메뉴 건너뛰기




Volumn 178, Issue 9, 1996, Pages 2564-2571

Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; COPPER ZINC SUPEROXIDE DISMUTASE;

EID: 0029958917     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.9.2564-2571.1996     Document Type: Article
Times cited : (104)

References (65)
  • 1
    • 0003243559 scopus 로고
    • MOLPHY: Programs for molecular phylogenetics I - PROTML: maximum likelihood inference of protein phylogeny
    • Adachi, J., and M. Hasegawa. 1992. MOLPHY: programs for molecular phylogenetics I - PROTML: maximum likelihood inference of protein phylogeny. Computer Monogr. 27:1-77.
    • (1992) Computer Monogr. , vol.27 , pp. 1-77
    • Adachi, J.1    Hasegawa, M.2
  • 3
    • 0024393445 scopus 로고
    • Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene
    • Asahara, H., P. M. Wistort, J. F. Bank, R. H. Bakerian, and R. P. Cunningham. 1989. Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene Biochemistry 28:4444-4449.
    • (1989) Biochemistry , vol.28 , pp. 4444-4449
    • Asahara, H.1    Wistort, P.M.2    Bank, J.F.3    Bakerian, R.H.4    Cunningham, R.P.5
  • 5
    • 0001246049 scopus 로고
    • Derivations and genotypes of some mutant derivatives of Escherichia coli K-12
    • F. C. Neidhardt, J. L Ingraham, K. B. Low, B. Magasanik, M Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D C
    • Bachmann, B. J. 1987. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12, p. 1190-1219. In F. C. Neidhardt, J. L Ingraham, K. B. Low, B. Magasanik, M Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol 2. American Society for Microbiology, Washington, D C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.2 , pp. 1190-1219
    • Bachmann, B.J.1
  • 6
    • 0023463279 scopus 로고
    • Aspects of the structure, function, and applications of superoxide dismutase
    • Bannister, J. V., W. H. Bannister, and G. Rotilio. 1987. Aspects of the structure, function, and applications of superoxide dismutase. Crit Rev. Biochem. 22:111-180.
    • (1987) Crit Rev. Biochem. , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 7
    • 0042663851 scopus 로고
    • The presence of a copper/zinc superoxide dismutase in the bacterium Photobacterium leiognathi: A likely case of gene transfer from eukaryotes to prokaryotes
    • Bannister, J. V., and M. W. Parker. 1985. The presence of a copper/zinc superoxide dismutase in the bacterium Photobacterium leiognathi: a likely case of gene transfer from eukaryotes to prokaryotes. Proc. Natl. Acad Sci USA 82:149-152.
    • (1985) Proc. Natl. Acad Sci USA , vol.82 , pp. 149-152
    • Bannister, J.V.1    Parker, M.W.2
  • 8
    • 0028841185 scopus 로고
    • Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli
    • Battistoni, A., and G. Rotilio. 1995. Isolation of an active and heat-stable monomeric form of Cu,Zn superoxide dismutase from the periplasmic space of Escherichia coli FEBS Lett. 374:199-202.
    • (1995) FEBS Lett. , vol.374 , pp. 199-202
    • Battistoni, A.1    Rotilio, G.2
  • 9
    • 0025016826 scopus 로고
    • A protein isolated from Brucella abortus is a Cu-Zn superoxide dismutase
    • Beck, B. L., L. B. Tabatabai, and J. E. Mayfield. 1990. A protein isolated from Brucella abortus is a Cu-Zn superoxide dismutase. Biochemistry 29: 372-376.
    • (1990) Biochemistry , vol.29 , pp. 372-376
    • Beck, B.L.1    Tabatabai, L.B.2    Mayfield, J.E.3
  • 10
    • 85035159673 scopus 로고
    • Duke University. Personal communication
    • Benov, B., W. F. Beyer, and I. Fridovich (Duke University). 1995. Personal communication
    • (1995)
    • Benov, B.1    Beyer, W.F.2    Fridovich, I.3
  • 11
    • 0029078783 scopus 로고
    • Copper, zinc superoxide dismutase in Escherichia coli: Periplasmic localization
    • Benov, L., L. Y. Chang, B. Day, and I. Fridovich. 1995. Copper, zinc superoxide dismutase in Escherichia coli: periplasmic localization. Arch. Biochem. Biophys. 319:508-511.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 508-511
    • Benov, L.1    Chang, L.Y.2    Day, B.3    Fridovich, I.4
  • 12
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- And zinc-containing superoxide dismutase
    • Benov, L. T., and I. Fridovich. 1994. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase J Biol. Chem. 269:25310-25314.
    • (1994) J Biol. Chem. , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 13
    • 0003191832 scopus 로고
    • ™ competent cells
    • ™ competent cells Bethesda Res. Lab. Focus 8:9.
    • (1986) Bethesda Res. Lab. Focus , vol.8 , pp. 9
  • 14
    • 0003691711 scopus 로고
    • Mechanisms of oxygen toxicity as revealed by studies of yeast mutants with changed response to oxidative stress
    • P A. Cerutti et al. (ed.), Alan R Liss, Inc., New York
    • Bilinski, T., Z. Krawiec, J. Litwinska, and M. Blaszczynski. 1988. Mechanisms of oxygen toxicity as revealed by studies of yeast mutants with changed response to oxidative stress, p. 109-123. In P A. Cerutti et al. (ed.), Oxyradicals in Molecular Biology and Pathology Alan R Liss, Inc., New York.
    • (1988) Oxyradicals in Molecular Biology and Pathology , pp. 109-123
    • Bilinski, T.1    Krawiec, Z.2    Litwinska, J.3    Blaszczynski, M.4
  • 15
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carlioz, A., and D. Touati. 1986. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 5:623-630.
    • (1986) EMBO J. , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 16
    • 0020058459 scopus 로고
    • Construction and characterization of new cloning vehicles. VI Plasmid pBR329, a new derivative of pBR328 lacking the 482-base-pair inverted duplication
    • Covarrubias, L., and F. Bolivar. 1982. Construction and characterization of new cloning vehicles. VI Plasmid pBR329, a new derivative of pBR328 lacking the 482-base-pair inverted duplication. Gene 17:79-89.
    • (1982) Gene , vol.17 , pp. 79-89
    • Covarrubias, L.1    Bolivar, F.2
  • 17
    • 0001298780 scopus 로고
    • Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase
    • Farr, S. B., R. D'Ari, and D. Touati. 1986. Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase. Proc Natl. Acad. Sci. USA 83:8268-8272.
    • (1986) Proc Natl. Acad. Sci. USA , vol.83 , pp. 8268-8272
    • Farr, S.B.1    D'Ari, R.2    Touati, D.3
  • 18
    • 0002795683 scopus 로고
    • Dihydroxyacid dehydratase: Isolation, characterization as Fe-S proteins, and sensitivity to inactivation by oxygen radicals
    • D. C. Z. Barak and J. V. Schloss (ed.), Deerfield, Borch and Balaban, Philadelphia
    • Flint, D. H., and M. H. Emptage. 1990. Dihydroxyacid dehydratase: isolation, characterization as Fe-S proteins, and sensitivity to inactivation by oxygen radicals In D. C. Z. Barak and J. V. Schloss (ed.), Biosynthesis of branched chain amino acids. Deerfield, Borch and Balaban, Philadelphia.
    • (1990) Biosynthesis of Branched Chain Amino Acids
    • Flint, D.H.1    Emptage, M.H.2
  • 19
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint, D. H., J. F. Tuminello, and M. H. Emptage. 1993. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol. Chem. 268: 22369-22376.
    • (1993) J Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 20
    • 0024308039 scopus 로고
    • Superoxide dismutases. An adaptation to a paramagnetic gas
    • Fridovich, I. 1989. Superoxide dismutases. An adaptation to a paramagnetic gas. J. Biol. Chem. 264:7761-7764.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7761-7764
    • Fridovich, I.1
  • 21
    • 0026011632 scopus 로고
    • Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase
    • Gardner, P. R., and I. Fridovich. 1991. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase J. Biol. Chem. 266:1478-1483.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1478-1483
    • Gardner, P.R.1    Fridovich, I.2
  • 22
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R., and I. Fridovich. 1991. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266:19328-19333.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 23
    • 0022273807 scopus 로고
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis
    • 2-induced manganese-containing superoxide dismutase from Bacteroides fragilis. Arch. Biochem. Biophys 238:83-89.
    • (1985) Arch. Biochem. Biophys , vol.238 , pp. 83-89
    • Gregory, E.M.1
  • 24
    • 0024330563 scopus 로고
    • Microbial superoxide dismutases
    • Hassan, H. M. 1989. Microbial superoxide dismutases. Adv. Genet 26:65-97.
    • (1989) Adv. Genet , vol.26 , pp. 65-97
    • Hassan, H.M.1
  • 25
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, S., and J. G. Henikoff. 1992. Amino acid substitution matrices from protein blocks. Proc Natl. Acad. Sci. USA 89:10915-10919.
    • (1992) Proc Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 26
    • 0029086244 scopus 로고
    • A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli
    • Imlay, J. A. 1995 A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli. J. Biol Chem. 270:19767-19777
    • (1995) J. Biol Chem. , vol.270 , pp. 19767-19777
    • Imlay, J.A.1
  • 27
    • 0025800392 scopus 로고
    • Assay of metabolic superoxide production in Escherichia coli
    • Imlay, J. A., and I. Fridovich. 1991. Assay of metabolic superoxide production in Escherichia coli J. Biol. Chem 266:6957-6965.
    • (1991) J. Biol. Chem , vol.266 , pp. 6957-6965
    • Imlay, J.A.1    Fridovich, I.2
  • 28
    • 0023192484 scopus 로고
    • Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide
    • Imlay, J. A., and S. Linn. 1987 Mutagenesis and stress responses induced in Escherichia coli by hydrogen peroxide. J Bacteriol. 169:2967-2976.
    • (1987) J Bacteriol. , vol.169 , pp. 2967-2976
    • Imlay, J.A.1    Linn, S.2
  • 29
    • 0025518475 scopus 로고
    • Sequence divergence of pea Cu/Zn superoxide dismutase II cDNAs
    • Isin, S. H., J. J. Burke, and R. D. Allen. 1990 Sequence divergence of pea Cu/Zn superoxide dismutase II cDNAs. Plant Mol. Biol. 15:789-791.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 789-791
    • Isin, S.H.1    Burke, J.J.2    Allen, R.D.3
  • 30
    • 0023664191 scopus 로고
    • Hybrid pUC vectors for addition of new restriction enzyme sites to the ends of DNA fragments
    • Kay, R., and J. McPherson. 1987. Hybrid pUC vectors for addition of new restriction enzyme sites to the ends of DNA fragments. Nucleic Acids Res. 15:2778.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 2778
    • Kay, R.1    McPherson, J.2
  • 31
    • 0028871420 scopus 로고
    • Superoxide and the production of oxidative DNA damage
    • Keyer, K., A. S. Gort, and J. A. Imlay. 1995. Superoxide and the production of oxidative DNA damage. J. Bacteriol. 177:6782-6790.
    • (1995) J. Bacteriol. , vol.177 , pp. 6782-6790
    • Keyer, K.1    Gort, A.S.2    Imlay, J.A.3
  • 32
    • 0025334980 scopus 로고
    • Improvements in protein secondary structure prediction by an enhanced neural network
    • Kneller, D. G., F. E. Cohen, and R. Langridge. 1990. Improvements in protein secondary structure prediction by an enhanced neural network. J. Mol. Biol. 214:171-182.
    • (1990) J. Mol. Biol. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 33
    • 0003875229 scopus 로고
    • Correlation between the physical and genetic maps of the Escherichia coli K-12 chromosome
    • K. Drlica and M. Riley (ed ), American Society for Microbiology, Washington, D.C.
    • Kohara, Y. 1990 Correlation between the physical and genetic maps of the Escherichia coli K-12 chromosome, p. 29-42. In K. Drlica and M. Riley (ed ), The bacterial chromosome. American Society for Microbiology, Washington, D.C.
    • (1990) The Bacterial Chromosome , pp. 29-42
    • Kohara, Y.1
  • 34
    • 0025885796 scopus 로고
    • Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae
    • Kroll, J. S., P. R. Langford, and B. M. Loynds. 1991. Copper-zinc superoxide dismutase of Haemophilus influenzae and H. parainfluenzae. J Bacteriol. 173:7449-7457
    • (1991) J Bacteriol. , vol.173 , pp. 7449-7457
    • Kroll, J.S.1    Langford, P.R.2    Loynds, B.M.3
  • 35
    • 0028804901 scopus 로고
    • Bacterial [Cu,Zn]-superoxide dismutase: Phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!
    • Kroll, J. S., P. R. Langford, K. E. Wilks, and A. D. Keil. 1995. Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all! Microbiology 141:2271-2279.
    • (1995) Microbiology , vol.141 , pp. 2271-2279
    • Kroll, J.S.1    Langford, P.R.2    Wilks, K.E.3    Keil, A.D.4
  • 36
    • 0023178381 scopus 로고
    • α,β-Dihydroxyisovalerate dehydratase: A superoxide-sensitive enzyme
    • Kuo, C.-F., T. Mashino, and I. Fridovich. 1987. α,β-Dihydroxyisovalerate dehydratase: a superoxide-sensitive enzyme. J. Biol Chem. 262:4724-4727.
    • (1987) J. Biol Chem. , vol.262 , pp. 4724-4727
    • Kuo, C.-F.1    Mashino, T.2    Fridovich, I.3
  • 37
    • 0026554637 scopus 로고
    • Copper-zinc superoxide dismutase in Haemophilus species
    • Langford, P. R., B. M. Loynds, and J. S. Kroll. 1992. Copper-zinc superoxide dismutase in Haemophilus species. J. Gen. Microbiol. 138:517-522.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 517-522
    • Langford, P.R.1    Loynds, B.M.2    Kroll, J.S.3
  • 40
    • 0020448702 scopus 로고
    • Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment
    • Lunn, C., and V. Pigiet. 1982. Localization of thioredoxin from Escherichia coli in an osmotically sensitive compartment. J. Biol. Chem. 257:11424-11430
    • (1982) J. Biol. Chem. , vol.257 , pp. 11424-11430
    • Lunn, C.1    Pigiet, V.2
  • 41
    • 0017876650 scopus 로고
    • Permeation of the erythrocyte stroma by superoxide radical
    • Lynch, R. E., and I. Fridovich. 1978. Permeation of the erythrocyte stroma by superoxide radical. J. Biol. Chem. 253:4697-4699.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4697-4699
    • Lynch, R.E.1    Fridovich, I.2
  • 42
    • 0023030627 scopus 로고
    • A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor
    • Martin, M. E., B. R. Byers, M. O. J. Olson, M. L. Salin, J. E. L. Arceneaux, and C. Tolbert. 1986. A Streptococcus mutans superoxide dismutase that is active with either manganese or iron as a cofactor. J Biol. Chem. 261:9361-9367.
    • (1986) J Biol. Chem. , vol.261 , pp. 9361-9367
    • Martin, M.E.1    Byers, B.R.2    Olson, M.O.J.3    Salin, M.L.4    Arceneaux, J.E.L.5    Tolbert, C.6
  • 43
    • 85035167873 scopus 로고    scopus 로고
    • Personal communication
    • 42a. Mayfield, J. Personal communication
    • Mayfield, J.1
  • 44
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M., and I. Fridovich. 1969. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 45
    • 0018245354 scopus 로고
    • The evolution of the environment and its influence on the evolution of life
    • Ochiai, E.-I. 1978. The evolution of the environment and its influence on the evolution of life. Origins Life 9:81-91.
    • (1978) Origins Life , vol.9 , pp. 81-91
    • Ochiai, E.-I.1
  • 46
    • 0016338605 scopus 로고
    • Origins of metal ions in biology
    • Osterberg, R. 1974. Origins of metal ions in biology. Nature (London) 249:382-383.
    • (1974) Nature (London) , vol.249 , pp. 382-383
    • Osterberg, R.1
  • 47
    • 0016207797 scopus 로고
    • Isolation of a new copper-containing superoxide dismutase bacteriocuprein
    • Puget, K., and A. M. Michelson. 1974. Isolation of a new copper-containing superoxide dismutase bacteriocuprein. Biochem. Biophys. Res. Commun 58:830-838.
    • (1974) Biochem. Biophys. Res. Commun , vol.58 , pp. 830-838
    • Puget, K.1    Michelson, A.M.2
  • 48
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 49
    • 0021243187 scopus 로고
    • Cloning of the iron superoxide dismutase gene (sodB) in Escherichia coli K-12
    • Sakamoto, H., and D. Touati. 1984. Cloning of the iron superoxide dismutase gene (sodB) in Escherichia coli K-12. J. Bacteriol. 159:418-420.
    • (1984) J. Bacteriol. , vol.159 , pp. 418-420
    • Sakamoto, H.1    Touati, D.2
  • 51
    • 0028800240 scopus 로고
    • Function and stationary phase induction of periplasmic copper-zinc superoxide dismutase and catalase/peroxidase in Caulobacter crescentus
    • Schnell, S., and H. M. Steinman. 1995. Function and stationary phase induction of periplasmic copper-zinc superoxide dismutase and catalase/peroxidase in Caulobacter crescentus J Bacteriol. 177:5924-5929.
    • (1995) J Bacteriol. , vol.177 , pp. 5924-5929
    • Schnell, S.1    Steinman, H.M.2
  • 52
    • 0026633193 scopus 로고
    • A comparison of evolutionary rates of the two major kinds of superoxide dismutase
    • Smith, M. W., and R. F. Doolittle. 1992. A comparison of evolutionary rates of the two major kinds of superoxide dismutase J. Mol. Evol. 34:175-184.
    • (1992) J. Mol. Evol. , vol.34 , pp. 175-184
    • Smith, M.W.1    Doolittle, R.F.2
  • 53
    • 0020412339 scopus 로고
    • Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel bacteriocuprein form of the enzyme
    • Steinman, H. M. 1982. Copper-zinc superoxide dismutase from Caulobacter crescentus CB15. A novel bacteriocuprein form of the enzyme. J. Biol. Chem. 257:10283-10293.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10283-10293
    • Steinman, H.M.1
  • 54
    • 0021827654 scopus 로고
    • Bacteriocuprein superoxide dismutases in pseudomonads
    • Steinman, H. M. 1985. Bacteriocuprein superoxide dismutases in pseudomonads. J. Bacteriol. 162:1255-1260.
    • (1985) J. Bacteriol. , vol.162 , pp. 1255-1260
    • Steinman, H.M.1
  • 55
    • 0023644523 scopus 로고
    • Bacteriocuprein superoxide dismutase of Photobacterium leiognathi
    • Steinman, H. M. 1987. Bacteriocuprein superoxide dismutase of Photobacterium leiognathi. J Biol. Chem. 262:1882-1887.
    • (1987) J Biol. Chem. , vol.262 , pp. 1882-1887
    • Steinman, H.M.1
  • 56
    • 0027502271 scopus 로고
    • Function of periplasmic copper-zinc superoxide dismutase in Caulobacter crescentus
    • Steinman, H. M. 1993. Function of periplasmic copper-zinc superoxide dismutase in Caulobacter crescentus. J. Bacteriol. 175:1198-1202.
    • (1993) J. Bacteriol. , vol.175 , pp. 1198-1202
    • Steinman, H.M.1
  • 57
    • 0025339960 scopus 로고
    • Copper-zinc superoxide dismutase of Caulobacter crescentus: Cloning, sequencing, and mapping of the gene and periplasmic location of the enzyme
    • Steinman, H. M., and B. Ely. 1990. Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing, and mapping of the gene and periplasmic location of the enzyme. J. Bacteriol. 172:2901-2910.
    • (1990) J. Bacteriol. , vol.172 , pp. 2901-2910
    • Steinman, H.M.1    Ely, B.2
  • 58
    • 0016264038 scopus 로고
    • Bovine erythrocyte superoxide dismutase. Complete amino acid sequence
    • Steinman, H. M., V. R. Naik, J. L. Abernethy, and R. L. Hill. 1974. Bovine erythrocyte superoxide dismutase. Complete amino acid sequence J. Biol. Chem. 249:7326-7338.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7326-7338
    • Steinman, H.M.1    Naik, V.R.2    Abernethy, J.L.3    Hill, R.L.4
  • 60
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 angstrom structure of copper, zinc superoxide dismutase
    • Tainer, J. A., E. D. Getzoff, K. M. Beem, J. S. Richardson, and D. C. Richardson. 1982. Determination and analysis of the 2 angstrom structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160:181-217.
    • (1982) J. Mol. Biol. , vol.160 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5
  • 63
    • 0026636510 scopus 로고
    • Construction of Cu-Zn superoxide dismutase deletion mutants of Brucella abortus: Analysis of survival in vitro in epithelial and phagocytic cells and in vivo in mice
    • Tatum, F. K., P. G. Detilleux, J. M. Sacks, and S. M. Halling. 1992. Construction of Cu-Zn superoxide dismutase deletion mutants of Brucella abortus: analysis of survival in vitro in epithelial and phagocytic cells and in vivo in mice. Infect. Immun. 50:2863-2869.
    • (1992) Infect. Immun. , vol.50 , pp. 2863-2869
    • Tatum, F.K.1    Detilleux, P.G.2    Sacks, J.M.3    Halling, S.M.4
  • 64
    • 0020605387 scopus 로고
    • Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12
    • Touati, D. 1983. Cloning and mapping of the manganese superoxide dismutase gene (sodA) of Escherichia coli K-12. J. Bacteriol. 155:1078-1087.
    • (1983) J. Bacteriol. , vol.155 , pp. 1078-1087
    • Touati, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.