • Heavy metal efects on Proteus mirabilis superoxide dismutase production
    • Eickhof J, Potts E, Valtos J, Niederhofer EC. 1995. Heavy metal efects on Proteus mirabilis superoxide dismutase production. FEMS Microbiol Lett 132: 271-276.
    • (1995) FEMS Microbiol Lett , vol.132 , pp. 271-276
    • Eickhof, J.1    Potts, E.2    Valtos, J.3    Niederhofer, E.C.4
  • 28
    • 7744246514 scopus 로고    scopus 로고
    • In vivo production of active nickel superoxide dismutase from Prochlorococcus marinus MIT9313 is dependent on its cognate peptidase
    • DOI 10.1128/JB.186.22.7821-7825.2004
    • Eitinger T. 2004. In vivo production of active nickel superoxide dismutase from Prochlorococcus marinus MIT9313 is dependent on its cognate peptidase. J Bacteriol 186: 7821-7825. (Pubitemid 39463752)
    • (2004) Journal of Bacteriology , vol.186 , Issue.22 , pp. 7821-7825
    • Eitinger, T.1
  • 31
    • 0036509440 scopus 로고    scopus 로고
    • Molecular evolution and structure-function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases
    • DOI 10.1006/abbi.2001.2739
    • Fink RC, Scandalios JG. 2002. Molecular evolution and structure- function relationships of the superoxide dismutase gene families in angiosperms and their relationship to other eukaryotic and prokaryotic superoxide dismutases. Arch Biochem Biophys 399: 19-36. (Pubitemid 34848307)
    • (2002) Archives of Biochemistry and Biophysics , vol.399 , Issue.1 , pp. 19-36
    • Fink, R.C.1    Scandalios, J.G.2
  • 32
    • 17044453540 scopus 로고    scopus 로고
    • Anti-inflammatory activity of Debaryomyces hansenii Cu,Zn-SOD
    • DOI 10.1016/S0188-0128(98)00005-0, PII S0188012898000050
    • García-González A, Ochoa JL. 1999. Anti-infammatory activity of Debaryomyces hansenii Cu,Zn-SOD. Arch Med Res 30: 69-73. (Pubitemid 29099518)
    • (1999) Archives of Medical Research , vol.30 , Issue.1 , pp. 69-73
    • Garcia-Gonzalez, A.1    Ochoa, J.L.2
  • 35
    • 0026413962 scopus 로고
    • Chiron buys Cetus: A tale of two companies
    • Gibbons A. 1991. Chiron buys Cetus: a tale of two companies. Science 253: 503-504.
    • (1991) Science , vol.253 , pp. 503-504
    • Gibbons, A.1
  • 36
    • 34247219638 scopus 로고    scopus 로고
    • A germin-like protein with superoxide dismutase activity in pea nodules with high protein sequence identity to a putative rhicadhesin receptor
    • DOI 10.1093/jxb/erl282
    • Gucciardo S, Wisniewski JP, Brewin NJ, Bornemann S. 2007. A germin-like protein with superoxide dismutase activity in pea nodules with high protein sequence identity to a putative rhicadhesin receptor. J Exp Bot 58: 1161-1171. (Pubitemid 46623323)
    • (2007) Journal of Experimental Botany , vol.58 , Issue.5 , pp. 1161-1171
    • Gucciardo, S.1    Wisniewski, J.-P.2    Brewin, N.J.3    Bornemann, S.4
  • 39
    • 0023113744 scopus 로고
    • Amino terminal acetylation of authentic human Cu,Zn superoxide dismutase produced in yeast
    • DOI 10.1038/nbt0487-363
    • Hallewell RA, Mills R, Tekamp-Olson P, Blacher R, Rosenberg S, Ötting F, Masiarz FR, Scandella CJ 1987. Amino terminal acetylation of authentic human Cu,Zn superoxide dismutase produced in yeast. Biotechnology 5: 363-366. (Pubitemid 17055042)
    • (1987) Bio/Technology , vol.5 , Issue.4 , pp. 363-366
    • Hallewell, R.A.1    Mills, R.2    Tekamp-Olson, P.3
  • 44
    • 0035996704 scopus 로고    scopus 로고
    • High-level expression of human extracellular superoxide dismutase in Escherichia coli and insect cells
    • He HJ, Yuan QS, Yang GZ, Wu XF. 2002. High-level expression of human extracellular superoxide dismutase in Escherichia coli and insect cells. Protein Expr Purif 24: 13-17.
    • (2002) Protein Expr Purif , vol.24 , pp. 13-17
    • He, H.J.1    Yuan, Q.S.2    Yang, G.Z.3    Wu, X.F.4
  • 45
    • 18044375778 scopus 로고    scopus 로고
    • Anti-inflammatory properties of a chimeric recombinant superoxide dismutase: SOD2/3
    • DOI 10.1016/j.biopha.2005.03.001
    • Hernandez-Saavedra D, Zhou H, McCord JM. 2005. Anti-infammatory properties of a chimeric recombinant superoxide dismutase: SOD2/3. Biomed Pharmacother 59: 204-208. (Pubitemid 40603334)
    • (2005) Biomedicine and Pharmacotherapy , vol.59 , Issue.4 , pp. 204-208
    • Hernandez-Saavedra, D.1    Zhou, H.2    McCord, J.M.3
  • 47
    • 0033952718 scopus 로고    scopus 로고
    • Production and characterization of recombinant Aspergillus fumigatus Cu,Zn superoxide dismutase and its recognition by immune human sera
    • Holdom MD, Lechenne B, Hay RJ, Hamilton AJ, Monod M. 2000. Production and characterization of recombinant Aspergillus fumigatus Cu,Zn superoxide dismutase and its recognition by immune human sera. J Clin Microbiol 38: 558-562. (Pubitemid 30082641)
    • (2000) Journal of Clinical Microbiology , vol.38 , Issue.2 , pp. 558-562
    • Holdom, M.D.1    Lechenne, B.2    Hay, R.J.3    Hamilton, A.J.4    Monod, M.5
  • 50
    • 3142709437 scopus 로고    scopus 로고
    • Heat-stable chloroplastic Cu/Zn superoxide dismutase in Chenopodium murale
    • DOI 10.1016/j.bbrc.2004.06.071, PII S0006291X0401349X
    • Khanna-Chopra R, Sabarinath S. 2004. Heat-stable chloroplastic Cu/Zn superoxide dismutase in Chenopodium murale. Biochem Biophys Res Commun 320: 1187-1192. (Pubitemid 38916669)
    • (2004) Biochemical and Biophysical Research Communications , vol.320 , Issue.4 , pp. 1187-1192
    • Khanna-Chopra, R.1    Sabarinath, S.2
  • 51
    • 77950638212 scopus 로고    scopus 로고
    • Protecting against antimicrobial efectors in the phagosome allows SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium
    • Kim B, Richards SM, Gunn JS, Slauch JM. 2010. Protecting against antimicrobial efectors in the phagosome allows SodCII to contribute to virulence in Salmonella enterica serovar Typhimurium. J Bacteriol 192: 2140-2149.
    • (2010) J Bacteriol , vol.192 , pp. 2140-2149
    • Kim, B.1    Richards, S.M.2    Gunn, J.S.3    Slauch, J.M.4
  • 52
    • 45049084143 scopus 로고    scopus 로고
    • Identifcation and characterization of a super-stable Cu-Zn SOD from leaves of turmeric (Curcuma longa L.)
    • Kochhar S, Kochhar VK. 2008. Identifcation and characterization of a super-stable Cu-Zn SOD from leaves of turmeric (Curcuma longa L.). Planta 288: 307-318.
    • (2008) Planta , vol.288 , pp. 307-318
    • Kochhar, S.1    Kochhar, V.K.2
  • 53
    • 33847268142 scopus 로고    scopus 로고
    • Improved production by fed-batch cultivation and some properties of Cu/Zn-superoxide dismutase from the fungal strain Humicola lutea 103
    • DOI 10.1016/j.enzmictec.2006.05.008, PII S0141022906002596
    • Krumova E, Dolashka-Angelova P, Pashova S, Stefanova L, Beeumen JV, Vassilev S, Angelova M. 2007. Improved production by fed-batch cultivation and some properties of Cu/Zn-superoxide dismutase from the fungal strain Humicola lutea 103. Enzyme Microb Technol 40: 524-532. (Pubitemid 46329045)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.4 , pp. 524-532
    • Krumova, E.1    Dolashka-Angelova, P.2    Pashova, S.3    Stefanova, L.4    Van Beeumen, J.5    Vassilev, S.6    Angelova, M.7
  • 58
    • 0037021636 scopus 로고    scopus 로고
    • Copper/zinc-superoxide dismutase from lemon cDNA and enzyme stability
    • Lin MW, Lin MT, Lin CT. 2002. Copper/zinc-superoxide dismutase from lemon cDNA and enzyme stability. J Agric Food Chem 50: 7264-7270.
    • (2002) J Agric Food Chem , vol.50 , pp. 7264-7270
    • Lin, M.W.1    Lin, M.T.2    Lin, C.T.3
  • 61
    • 70350571906 scopus 로고    scopus 로고
    • Yarrowia lipolytica growth under increased air pressure: Infuence on enzyme production
    • Lopes M, Gomes N, Mota M, Belo I. 2009. Yarrowia lipolytica growth under increased air pressure: infuence on enzyme production. Appl Biochem Biotechnol 159: 46-53.
    • (2009) Appl Biochem Biotechnol , vol.159 , pp. 46-53
    • Lopes, M.1    Gomes, N.2    Mota, M.3    Belo, I.4
  • 62
    • 4644320225 scopus 로고    scopus 로고
    • Vaccination with antioxidant enzymes confers protective immunity against challenge infection with Schistosoma mansoni
    • LoVerde PT, Carvalho-Queirozm C, Cook R. 2004. Vaccination with antioxidant enzymes confers protective immunity against challenge infection with Schistosoma mansoni. Mem Inst Oswaldo Cruz 99: 37-43. (Pubitemid 39278615)
    • (2004) Memorias do Instituto Oswaldo Cruz , vol.99 , Issue.5 , pp. 37-43
    • LoVerde, P.T.1    Carvalho-Queiroz, C.2    Cook, R.3
  • 63
    • 67650715015 scopus 로고    scopus 로고
    • Comparative mutagenic efects of structurally similar favonoids quercetin and taxifolin on tester strains Salmonella typhimurium TA102 and Escherichia coli WP-2 uvrA
    • Makena PS, Pierce SC, Chung KT, Sinclair SE. 2009. Comparative mutagenic efects of structurally similar favonoids quercetin and taxifolin on tester strains Salmonella typhimurium TA102 and Escherichia coli WP-2 uvrA. Environ Mol Mutagen 50: 451-459.
    • (2009) Environ Mol Mutagen , vol.50 , pp. 451-459
    • Makena, P.S.1    Pierce, S.C.2    Chung, K.T.3    Sinclair, S.E.4
  • 67
    • 67349171043 scopus 로고    scopus 로고
    • Economic evaluation of recombinant human copper zinc superoxide dismutase administered at birth to premature infants
    • McBride JA, Parad RB, Davis JM, Zheng Z, Zupancic JA. 2009. Economic evaluation of recombinant human copper zinc superoxide dismutase administered at birth to premature infants. J Perinatol 29: 364-371.
    • (2009) J Perinatol , vol.29 , pp. 364-371
    • McBride, J.A.1    Parad, R.B.2    Davis, J.M.3    Zheng, Z.4    Zupancic, J.A.5
  • 68
    • 0027363967 scopus 로고
    • Human disease, free radicals, and the oxidant/antioxidant balance
    • DOI 10.1016/0009-9120(93)90111-I
    • McCord JM. 1993. Human disease, free radicals, and the oxidant/ antioxidant balance. Clin Biochem 26: 351-357. (Pubitemid 23326737)
    • (1993) Clinical Biochemistry , vol.26 , Issue.5 , pp. 351-357
    • McCord, J.M.1
  • 69
    • 0014691242 scopus 로고
    • Superoxide dismutase. an enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. 1969. Superoxide dismutase. an enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049.
    • (1969) J Biol Chem , vol.244 , pp. 6049
    • McCord, J.M.1    Fridovich, I.2
  • 71
    • 0027414276 scopus 로고
    • Improving the outcome of severe head injury with the oxygen radical scavenger polyethylene glycol-conjugated superoxide dismutase: A Phase II trial
    • Muizelaar JP, Marmarou A, Young HF, Choi SC, Wolf A, Schneider RL, Kontos HA. 1993. Improving the outcome of severe head injury with the oxygen radical scavenger polyethylene glycol-conjugated superoxide dismutase: a phase II trial. J Neurosurg 78: 375-382. (Pubitemid 23073205)
    • (1993) Journal of Neurosurgery , vol.78 , Issue.3 , pp. 375-382
    • Muizelaar, J.P.1    Marmarou, A.2    Young, H.F.3    Choi, S.C.4    Wolf, A.5    Schneider, R.L.6    Kontos, H.A.7
  • 72
    • 18044368456 scopus 로고    scopus 로고
    • Oxidative stress in organ preservation: A multifaceted approach to cardioplegia
    • DOI 10.1016/j.biopha.2005.03.007
    • Nelson SK, Bose S, Rizeq M, McCord JM. 2005. Oxidative stress in organ preservation: a multifaceted approach to cardioplegia. Biomed Pharmacother 59: 149-157. (Pubitemid 40603326)
    • (2005) Biomedicine and Pharmacotherapy , vol.59 , Issue.4 , pp. 149-157
    • Nelson, S.K.1    Bose, S.2    Rizeq, M.3    McCord, J.M.4
  • 73
    • 49649112708 scopus 로고    scopus 로고
    • Copper, zinc-superoxide dismutase enhances the mutagenicity in Salmonella typhimurium induced by 2-amino-6-methyldipyrido[1,2-a:3′,2′-d] imidazole
    • Nii H, Tsutsui M, Kondo J, Toyohira Y, Ueno S, Yanagihara N. 2008. Copper, zinc-superoxide dismutase enhances the mutagenicity in Salmonella typhimurium induced by 2-amino-6-methyldipyrido[1,2-a:3′,2′-d] imidazole. Mutat Res 653: 14-22.
    • (2008) Mutat Res , vol.653 , pp. 14-22
    • Nii, H.1    Tsutsui, M.2    Kondo, J.3    Toyohira, Y.4    Ueno, S.5    Yanagihara, N.6
  • 74
    • 0032731765 scopus 로고    scopus 로고
    • Maternal serum superoxide dismutase (SOD): A possible marker for screening Down syndrome afected pregnancies
    • Ognibene A, Ciuti R, Tozzi P, Messeri G. 1999. Maternal serum superoxide dismutase (SOD): a possible marker for screening Down syndrome afected pregnancies. Prenat Diagn 19: 1058-1060.
    • (1999) Prenat Diagn , vol.19 , pp. 1058-1060
    • Ognibene, A.1    Ciuti, R.2    Tozzi, P.3    Messeri, G.4
  • 77
    • 37549056972 scopus 로고    scopus 로고
    • Reduced mitochondrial SOD displays mortality characteristics reminiscent of natural aging
    • DOI 10.1016/j.mad.2007.10.013, PII S0047637407001649
    • Paul A, Belton A, Nag S, Martin I, Grotewiel MS, Duttaroy A. 2007. Reduced mitochondrial SOD displays mortality characteristics reminiscent of natural aging. Mech Ageing Dev 128: 706-716. (Pubitemid 50012362)
    • (2007) Mechanisms of Ageing and Development , vol.128 , Issue.11-12 , pp. 706-716
    • Paul, A.1    Belton, A.2    Nag, S.3    Martin, I.4    Grotewiel, M.S.5    Duttaroy, A.6
  • 80
    • 77955919025 scopus 로고    scopus 로고
    • Te epidemiology of CuZn-SOD mutations in Germany: A study of 217 families
    • doi: 10.1007/s0045-010-5512-9
    • Rabe M, Felbecker A, Waibel S, Steinbach P, Winter P, Ludolph AC. 2010. Te epidemiology of CuZn-SOD mutations in Germany: a study of 217 families. J Neurol doi: 10.1007/s0045-010-5512-9.
    • (2010) J Neurol
    • Rabe, M.1    Felbecker, A.2    Waibel, S.3    Steinbach, P.4    Winter, P.5    Ludolph, A.C.6
  • 82
    • 38049174883 scopus 로고    scopus 로고
    • Characterization of the superoxide dismutase SOD1 gene of Kluyveromyces marxianus L3 and improved production of SOD activity
    • Raimondi S, Uccelletti D, Matteuzzi D, Pagnoni UM, Rossi M, Palleschi C. 2008. Characterization of the superoxide dismutase SOD1 gene of Kluyveromyces marxianus L3 and improved production of SOD activity. Appl Microbiol Biotechnol 77: 1269-1277.
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 1269-1277
    • Raimondi, S.1    Uccelletti, D.2    Matteuzzi, D.3    Pagnoni, U.M.4    Rossi, M.5    Palleschi, C.6
  • 84
    • 33745600868 scopus 로고    scopus 로고
    • Role of antioxidants in prophylaxis and therapy: A pharmaceutical perspective
    • DOI 10.1016/j.jconrel.2006.04.015, PII S0168365906002057
    • Ratnam DV, Ankola DD, Bhardwaj V, Sahana DK, Ravi Kumar MNV. 2006. Role of antioxidants in prophylaxis and therapy: a pharmaceutical perspective. J Control Release 113: 189-207. (Pubitemid 43983041)
    • (2006) Journal of Controlled Release , vol.113 , Issue.3 , pp. 189-207
    • Ratnam, D.V.1    Ankola, D.D.2    Bhardwaj, V.3    Sahana, D.K.4    Kumar, M.N.V.R.5
  • 86
    • 78650569645 scopus 로고    scopus 로고
    • Cigarette smoke condensate causes a decrease of the gene expression of Cu-Zn superoxide dismutase, Mn superoxide dismutase, glutathione peroxidase, catalase, and free radical-induced cell injury in SH-SY5Y human neuroblastoma cells
    • doi: 10.1007/s12640-009-9138-6
    • Russo M, Cocco S, Secondo A, Adornetto A, Bassi A, Nunziata A, Polichetti G, De Felice B, Damiano S, Serù R, Mondola P, Di Renzo G. 2009. Cigarette smoke condensate causes a decrease of the gene expression of Cu-Zn superoxide dismutase, Mn superoxide dismutase, glutathione peroxidase, catalase, and free radical-induced cell injury in SH-SY5Y human neuroblastoma cells. Neurotox Res doi: 10.1007/s12640-009-9138-6.
    • (2009) Neurotox Res
    • Russo, M.1    Cocco, S.2    Secondo, A.3    Adornetto, A.4    Bassi, A.5    Nunziata, A.6    Polichetti, G.7    De Felice, B.8    Damiano, S.9    Serù, R.10    Mondola, P.11    Di Renzo, G.12
  • 87
    • 0034882377 scopus 로고    scopus 로고
    • Induction of a new isozyme of superoxide dismutase at low temperature in Potentilla astrisanguinea Lodd. variety argyrophylla (Wall. ex. Lehm) Griers
    • Sahoo R, Kumar S, Ahuja PS. 2001. Induction of a new isozyme of superoxide dismutase at low temperature in Potentilla astrisanguinea lodd. variety argyrophylla (Wall, ex. Lehm) Griers. J Plant Physiol 158: 1093-1097. (Pubitemid 32773682)
    • (2001) Journal of Plant Physiology , vol.158 , Issue.8 , pp. 1093-1097
    • Sahoo, R.1    Kumar, S.2    Ahuja, P.S.3
  • 89
    • 0346788888 scopus 로고    scopus 로고
    • Iron superoxide dismutases: Structure and function of an archaic enzyme
    • Schafer G, Kardinahl S. 2003. Iron superoxide dismutases: structure and function of an archaic enzyme. Biochem Soc Trans 31: 1330-1334. (Pubitemid 38030969)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1330-1334
    • Schafer, G.1    Kardinahl, S.2
  • 91
    • 79951815283 scopus 로고    scopus 로고
    • Superoxide dismutase-like activity of boar semen and efect of SOD on the preservation of boar spermatozoa
    • Shizuka T, Mikiko S, Nobuhiko Y, Masaya G, Takashi N, Tsutomu H, Hiroshi M. 1999. Superoxide dismutase-like activity of boar semen and efect of SOD on the preservation of boar spermatozoa. Jpn J Swine Sci 36: 42-46.
    • (1999) Jpn J Swine Sci , vol.36 , pp. 42-46
    • Shizuka, T.1    Mikiko, S.2    Nobuhiko, Y.3    Masaya, G.4    Takashi, N.5    Tsutomu, H.6    Hiroshi, M.7
  • 96
    • 67649443897 scopus 로고    scopus 로고
    • Epigenetic regulation of human buccal mucosa mitochondrial superoxide dismutase gene expression by diet
    • Talera R, Karlica H, Rusta P, Haslberger AG. 2009. Epigenetic regulation of human buccal mucosa mitochondrial superoxide dismutase gene expression by diet. Br J Nutr 101: 743-749.
    • (2009) Br J Nutr , vol.101 , pp. 743-749
    • Talera, R.1    Karlica, H.2    Rusta, P.3    Haslberger, A.G.4
  • 97
    • 0037093140 scopus 로고    scopus 로고
    • Superoxide dismutase-based third-generation biosensor for superoxide anion
    • DOI 10.1021/ac0157270
    • Tian Y, Mao L, Okajima T, Ohsaka T. 2002. Superoxide dismutase-based third-generation biosensor for superoxide anion. Anal Chem 74: 2428-2434. (Pubitemid 34526051)
    • (2002) Analytical Chemistry , vol.74 , Issue.10 , pp. 2428-2434
    • Tian, Y.1    Mao, L.2    Okajima, T.3    Ohsaka, T.4
  • 98
    • 0023607878 scopus 로고
    • Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product
    • Tibell L, Hjalmarsson K, Edlund T, Skogman G, Engström A, Marklund SL. 1987. Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product. Proc Natl Acad Sci USA 84: 6634-6638.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6634-6638
    • Tibell, L.1    Hjalmarsson, K.2    Edlund, T.3    Skogman, G.4    Engström, A.5    Marklund, S.L.6
  • 99
    • 0037124547 scopus 로고    scopus 로고
    • Polyethylene glycol-superoxide dismutase, a conjugate in search of exploitation
    • DOI 10.1016/S0169-409X(02)00029-7, PII S0169409X02000297
    • Veronese FM, Caliceti P, Schiavon O, Sergi M. 2002. Polyethylene glycol-superoxide dismutase, a conjugate in search of exploitation. Adv Drug Deliv Rev 54: 587-606. (Pubitemid 34615549)
    • (2002) Advanced Drug Delivery Reviews , vol.54 , Issue.4 , pp. 587-606
    • Veronese, F.M.1    Caliceti, P.2    Schiavon, O.3    Sergi, M.4
  • 100
    • 20444366547 scopus 로고    scopus 로고
    • Intracellular monitoring of superoxide dismutase expression in an Escherichia coli fed-batch cultivation using on-line disruption with at-line surface plasmon resonance detection
    • DOI 10.1016/j.ab.2005.03.055, PII S0003269705002708
    • Vostiar I, Tkac J, Mandenius CF. 2005. Intracellular monitoring of superoxide dismutase expression in an Escherichia coli fed-batch cultivation using on-line disruption with at-line surface plasmon resonance detection. Anal Biochem 342: 152-159. (Pubitemid 40805639)
    • (2005) Analytical Biochemistry , vol.342 , Issue.1 , pp. 152-159
    • Vostiar, I.1    Tkac, J.2    Mandenius, C.-F.3
  • 101
    • 14844296974 scopus 로고    scopus 로고
    • Purification and partial characterization of a low temperature responsive Mn-SOD from tea (Camellia sinensis (L.) O. Kuntze)
    • DOI 10.1016/j.bbrc.2005.02.051
    • Vyas D, Kumar S. 2005. Purifcation and partial characterization of a low temperature responsive Mn-SOD from tea (Camellia sinensis (L.) O. Kuntze). Biochem Biophys Res Commun 329: 831-838. (Pubitemid 40341353)
    • (2005) Biochemical and Biophysical Research Communications , vol.329 , Issue.3 , pp. 831-838
    • Vyas, D.1    Kumar, S.2
  • 102
    • 0033521027 scopus 로고    scopus 로고
    • Thermally triggered metal binding by recombinant Thermus thermophilus manganese superoxide dismutase, expressed as the apo-enzyme
    • Whittaker MM, Whittaker JW. 1999. Termally triggered metal binding by recombinant Termus thermophilus manganese superoxide dismutase, expressed as the apo-enzyme. J Biol Chem 274: 34751-34757. (Pubitemid 129509517)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34751-34757
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 104
    • 20644461904 scopus 로고    scopus 로고
    • The role and evolution of superoxide dismutases in algae
    • DOI 10.1111/j.1529-8817.2005.00086.x
    • Wolfe-Simon F, Grzebyk D, Schofeld O, Falkowski PG. 2005. Te role and evolution of superoxide dismutases in algae. J Phycol 41: 453-465. (Pubitemid 40832004)
    • (2005) Journal of Phycology , vol.41 , Issue.3 , pp. 453-465
    • Wolfe-Simon, F.1    Grzebyk, D.2    Schofield, O.3    Falkowski, P.G.4
  • 106
    • 40549145170 scopus 로고    scopus 로고
    • Improvement of recombinant baculovirus infection efciency to express manganese superoxide dismutase in silkworm larvae through dual promoters of Pph and Pp10
    • Yue WF, Li XH, Wu WC, Roy B, Li GL, Liu JM, Wu XF, Zhou JY, Zhang CX, David WCC, Miao YG. 2008. Improvement of recombinant baculovirus infection efciency to express manganese superoxide dismutase in silkworm larvae through dual promoters of Pph and Pp10. Appl Microbiol Biotechnol 78: 651-657.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 651-657
    • Yue, W.F.1    Li, X.H.2    Wu, W.C.3    Roy, B.4    Li, G.L.5    Liu, J.M.6    Wu, X.F.7    Zhou, J.Y.8    Zhang, C.X.9    Wcc, D.10    Miao, Y.G.11
  • 107
    • 29244432460 scopus 로고    scopus 로고
    • Purification and characterization of a cold-active iron superoxide dismutase from a psychrophilic bacterium, Marinomonas sp. NJ522
    • DOI 10.1007/s10529-005-4951-3
    • Zheng Z, Jiang YH, Miao JL, Wang QF, Zhang BT, Li GY. 2006. Purifcation and characterization of a cold-active iron superoxide dismutase from a psychrophilic bacterium, Marinomonas sp. NJ522. Biotechnol Lett 28: 85-88. (Pubitemid 41821477)
    • (2006) Biotechnology Letters , vol.28 , Issue.2 , pp. 85-88
    • Zheng, Z.1    Jiang, Y.-H.2    Miao, J.-L.3    Wang, Q.-F.4    Zhang, B.-T.5    Li, G.-Y.6


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