References
- Verlage Chemie Weinhein. v.1 Methods of Enzymatic Analysis Bergmyer,H.U.
- J. Bacteriol. v.131 Intracellular localization of the superoxide dismutase of E.coli ; Intracellular localization and function Britton,C.J.;I.Fridovich
- J. Biol. Chem. v.259 Anaerobic Biosythesis of the Manganese-containing Superoxide Dismutase in E. coli Camella,S.M.;H.M.Hassan
- Cell. v.70 A novel biological Messenger Charles J.Lwenstein;Solomon H.Synder Nitric OxIDE
- J. Biol. Chem. v.259 A hybrid superoxide dismutase containing both functional iron and manganese Clare,D.A.;J.Blum;I.Fridovich
- J. Exp. Bot. v.52 Leaf senscence: Correlated with increased levels of membrane permeability and lipid peroxidation and decreased levels of superoxide dismutase and catalase Dhindsa,R.S.;P.P.Dhindsa;T.A.Thorpe
- Adv. Enzymol. v.58 Superoxide dismutase Fridovich,I.
- Plant Physiol. v.59 Superoxide dismutase, I, Occurrence in higher plants Giannopolitis,C.N.;S.K.Ries https://doi.org/10.1104/pp.59.2.309
- Arch. Biochem. Biophys. v.220 Isolationo of iron-containing superoxide dismutase from Bacterioides fragilis: Reconstitution as a Mn-containing enzyme Gregory,E.M.;C.H.Dapper https://doi.org/10.1016/0003-9861(83)90413-7
- Biochem, J. v.184 Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and lipid peroxidation by desferrioxane Gutteridge,J.M.;R.Riohmond;B.Halliwell https://doi.org/10.1042/bj1840469
- Free radicals in Biology and Medicine Halliwell,B.;J.M.C.Gutteridge
- Proc. Natl. Acad. Sci. v.83 High-level espression of enzymatically active human CuZn-superoxide dismutase in E.coli Hartman,J.R.;T.Geller;Z.Yavin;D.Bartfeld;D.Kanner;H.Aviv;M.Gorecki https://doi.org/10.1073/pnas.83.19.7142
- J. Biol. Chem. v.252 Regulation of the Synthesis of Superoxide Dismutase in Escherichia coli Hassan,H.M.;I.Fridovich
- Proc. Acad. Sci. v.84 Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase Hjalmarsson,K.;S.I.Marklund;A.Engstrom;T.Edlund https://doi.org/10.1073/pnas.84.18.6340
- J. Biol. Chem. v.262 Purification an characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata Hochman,A.;A.Shemesh
- Biochem. Biophys. Acta. v.1077 Purification an characterization of a catalase-peroxidase and a typical catalase from the Klebsiella pneumoniae Hochman,A.;I.Goldberg https://doi.org/10.1016/0167-4838(91)90544-A
- Korean J. Biotechnol. Bioeng. v.12 Production of δ-Aminolevulinic acid by Rhodospirillium rubrum DM Jin Sook Lee;In Ho Park;Hye Joo Lee
- Biochem. Biophys. Res. Commun. v.196 Conversion of nitroxyl to nitric oxide in biological systems: the role of physiological oxidants and relevance to the biological activity of HNO₃ John M.Fukuto;Adrian J.Hobbs;Louis J Ignarro https://doi.org/10.1006/bbrc.1993.2307
- J. Biol. Chem. v.256 Evidence for a Natural gene transfer from the ponyfish to its bioluminescent bacterial symbiont Photobacter leiognathi Joseph,P.;Jr.Martin;I.Fridovich
- Mol. Microbiol. v.27 Transcriptional and post-transcriptional regulation by nickel of sodN gene encoding nickel-containing superoxide dismutase from Streptomyces coelicolor Muller Kim E.J.;H.J.Chung;B.Suh;Y.C.Hah;J.H.Roe https://doi.org/10.1046/j.1365-2958.1998.00674.x
- Bull. of Basic Sciences. v.12 Identification of Photosynthetic bacterium producing α-aminolevulinic acid Lee,Hye Joo
- Kor. J. Microbiol. v.24 Characterization of a hydrogen evolving strain of Rhodopseudomonas sphaeroides Lee,H.J.
- Methods Enzymol. v.349 Nickel-containing superoxide dismutase Lee J.W.;J.H.Roe;S.O.Kang https://doi.org/10.1016/S0076-6879(02)49324-X
- J. Biol. Chem. v.193 Protein measurement with the folin phenol reagent Lowry,O.H.;N.J.Rosebrough;A.L.Farr;R.J.Randall
- Biochem. J. v.220 Properties of extracellular superoxide dismutase from human lung Marklund,S.L. https://doi.org/10.1042/bj2200269
- J. Biol. Chem. v.244 Superoxide dismutase McCord,J.M.;I.Fridovich
- J. Biol. Chem. v.247 The purification and properties of superoxide dismutase from Neurospora crassa Misra,H.P.;I.Fridovich
- Trichoplusia ni. Insect Biochem. v.882 Purification and properties of highly activive catalase from cabbage loopers Mitchell,M.J.;S.Ahmad;R.S.Pardini
- J. Bacteriol. v.176 rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis Nakayama,K. https://doi.org/10.1128/jb.176.7.1939-1943.1994
- Arch. Biochem. Biophys. v.94 Light-dependent utilization of organic compounds and photoproduction of moleculay hydrogen by photosynthetic bacteria;Relationship with nitrogen metabolism Ormerod,J.G.;K.S.Ormerod;H.Gest https://doi.org/10.1016/0003-9861(61)90073-X
- Superoxide and medicine Oyanagui,Y.
- Free Rad. Biol. Med. v.3 Effects of paraquat on the green alga Dunaliella salina: protection by the mimic of superoxide dismutase,desferal-Mn(IV) Rabinowitch,H.D.;C.T.Privalle;I.Fridovich https://doi.org/10.1016/S0891-5849(87)80007-2
- J. Ferment. Technol. v.65 Production of δ-aminolevulinic acid by photosynthetic bacteria Sasaki,K;I.Satoshi https://doi.org/10.1016/0385-6380(87)90109-9
- J. Bacteriol. v.177 Function and stationary phage induction of periplasmic copper-zinc superoxide dismutase and catalase/peroxidase in Caulobacter crescentus Schnell,S.;H.M.Steinman https://doi.org/10.1128/jb.177.20.5924-5929.1995
- J. Biol. Chem. v.253 The amino acid sequence of mangao superoxide dismutase from E. coli B Steinman,H.M.
- Proc. Natl. Acad. Sc. v.70 Sequence homologies among bacterial and mitochondrial superoxide dismutase Steinman,H.M.;R.L.Hill https://doi.org/10.1073/pnas.70.12.3725
- J. Bacteriol. v.162 Bacteriocuprein superoxide dismutase in Pseudomonas Steinman,H.M.
- J. Biol. Chem. v.262 Bacteriocuprein superoxide dismutase in Photobacterium leiognathi : Isolation and sequence of the gene and evidence for a precursor form Steinman,H.M.
- Handbook of enzyme Inhibitor Zollner,H.