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Volumn 20, Issue 15, 2014, Pages 2416-2436

Simple biological systems for assessing the activity of superoxide dismutase mimics

Author keywords

[No Author keywords available]

Indexed keywords

MANGANESE; PORPHYRIN; PORPHYRIN DERIVATIVE; SUPEROXIDE DISMUTASE; METALLOPORPHYRIN;

EID: 84899721306     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2013.5576     Document Type: Review
Times cited : (42)

References (131)
  • 1
    • 0036612888 scopus 로고    scopus 로고
    • Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli
    • Al-Maghrebi M, Fridovich I, and Benov L. Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli. Arch Biochem Biophys 402: 104-109, 2002.
    • (2002) Arch Biochem Biophys , vol.402 , pp. 104-109
    • Al-Maghrebi, M.1    Fridovich, I.2    Benov, L.3
  • 2
    • 33645106563 scopus 로고    scopus 로고
    • Photosensitizing action of isomeric zinc N-methylpyridylporphyrins in human carcinoma cells
    • Al-Mutairi DA, Craik JD, Batinic-Haberle I, and Benov LT. Photosensitizing action of isomeric zinc N-methylpyridylporphyrins in human carcinoma cells. Free Radic Res 40: 477-483, 2006.
    • (2006) Free Radic Res , vol.40 , pp. 477-483
    • Al-Mutairi, D.A.1    Craik, J.D.2    Batinic-Haberle, I.3    Benov, L.T.4
  • 3
    • 34848837937 scopus 로고    scopus 로고
    • Inactivation of metabolic enzymes by photo-treatment with zinc meta N-methylpyridylporphyrin
    • Al-Mutairi DA, Craik JD, Batinic-Haberle I, and Benov LT. Inactivation of metabolic enzymes by photo-treatment with zinc meta N-methylpyridylporphyrin. Biochim Biophys Acta 1770: 1520-1527, 2007.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 1520-1527
    • Al-Mutairi, D.A.1    Craik, J.D.2    Batinic-Haberle, I.3    Benov, L.T.4
  • 4
    • 33845411007 scopus 로고    scopus 로고
    • Induction of oxidative cell damage by photo-treatment with zinc N-methylpyridylporphyrin
    • Al-Mutairi DA, Craik JD, Batinic-Haberle I, and Benov LT. Induction of oxidative cell damage by photo-treatment with zinc N-methylpyridylporphyrin. Free Radic Res 41: 89-96, 2007.
    • (2007) Free Radic Res , vol.41 , pp. 89-96
    • Al-Mutairi, D.A.1    Craik, J.D.2    Batinic-Haberle, I.3    Benov, L.T.4
  • 5
    • 84860851659 scopus 로고    scopus 로고
    • Mononuclear iron enzymes are primary targets of hydrogen peroxide stress
    • Anjem A, and Imlay JA. Mononuclear iron enzymes are primary targets of hydrogen peroxide stress. J Biol Chem 287: 15544-15556, 2012.
    • (2012) J Biol Chem , vol.287 , pp. 15544-15556
    • Anjem, A.1    Imlay, J.A.2
  • 6
    • 0019475137 scopus 로고
    • Manganese and defenses against oxygen toxicity in Lactobacillus plantarum
    • Archibald FS, and Fridovich I. Manganese and defenses against oxygen toxicity in Lactobacillus plantarum. J Bacteriol 145: 442-451, 1981.
    • (1981) J Bacteriol , vol.145 , pp. 442-451
    • Archibald, F.S.1    Fridovich, I.2
  • 7
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes: In vitro
    • Archibald FS, and Fridovich I. The scavenging of superoxide radical by manganous complexes: in vitro. Arch Biochem Biophys 214: 452-463, 1982.
    • (1982) Arch Biochem Biophys , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 10
    • 84860798289 scopus 로고    scopus 로고
    • Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds
    • Barnese K, Gralla E, Valentine J, and Cabelli DE. Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds. Proc Natl Acad Sci U S A 109: 6892-6897, 2012.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6892-6897
    • Barnese, K.1    Gralla, E.2    Valentine, J.3    Cabelli, D.E.4
  • 11
    • 78651326846 scopus 로고    scopus 로고
    • Chemistry, biology and medical effects of water soluble metalloporphyrins
    • edited by Kadish KM, Smith KM, and Guillard R. Singapore: World Scientific
    • Batinic-Haberle I, Reboucas JS, Benov L, and Spasojevi I. Chemistry, biology and medical effects of water soluble metalloporphyrins. In: Handbook of Porphyrin Science, edited by Kadish KM, Smith KM, and Guillard R. Singapore: World Scientific, 2011, pp. 291-393.
    • (2011) Handbook of Porphyrin Science , pp. 291-393
    • Batinic-Haberle, I.1    Reboucas, J.S.2    Benov, L.3    Spasojevi, I.4
  • 12
    • 0032544579 scopus 로고    scopus 로고
    • The ortho effect makes manganese(III) meso-tetrakis(Nmethylpyridinium- 2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic
    • Batinic-Haberle I, Benov L, Spasojevic I, and Fridovich I. The ortho effect makes manganese(III) meso-tetrakis(Nmethylpyridinium- 2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic. J Biol Chem 273: 24521-24528, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 24521-24528
    • Batinic-Haberle, I.1    Benov, L.2    Spasojevic, I.3    Fridovich, I.4
  • 13
    • 58049131646 scopus 로고    scopus 로고
    • Pure MnTBAP selectively scavenges peroxynitrite over superoxide: Comparison of pure and commercial MnTBAP samples to MnTE-2-PyP in two models of oxidative stress injury, an SOD-specific Escherichia coli model and carrageenan-induced pleurisy
    • Batinic-Haberle I, Cuzzocrea S, Rebouças JS, Ferrer-Sueta G, Mazzon E, Di Paola R, Radi R, Spasojevic I, Benov L, and Salvemini D. Pure MnTBAP selectively scavenges peroxynitrite over superoxide: comparison of pure and commercial MnTBAP samples to MnTE-2-PyP in two models of oxidative stress injury, an SOD-specific Escherichia coli model and carrageenan-induced pleurisy. Free Radic Biol Med 46: 192-201, 2009.
    • (2009) Free Radic Biol Med , vol.46 , pp. 192-201
    • Batinic-Haberle, I.1    Cuzzocrea, S.2    Rebouças, J.S.3    Ferrer-Sueta, G.4    Mazzon, E.5    Di Paola, R.6    Radi, R.7    Spasojevic, I.8    Benov, L.9    Salvemini, D.10
  • 14
    • 0031571101 scopus 로고    scopus 로고
    • A potent superoxide dismutase mimic: Manganese betaoctabromo-meso- tetrakis-(N-methylpyridinium-4-yl) porphyrin
    • Batinic-Haberle I, Liochev SI, Spasojevic I, and Fridovich I. A potent superoxide dismutase mimic: manganese betaoctabromo-meso-tetrakis-(N- methylpyridinium-4-yl) porphyrin. Arch Biochem Biophys 343: 225-233, 1997.
    • (1997) Arch Biochem Biophys , vol.343 , pp. 225-233
    • Batinic-Haberle, I.1    Liochev, S.I.2    Spasojevic, I.3    Fridovich, I.4
  • 15
    • 79953772429 scopus 로고    scopus 로고
    • A combination of two antioxidants (an SOD mimic and ascorbate) produces a pro-oxidative effect forcing Escherichia coli to adapt via induction of oxyR regulon
    • Batinić-Haberle I, Rajić Z, and Benov L. A combination of two antioxidants (an SOD mimic and ascorbate) produces a pro-oxidative effect forcing Escherichia coli to adapt via induction of oxyR regulon. Anticancer Agents Med Chem 11: 329-340, 2011.
    • (2011) Anticancer Agents Med Chem , vol.11 , pp. 329-340
    • Batinić-Haberle, I.1    Rajić, Z.2    Benov, L.3
  • 17
    • 77954735594 scopus 로고    scopus 로고
    • Superoxide dismutase mimics: Chemistry, pharmacology, and therapeutic potential
    • Batinić-Haberle I, Rebouças JS, and Spasojević I. Superoxide dismutase mimics: chemistry, pharmacology, and therapeutic potential. Antioxid Redox Signal 13: 877-918, 2010.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 877-918
    • Batinić-Haberle, I.1    Rebouças, J.S.2    Spasojević, I.3
  • 18
    • 3042632985 scopus 로고    scopus 로고
    • Tetrahydrobiopterin rapidly reduces the SOD mimic Mn(III) ortho-tetrakis(N-ethylpyridinium-2-yl)porphyrin
    • Batinic-Haberle I, Spasojevic I, and Fridovich I. Tetrahydrobiopterin rapidly reduces the SOD mimic Mn(III) ortho-tetrakis(N-ethylpyridinium-2-yl) porphyrin. Free Radic Biol Med 37: 367-374, 2004.
    • (2004) Free Radic Biol Med , vol.37 , pp. 367-374
    • Batinic-Haberle, I.1    Spasojevic, I.2    Fridovich, I.3
  • 19
    • 0000363321 scopus 로고    scopus 로고
    • Relationship among redox potentials, proton dissociation constants of pyrrolic nitrogens, and in vivo and in vitro superoxide dismutating activities of manganese(III) and iron(III) water-soluble porphyrins
    • Batinic-Haberle I, Spasojevic I, Hambright P, Benov L, Cmmbliss AL, and Fridovich I. Relationship among redox potentials, proton dissociation constants of pyrrolic nitrogens, and in vivo and in vitro superoxide dismutating activities of manganese(III) and iron(III) water-soluble porphyrins. Inorg Chem 38: 4011-4022, 1999.
    • (1999) Inorg Chem , vol.38 , pp. 4011-4022
    • Batinic-Haberle, I.1    Spasojevic, I.2    Hambright, P.3    Benov, L.4    Cmmbliss, A.L.5    Fridovich, I.6
  • 22
    • 84899764816 scopus 로고    scopus 로고
    • SOD therapeutics: Latest insights into their structure-activity relationships and impact on the cellular redox-based signaling pathways
    • Batinic-Haberle I, Tovmasyan A, Roberts ERH, Vujaskovic Z, Leong KW, and Spasojevic I. SOD therapeutics: latest insights into their structure-activity relationships and impact on the cellular redox-based signaling pathways. Antioxid Redox Signal 20: 2372-2415, 2014.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 2372-2415
    • Batinic-Haberle, I.1    Tovmasyan, A.2    Roberts, E.R.H.3    Vujaskovic, Z.4    Leong, K.W.5    Spasojevic, I.6
  • 23
    • 33947323759 scopus 로고    scopus 로고
    • Lost in translation: Treatment trials in the SOD1 mouse and in human ALS
    • Benatar M. Lost in translation: treatment trials in the SOD1 mouse and in human ALS. Neurobiol Dis 26: 1-13, 2007.
    • (2007) Neurobiol Dis , vol.26 , pp. 1-13
    • Benatar, M.1
  • 24
    • 0037098409 scopus 로고    scopus 로고
    • Isomeric N-alkylpyridylporphyrins and their Zn(II) complexes: Inactive as SOD mimics but powerful photosensitizers
    • Benov L, Batinic-Haberle I, Spasojevic I, and Fridovich I. Isomeric N-alkylpyridylporphyrins and their Zn(II) complexes: inactive as SOD mimics but powerful photosensitizers. Arch Biochem Biophys 402: 159-165, 2002.
    • (2002) Arch Biochem Biophys , vol.402 , pp. 159-165
    • Benov, L.1    Batinic-Haberle, I.2    Spasojevic, I.3    Fridovich, I.4
  • 25
    • 0029078783 scopus 로고
    • Copper, zinc superoxide dismutase in Escherichia coli periplasmic localization
    • Benov L, Chang LY, Day B, and Fridovich I. Copper, zinc superoxide dismutase in Escherichia coli periplasmic localization. Arch Biochem Biophys 319: 508-511, 1995.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 508-511
    • Benov, L.1    Chang, L.Y.2    Day, B.3    Fridovich, I.4
  • 26
    • 79953797299 scopus 로고    scopus 로고
    • The potential of Zn(II) N-alkylpyridylporphyrins for anticancer therapy
    • Benov L, Craik J, and Batinic-Haberle I. The potential of Zn(II) N-alkylpyridylporphyrins for anticancer therapy. Anticancer Agents Med Chem 11: 233-241, 2011.
    • (2011) Anticancer Agents Med Chem , vol.11 , pp. 233-241
    • Benov, L.1    Craik, J.2    Batinic-Haberle, I.3
  • 27
    • 84858155372 scopus 로고    scopus 로고
    • Protein damage by photo-activated Zn(II) N-alkylpyridylporphyrins
    • Benov L, Craik J, and Batinic-Haberle I. Protein damage by photo-activated Zn(II) N-alkylpyridylporphyrins. Amino Acids 42: 117-128, 2012.
    • (2012) Amino Acids , vol.42 , pp. 117-128
    • Benov, L.1    Craik, J.2    Batinic-Haberle, I.3
  • 28
    • 0029075602 scopus 로고
    • Superoxide dismutase protects against aerobic heat shock in Escherichia coli
    • Benov L, and Fridovich I. Superoxide dismutase protects against aerobic heat shock in Escherichia coli. J Bacteriol 177: 3344-3346, 1995.
    • (1995) J Bacteriol , vol.177 , pp. 3344-3346
    • Benov, L.1    Fridovich, I.2
  • 29
    • 0030601870 scopus 로고    scopus 로고
    • The rate of adaptive mutagenesis in Escherichia coli is enhanced by oxygen (superoxide)
    • Benov L, and Fridovich I. The rate of adaptive mutagenesis in Escherichia coli is enhanced by oxygen (superoxide). Mutat Res 357: 231-236, 1996.
    • (1996) Mutat Res , vol.357 , pp. 231-236
    • Benov, L.1    Fridovich, I.2
  • 30
    • 0033548265 scopus 로고    scopus 로고
    • Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli: The transketolase connection
    • Benov L, and Fridovich I. Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli: the transketolase connection. J Biol Chem 274: 4202-4206, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 4202-4206
    • Benov, L.1    Fridovich, I.2
  • 31
    • 0029787379 scopus 로고    scopus 로고
    • The mechanism of the auxotrophy for sulfur-containing amino acids imposed upon Escherichia coli by superoxide
    • Benov L, Kredich NM, and Fridovich I. The mechanism of the auxotrophy for sulfur-containing amino acids imposed upon Escherichia coli by superoxide. J Biol Chem 271: 21037-21040, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 21037-21040
    • Benov, L.1    Kredich, N.M.2    Fridovich, I.3
  • 32
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- and zinc-containing superoxide dismutase
    • Benov LT, and Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem 269: 25310-25314, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 35
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carlioz A, and Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J 5: 623-630, 1986.
    • (1986) EMBO J , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 37
    • 84864600170 scopus 로고    scopus 로고
    • Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria
    • Chiang SM, and Schellhorn HE. Regulators of oxidative stress response genes in Escherichia coli and their functional conservation in bacteria. Arch Biochem Biophys 525: 161-169, 2012.
    • (2012) Arch Biochem Biophys , vol.525 , pp. 161-169
    • Chiang, S.M.1    Schellhorn, H.E.2
  • 38
    • 84055192382 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: From research to therapeutic attempts and therapeutic perspectives
    • Contestabile A. Amyotrophic lateral sclerosis: from research to therapeutic attempts and therapeutic perspectives. Curr Med Chem 18: 5655-5665, 2011.
    • (2011) Curr Med Chem , vol.18 , pp. 5655-5665
    • Contestabile, A.1
  • 39
    • 0024227792 scopus 로고
    • The uniqueness of superoxide dismutase (SOD)-why cannot most copper compounds substitute SOD in vivo?
    • Czapski G, and Goldstein S. The uniqueness of superoxide dismutase (SOD)-why cannot most copper compounds substitute SOD in vivo? Free Radic Res Commun 4: 225-229, 1988.
    • (1988) Free Radic Res Commun , vol.4 , pp. 225-229
    • Czapski, G.1    Goldstein, S.2
  • 40
    • 14644400014 scopus 로고
    • Requirements for SOD mimics operating in vitro to work also in vivo
    • Czapski G, and Goldstein S. Requirements for SOD mimics operating in vitro to work also in vivo. Free Radic Res Commun 12-13 Pt 1: 167-171, 1991.
    • (1991) Free Radic Res Commun , vol.12-13 , Issue.PART 1 , pp. 167-171
    • Czapski, G.1    Goldstein, S.2
  • 41
    • 0034697370 scopus 로고    scopus 로고
    • Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis: Role of oxidative stress in iron metabolism
    • De Freitas JM, Liba A, Meneghini R, Valentine JS, and Gralla EB. Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis: role of oxidative stress in iron metabolism. J Biol Chem 275: 11645-11649, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 11645-11649
    • De Freitas, J.M.1    Liba, A.2    Meneghini, R.3    Valentine, J.S.4    Gralla, E.B.5
  • 43
  • 45
    • 77954892372 scopus 로고    scopus 로고
    • Salen manganese complexes: Multifunctional catalytic antioxidants protective in models for neurodegenerative diseases of aging in medicinal inorganic chemistry
    • ACS, edited by Sessler J, Doctrow SR, McMurry T, and Lippard S. Oxford University Press
    • Doctrow SR, Baudry M, Huffman K, Malfroy B, and Melov S. Salen manganese complexes: multifunctional catalytic antioxidants protective in models for neurodegenerative diseases of aging in medicinal inorganic chemistry. In: American Chemical Society Symposium Series 903, ACS, edited by Sessler J, Doctrow SR, McMurry T, and Lippard S. Oxford University Press, 2005, pp. 319-347.
    • (2005) American Chemical Society Symposium Series 903 , pp. 319-347
    • Doctrow, S.R.1    Baudry, M.2    Huffman, K.3    Malfroy, B.4    Melov, S.5
  • 47
    • 0019860499 scopus 로고
    • Orgotein efficacy in ameliorating side effects due to radiation therapy
    • Edsmyr F, and Menander-Huber KB. Orgotein efficacy in ameliorating side effects due to radiation therapy. Eur J Rheumatol Inflamm 4: 228-236, 1981.
    • (1981) Eur J Rheumatol Inflamm , vol.4 , pp. 228-236
    • Edsmyr, F.1    Menander-Huber, K.B.2
  • 48
    • 84889649896 scopus 로고    scopus 로고
    • Mn porphyrin in combination with ascorbate acts as a prooxidant and mediates caspase-independent cancer cell death
    • (in press)
    • Evans MK, Tovmasyan A, Batinic-Haberle I, and Devi GR. Mn porphyrin in combination with ascorbate acts as a prooxidant and mediates caspase-independent cancer cell death. Free Radic Biol Med, 2013 (in press).
    • (2013) Free Radic Biol Med
    • Evans, M.K.1    Tovmasyan, A.2    Batinic-Haberle, I.3    Devi, G.R.4
  • 49
    • 0001298780 scopus 로고
    • Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase
    • Farr SB, D'Ari R, and Touati D. Oxygen-dependent mutagenesis in Escherichia coli lacking superoxide dismutase. Proc Natl Acad Sci U S A 83: 8268-8272, 1986.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 8268-8272
    • Farr, S.B.1    D'Ari, R.2    Touati, D.3
  • 50
    • 0027989826 scopus 로고
    • Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo
    • Faulkner KM, Liochev SI, and Fridovich I. Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo. J Biol Chem 269: 23471-23476, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 23471-23476
    • Faulkner, K.M.1    Liochev, S.I.2    Fridovich, I.3
  • 51
    • 84964127559 scopus 로고
    • Cancer detection and therapy: Affinity of neoplastic, embryonic, and traumatized tissues for porphyrins and metalloporphyrins
    • Figge FH, Weiland GS, and Manganiello LO. Cancer detection and therapy: affinity of neoplastic, embryonic, and traumatized tissues for porphyrins and metalloporphyrins. Proc Soc Exp Biol Med 68: 640, 1948.
    • (1948) Proc Soc Exp Biol Med , vol.68 , pp. 640
    • Figge, F.H.1    Weiland, G.S.2    Manganiello, L.O.3
  • 52
    • 84884903879 scopus 로고    scopus 로고
    • Nitrone-based therapeutics for neurodegenerative diseases: Their use alone or in combination with lanthionines
    • Floyd RA, Castro Faria Neto HC, Zimmerman GA, Hensley K, and Towner RA. Nitrone-based therapeutics for neurodegenerative diseases: their use alone or in combination with lanthionines. Free Radic Biol Med 62: 145-156, 2013.
    • (2013) Free Radic Biol Med , vol.62 , pp. 145-156
    • Floyd, R.A.1    Castro Faria-Neto, H.C.2    Zimmerman, G.A.3    Hensley, K.4    Towner, R.A.5
  • 53
    • 79958116230 scopus 로고    scopus 로고
    • Anti-cancer activity of nitrones and observations on mechanism of action
    • Floyd RA, Chandru HK, He T, and Towner R. Anti-cancer activity of nitrones and observations on mechanism of action. Anticancer Agents Med Chem 11: 373-379, 2011.
    • (2011) Anticancer Agents Med Chem , vol.11 , pp. 373-379
    • Floyd, R.A.1    Chandru, H.K.2    He, T.3    Towner, R.4
  • 54
  • 55
    • 0032053161 scopus 로고    scopus 로고
    • Oxygen toxicity: A radical explanation
    • Fridovich I. Oxygen toxicity: a radical explanation. J Exp Biol 201: 1203-1209, 1998.
    • (1998) J Exp Biol , vol.201 , pp. 1203-1209
    • Fridovich, I.1
  • 56
    • 84873660953 scopus 로고    scopus 로고
    • Oxygen: How do we stand it?
    • Fridovich I. Oxygen: how do we stand it? Med Princ Pract 22: 131-137, 2013.
    • (2013) Med Princ Pract , vol.22 , pp. 131-137
    • Fridovich, I.1
  • 58
    • 13744258600 scopus 로고    scopus 로고
    • Cryptococcus neoformans mitochondrial superoxide dismutase: An essential link between antioxidant function and hightemperature growth
    • Giles SS, Batinic-Haberle I, Perfect JR, and Cox GM. Cryptococcus neoformans mitochondrial superoxide dismutase: an essential link between antioxidant function and hightemperature growth. Eukaryot Cell 4: 46-54, 2005.
    • (2005) Eukaryot Cell , vol.4 , pp. 46-54
    • Giles, S.S.1    Batinic-Haberle, I.2    Perfect, J.R.3    Cox, G.M.4
  • 59
    • 0031938051 scopus 로고    scopus 로고
    • Balance between endogenous superoxide stress and antioxidant defenses
    • Gort AS, and Imlay JA. Balance between endogenous superoxide stress and antioxidant defenses. J Bacteriol 180: 1402-1410, 1998.
    • (1998) J Bacteriol , vol.180 , pp. 1402-1410
    • Gort, A.S.1    Imlay, J.A.2
  • 60
    • 0025938799 scopus 로고
    • Null mutants of Saccharomyces cerevisiae Cu, Zn superoxide dismutase: Characterization and spontaneous mutation rates
    • Gralla EB, and Valentine JS. Null mutants of Saccharomyces cerevisiae Cu, Zn superoxide dismutase: characterization and spontaneous mutation rates. J Bacteriol 173: 5918-5920, 1991.
    • (1991) J Bacteriol , vol.173 , pp. 5918-5920
    • Gralla, E.B.1    Valentine, J.S.2
  • 62
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay JA. Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 77: 755-776, 2008.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 63
    • 0025851382 scopus 로고
    • Isolation and genetic analysis of a mutation that suppresses the auxotrophies of superoxide dismutase-deficient Escherichia coli K12
    • Imlay JA, and Fridovich I. Isolation and genetic analysis of a mutation that suppresses the auxotrophies of superoxide dismutase-deficient Escherichia coli K12. Mol Gen Genet 228: 410-416, 1991.
    • (1991) Mol Gen Genet , vol.228 , pp. 410-416
    • Imlay, J.A.1    Fridovich, I.2
  • 64
    • 0026508915 scopus 로고
    • Suppression of oxidative envelope damage by pseudoreversion of a superoxide dismutase-deficient mutant of Escherichia coli
    • Imlay JA, and Fridovich I. Suppression of oxidative envelope damage by pseudoreversion of a superoxide dismutase-deficient mutant of Escherichia coli. J Bacteriol 174: 953-961, 1992.
    • (1992) J Bacteriol , vol.174 , pp. 953-961
    • Imlay, J.A.1    Fridovich, I.2
  • 65
    • 2942555103 scopus 로고    scopus 로고
    • Superoxide dismutase mimetics elevate superoxide dismutase activity in vivo but do not retard aging in the nematode Caenorhabditis elegans
    • Keaney M, Matthijssens F, Sharpe M, Vanfleteren J, and Gems D. Superoxide dismutase mimetics elevate superoxide dismutase activity in vivo but do not retard aging in the nematode Caenorhabditis elegans. Free Radic Biol Med 37: 239-250, 2004.
    • (2004) Free Radic Biol Med , vol.37 , pp. 239-250
    • Keaney, M.1    Matthijssens, F.2    Sharpe, M.3    Vanfleteren, J.4    Gems, D.5
  • 66
    • 72249085979 scopus 로고    scopus 로고
    • High lipophilicity of meta Mn(III) N-alkylpyridylporphyrin-based superoxide dismutase mimics compensates for their lower antioxidant potency and makes them as effective as ortho analogues in protecting superoxide dismutase-deficient Escherichia coli
    • Kos I, Benov L, Spasojević I, Rebouças JS, and Batinić-Haberle I. High lipophilicity of meta Mn(III) N-alkylpyridylporphyrin-based superoxide dismutase mimics compensates for their lower antioxidant potency and makes them as effective as ortho analogues in protecting superoxide dismutase-deficient Escherichia coli. J Med Chem 52: 7868-7872, 2009.
    • (2009) J Med Chem , vol.52 , pp. 7868-7872
    • Kos, I.1    Benov, L.2    Spasojević, I.3    Rebouças, J.S.4    Batinić-Haberle, I.5
  • 69
    • 0028889152 scopus 로고
    • Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase
    • Lapinskas PJ, Cunningham KW, Xiu Fen L, Fink GR, and Culotta VC. Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase. Mol Cell Biol 15: 1382-1388, 1995.
    • (1995) Mol Cell Biol , vol.15 , pp. 1382-1388
    • Lapinskas, P.J.1    Cunningham, K.W.2    Xiu Fen, L.3    Fink, G.R.4    Culotta, V.C.5
  • 70
    • 0029039920 scopus 로고
    • The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity
    • Lin SJ, and Culotta VC. The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc Natl Acad Sci U S A 92: 3784-3788, 1995.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3784-3788
    • Lin, S.J.1    Culotta, V.C.2
  • 71
    • 0032619789 scopus 로고    scopus 로고
    • The mechanism of "Fenton-like" reactions and their importance for biological systems: A biologist's view
    • Liochev SI. The mechanism of "Fenton-like" reactions and their importance for biological systems: a biologist's view. Met Ions Biol Syst 36: 1-39, 1999.
    • (1999) Met Ions Biol Syst , vol.36 , pp. 1-39
    • Liochev, S.I.1
  • 72
    • 0014189487 scopus 로고
    • Hematoporphyrin derivative for detection and management of cancer
    • Lipson RL, Baldes EJ, and Gray MJ. Hematoporphyrin derivative for detection and management of cancer. Cancer 20: 2255-2257, 1967.
    • (1967) Cancer , vol.20 , pp. 2255-2257
    • Lipson, R.L.1    Baldes, E.J.2    Gray, M.J.3
  • 73
    • 84874397642 scopus 로고    scopus 로고
    • Mn (III) tetrakis (4- benzoic acid) porphyrin scavenges reactive species, reduces oxidative stress, and improves functional recovery after experimental spinal cord injury in rats: Comparison with methylprednisolone
    • Liu D, Shan Y, Valluru L, and Bao F. Mn (III) tetrakis (4- benzoic acid) porphyrin scavenges reactive species, reduces oxidative stress, and improves functional recovery after experimental spinal cord injury in rats: comparison with methylprednisolone. BMC Neurosci 14: 23, 2013.
    • (2013) BMC Neurosci , vol.14 , pp. 23
    • Liu, D.1    Shan, Y.2    Valluru, L.3    Bao, F.4
  • 74
    • 0028134969 scopus 로고
    • The requirement for yeast superoxide dismutase is bypassed through mutations in BSD2, a novel metal homeostasis gene
    • Liu XF, and Culotta VC. The requirement for yeast superoxide dismutase is bypassed through mutations in BSD2, a novel metal homeostasis gene. Mol Cell Biol 14: 7037-7045, 1994.
    • (1994) Mol Cell Biol , vol.14 , pp. 7037-7045
    • Liu, X.F.1    Culotta, V.C.2
  • 75
    • 15844429977 scopus 로고    scopus 로고
    • Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae: Mitochondrial production of toxic oxygen species in vivo
    • Longo VD, Gralla EB, and Valentine JS. Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae: mitochondrial production of toxic oxygen species in vivo. J Biol Chem 271: 12275-12280, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 12275-12280
    • Longo, V.D.1    Gralla, E.B.2    Valentine, J.S.3
  • 77
    • 33947364844 scopus 로고    scopus 로고
    • Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli
    • Macomber L, Rensing C, and Imlay JA. Intracellular copper does not catalyze the formation of oxidative DNA damage in Escherichia coli. J Bacteriol 189: 1616-1626, 2007.
    • (2007) J Bacteriol , vol.189 , pp. 1616-1626
    • MacOmber, L.1    Rensing, C.2    Imlay, J.A.3
  • 78
    • 48449087835 scopus 로고    scopus 로고
    • Prooxidant activity of the superoxide dismutase (SOD)- mimetic EUK-8 in proliferating and growth-arrested Escherichia coli cells
    • Matthijssens F, Back P, Braeckman BP, and Vanfleteren JR. Prooxidant activity of the superoxide dismutase (SOD)- mimetic EUK-8 in proliferating and growth-arrested Escherichia coli cells. Free Radic Biol Med 45: 708-715, 2008.
    • (2008) Free Radic Biol Med , vol.45 , pp. 708-715
    • Matthijssens, F.1    Back, P.2    Braeckman, B.P.3    Vanfleteren, J.R.4
  • 81
    • 0019860029 scopus 로고
    • Orgotein in the treatment of rheumatoid arthritis
    • Menander-Huber KB. Orgotein in the treatment of rheumatoid arthritis. Eur J Rheumatol Inflamm 4: 201-211, 1981.
    • (1981) Eur J Rheumatol Inflamm , vol.4 , pp. 201-211
    • Menander-Huber, K.B.1
  • 84
    • 34247213906 scopus 로고    scopus 로고
    • MnTMPyP, a metalloporphyrin-based superoxide dismutase/catalase mimetic, protects INS-1 cells and human pancreatic islets from an in vitro oxidative challenge
    • Moriscot C, Candel S, Sauret V, Kerr-Conte J, Richard MJ, Favrot MC, and Benhamou PY. MnTMPyP, a metalloporphyrin-based superoxide dismutase/catalase mimetic, protects INS-1 cells and human pancreatic islets from an in vitro oxidative challenge. Diabetes Metab 33: 44-53, 2007.
    • (2007) Diabetes Metab , vol.33 , pp. 44-53
    • Moriscot, C.1    Candel, S.2    Sauret, V.3    Kerr-Conte, J.4    Richard, M.J.5    Favrot, M.C.6    Benhamou, P.Y.7
  • 85
    • 35348836631 scopus 로고    scopus 로고
    • Only one of a wide assortment of manganese-containing SOD mimicking compounds rescues the slow aerobic growth phenotypes of both Escherichia coli and Saccharomyces cerevisiae strains lacking superoxide dismutase enzymes
    • Munroe W, Kingsley C, Durazo A, Gralla EB, Imlay JA, Srinivasan C, and Valentine JS. Only one of a wide assortment of manganese-containing SOD mimicking compounds rescues the slow aerobic growth phenotypes of both Escherichia coli and Saccharomyces cerevisiae strains lacking superoxide dismutase enzymes. J Inorg Biochem 101: 1875-1882, 2007.
    • (2007) J Inorg Biochem , vol.101 , pp. 1875-1882
    • Munroe, W.1    Kingsley, C.2    Durazo, A.3    Gralla, E.B.4    Imlay, J.A.5    Srinivasan, C.6    Valentine, J.S.7
  • 87
    • 0023265273 scopus 로고
    • Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants
    • Natvig DO, Imlay K, Touati D, and Hallewell RA. Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants. J Biol Chem 262: 14697-14701, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 14697-14701
    • Natvig, D.O.1    Imlay, K.2    Touati, D.3    Hallewell, R.A.4
  • 88
    • 3042525915 scopus 로고    scopus 로고
    • Complementation of SOD-deficient Escherichia coli by manganese porphyrin mimics of superoxide dismutase activity
    • Okado-Matsumoto A, Batinic-Haberle I, and Fridovich I. Complementation of SOD-deficient Escherichia coli by manganese porphyrin mimics of superoxide dismutase activity. Free Radic Biol Med 37: 401-410, 2004.
    • (2004) Free Radic Biol Med , vol.37 , pp. 401-410
    • Okado-Matsumoto, A.1    Batinic-Haberle, I.2    Fridovich, I.3
  • 89
    • 0000765496 scopus 로고
    • Superoxide dismutase activities of an iron porphyrin and other iron complexes
    • Pasternack RF, and Halliwell B. Superoxide dismutase activities of an iron porphyrin and other iron complexes. J Am Chem Soc 101: 1026-1031, 1979.
    • (1979) J Am Chem Soc , vol.101 , pp. 1026-1031
    • Pasternack, R.F.1    Halliwell, B.2
  • 90
    • 80053320061 scopus 로고    scopus 로고
    • Microbial growth curves: What the models tell us and what they cannot
    • Peleg M, and Corradini MG. Microbial growth curves: what the models tell us and what they cannot. Crit Rev Food Sci Nutr 51: 917-945, 2011.
    • (2011) Crit Rev Food Sci Nutr , vol.51 , pp. 917-945
    • Peleg, M.1    Corradini, M.G.2
  • 92
    • 79953760361 scopus 로고    scopus 로고
    • Cationic Mn porphyrins change their action from anti- to pro-oxidative in the presence of cellular reductants: Relevance to understanding the beneficial therapeutic effects of SOD mimics in vivo
    • Rajic Z, Benov L, Kos I, Tovmasyan A, and Batinic-Haberle I. Cationic Mn porphyrins change their action from anti- to pro-oxidative in the presence of cellular reductants: relevance to understanding the beneficial therapeutic effects of SOD mimics in vivo. Free Radic Biol Med 49: S194-S194, 2010.
    • (2010) Free Radic Biol Med , vol.49
    • Rajic, Z.1    Benov, L.2    Kos, I.3    Tovmasyan, A.4    Batinic-Haberle, I.5
  • 94
    • 0016791470 scopus 로고
    • Isolation and characterization of a manganese-containing superoxide dismutase from yeast
    • Ravindranath SD, and Fridovich I. Isolation and characterization of a manganese-containing superoxide dismutase from yeast. J Biol Chem 250: 6107-6112, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 6107-6112
    • Ravindranath, S.D.1    Fridovich, I.2
  • 95
    • 84892713567 scopus 로고    scopus 로고
    • Potential of manganoporphyrins to enhance the efficacy of pharmacological ascorbate in the treatment of pancreatic cancer
    • Rawal M, Schroeder SR, Wagner BA, Du J, Buettner GR, and Cullen JJ. Potential of manganoporphyrins to enhance the efficacy of pharmacological ascorbate in the treatment of pancreatic cancer. Free Radic Biol Med 53: S115-S115, 2012.
    • (2012) Free Radic Biol Med , vol.53
    • Rawal, M.1    Schroeder, S.R.2    Wagner, B.A.3    Du, J.4    Buettner, G.R.5    Cullen, J.J.6
  • 96
    • 44649184942 scopus 로고    scopus 로고
    • Impact of electrostatics in redox modulation of oxidative stress by Mn porphyrins: Protection of SOD-deficient Escherichia coli via alternative mechanism where Mn porphyrin acts as a Mn carrier
    • Rebouças JS, DeFreitas-Silva G, Spasojevic I, Idemori YM, Benov L, and Batinic-Haberle I. Impact of electrostatics in redox modulation of oxidative stress by Mn porphyrins: protection of SOD-deficient Escherichia coli via alternative mechanism where Mn porphyrin acts as a Mn carrier. Free Radic Biol Med 45: 201-210, 2008.
    • (2008) Free Radic Biol Med , vol.45 , pp. 201-210
    • Rebouças, J.S.1    Defreitas-Silva, G.2    Spasojevic, I.3    Idemori, Y.M.4    Benov, L.5    Batinic-Haberle, I.6
  • 97
    • 70349172939 scopus 로고    scopus 로고
    • Determination of residual manganese in Mn porphyrinbased superoxide dismutase (SOD) and peroxynitrite reductase mimics
    • Reboucas JS, Kos I, Vujaskovic Z, and Batinic-Haberle I. Determination of residual manganese in Mn porphyrinbased superoxide dismutase (SOD) and peroxynitrite reductase mimics. J Pharm Biomed Anal 50: 1088-1091, 2009.
    • (2009) J Pharm Biomed Anal , vol.50 , pp. 1088-1091
    • Reboucas, J.S.1    Kos, I.2    Vujaskovic, Z.3    Batinic-Haberle, I.4
  • 98
    • 38649139361 scopus 로고    scopus 로고
    • Pure manganese(III) 5,10,15,20-tetrakis(4-benzoic acid)porphyrin (MnTBAP) is not a superoxide dismutase mimic in aqueous systems: A case of structure-activity relationship as a watchdog mechanism in experimental therapeutics and biology
    • Reboucas JS, Spasojevic I, and Batinic-Haberle I. Pure manganese(III) 5,10,15,20-tetrakis(4-benzoic acid)porphyrin (MnTBAP) is not a superoxide dismutase mimic in aqueous systems: a case of structure-activity relationship as a watchdog mechanism in experimental therapeutics and biology. J Biol Inorg Chem 13: 289-302, 2008.
    • (2008) J Biol Inorg Chem , vol.13 , pp. 289-302
    • Reboucas, J.S.1    Spasojevic, I.2    Batinic-Haberle, I.3
  • 99
    • 53049101719 scopus 로고    scopus 로고
    • Quality of potent Mn porphyrin-based SOD mimics and peroxynitrite scavengers for pre-clinical mechanistic/therapeutic purposes
    • Reboucas JS, Spasojevic I, and Batinic-Haberle I. Quality of potent Mn porphyrin-based SOD mimics and peroxynitrite scavengers for pre-clinical mechanistic/therapeutic purposes. J Pharm Biomed Anal 48: 1046-1049, 2008.
    • (2008) J Pharm Biomed Anal , vol.48 , pp. 1046-1049
    • Reboucas, J.S.1    Spasojevic, I.2    Batinic-Haberle, I.3
  • 102
    • 0030844885 scopus 로고    scopus 로고
    • Toward the rational design of superoxide dismutase mimics: Mechanistic studies for the elucidation of substituent effects on the catalytic activity of macrocyclic manganese(II) complexes
    • Riley DP, Lennon PJ, Neumann WL, and Weiss RH. Toward the rational design of superoxide dismutase mimics: mechanistic studies for the elucidation of substituent effects on the catalytic activity of macrocyclic manganese(II) complexes. J Am Chem Soc 119: 6522-6528, 1997.
    • (1997) J Am Chem Soc , vol.119 , pp. 6522-6528
    • Riley, D.P.1    Lennon, P.J.2    Neumann, W.L.3    Weiss, R.H.4
  • 107
    • 0034707095 scopus 로고    scopus 로고
    • Surface active drugs: Self-association and interaction with membranes and surfactants. Physicochemical and biological aspects
    • Schreier S, Malheiros SVP, and De Paula E. Surface active drugs: self-association and interaction with membranes and surfactants. Physicochemical and biological aspects. Biochim Biophys Acta 1508: 210-234, 2000.
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 210-234
    • Schreier, S.1    Malheiros, S.V.P.2    De Paula, E.3
  • 114
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae: Identification of proteins predicted to mediate iron-sulfur cluster assembly
    • Strain J, Lorenz CR, Bode J, Garland S, Smolen GA, Ta DT, Vickery LE, and Culotta VC. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae: identification of proteins predicted to mediate iron-sulfur cluster assembly. J Biol Chem 273: 31138-31144, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 31138-31144
    • Strain, J.1    Lorenz, C.R.2    Bode, J.3    Garland, S.4    Smolen, G.A.5    Ta, D.T.6    Vickery, L.E.7    Culotta, V.C.8
  • 115
    • 0036821898 scopus 로고    scopus 로고
    • Part I: Pathogenetic role of peroxynitrite in the development of diabetes and diabetic vascular complications: Studies with FP15, a novel potent peroxynitrite decomposition catalyst
    • Szabo C, Mabley JG, Moeller SM, Shimanovich R, Pacher P, Virag L, Soriano FG, Van Duzer JH, Williams W, Salzman AL, and Groves JT. Part I: pathogenetic role of peroxynitrite in the development of diabetes and diabetic vascular complications: studies with FP15, a novel potent peroxynitrite decomposition catalyst. Mol Med 8: 571-580, 2002.
    • (2002) Mol Med , vol.8 , pp. 571-580
    • Szabo, C.1    Mabley, J.G.2    Moeller, S.M.3    Shimanovich, R.4    Pacher, P.5    Virag, L.6    Soriano, F.G.7    Van Duzer, J.H.8    Williams, W.9    Salzman, A.L.10    Groves, J.T.11
  • 117
    • 77956159580 scopus 로고    scopus 로고
    • Metalloporphyrin synergizes with ascorbic acid to inhibit cancer cell growth through Fenton chemistry
    • Tian J, Peehl DM, and Knox SJ. Metalloporphyrin synergizes with ascorbic acid to inhibit cancer cell growth through Fenton chemistry. Cancer Biother Radiopharm 25: 439-448, 2010.
    • (2010) Cancer Biother Radiopharm , vol.25 , pp. 439-448
    • Tian, J.1    Peehl, D.M.2    Knox, S.J.3
  • 118
    • 0024215148 scopus 로고
    • Molecular genetics of superoxide dismutases
    • Touati D. Molecular genetics of superoxide dismutases. Free Radic Biol Med 5: 393-402, 1988.
    • (1988) Free Radic Biol Med , vol.5 , pp. 393-402
    • Touati, D.1
  • 119
    • 2642648260 scopus 로고
    • The molecular genetics of superoxide dismutase in E. Coli
    • Touati D. The molecular genetics of superoxide dismutase in E. coli. Free Radic Res Commun 12-13 Pt 1: 379-382, 1991.
    • (1991) Free Radic Res Commun , vol.12-13 , Issue.PART 1 , pp. 379-382
    • Touati, D.1
  • 122
    • 84877992025 scopus 로고    scopus 로고
    • Differential coordination demands in Fe versus Mn water-soluble cationic metalloporphyrins translate into remarkably different aqueous redox chemistry and biology
    • Tovmasyan A, Weitner T, Sheng H, Lu M, Rajic Z, Warner DS, Spasojevic I, Reboucas JS, Benov L, and Batinic-Haberle I. Differential coordination demands in Fe versus Mn water-soluble cationic metalloporphyrins translate into remarkably different aqueous redox chemistry and biology. Inorg Chem 52: 5677-5691, 2013.
    • (2013) Inorg Chem , vol.52 , pp. 5677-5691
    • Tovmasyan, A.1    Weitner, T.2    Sheng, H.3    Lu, M.4    Rajic, Z.5    Warner, D.S.6    Spasojevic, I.7    Reboucas, J.S.8    Benov, L.9    Batinic-Haberle, I.10
  • 123
    • 79953763716 scopus 로고    scopus 로고
    • Methoxy-derivatization of alkyl chains increases the in vivo efficacy of cationic Mn porphyrins: Synthesis, characterization, SOD-like activity, and SOD-deficient e. Coli study of meta Mn(iii) N-methoxyalkylpyridylporphyrins
    • Tovmasyan AG, Rajic Z, Spasojevic I, Reboucas JS, Chen X, Salvemini D, Sheng H, Warner DS, Benov L, and Batinic-Haberle I. Methoxy-derivatization of alkyl chains increases the in vivo efficacy of cationic Mn porphyrins: synthesis, characterization, SOD-like activity, and SOD-deficient E. coli study of meta Mn(iii) N-methoxyalkylpyridylporphyrins. Dalton Trans 40: 4111-4121, 2011.
    • (2011) Dalton Trans , vol.40 , pp. 4111-4121
    • Tovmasyan, A.G.1    Rajic, Z.2    Spasojevic, I.3    Reboucas, J.S.4    Chen, X.5    Salvemini, D.6    Sheng, H.7    Warner, D.S.8    Benov, L.9    Batinic-Haberle, I.10
  • 124
    • 0039604509 scopus 로고
    • A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen
    • Van Loon APGM, Pesold-Hurt B, and Schatz G. A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen. Proc Natl Acad Sci U S A 83: 3820-3824, 1986.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3820-3824
    • Van Loon, A.P.G.M.1    Pesold-Hurt, B.2    Schatz, G.3
  • 125
    • 3542993226 scopus 로고    scopus 로고
    • Superoxide inhibits 4Fe-4S cluster enzymes involved in amino acid biosynthesis: Cross-compartment protection by CuZn-superoxide dismutase
    • Wallace MA, Liou LL, Martins J, Clement MHS, Bailey S, Longo VD, Valentine JS, and Gralla EB. Superoxide inhibits 4Fe-4S cluster enzymes involved in amino acid biosynthesis: cross-compartment protection by CuZn-superoxide dismutase. J Biol Chem 279: 32055-32062, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 32055-32062
    • Wallace, M.A.1    Liou, L.L.2    Martins, J.3    Clement, M.H.S.4    Bailey, S.5    Longo, V.D.6    Valentine, J.S.7    Gralla, E.B.8
  • 128
    • 84862577216 scopus 로고    scopus 로고
    • Stability, disposition, and penetration of catalytic antioxidants Mn-porphyrin and Mnsalen and of methylprednisolone in spinal cord injury
    • Wu L, Shan Y, and Liu D. Stability, disposition, and penetration of catalytic antioxidants Mn-porphyrin and Mnsalen and of methylprednisolone in spinal cord injury. Cent Nerv Syst Agents Med Chem 12: 122-130, 2012.
    • (2012) Cent Nerv Syst Agents Med Chem , vol.12 , pp. 122-130
    • Wu, L.1    Shan, Y.2    Liu, D.3
  • 131
    • 27644514012 scopus 로고    scopus 로고
    • Yeast as a biosensor for antioxidants: Simple growth tests employing a Saccharomyces cerevisiae mutant defective in superoxide dismutase
    • Zyracka E, Zadrag R, Kozioł S, Krzepiłko A, Bartosz G, and Biliń ski T. Yeast as a biosensor for antioxidants: simple growth tests employing a Saccharomyces cerevisiae mutant defective in superoxide dismutase. Acta Biochim Pol 52: 679-684, 2005.
    • (2005) Acta Biochim Pol , vol.52 , pp. 679-684
    • Zyracka, E.1    Zadrag, R.2    Kozioł, S.3    Krzepiłko, A.4    Bartosz, G.5    Biliń Ski, T.6


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