| Year |
Citation |
Score |
| 2014 |
McCord JM, Fridovich I. Superoxide dismutases: you've come a long way, baby. Antioxidants & Redox Signaling. 20: 1548-9. PMID 23924157 DOI: 10.1089/ars.2013.5547 |
0.634 |
|
| 2013 |
Liochev SI, Fridovich I. Does MitoSOD protect against the toxicity of paraquat toward mitochondria by acting as a superoxide dismutase mimic? Free Radical Biology & Medicine. 65: 1534. PMID 23434767 DOI: 10.1016/J.Freeradbiomed.2013.02.010 |
0.336 |
|
| 2013 |
Fridovich I. Oxygen: how do we stand it?. Medical Principles and Practice : International Journal of the Kuwait University, Health Science Centre. 22: 131-7. PMID 22759590 DOI: 10.1159/000339212 |
0.432 |
|
| 2011 |
Liochev SI, Fridovich I. Is superoxide able to induce SoxRS? Free Radical Biology & Medicine. 50: 1813. PMID 21459140 DOI: 10.1016/J.Freeradbiomed.2011.03.029 |
0.309 |
|
| 2011 |
Fridovich I. Superoxide dismutases: anti- versus pro- oxidants? Anti-Cancer Agents in Medicinal Chemistry. 11: 175-7. PMID 21182471 DOI: 10.2174/187152011795255966 |
0.418 |
|
| 2010 |
Liochev SI, Fridovich I. Mechanism of the peroxidase activity of Cu, Zn superoxide dismutase. Free Radical Biology & Medicine. 48: 1565-9. PMID 20211248 DOI: 10.1016/J.Freeradbiomed.2010.02.036 |
0.425 |
|
| 2010 |
Forman HJ, Fridovich I. Electrolytic univalent reduction of oxygen in aqueous solution demonstrated with superoxide dismutase. Science (New York, N.Y.). 175: 339. PMID 17814545 DOI: 10.1126/Science.175.4019.339 |
0.403 |
|
| 2007 |
Okado-Matsumoto A, Fridovich I. Putative denitrosylase activity of Cu,Zn-superoxide dismutase. Free Radical Biology & Medicine. 43: 830-6. PMID 17664146 DOI: 10.1016/J.Freeradbiomed.2007.05.038 |
0.361 |
|
| 2007 |
Liochev SI, Fridovich I. The effects of superoxide dismutase on H2O2 formation. Free Radical Biology & Medicine. 42: 1465-9. PMID 17448892 DOI: 10.1016/J.Freeradbiomed.2007.02.015 |
0.394 |
|
| 2006 |
Goldstone AB, Liochev SI, Fridovich I. Inactivation of copper, zinc superoxide dismutase by H2O2 : mechanism of protection. Free Radical Biology & Medicine. 41: 1860-3. PMID 17157188 DOI: 10.1016/J.Freeradbiomed.2006.09.015 |
0.397 |
|
| 2006 |
Okado-Matsumoto A, Guan Z, Fridovich I. Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Free Radical Biology & Medicine. 41: 1837-46. PMID 17157186 DOI: 10.1016/J.Freeradbiomed.2006.09.011 |
0.306 |
|
| 2006 |
Goldstein S, Fridovich I, Czapski G. Kinetic properties of Cu,Zn-superoxide dismutase as a function of metal content--order restored. Free Radical Biology & Medicine. 41: 937-41. PMID 16934676 DOI: 10.1016/J.Freeradbiomed.2006.05.026 |
0.349 |
|
| 2006 |
Liochev SI, Fridovich I. The role of CO2 in metal-catalyzed peroxidations. Journal of Inorganic Biochemistry. 100: 694-6. PMID 16500710 DOI: 10.1016/J.Jinorgbio.2006.01.030 |
0.36 |
|
| 2006 |
Batinić-Haberle I, Spasojević I, Stevens RD, Bondurant B, Okado-Matsumoto A, Fridovich I, Vujasković Z, Dewhirst MW. New PEG-ylated Mn(III) porphyrins approaching catalytic activity of SOD enzyme. Dalton Transactions (Cambridge, England : 2003). 617-24. PMID 16402149 DOI: 10.1039/B513761F |
0.379 |
|
| 2005 |
Liochev SI, Fridovich I. The role of CO2 in cobalt-catalyzed peroxidations. Archives of Biochemistry and Biophysics. 439: 99-104. PMID 15946639 DOI: 10.1016/J.Abb.2005.05.011 |
0.359 |
|
| 2005 |
Liochev SI, Fridovich I. Cross-compartment protection by SOD1. Free Radical Biology & Medicine. 38: 146-7. PMID 15589383 DOI: 10.1016/J.Freeradbiomed.2004.10.017 |
0.363 |
|
| 2004 |
Liochev SI, Fridovich I. Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions. Proceedings of the National Academy of Sciences of the United States of America. 101: 12485-90. PMID 15310847 DOI: 10.1073/Pnas.0404911101 |
0.393 |
|
| 2004 |
Batinić-Haberle I, Spasojević I, Stevens RD, Hambright P, Neta P, Okado-Matsumoto A, Fridovich I. New class of potent catalysts of O2.-dismutation. Mn(III) ortho-methoxyethylpyridyl- and di-ortho-methoxyethylimidazolylporphyrins. Dalton Transactions (Cambridge, England : 2003). 1696-702. PMID 15252564 DOI: 10.1039/B400818A |
0.32 |
|
| 2004 |
Batini?-Haberle I, Spasojevi? I, Fridovich I. Tetrahydrobiopterin rapidly reduces the SOD mimic Mn(III) ortho-tetrakis(N-ethylpyridinium-2-yl)porphyrin. Free Radical Biology & Medicine. 37: 367-74. PMID 15223070 DOI: 10.1016/J.Freeradbiomed.2004.04.041 |
0.366 |
|
| 2004 |
Liochev SI, Fridovich I. Bicarbonate-enhanced peroxidase activity of Cu,Zn SOD: is the distal oxidant bound or diffusible? Archives of Biochemistry and Biophysics. 421: 255-9. PMID 14984205 DOI: 10.1016/J.Abb.2003.11.015 |
0.349 |
|
| 2004 |
Fridovich I. Mitochondria: are they the seat of senescence? Aging Cell. 3: 13-6. PMID 14965350 DOI: 10.1046/J.1474-9728.2003.00075.X |
0.403 |
|
| 2004 |
Liochev SI, Fridovich I. CO2, not HCO3-, facilitates oxidations by Cu,Zn superoxide dismutase plus H2O2. Proceedings of the National Academy of Sciences of the United States of America. 101: 743-4. PMID 14711995 DOI: 10.1073/Pnas.0307635100 |
0.386 |
|
| 2003 |
Liochev SI, Fridovich I. The mode of decomposition of Angeli's salt (Na2N2O3) and the effects thereon of oxygen, nitrite, superoxide dismutase, and glutathione. Free Radical Biology & Medicine. 34: 1399-404. PMID 12757850 DOI: 10.1016/S0891-5849(03)00111-4 |
0.388 |
|
| 2003 |
Liochev SI, Fridovich I. Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: evaluation of oxidative hypotheses. Free Radical Biology & Medicine. 34: 1383-9. PMID 12757848 DOI: 10.1016/S0891-5849(03)00153-9 |
0.404 |
|
| 2003 |
Liochev SI, Fridovich I. Reversal of the superoxide dismutase reaction revisited. Free Radical Biology & Medicine. 34: 908-10. PMID 12654479 DOI: 10.1016/S0891-5849(03)00024-8 |
0.419 |
|
| 2002 |
Benov L, Fridovich I. Is reduction of the sulfonated tetrazolium 2,3-bis (2-methoxy-4-nitro-5-sulfophenyl)-2-tetrazolium 5-carboxanilide a reliable measure of intracellular superoxide production? Analytical Biochemistry. 310: 186-90. PMID 12423637 DOI: 10.1016/S0003-2697(02)00310-X |
0.372 |
|
| 2002 |
Spasojevi? I, Menzeleev R, White PS, Fridovich I. Rotational isomers of N-alkylpyridylporphyrins and their metal complexes. HPLC separation, (1)H NMR and X-ray structural characterization, electrochemistry, and catalysis of O(2)(.-) disproportionation. Inorganic Chemistry. 41: 5874-81. PMID 12401096 DOI: 10.1021/Ic025556X |
0.302 |
|
| 2002 |
Benov L, Fridovich I. Induction of the soxRS regulon of Escherichia coli by glycolaldehyde. Archives of Biochemistry and Biophysics. 407: 45-8. PMID 12392714 DOI: 10.1016/S0003-9861(02)00498-8 |
0.42 |
|
| 2002 |
Liochev SI, Fridovich I. Copper, zinc superoxide dismutase and H2O2. Effects of bicarbonate on inactivation and oxidations of NADPH and urate, and on consumption of H2O2. The Journal of Biological Chemistry. 277: 34674-8. PMID 12107177 DOI: 10.1074/Jbc.M204726200 |
0.425 |
|
| 2002 |
Liochev SI, Fridovich I. Superoxide and nitric oxide: consequences of varying rates of production and consumption: a theoretical treatment. Free Radical Biology & Medicine. 33: 137-41. PMID 12086691 DOI: 10.1016/S0891-5849(02)00864-X |
0.376 |
|
| 2002 |
Al-Maghrebi M, Fridovich I, Benov L. Manganese supplementation relieves the phenotypic deficits seen in superoxide-dismutase-null Escherichia coli. Archives of Biochemistry and Biophysics. 402: 104-9. PMID 12051688 DOI: 10.1016/S0003-9861(02)00065-6 |
0.331 |
|
| 2002 |
Liochev SI, Fridovich I. Nitroxyl (NO-): a substrate for superoxide dismutase. Archives of Biochemistry and Biophysics. 402: 166-71. PMID 12051660 DOI: 10.1016/S0003-9861(02)00074-7 |
0.407 |
|
| 2001 |
Okado-Matsumoto A, Fridovich I. Assay of superoxide dismutase: cautions relevant to the use of cytochrome c, a sulfonated tetrazolium, and cyanide. Analytical Biochemistry. 298: 337-42. PMID 11700991 DOI: 10.1006/Abio.2001.5385 |
0.361 |
|
| 2001 |
Kachadourian R, Liochev SI, Cabelli DE, Patel MN, Fridovich I, Day BJ. 2-methoxyestradiol does not inhibit superoxide dismutase. Archives of Biochemistry and Biophysics. 392: 349-53. PMID 11488612 DOI: 10.1006/Abbi.2001.2455 |
0.369 |
|
| 2001 |
Liochev SI, Fridovich I. Copper,zinc superoxide dismutase as a univalent NO(-) oxidoreductase and as a dichlorofluorescin peroxidase. The Journal of Biological Chemistry. 276: 35253-7. PMID 11461912 DOI: 10.1074/Jbc.M104237200 |
0.414 |
|
| 2001 |
Mackensen GB, Patel M, Sheng H, Calvi CL, Batinic-Haberle I, Day BJ, Liang LP, Fridovich I, Crapo JD, Pearlstein RD, Warner DS. Neuroprotection from delayed postischemic administration of a metalloporphyrin catalytic antioxidant. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 21: 4582-92. PMID 11425886 DOI: 10.1523/Jneurosci.21-13-04582.2001 |
0.473 |
|
| 2001 |
Liochev SI, Fridovich I. The oxidation of 3-hydroxyanthranilic acid by Cu,Zn superoxide dismutase: mechanism and possible consequences. Archives of Biochemistry and Biophysics. 388: 281-4. PMID 11368166 DOI: 10.1006/Abbi.2001.2296 |
0.352 |
|
| 2001 |
Spasojević I, Batinić-Haberle I, Stevens RD, Hambright P, Thorpe AN, Grodkowski J, Neta P, Fridovich I. Manganese(III) biliverdin IX dimethyl ester: a powerful catalytic scavenger of superoxide employing the Mn(III)/Mn(IV) redox couple. Inorganic Chemistry. 40: 726-39. PMID 11225116 DOI: 10.1021/Ic0004986 |
0.41 |
|
| 2000 |
Spasojevic I, Batinic-Haberle I, Fridovich I. Nitrosylation of manganese(II) tetrakis(N-ethylpyridinium-2-yl)porphyrin: a simple and sensitive spectrophotometric assay for nitric oxide. Nitric Oxide : Biology and Chemistry / Official Journal of the Nitric Oxide Society. 4: 526-33. PMID 11020341 DOI: 10.1006/Niox.2000.0303 |
0.373 |
|
| 2000 |
Liochev SI, Fridovich I. Copper- and zinc-containing superoxide dismutase can act as a superoxide reductase and a superoxide oxidase. The Journal of Biological Chemistry. 275: 38482-5. PMID 11005823 DOI: 10.1074/Jbc.M007891200 |
0.453 |
|
| 2000 |
Okado-Matsumoto A, Fridovich I. The role of alpha,beta -dicarbonyl compounds in the toxicity of short chain sugars. The Journal of Biological Chemistry. 275: 34853-7. PMID 10931845 DOI: 10.1074/Jbc.M005536200 |
0.369 |
|
| 2000 |
Spasojevic I, Liochev SI, Fridovich I. Lucigenin: redox potential in aqueous media and redox cycling with O-(2) production. Archives of Biochemistry and Biophysics. 373: 447-50. PMID 10620371 DOI: 10.1006/Abbi.1999.1579 |
0.337 |
|
| 1999 |
Liochev SI, Fridovich I. Superoxide and iron: partners in crime. Iubmb Life. 48: 157-61. PMID 10794591 DOI: 10.1080/713803492 |
0.393 |
|
| 1999 |
Fridovich I. Fundamental aspects of reactive oxygen species, or what's the matter with oxygen? Annals of the New York Academy of Sciences. 893: 13-8. PMID 10672226 DOI: 10.1111/J.1749-6632.1999.Tb07814.X |
0.438 |
|
| 1999 |
Liochev SI, Fridovich I. On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase. Free Radical Biology & Medicine. 27: 1444-7. PMID 10641739 DOI: 10.1016/S0891-5849(99)00190-2 |
0.391 |
|
| 1999 |
Batinic-Haberle I, Benov L, Fridovich I. An anionic impurity in preparations of cytochrome c interferes with assays of cationic catalysts of the dismutation of the superoxide anion radical. Analytical Biochemistry. 275: 267. PMID 10552917 DOI: 10.1016/S0891-5849(99)90939-5 |
0.319 |
|
| 1999 |
Ferrer-Sueta G, Batini?-Haberle I, Spasojevi? I, Fridovich I, Radi R. Catalytic scavenging of peroxynitrite by isomeric Mn(III) N-methylpyridylporphyrins in the presence of reductants. Chemical Research in Toxicology. 12: 442-9. PMID 10328755 DOI: 10.1021/Tx980245D |
0.356 |
|
| 1999 |
Liochev SI, Hausladen A, Fridovich I. Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 96: 3537-9. PMID 10097071 DOI: 10.1073/Pnas.96.7.3537 |
0.333 |
|
| 1999 |
Liochev SI, Benov L, Touati D, Fridovich I. Induction of the soxRS regulon of Escherichia coli by superoxide. The Journal of Biological Chemistry. 274: 9479-81. PMID 10092630 DOI: 10.1074/Jbc.274.14.9479 |
0.376 |
|
| 1999 |
Benov L, Fridovich I. Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli. The transketolase connection. The Journal of Biological Chemistry. 274: 4202-6. PMID 9933617 DOI: 10.1074/Jbc.274.7.4202 |
0.404 |
|
| 1999 |
Batini?-Haberle I, Spasojevi? I, Hambright P, Benov L, Cmmbliss AL, 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 Inorganic Chemistry. 38: 4011-4022. DOI: 10.1021/Ic990118K |
0.304 |
|
| 1999 |
Spasojevic I, Liochev SI, Fridovich I. Lucigenin: Redox potential in aqueous media and redox cycling with O2 β Production Free Radical Biology and Medicine. 27. DOI: 10.1016/S0891-5849(99)90543-9 |
0.303 |
|
| 1998 |
Fridovich I. Oxygen: The dark side. Age. 21: 77. PMID 23604353 DOI: 10.1007/S11357-998-0008-6 |
0.433 |
|
| 1998 |
Liochev SI, Fridovich I. Lucigenin as mediator of superoxide production: revisited. Free Radical Biology & Medicine. 25: 926-8. PMID 9840737 DOI: 10.1016/S0891-5849(98)00121-X |
0.365 |
|
| 1998 |
Benov L, Sztejnberg L, Fridovich I. Critical evaluation of the use of hydroethidine as a measure of superoxide anion radical. Free Radical Biology & Medicine. 25: 826-31. PMID 9823548 DOI: 10.1016/S0891-5849(98)00163-4 |
0.409 |
|
| 1998 |
Benov L, Fridovich I. Superoxide dependence of the toxicity of short chain sugars. The Journal of Biological Chemistry. 273: 25741-4. PMID 9748243 DOI: 10.1074/Jbc.273.40.25741 |
0.377 |
|
| 1998 |
Batini?-Haberle I, Benov L, Spasojevi? I, Fridovich I. The ortho effect makes manganese(III) meso-tetrakis(N-methylpyridinium-2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic. The Journal of Biological Chemistry. 273: 24521-8. PMID 9733746 DOI: 10.1074/Jbc.273.38.24521 |
0.315 |
|
| 1998 |
Fridovich I. Adverse effects of superoxide and defenses: studies with Escherichia coli. Drug Metabolism Reviews. 30: 277-83. PMID 9606604 DOI: 10.3109/03602539808996312 |
0.336 |
|
| 1998 |
Liochev SI, Chen LL, Hallewell RA, Fridovich I. The familial amyotrophic lateral sclerosis-associated amino acid substitutions E100G, G93A, and G93R do not influence the rate of inactivation of copper- and zinc-containing superoxide dismutase by H2O2. Archives of Biochemistry and Biophysics. 352: 237-9. PMID 9587411 DOI: 10.1006/Abbi.1998.0616 |
0.334 |
|
| 1998 |
Benov L, Fridovich I. Growth in iron-enriched medium partially compensates Escherichia coli for the lack of manganese and iron superoxide dismutase. The Journal of Biological Chemistry. 273: 10313-6. PMID 9553085 DOI: 10.1074/Jbc.273.17.10313 |
0.338 |
|
| 1998 |
Fridovich I. Oxygen toxicity: a radical explanation. The Journal of Experimental Biology. 201: 1203-9. PMID 9510531 |
0.339 |
|
| 1997 |
Day BJ, Fridovich I, Crapo JD. Manganic porphyrins possess catalase activity and protect endothelial cells against hydrogen peroxide-mediated injury. Archives of Biochemistry and Biophysics. 347: 256-62. PMID 9367533 DOI: 10.1006/Abbi.1997.0341 |
0.529 |
|
| 1997 |
Liochev SI, Chen LL, Hallewell RA, Fridovich I. Superoxide-dependent peroxidase activity of H48Q: a superoxide dismutase variant associated with familial amyotrophic lateral sclerosis. Archives of Biochemistry and Biophysics. 346: 263-8. PMID 9343373 DOI: 10.1006/Abbi.1997.0298 |
0.403 |
|
| 1997 |
Liochev SI, Fridovich I. A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (desulfoferrodoxin) from Desulfoarculus baarsii. The Journal of Biological Chemistry. 272: 25573-5. PMID 9325275 DOI: 10.1074/Jbc.272.41.25573 |
0.398 |
|
| 1997 |
Fridovich I. Superoxide anion radical (O2-.), superoxide dismutases, and related matters. The Journal of Biological Chemistry. 272: 18515-7. PMID 9228011 DOI: 10.1074/Jbc.272.30.18515 |
0.391 |
|
| 1997 |
Batini?-Haberle I, Liochev SI, Spasojevi? I, Fridovich I. A potent superoxide dismutase mimic: manganese beta-octabromo-meso-tetrakis-(N-methylpyridinium-4-yl) porphyrin. Archives of Biochemistry and Biophysics. 343: 225-33. PMID 9224734 DOI: 10.1006/Abbi.1997.0157 |
0.338 |
|
| 1997 |
Liochev SI, Fridovich I. How does superoxide dismutase protect against tumor necrosis factor: a hypothesis informed by effect of superoxide on "free" iron. Free Radical Biology & Medicine. 23: 668-71. PMID 9215812 DOI: 10.1016/S0891-5849(97)00060-9 |
0.387 |
|
| 1997 |
Benov L, Sage H, Fridovich I. The copper- and zinc-containing superoxide dismutase from Escherichia coli: molecular weight and stability. Archives of Biochemistry and Biophysics. 340: 305-10. PMID 9143335 DOI: 10.1006/Abbi.1997.9940 |
0.302 |
|
| 1997 |
Liochev SI, Fridovich I. Lucigenin luminescence as a measure of intracellular superoxide dismutase activity in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 94: 2891-6. PMID 9096317 DOI: 10.1073/Pnas.94.7.2891 |
0.438 |
|
| 1997 |
Liochev SI, Fridovich I. Lucigenin (bis-N-methylacridinium) as a mediator of superoxide anion production. Archives of Biochemistry and Biophysics. 337: 115-20. PMID 8990275 DOI: 10.1006/Abbi.1997.9766 |
0.361 |
|
| 1996 |
FRIDOVICH I. SYNERGISTIC INHIBITION OF XANTHINE OXIDASE BY GUANIDINIUM PLUS THIOCYANATE. Archives of Biochemistry and Biophysics. 109: 511-5. PMID 14320492 DOI: 10.1016/0003-9861(65)90395-4 |
0.306 |
|
| 1996 |
Benov L, Fridovich I. The rate of adaptive mutagenesis in Escherichia coli is enhanced by oxygen (superoxide). Mutation Research. 357: 231-6. PMID 8876699 DOI: 10.1016/0027-5107(96)00128-5 |
0.358 |
|
| 1996 |
Hausladen A, Fridovich I. Measuring nitric oxide and superoxide: rate constants for aconitase reactivity. Methods in Enzymology. 269: 37-41. PMID 8791635 DOI: 10.1016/S0076-6879(96)69007-7 |
0.348 |
|
| 1996 |
Patel M, Day BJ, Crapo JD, Fridovich I, McNamara JO. Requirement for superoxide in excitotoxic cell death. Neuron. 16: 345-55. PMID 8789949 DOI: 10.1016/S0896-6273(00)80052-5 |
0.536 |
|
| 1996 |
Benov L, Kredich NM, Fridovich I. The mechanism of the auxotrophy for sulfur-containing amino acids imposed upon Escherichia coli by superoxide. The Journal of Biological Chemistry. 271: 21037-40. PMID 8702868 DOI: 10.1074/Jbc.271.35.21037 |
0.354 |
|
| 1996 |
De La Paz MA, Zhang J, Fridovich I. Red blood cell antioxidant enzymes in age-related macular degeneration. The British Journal of Ophthalmology. 80: 445-50. PMID 8695567 DOI: 10.1136/Bjo.80.5.445 |
0.348 |
|
| 1996 |
Liochev SI, Kuchumov AR, Vinogradov SN, Fridovich I. Superoxide dismutase activity in the giant hemoglobin of the earthworm, Lumbricus terrestris. Archives of Biochemistry and Biophysics. 330: 281-4. PMID 8660657 DOI: 10.1006/Abbi.1996.0254 |
0.383 |
|
| 1996 |
De La Paz MA, Zhang J, Fridovich I. Antioxidant enzymes of the human retina: effect of age on enzyme activity of macula and periphery. Current Eye Research. 15: 273-8. PMID 8654107 DOI: 10.3109/02713689609007621 |
0.355 |
|
| 1996 |
Benov L, Fridovich I. Functional significance of the Cu,ZnSOD in Escherichia coli. Archives of Biochemistry and Biophysics. 327: 249-53. PMID 8619610 DOI: 10.1006/Abbi.1996.0117 |
0.343 |
|
| 1995 |
Benov L, Fridovich I. Superoxide dismutase protects against aerobic heat shock in Escherichia coli Journal of Bacteriology. 177: 3344-3346. PMID 7768839 DOI: 10.1128/Jb.177.11.3344-3346.1995 |
0.319 |
|
| 1995 |
Darr D, Fridovich I. Adaptation to oxidative stress in young, but not in mature or old, caenorhabditis elegans Free Radical Biology and Medicine. 18: 195-201. PMID 7744302 DOI: 10.1016/0891-5849(94)00118-4 |
0.359 |
|
| 1995 |
Liochev SI, Fridovich I. Superoxide from glucose oxidase or from nitroblue tetrazolium Archives of Biochemistry and Biophysics. 318: 408-410. PMID 7733670 DOI: 10.1006/Abbi.1995.1247 |
0.374 |
|
| 1995 |
Liochev SI, Fridovich I. A cationic manganic porphyrin inhibits uptake of paraquat by Escherichia coli Archives of Biochemistry and Biophysics. 321: 271-275. PMID 7639531 DOI: 10.1006/Abbi.1995.1395 |
0.387 |
|
| 1995 |
Fridovich I. Superoxide radical and superoxide dismutases Annual Review of Biochemistry. 64: 97-112. PMID 7574505 DOI: 10.1021/Ar50058A001 |
0.412 |
|
| 1995 |
Liochev SI, Batinic-Haberle I, Fridovich I. The effect of detergents on the reduction of tetrazolium salts. Archives of Biochemistry and Biophysics. 324: 48-52. PMID 7503558 DOI: 10.1006/Abbi.1995.9931 |
0.394 |
|
| 1994 |
Liochev SI, Fridovich I. The role of O2 .- in the production of HO.: in vitro and in vivo Free Radical Biology and Medicine. 16: 29-33. PMID 8299992 DOI: 10.1016/0891-5849(94)90239-9 |
0.356 |
|
| 1994 |
Faulkner KM, Stevens RD, Fridovich I. Characterization of Mn(III) complexes of linear and cyclic desferrioxamines as mimics of superoxide dismutase activity. Archives of Biochemistry and Biophysics. 310: 341-6. PMID 8179317 DOI: 10.1006/Abbi.1994.1176 |
0.309 |
|
| 1994 |
Darr D, Fridovich I. Free radicals in cutaneous biology Journal of Investigative Dermatology. 102: 671-675. PMID 8176246 DOI: 10.1111/1523-1747.Ep12374036 |
0.344 |
|
| 1994 |
Liochev SI, Hausladen A, Beyer WF, Fridovich I. NADPH:ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon Proceedings of the National Academy of Sciences of the United States of America. 91: 1328-1331. PMID 8108411 DOI: 10.1073/Pnas.91.4.1328 |
0.368 |
|
| 1994 |
Liochev SI, Fridovich I. Paraquat diaphorases in Escherichia coli Free Radical Biology and Medicine. 16: 555-559. PMID 8026798 DOI: 10.1016/0891-5849(94)90055-8 |
0.321 |
|
| 1993 |
Gardner PR, Fridovich I. NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro. The Journal of Biological Chemistry. 268: 12958-63. PMID 8509428 |
0.654 |
|
| 1993 |
Liochev SI, Fridovich I. Modulation of the fumarases of Escherichia coli in response to oxidative stress Archives of Biochemistry and Biophysics. 301: 379-384. PMID 8460946 DOI: 10.1006/Abbi.1993.1159 |
0.402 |
|
| 1993 |
Privalle CT, Kong SE, Fridovich I. Induction of manganese-containing superoxide dismutase in anaerobic Escherichia coli by diamide and 1,10-phenanthroline: Sites of transcriptional regulation Proceedings of the National Academy of Sciences of the United States of America. 90: 2310-2314. PMID 8460139 DOI: 10.1073/Pnas.90.6.2310 |
0.352 |
|
| 1993 |
Gardner PR, Fridovich I. Effect of glutathione on aconitase in Escherichia coli. Archives of Biochemistry and Biophysics. 301: 98-102. PMID 8382910 DOI: 10.1006/Abbi.1993.1120 |
0.692 |
|
| 1993 |
Faulkner K, Fridovich I. Luminol and lucigenin as detectors for O2 ṡ- Free Radical Biology and Medicine. 15: 447-451. PMID 8225026 DOI: 10.1016/0891-5849(93)90044-U |
0.356 |
|
| 1993 |
Privalle CT, Fridovich I. Induction of MnSOD in Escherichia coli by nitric oxide, diamide and 1, 10-phenanthroline: Sites of transcriptional regulation Free Radical Biology and Medicine. 15: 547. DOI: 10.1016/0891-5849(93)90473-8 |
0.328 |
|
| 1993 |
Fridovich I. Superoxide and superoxide dismutases Free Radical Biology and Medicine. 15: 472. DOI: 10.1016/0891-5849(93)90188-z |
0.309 |
|
| 1992 |
Imlay JA, Fridovich I. Suppression of oxidative envelope damage by pseudoreversion of a superoxide dismutase-deficient mutant of Escherichia coli Journal of Bacteriology. 174: 953-961. PMID 1732228 DOI: 10.1128/Jb.174.3.953-961.1992 |
0.62 |
|
| 1992 |
Liochev SI, Fridovich I. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon Proceedings of the National Academy of Sciences of the United States of America. 89: 5892-5896. PMID 1631070 DOI: 10.1073/Pnas.89.13.5892 |
0.325 |
|
| 1992 |
Kong S, Liochev S, Fridovich I. Aluminum(III) facilitates the oxidation of NADH by the superoxide anion Free Radical Biology and Medicine. 13: 79-81. PMID 1321073 DOI: 10.1016/0891-5849(92)90168-G |
0.376 |
|
| 1992 |
Imlay J, Fridovich I. Exogenous quinones directly inhibit the respiratory NADH dehydrogenase in Escherichia coli Archives of Biochemistry and Biophysics. 296: 337-346. PMID 1318694 DOI: 10.1016/0003-9861(92)90581-G |
0.673 |
|
| 1992 |
Gardner PR, Fridovich I. Inactivation-reactivation of aconitase in Escherichia coli. A sensitive measure of superoxide radical. The Journal of Biological Chemistry. 267: 8757-63. PMID 1315737 |
0.69 |
|
| 1992 |
Liochev SI, Fridovich I. Superoxide generated by glutathione reductase initiates a vanadate-dependent free radical chain oxidation of NADH Archives of Biochemistry and Biophysics. 294: 403-406. PMID 1314540 DOI: 10.1016/0003-9861(92)90703-Y |
0.4 |
|
| 1991 |
Imlay JA, Fridovich I. Isolation and genetic analysis of a mutation that suppresses the auxotrophies of superoxide dismutase-deficient Escherichia coli K12 Mgg Molecular & General Genetics. 228: 410-416. PMID 1896012 DOI: 10.1007/Bf00260634 |
0.605 |
|
| 1991 |
Beyer W, Imlay J, Fridovich I. Superoxide dismutases. Progress in Nucleic Acid Research and Molecular Biology. 40: 221-53. PMID 1851570 DOI: 10.1016/s0079-6603(08)60843-0 |
0.307 |
|
| 1991 |
Imlay JA, Fridovich I. Assay of metabolic superoxide production in Escherichia coli Journal of Biological Chemistry. 266: 6957-6965. PMID 1849898 |
0.626 |
|
| 1991 |
Beyer WF, Fridovich I. Phosphate, not superoxide dismutase, facilitates electron transfer from ferrous salts to cytochrome c Archives of Biochemistry and Biophysics. 285: 60-63. PMID 1846733 DOI: 10.1016/0003-9861(91)90328-G |
0.382 |
|
| 1991 |
Gardner PR, Fridovich I. Quinolinate synthetase: the oxygen-sensitive site of de novo NAD(P)+ biosynthesis. Archives of Biochemistry and Biophysics. 284: 106-11. PMID 1846509 DOI: 10.1016/0003-9861(91)90270-S |
0.725 |
|
| 1991 |
Gardner PR, Fridovich I. Superoxide sensitivity of the Escherichia coli 6-phosphogluconate dehydratase. The Journal of Biological Chemistry. 266: 1478-83. PMID 1846355 |
0.73 |
|
| 1991 |
Liochev SI, Fridovich I. The roles of O2 -, HO., and secondarily derived radicals in oxidation reactions catalyzed by vanadium salts Archives of Biochemistry and Biophysics. 291: 379-382. PMID 1659326 DOI: 10.1016/0003-9861(91)90149-D |
0.383 |
|
| 1991 |
Gardner PR, Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. The Journal of Biological Chemistry. 266: 19328-33. PMID 1655783 |
0.713 |
|
| 1991 |
Bhuyan KC, Bhuyan DK, Chiu W, Malik S, Fridovich I. Desferal-Mn(III) in the therapy of diquat-induced cataract in rabbit Archives of Biochemistry and Biophysics. 288: 525-532. PMID 1654836 DOI: 10.1016/0003-9861(91)90230-G |
0.335 |
|
| 1991 |
Imlay JA, Fridovich I. Superoxide production by respiring membranes of escherichia coli Free Radical Research. 12: 59-66. PMID 1649104 DOI: 10.3109/10715769109145768 |
0.627 |
|
| 1991 |
Imlay JA, Fridovich I. Endogenous Superoxide Generation Threatens Sensitive Enzymes In Escherichia Coli Oxidative Damage & Repairchemical, Biological and Medical Aspects. 126-131. DOI: 10.1016/B978-0-08-041749-3.50028-0 |
0.636 |
|
| 1991 |
Fridovich I. Superoxide Versus The Hydroxyl Radical: A Historical Perspective Oxidative Damage & Repairchemical, Biological and Medical Aspects. 98-101. DOI: 10.1016/B978-0-08-041749-3.50023-1 |
0.35 |
|
| 1990 |
Minakami H, Kitzler JW, Fridovich I. Effects of pH, glucose, and chelating agents on lethality of paraquat to Escherichia coli Journal of Bacteriology. 172: 691-695. PMID 2404952 DOI: 10.1128/Jb.172.2.691-695.1990 |
0.309 |
|
| 1990 |
Ishii T, Iwahashi H, Sugata R, Kido R, Fridovich I. Superoxide dismutases enhance the rate of autoxidation of 3-hydroxyanthranilic acid Archives of Biochemistry and Biophysics. 276: 248-250. PMID 2404453 DOI: 10.1016/0003-9861(90)90034-V |
0.433 |
|
| 1990 |
Ishii T, Fridovich I. Dual effects of superoxide dismutase on the autoxidation of 1,4-naphthohydroquinone Free Radical Biology and Medicine. 8: 21-24. PMID 2323580 DOI: 10.1016/0891-5849(90)90140-E |
0.457 |
|
| 1990 |
Beyer WF, Fridovich I. Superoxide dismutase mimic prepared from desferrioxamine and manganese dioxide Methods in Enzymology. 186: 242-249. PMID 2233297 DOI: 10.1016/0076-6879(90)86115-C |
0.333 |
|
| 1990 |
Liochev SI, Fridovich I. Vanadate-stimulated oxidation of NAD(P)H in the presence of biological membranes and other sources of O2 - Archives of Biochemistry and Biophysics. 279: 1-7. PMID 2186701 DOI: 10.1016/0003-9861(90)90454-7 |
0.328 |
|
| 1990 |
Minakami H, Fridovich I. Relationship between growth of Escherichia coli and susceptibility to the lethal effect of paraquat Faseb Journal. 4: 3239-3244. PMID 2172063 DOI: 10.1096/Fasebj.4.14.2172063 |
0.318 |
|
| 1990 |
Gardner PR, Fridovich I. Quinolinate phosphoribosyl transferase is not the oxygen-sensitive site of nicotinamide adenine dinucleotide biosynthesis. Free Radical Biology & Medicine. 8: 117-9. PMID 2139630 DOI: 10.1016/0891-5849(90)90083-U |
0.707 |
|
| 1990 |
Privalle CT, Fridovich I. Biosynthesis of the manganese-containing superoxide dismutase in Escherichia coli: Anaerobic induction of active MnSOD by diamine Free Radical Biology and Medicine. 9: 2. DOI: 10.1016/B978-0-08-041749-3.50014-0 |
0.397 |
|
| 1990 |
Gardner PR, Fridovich I. Superoxide and chemical sensitivities of the 6-phosphogluconate dehydratase Free Radical Biology and Medicine. 9: 84. DOI: 10.1016/0891-5849(90)90469-Y |
0.662 |
|
| 1990 |
Imlay JA, Fridovich I. Quantity and mechanism of superoxide formation in aerobic Escherichia coli Free Radical Biology and Medicine. 9: 28. DOI: 10.1016/0891-5849(90)90266-L |
0.616 |
|
| 1989 |
Fridovich I. Oxygen radicals from acetaldehyde Free Radical Biology and Medicine. 7: 557-558. PMID 2693224 DOI: 10.1016/0891-5849(89)90032-4 |
0.366 |
|
| 1989 |
Beyer WF, Reynolds JA, Fridovich I. Differences between the manganese- and the iron-containing superoxide dismutases of Escherichia coli detected through sedimentation equilibrium, hydrodynamic, and spectroscopic studies Biochemistry. 28: 4403-4409. PMID 2669953 DOI: 10.1021/Bi00436A042 |
0.333 |
|
| 1989 |
Liochev SI, Fridovich I. Hydroxyl radical is not a significant intermediate in the vanadate-stimulated oxidation of NAD(P)H by O2 - Archives of Biochemistry and Biophysics. 275: 40-43. PMID 2554810 DOI: 10.1016/0003-9861(89)90347-0 |
0.415 |
|
| 1989 |
Liochev SI, Fridovich I. Vanadate-stimulated oxidation of NAD(P)H. Free Radical Biology & Medicine. 6: 617-22. PMID 2546865 DOI: 10.1016/0891-5849(89)90069-5 |
0.336 |
|
| 1989 |
Liochev S, Ivancheva E, Fridovich I. Effects of vanadate on the oxidation of NADH by xanthine oxidase Archives of Biochemistry and Biophysics. 269: 188-193. PMID 2537057 DOI: 10.1016/0003-9861(89)90099-4 |
0.372 |
|
| 1989 |
Rabinowitch HD, Rosen GM, Fridovich I. A mimic of superoxide dismutase activity protects Chlorella sorokiniana against the toxicity of sulfite Free Radical Biology and Medicine. 6: 45-48. PMID 2536342 DOI: 10.1016/0891-5849(89)90158-5 |
0.436 |
|
| 1988 |
Maskino T, Fridovich I. NADPH mediates the inactivation of bovine liver catalase by monochloroamine Archives of Biochemistry and Biophysics. 265: 279-285. PMID 3421706 DOI: 10.1016/0003-9861(88)90129-4 |
0.348 |
|
| 1988 |
Beyer WF, Fridovich I. An ultrasensitive colorimetric assay for manganese Analytical Biochemistry. 170: 512-519. PMID 3394949 DOI: 10.1016/0003-2697(88)90666-5 |
0.323 |
|
| 1988 |
Privalle CT, Fridovich I. Inductions of superoxide dismutases in Escherichia coli under anaerobic conditions. Accumulation of an inactive form of the manganese enzyme Journal of Biological Chemistry. 263: 4274-4279. PMID 3279033 |
0.346 |
|
| 1988 |
McCord JM, Fridovich I. Superoxide dismutase: the first twenty years (1968-1988). Free Radical Biology & Medicine. 5: 363-9. PMID 2855736 DOI: 10.1016/0891-5849(88)90109-8 |
0.657 |
|
| 1988 |
Beyer WF, Fridovich I. Does copper(II) ethylenediaminetetraacetate disproportionate superoxide? Analytical Biochemistry. 173: 160-165. PMID 2847587 DOI: 10.1016/0003-2697(88)90173-X |
0.337 |
|
| 1988 |
Mashino T, Fridovich I. Reactions of hypochlorite with catalase Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 956: 63-69. PMID 2841981 DOI: 10.1016/0167-4838(88)90298-1 |
0.339 |
|
| 1988 |
Liochev S, Fridovich I. Superoxide is responsible for the vanadate stimulation of NAD(P)H oxidation by biological membranes Archives of Biochemistry and Biophysics. 263: 299-304. PMID 2837149 DOI: 10.1016/0003-9861(88)90639-X |
0.383 |
|
| 1988 |
Beyer WF, Fridovich I. Catalases—With and Without Heme Basic Life Sciences. 49: 651-661. DOI: 10.1007/978-1-4684-5568-7_103 |
0.355 |
|
| 1987 |
Mashino T, Fridovich I. Effects of urea and trimethylamine-N-oxide on enzyme activity and stability Archives of Biochemistry and Biophysics. 258: 356-360. PMID 3674879 DOI: 10.1016/0003-9861(87)90355-9 |
0.375 |
|
| 1987 |
Rabinowitch HD, Privalle CT, Fridovich I. Effects of paraquat on the green alga Dunaliella salina: protection by the mimic of superoxide dismutase, Desferal-Mn(IV). Free Radical Biology & Medicine. 3: 125-31. PMID 3666516 DOI: 10.1016/S0891-5849(87)80007-2 |
0.373 |
|
| 1987 |
Beyer WF, Fridovich I. Effect of hydrogen peroxide on the iron-containing superoxide dismutase of Escherichia colli Biochemistry. 26: 1251-1257. PMID 3552043 DOI: 10.1021/Bi00379A008 |
0.402 |
|
| 1987 |
Gardner PR, Fridovich I. Controls on the biosynthesis of the manganese-containing superoxide dismutase of Escherichia coli. Effects of thiols. The Journal of Biological Chemistry. 262: 17591-5. PMID 3320044 |
0.681 |
|
| 1987 |
Kitzler J, Fridovich I. The effects of paraquat on Escherichia coli: distinction between bacteriostasis and lethality. Journal of Free Radicals in Biology & Medicine. 2: 245-8. PMID 3294990 DOI: 10.1016/S0748-5514(86)80005-8 |
0.303 |
|
| 1987 |
Liochev S, Fridovich I. The oxidation of NADH by tetravalent vanadium. Archives of Biochemistry and Biophysics. 255: 274-8. PMID 3036003 DOI: 10.1016/0003-9861(87)90394-8 |
0.383 |
|
| 1987 |
Mashino T, Fridovich I. Superoxide radical initiates the autoxidation of dihydroxyacetone. Archives of Biochemistry and Biophysics. 254: 547-51. PMID 3034165 DOI: 10.1016/0003-9861(87)90136-6 |
0.422 |
|
| 1987 |
Beyer WF, Fridovich I. Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions. Analytical Biochemistry. 161: 559-66. PMID 3034103 DOI: 10.1016/0003-2697(87)90489-1 |
0.395 |
|
| 1987 |
Liochev S, Fridovich I. The oxidation of NADH by vanadate plus sugars. Biochimica Et Biophysica Acta. 924: 319-22. PMID 3032275 DOI: 10.1016/0304-4165(87)90029-8 |
0.428 |
|
| 1987 |
Mashino T, Fridovich I. Mechanism of the cyanide-catalyzed oxidation of alpha-ketoaldehydes and alpha-ketoalcohols. Archives of Biochemistry and Biophysics. 252: 163-70. PMID 3028255 DOI: 10.1016/0003-9861(87)90020-8 |
0.33 |
|
| 1987 |
Kuo CF, Fridovich I. Free-radical chain oxidation of 2-nitropropane initiated and propagated by superoxide. The Biochemical Journal. 237: 505-10. PMID 3026320 DOI: 10.1042/BJ2370505 |
0.31 |
|
| 1987 |
Beyer WF, Wang Y, Fridovich I. Phosphate inhibition of the copper- and zinc-containing superoxide dismutase: a reexamination. Biochemistry. 25: 6084-8. PMID 3024700 DOI: 10.1021/Bi00368A037 |
0.425 |
|
| 1987 |
Darr D, Zarilla KA, Fridovich I. A mimic of superoxide dismutase activity based upon desferrioxamine B and manganese(IV) Archives of Biochemistry and Biophysics. 258: 351-355. PMID 2823713 DOI: 10.1016/0003-9861(87)90354-7 |
0.356 |
|
| 1987 |
Kuo CF, Mashino T, Fridovich I. An activity stain for dihydroxy-acid dehydratase Analytical Biochemistry. 164: 526-530. PMID 2445227 DOI: 10.1016/0003-2697(87)90528-8 |
0.321 |
|
| 1986 |
Fridovich I. Superoxide dismutases. Advances in Enzymology and Related Areas of Molecular Biology. 58: 61-97. PMID 3521218 DOI: 10.1002/9780470123041.ch2 |
0.307 |
|
| 1986 |
Miller EK, Fridovich I. A demonstration that O2- is a crucial intermediate in the high quantum yield luminescence of luminol. Journal of Free Radicals in Biology & Medicine. 2: 107-10. PMID 3029206 DOI: 10.1016/S0748-5514(86)80058-7 |
0.408 |
|
| 1986 |
Liochev S, Fridovich I. The vanadate-stimulated oxidation of NAD(P)H by biomembranes is a superoxide-initiated free radical chain reaction. Archives of Biochemistry and Biophysics. 250: 139-45. PMID 3021060 DOI: 10.1016/0003-9861(86)90710-1 |
0.36 |
|
| 1986 |
Liochev S, Fridovich I. Further studies of the mechanism of the enhancement of NADH oxidation by vanadate. Journal of Free Radicals in Biology & Medicine. 1: 287-92. PMID 3013979 DOI: 10.1016/0748-5514(85)90133-3 |
0.414 |
|
| 1986 |
Fridovich I. Biological effects of the superoxide radical. Archives of Biochemistry and Biophysics. 247: 1-11. PMID 3010872 DOI: 10.1016/0003-9861(86)90526-6 |
0.363 |
|
| 1985 |
Borders CL, Fridovich I. A comparison of the effects of cyanide, hydrogen peroxide, and phenylglyoxal on eucaryotic and procaryotic Cu,Zn superoxide dismutases. Archives of Biochemistry and Biophysics. 241: 472-6. PMID 4037799 DOI: 10.1016/0003-9861(85)90572-7 |
0.373 |
|
| 1985 |
Darr D, Fridovich I. Vanadate enhancement of the oxidation of NADH by O2-: effects of phosphate and chelating agents. Archives of Biochemistry and Biophysics. 243: 220-7. PMID 3851646 DOI: 10.1016/0003-9861(85)90790-8 |
0.403 |
|
| 1985 |
Nagano T, Fridovich I. The co-oxidation of ammonia to nitrite during the aerobic xanthine oxidase reaction Archives of Biochemistry and Biophysics. 241: 596-601. PMID 3839996 DOI: 10.1016/0003-9861(85)90585-5 |
0.428 |
|
| 1985 |
Nagano T, Fridovich I. Does the aerobic xanthine oxidase reaction generate singlet oxygen? Photochemistry and Photobiology. 41: 33-37. PMID 3838588 DOI: 10.1111/J.1751-1097.1985.Tb03444.X |
0.417 |
|
| 1985 |
Nagano T, Fridovich I. Superoxide radical from xanthine oxidase acting upon lumazine Journal of Free Radicals in Biology and Medicine. 1: 39-42. PMID 3013970 DOI: 10.1016/0748-5514(85)90027-3 |
0.389 |
|
| 1985 |
Blum J, Fridovich I. Inactivation of glutathione peroxidase by superoxide radical. Archives of Biochemistry and Biophysics. 240: 500-8. PMID 2992378 DOI: 10.1016/0003-9861(85)90056-6 |
0.463 |
|
| 1984 |
Blum J, Fridovich I. Enzymatic defenses against oxygen toxicity in the hydrothermal vent animals Riftia pachyptila and Calyptogena magnifica. Archives of Biochemistry and Biophysics. 228: 617-20. PMID 6696449 DOI: 10.1016/0003-9861(84)90030-4 |
0.36 |
|
| 1984 |
Fridovich I. Overview: biological sources of O2-. Methods in Enzymology. 105: 59-61. PMID 6328206 DOI: 10.1016/S0076-6879(84)05008-4 |
0.382 |
|
| 1984 |
Picker SD, Fridovich I. On the mechanism of production of superoxide radical by reaction mixtures containing NADH, phenazine methosulfate, and nitroblue tetrazolium. Archives of Biochemistry and Biophysics. 228: 155-8. PMID 6320732 DOI: 10.1016/0003-9861(84)90056-0 |
0.454 |
|
| 1984 |
Diguiseppi J, Fridovich I, McCord JM. The toxicology of molecular oxygen Critical Reviews in Toxicology. 12: 315-342. PMID 6204814 DOI: 10.3109/10408448409044213 |
0.679 |
|
| 1984 |
Clare DA, Minh Ngoc Duong, Darr D, Archibald F, Fridovich I. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase Analytical Biochemistry. 140: 532-537. PMID 6091498 DOI: 10.1016/0003-2697(84)90204-5 |
0.417 |
|
| 1984 |
Darr D, Fridovich I. Vanadate and molybdate stimulate the oxidation of NADH by superoxide radical. Archives of Biochemistry and Biophysics. 232: 562-5. PMID 6087731 DOI: 10.1016/0003-9861(84)90573-3 |
0.425 |
|
| 1983 |
Kirby TW, Fridovich I. A picomolar spectrophotometric assay for superoxide dismutase. Analytical Biochemistry. 127: 435-40. PMID 6762113 DOI: 10.1016/0003-2697(82)90200-7 |
0.366 |
|
| 1983 |
Blum J, Fridovich I. Superoxide, hydrogen peroxide, and oxygen toxicity in two free-living nematode species. Archives of Biochemistry and Biophysics. 222: 35-43. PMID 6687666 DOI: 10.1016/0003-9861(83)90499-X |
0.427 |
|
| 1983 |
Rabinowitch HD, Clare DA, Crapo JD, Fridovich I. Positive correlation between superoxide dismutase and resistance to paraquat toxicity in the green alga Chlorella sorokiniana. Archives of Biochemistry and Biophysics. 225: 640-8. PMID 6625604 DOI: 10.1016/0003-9861(83)90075-9 |
0.518 |
|
| 1983 |
Benovic J, Tillman T, Cudd A, Fridovich I. Electrostatic facilitation of the reaction catalyzed by the manganese-containing and the iron-containing superoxide dismutases Archives of Biochemistry and Biophysics. 221: 329-332. PMID 6340608 DOI: 10.1016/0003-9861(83)90151-0 |
0.368 |
|
| 1983 |
Fridovich I. Superoxide radical: an endogenous toxicant. Annual Review of Pharmacology and Toxicology. 23: 239-57. PMID 6307121 DOI: 10.1146/Annurev.Pa.23.040183.001323 |
0.382 |
|
| 1983 |
Archibald FS, Fridovich I. Oxygen radicals, oxygen toxicity and the life of microorganisms. Acta MéDica Portuguesa. 4: 101-112. DOI: 10.20344/Amp.3779 |
0.379 |
|
| 1983 |
Rabinowitch HD, Fridovich I. SUPEROXIDE RADICALS, SUPEROXIDE DISMUTASES and OXYGEN TOXICITY IN PLANTS Photochemistry and Photobiology. 37: 679-690. DOI: 10.1111/J.1751-1097.1983.Tb04540.X |
0.388 |
|
| 1982 |
Fridovich I. Superoxide dismutases: exploration of apparent anomalies: a gene transfer and a functional replacement. Biochemical Society Transactions. 10: 67-8. PMID 7067913 DOI: 10.1042/Bst0100067 |
0.376 |
|
| 1982 |
Cudd A, Fridovich I. Parallel electrostatic effects in the interactions of superoxide with cytochrome c and with superoxide dismutase Febs Letters. 144: 181-182. PMID 6286357 DOI: 10.1016/0014-5793(82)80596-6 |
0.344 |
|
| 1982 |
Archibald FS, Fridovich I. The scavenging of superoxide radical by manganous complexes: in vitro. Archives of Biochemistry and Biophysics. 214: 452-63. PMID 6284026 DOI: 10.1016/0003-9861(82)90049-2 |
0.416 |
|
| 1982 |
Robertson P, Fridovich I. A reaction of the superoxide radical with tetrapyrroles. Archives of Biochemistry and Biophysics. 213: 353-7. PMID 6280613 DOI: 10.1016/0003-9861(82)90560-4 |
0.407 |
|
| 1982 |
Fridovich I. How innocuous is superoxide? Comments Accounts of Chemical Research. 15: 200-200. DOI: 10.1021/Ar00079A001 |
0.381 |
|
| 1981 |
Kirby TW, Lancaster JR, Fridovich I. Isolation and characterization of the iron-containing superoxide dismutase of Methanobacterium bryantii Archives of Biochemistry and Biophysics. 210: 140-148. PMID 7294823 DOI: 10.1016/0003-9861(81)90174-0 |
0.367 |
|
| 1981 |
Robertson P, Fridovich SE, Misra HP, Fridovich I. Cyanide catalyzes the oxidation of alpha-hydroxyaldehydes and related compounds: monitored as the reduction of dioxygen, cytochrome c, and nitroblue tetrazolium. Archives of Biochemistry and Biophysics. 207: 282-9. PMID 6264858 DOI: 10.1016/0003-9861(81)90035-7 |
0.629 |
|
| 1981 |
Brawn K, Fridovich I. DNA strand scission by enzymically generated oxygen radicals. Archives of Biochemistry and Biophysics. 206: 414-9. PMID 6261698 DOI: 10.1016/0003-9861(81)90108-9 |
0.346 |
|
| 1981 |
Diguiseppi J, Fridovich I. Ethylene from 2-keto-4-thiomethyl butyric acid: the Haber-Weiss reaction. Archives of Biochemistry and Biophysics. 205: 323-9. PMID 6258481 DOI: 10.1016/0003-9861(80)90114-9 |
0.365 |
|
| 1981 |
Archibald FS, Fridovich I. Manganese and defenses against oxygen toxicity in Lactobacillus plantarum. Journal of Bacteriology. 145: 442-51. PMID 6257639 DOI: 10.1128/Jb.145.1.442-451.1981 |
0.39 |
|
| 1981 |
Robertson P, Fridovich I. Does copper-D-penicillamine catalyze the dismutation of O2-? Archives of Biochemistry and Biophysics. 203: 830-1. PMID 6257182 DOI: 10.1016/0003-9861(80)90246-5 |
0.315 |
|
| 1981 |
Robertson P, Fridovich I. Continuous colorimetric monitoring of the fructose bisphosphate aldolase reaction. Analytical Biochemistry. 108: 332-4. PMID 6257144 DOI: 10.1016/0003-2697(80)90594-1 |
0.335 |
|
| 1980 |
Kirby T, Blum J, Kahane I, Fridovich I. Distinguishing between Mn-containing and Fe-containing superoxide dismutases in crude extracts of cells. Archives of Biochemistry and Biophysics. 201: 551-5. PMID 6994652 DOI: 10.1016/0003-9861(80)90544-5 |
0.371 |
|
| 1980 |
Diguiseppi J, Fridovich I. Putative superoxide dismutase activity of iron-EDTA: a reexamination. Archives of Biochemistry and Biophysics. 203: 145-50. PMID 6250482 DOI: 10.1016/0003-9861(80)90162-9 |
0.341 |
|
| 1980 |
Hassan HM, Dougherty H, Fridovich I. Inhibitors of superoxide dismutases: A cautionary tale Archives of Biochemistry and Biophysics. 199: 349-354. PMID 6244777 DOI: 10.1016/0003-9861(80)90290-8 |
0.451 |
|
| 1980 |
Hassan HM, Fridovich I. Mechanism of the antibiotic action of pyocyanine Journal of Bacteriology. 141: 156-163. PMID 6243619 DOI: 10.1128/Jb.141.1.156-163.1980 |
0.329 |
|
| 1980 |
Lynch RE, Fridovich I. Autoinactivation of xanthine oxidase: the role of superoxide radical and hydrogen peroxide. Biochimica Et Biophysica Acta. 571: 195-200. PMID 228731 DOI: 10.1016/0005-2744(79)90090-1 |
0.451 |
|
| 1980 |
Brawn K, Fridovich I. Superoxide Radical and Superoxide Dismutases: Threat and Defense Acta Physiologica Scandinavica. 492: 9-18. DOI: 10.1007/978-1-4757-9351-2_24 |
0.424 |
|
| 1979 |
Malinowski DP, Fridovich I. Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase Biochemistry. 18: 5909-5917. PMID 518876 DOI: 10.1021/Bi00593A023 |
0.36 |
|
| 1979 |
Claiborne A, Fridovich I. Chemical and enzymatic intermediates in the peroxidation of o-dianisidine by horseradish peroxidase. 2. Evidence for a substrate radical--enzyme complex and its reaction with nucleophiles. Biochemistry. 18: 2329-35. PMID 444459 DOI: 10.1021/Bi00578A030 |
0.428 |
|
| 1979 |
Britton L, Fridovich I. Streptomycin: irreversible association with superoxide dismutases. Archives of Biochemistry and Biophysics. 191: 198-204. PMID 367274 DOI: 10.1016/0003-9861(78)90082-6 |
0.379 |
|
| 1979 |
Hassan HM, Fridovich I. Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds Archives of Biochemistry and Biophysics. 196: 385-395. PMID 225995 DOI: 10.1016/0003-9861(79)90289-3 |
0.389 |
|
| 1979 |
Fridovich I. Superoxide dismutases: defence against endogenous superoxide radical. Ciba Foundation Symposium. 77-93. PMID 225147 DOI: 10.1002/9780470715413.CH6 |
0.322 |
|
| 1979 |
Claiborne A, Fridovich I. Chemical and enzymatic intermediates in the peroxidation of o-dianisidine by horseradish peroxidase. 1. Spectral properties of the products of dianisidine oxidation. Biochemistry. 18: 2324-9. PMID 221005 DOI: 10.1021/Bi00578A029 |
0.414 |
|
| 1979 |
Fridovich I. Superoxide radicals, superoxide dismutases and the aerobic lifestyle. Photochemistry and Photobiology. 28: 733-41. PMID 216032 DOI: 10.1111/J.1751-1097.1978.Tb07009.X |
0.447 |
|
| 1979 |
Malinowski DP, Fridovich I. Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents Biochemistry. 18: 5055-5060. PMID 115491 DOI: 10.1021/Bi00590A005 |
0.342 |
|
| 1979 |
Ose DE, Fridovich I. Manganese-containing superoxide dismutase from Escherichia coli: reversible resolution and metal replacements. Archives of Biochemistry and Biophysics. 194: 360-4. PMID 36037 DOI: 10.1016/0003-9861(79)90628-3 |
0.325 |
|
| 1979 |
Hassan HM, Fridovich I. Superoxide, Hydrogen Peroxide, and Oxygen Tolerance of Oxygen-Sensitive Mutants of Escherichia coli Clinical Infectious Diseases. 1: 357-369. DOI: 10.1093/Clinids/1.2.357 |
0.413 |
|
| 1979 |
Fridovich I, Hassan HM. Paraquat and the exacerbation of oxygen toxicity Trends in Biochemical Sciences. 4: 113-115. DOI: 10.1016/0968-0004(79)90395-5 |
0.405 |
|
| 1978 |
Crapo JD, McCord JM, Fridovich I. Preparation and assay of superoxide dismutases. Methods in Enzymology. 53: 382-93. PMID 362127 DOI: 10.1016/S0076-6879(78)53044-9 |
0.775 |
|
| 1978 |
Misra HP, Fridovich I. Inhibition of superoxide dismutases by azide. Archives of Biochemistry and Biophysics. 189: 317-22. PMID 213023 DOI: 10.1016/0003-9861(78)90218-7 |
0.579 |
|
| 1978 |
Fridovich I. The biology of oxygen radicals. Science (New York, N.Y.). 201: 875-80. PMID 210504 DOI: 10.1126/Science.210504 |
0.432 |
|
| 1978 |
McCord JM, Fridovich I. The biology and pathology of oxygen radicals. Annals of Internal Medicine. 89: 122-7. PMID 208444 DOI: 10.7326/0003-4819-89-1-122 |
0.733 |
|
| 1978 |
Britton L, Malinowski DP, Fridovich I. Superoxide dismutase and oxygen metabolism in Streptococcus faecalis and comparisons with other organisms Journal of Bacteriology. 134: 229-236. PMID 206536 DOI: 10.1128/Jb.134.1.229-236.1978 |
0.42 |
|
| 1978 |
Crapo JD, McCord JM, Fridovich I. [41] Preparation and assay of superioxide dismutases Methods in Enzymology. 53: 382-393. DOI: 10.1016/S0076-6879(78)53044-9 |
0.694 |
|
| 1977 |
Misra HP, Fridovich I. Purification and properties of superoxide dismutase from a red alga, Porphyridium cruentum. The Journal of Biological Chemistry. 252: 6421-3. PMID 893415 |
0.564 |
|
| 1977 |
Misra HP, Fridovich I. Superoxide dismutase and peroxidase: a positive activity stain applicable to polyacrylamide gel electropherograms. Archives of Biochemistry and Biophysics. 183: 511-5. PMID 335977 DOI: 10.1016/0003-9861(77)90386-1 |
0.614 |
|
| 1977 |
Moustafa Hassan H, Fridovich I. Regulation of superoxide dismutase synthesis in Escherichia coli: glucose effect. Journal of Bacteriology. 132: 505-10. PMID 21164 DOI: 10.1128/Jb.132.2.505-510.1977 |
0.326 |
|
| 1977 |
Misra HP, Fridovich I. Superoxide dismutase: a photochemical augmentation assay. Archives of Biochemistry and Biophysics. 181: 308-12. PMID 18108 DOI: 10.1016/0003-9861(77)90509-4 |
0.633 |
|
| 1977 |
Misra HP, Fridovich I. Superoxide dismutase: "positive" spectrophotometric assays. Analytical Biochemistry. 79: 553-60. PMID 17332 DOI: 10.1016/0003-2697(77)90429-8 |
0.629 |
|
| 1976 |
Misra HP, Fridovich I. A convenient calibration of the Clark oxygen electrode. Analytical Biochemistry. 70: 632-4. PMID 1267153 DOI: 10.1016/0003-2697(76)90492-9 |
0.544 |
|
| 1976 |
Hodgson EK, Fridovich I. The mechanism of the activity-dependent luminescence of xanthine oxidase. Archives of Biochemistry and Biophysics. 172: 202-5. PMID 1252075 DOI: 10.1016/0003-9861(76)90067-9 |
0.352 |
|
| 1976 |
Misra HP, Fridovich I. Superoxide dismutase and the oxygen enhancement of radiation lethality Archives of Biochemistry and Biophysics. 176: 577-581. PMID 791148 DOI: 10.1016/0003-9861(76)90201-0 |
0.594 |
|
| 1976 |
Yost FJ, Fridovich I. Superoxide and hydrogen peroxide in oxygen damage. Archives of Biochemistry and Biophysics. 175: 514-9. PMID 183117 DOI: 10.1016/0003-9861(76)90539-7 |
0.393 |
|
| 1976 |
Misra HP, Fridovich I. The oxidation of phenylhydrazine: superoxide and mechanism. Biochemistry. 15: 681-7. PMID 175827 DOI: 10.1021/Bi00648A036 |
0.643 |
|
| 1976 |
Hodgson EK, Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry. 14: 5299-303. PMID 172122 DOI: 10.1021/Bi00695A011 |
0.443 |
|
| 1976 |
Fridovich I. Superoxide dismutases: studies of structure and mechanism. Advances in Experimental Medicine and Biology. 74: 530-9. PMID 134628 DOI: 10.1007/978-1-4684-3270-1_44 |
0.446 |
|
| 1976 |
Hodgson EK, Fridovich I. The accumulation of superoxide radical during the aerobic action of xanthine oxidase. A requiem for H2O4. Biochimica Et Biophysica Acta. 430: 182-8. PMID 4144 DOI: 10.1016/0005-2728(76)90233-4 |
0.421 |
|
| 1976 |
Hodgson EK, Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry. 14: 5294-9. PMID 49 DOI: 10.1021/Bi00695A010 |
0.422 |
|
| 1975 |
Pick M, Rabani J, Yost F, Fridovich I. The catalytic mechanism of the manganese-containing superoxide dismutase of Escherichia coli studied by pulse radiolysis. Journal of the American Chemical Society. 96: 7329-33. PMID 4610039 DOI: 10.1021/Ja00830A026 |
0.315 |
|
| 1975 |
Fridovich I. Superoxide dismutases. Advances in Enzymology and Related Areas of Molecular Biology. 41: 35-97. PMID 4371571 DOI: 10.1002/9780470122860.ch2 |
0.307 |
|
| 1975 |
Fridovich I. Superoxide dismutases. Annual Review of Biochemistry. 44: 147-59. PMID 1094908 DOI: 10.1146/annurev.bi.44.070175.001051 |
0.307 |
|
| 1975 |
Cassell RH, Fridovich I. The role of superoxide radical in the autoxidation of cytochrome c Biochemistry. 14: 1866-1868. PMID 164898 DOI: 10.1021/Bi00680A010 |
0.402 |
|
| 1975 |
Fridovich I. Chapter 26. A Free Radical Pathology: Superoxide Radical and Superoxide Dismutases Annual Reports in Medicinal Chemistry. 10: 257-264. DOI: 10.1016/S0065-7743(08)61014-3 |
0.462 |
|
| 1974 |
Gregory EM, Fridovich I. Oxygen metabolism in Lactobacillus plantarum Journal of Bacteriology. 117: 166-169. PMID 4808898 DOI: 10.1128/Jb.117.1.166-169.1974 |
0.392 |
|
| 1974 |
Hodgson EK, Fridovich I. The role of O2- in the chemiluminescence of luminol. Photochemistry and Photobiology. 18: 451-5. PMID 4773935 DOI: 10.1111/J.1751-1097.1973.Tb06449.X |
0.392 |
|
| 1974 |
Yost FJ, Fridovich I. Superoxide radicals and phagocytosis. Archives of Biochemistry and Biophysics. 161: 395-401. PMID 4599312 DOI: 10.1016/0003-9861(74)90320-8 |
0.329 |
|
| 1974 |
Fridovich I. Evidence for the symbiotic origin of mitochondria. Life Sciences. 14: 819-26. PMID 4597494 DOI: 10.1016/0024-3205(74)90071-X |
0.342 |
|
| 1974 |
Gregory EM, Goscin SA, Fridovich I. Superoxide dismutase and oxygen toxicity in a eukaryote Journal of Bacteriology. 117: 456-460. PMID 4590469 DOI: 10.1128/Jb.117.2.456-460.1974 |
0.421 |
|
| 1974 |
Saltzman HA, Fridovich I. Editorial: Oxygen toxicity. Introduction to a protective enzyme: superoxide dismutase. Circulation. 48: 921-3. PMID 4584616 DOI: 10.1161/01.Cir.48.5.921 |
0.41 |
|
| 1974 |
Gregory EM, Fridovich I. Visualization of catalase on acrylamide gels Analytical Biochemistry. 58: 57-62. PMID 4207639 DOI: 10.1016/0003-2697(74)90440-0 |
0.427 |
|
| 1973 |
Hodgson EK, Fridovich I. Reversal of the superoxide dismutase reaction. Biochemical and Biophysical Research Communications. 54: 270-4. PMID 4795366 DOI: 10.1016/0006-291X(73)90918-2 |
0.433 |
|
| 1973 |
Beauchamp CO, Fridovich I. Isozymes of superoxide dismutase from wheat germ. Biochimica Et Biophysica Acta. 317: 50-64. PMID 4723247 DOI: 10.1016/0005-2795(73)90198-0 |
0.36 |
|
| 1973 |
Hodgson EK, McCord JM, Fridovich I. Anaerobic spectrophotometry: an improved cuvette. Analytical Biochemistry. 51: 470-3. PMID 4700195 DOI: 10.1016/0003-2697(73)90502-2 |
0.632 |
|
| 1973 |
Goscin SA, Fridovich I. The role of superoxide radical in a nonenzymatic hydroxylation. Archives of Biochemistry and Biophysics. 153: 778-83. PMID 4676909 DOI: 10.1016/0003-9861(72)90398-0 |
0.41 |
|
| 1973 |
Klug-Roth D, Fridovich I, Rabani J. Pulse radiolytic investigations of superoxide catalyzed disproportionation. Mechanism for bovine superoxide dismutase. Journal of the American Chemical Society. 95: 2786-90. PMID 4632912 DOI: 10.1021/Ja00790A007 |
0.306 |
|
| 1973 |
Gregory EM, Yost FJ, Fridovich I. Superoxide dismutases of Escherichia coli: intracellular localization and functions Journal of Bacteriology. 115: 987-991. PMID 4580575 DOI: 10.1128/Jb.115.3.987-991.1973 |
0.352 |
|
| 1973 |
McCord JM, Fridovich I. Production of O2- in photolyzed water demonstrated through the use of superoxide dismutase. Photochemistry and Photobiology. 17: 115-21. PMID 4364821 DOI: 10.1111/J.1751-1097.1973.Tb06340.X |
0.733 |
|
| 1973 |
Forman HJ, Fridovich I. Superoxide dismutase: a comparison of rate constants. Archives of Biochemistry and Biophysics. 158: 396-400. PMID 4354035 DOI: 10.1016/0003-9861(73)90636-X |
0.569 |
|
| 1973 |
Misra HP, Fridovich I. A peroxide-dependent reduction of cytochrome c by NADH. Biochimica Et Biophysica Acta. 292: 815-24. PMID 4350261 DOI: 10.1016/0005-2728(73)90028-5 |
0.617 |
|
| 1973 |
Forman HJ, Evans HJ, Hill RL, Fridovich I. Histidine at the active site of superoxide dismutase. Biochemistry. 12: 823-7. PMID 4346922 DOI: 10.1021/Bi00729A006 |
0.517 |
|
| 1973 |
Goscin SA, Fridovich I. The purification and properties of superoxide dismutase from Saccharomyces cerevisiae. Biochimica Et Biophysica Acta. 289: 276-83. PMID 4346514 DOI: 10.1016/0005-2744(72)90078-2 |
0.38 |
|
| 1973 |
Gregory EM, Fridovich I. Oxygen toxicity and the superoxide dismutase Journal of Bacteriology. 114: 1193-1197. PMID 4197269 DOI: 10.1128/Jb.114.3.1193-1197.1973 |
0.426 |
|
| 1973 |
Gregory EM, Fridovich I. Induction of superoxide dismutase by molecular oxygen Journal of Bacteriology. 114: 543-548. PMID 4196244 DOI: 10.1128/Jb.114.2.543-548.1973 |
0.406 |
|
| 1973 |
Goscin SA, Fridovich I. Superoxide Dismutase and the Oxygen Effect Radiation Research. 56: 565. DOI: 10.2307/3573726 |
0.405 |
|
| 1973 |
Lippitt B, Fridovich I. Tetrazolium oxidase and superoxide dismutase: Evidence for identity Archives of Biochemistry and Biophysics. 159: 738-741. DOI: 10.1016/0003-9861(73)90514-6 |
0.371 |
|
| 1973 |
KLUG-ROTH D, FRIDOVICH I, RABANI J. ChemInform Abstract: PULSRADIOLYTISCHE UNTERSUCHUNGEN DER PEROXID-KATALYSIERTEN DISPROPORTIONIERUNG, MECHANISMUS FUER RINDER-PEROXID-DISMUTASE Chemischer Informationsdienst. 4: no-no. DOI: 10.1002/Chin.197327141 |
0.368 |
|
| 1972 |
Lippitt B, McCord JM, Fridovich I. The sonochemical reduction of cytochrome c and its inhibition by superoxide dismutase. The Journal of Biological Chemistry. 247: 4688-90. PMID 5065128 |
0.66 |
|
| 1972 |
Beauchamp C, Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Analytical Biochemistry. 44: 276-87. PMID 4943714 DOI: 10.1016/0003-2697(71)90370-8 |
0.389 |
|
| 1972 |
Misra HP, Fridovich I. The generation of superoxide radical during the autoxidation of hemoglobin. The Journal of Biological Chemistry. 247: 6960-2. PMID 4673289 |
0.553 |
|
| 1972 |
Misra HP, Fridovich I. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. The Journal of Biological Chemistry. 247: 3170-5. PMID 4623845 |
0.565 |
|
| 1972 |
Misra HP, Fridovich I. The univalent reduction of oxygen by reduced flavins and quinones. The Journal of Biological Chemistry. 247: 188-92. PMID 4401581 |
0.548 |
|
| 1972 |
Misra HP, Fridovich I. The purification and properties of superoxide dismutase from Neurospora crassa. The Journal of Biological Chemistry. 247: 3410-4. PMID 4337853 |
0.53 |
|
| 1972 |
Rabani J, Klug D, Fridovich I. Decay of the HO2and O−2Radicals Catalyzed by Superoxide Dismutase. A Pulse Radiolytic Investigation Israel Journal of Chemistry. 10: 1095-1106. DOI: 10.1002/Ijch.197200117 |
0.37 |
|
| 1971 |
McCord JM, Keele BB, Fridovich I. An enzyme-based theory of obligate anaerobiosis: the physiological function of superoxide dismutase. Proceedings of the National Academy of Sciences of the United States of America. 68: 1024-7. PMID 4995818 DOI: 10.1073/Pnas.68.5.1024 |
0.719 |
|
| 1971 |
Misra HP, Fridovich I. The generation of superoixide radical during the autoxidation of ferredoxins. The Journal of Biological Chemistry. 246: 6886-90. PMID 4399476 |
0.526 |
|
| 1971 |
Keele BB, McCord JM, Fridovich I. Further characterization of bovine superoxide dismutase and its isolation from bovine heart. The Journal of Biological Chemistry. 246: 2875-80. PMID 4324341 |
0.619 |
|
| 1970 |
McCord JM, Fridovich I. The utility of superoxide dismutase in studying free radical reactions. II. The mechanism of the mediation of cytochrome c reduction by a variety of electron carriers. The Journal of Biological Chemistry. 245: 1374-7. PMID 5462997 |
0.667 |
|
| 1970 |
Frankfater A, Fridovich I. The purification and properties of oxidized derivatives of l-histidine ammonia-lyase Bba - Enzymology. 206: 457-472. PMID 4989951 DOI: 10.1016/0005-2744(70)90161-0 |
0.749 |
|
| 1970 |
Keele BB, McCord JM, Fridovich I. Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. The Journal of Biological Chemistry. 245: 6176-81. PMID 4921969 |
0.67 |
|
| 1969 |
McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). The Journal of Biological Chemistry. 244: 6049-55. PMID 5389100 |
0.667 |
|
| 1969 |
McCord JM, Fridovich I. The utility of superoxide dismutase in studying free radical reactions. I. Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen. The Journal of Biological Chemistry. 244: 6056-63. PMID 4981789 |
0.682 |
|
| 1968 |
McCord JM, Fridovich I. The reduction of cytochrome c by milk xanthine oxidase. The Journal of Biological Chemistry. 243: 5753-60. PMID 4972775 |
0.641 |
|
| 1962 |
RAJAGOPALAN KV, FRIDOVICH I, HANDLER P. Hepatic aldehyde oxidase. I. Purification and properties. The Journal of Biological Chemistry. 237: 922-8. PMID 14489970 |
0.414 |
|
| 1962 |
GREENLEE L, FRIDOVICH I, HANDLER P. Chemiluminescence induced by operation of iron-flavoproteins. Biochemistry. 1: 779-83. PMID 13950196 DOI: 10.1021/Bi00911A008 |
0.468 |
|
| 1962 |
FRIDOVICH I, HANDLER P. Xanthine oxidase. V. Differential inhibition of the reduction of various electron acceptors. The Journal of Biological Chemistry. 237: 916-21. PMID 13895169 |
0.425 |
|
| 1962 |
Farkas W, Macleod RW, Fridovich I, Handler P. [131] Sulfite cytochrome c reductase. 2 Ferricytochrome c + SO3 + H2O = SO4 + 2 Ferrocytochrome c + 2H+ SO3 + 1 2 O2 = SO4 Methods in Enzymology. 5: 983-986. DOI: 10.1016/S0076-6879(62)05345-8 |
0.525 |
|
| 1961 |
CAREY FG, FRIDOVICH I, HANDLER P. Preparation of several forms of xanthine oxidase by enzymic proteolysis. Biochimica Et Biophysica Acta. 53: 440-2. PMID 13876561 DOI: 10.1016/0006-3002(61)90468-1 |
0.558 |
|
| 1961 |
MACLEOD RM, FRIDOVICH I, HANDLER P. Mechanism of the factitious stimulation of biological oxidations by hypoxanthine. The Journal of Biological Chemistry. 236: 1847-9. PMID 13764979 |
0.467 |
|
| 1961 |
MACLEOD RM, FARKAS W, FRIDOVICH I, HANDLER P. Purification and properties of hepatic sulfite oxidase. The Journal of Biological Chemistry. 236: 1841-6. PMID 13764978 |
0.408 |
|
| 1961 |
RAJAGOPALAN KV, FRIDOVICH I, HANDLER P. Competitive inhibition of enzyme activity by urea. The Journal of Biological Chemistry. 236: 1059-65. PMID 13739212 |
0.492 |
|
| 1961 |
FRIDOVICH I, HANDLER P. Detection of free radicals generated during enzymic oxidations by the initiation of sulfite oxidation. The Journal of Biological Chemistry. 236: 1836-40. PMID 13701912 |
0.548 |
|
| 1960 |
FRIDOVICH I, HANDLER P. Detection of free radicals in illuminated dye solutions by the initiation of sulfite oxidation. The Journal of Biological Chemistry. 235: 1835-8. PMID 13825011 |
0.492 |
|
| 1959 |
FRIDOVICH I, HANDLER P. Utilization of the photosensitized oxidation of sulfite for manometric actinometry. Biochimica Et Biophysica Acta. 35: 546-7. PMID 13825012 DOI: 10.1016/0006-3002(59)90409-3 |
0.551 |
|
| 1958 |
FRIDOVICH I, FARKAS W, HANDLER P. Sulfite oxidation in rat liver. Bulletin De La SociéTé De Chimie Biologique. 40: 1795-801. PMID 13629220 |
0.445 |
|
| 1958 |
FRIDOVICH I, HANDLER P. Xanthine oxidase. IV. Participation of iron in internal electron transport. The Journal of Biological Chemistry. 233: 1581-5. PMID 13610877 |
0.41 |
|
| 1958 |
FRIDOVICH I, HANDLER P. Xanthine oxidase. III. Sulfite oxidation as an ultra sensitive assay. The Journal of Biological Chemistry. 233: 1578-80. PMID 13610876 |
0.513 |
|
| 1958 |
FRIDOVICH I, HANDLER P. Xanthine oxidase. II. Studies of the active site. The Journal of Biological Chemistry. 231: 899-911. PMID 13539025 |
0.434 |
|
| 1957 |
FRIDOVICH I, HANDLER P. Xanthine oxidase. I. The oxidation of sulfite. The Journal of Biological Chemistry. 228: 67-76. PMID 13475296 |
0.512 |
|
| 1957 |
MACLEOD RM, FRIDOVICH I, HANDLER P. Influence of sulfhydryl compounds on the equilibrium of the alcohol dehydrogenase reaction. Archives of Biochemistry and Biophysics. 72: 239-41. PMID 13471081 DOI: 10.1016/0003-9861(57)90193-5 |
0.464 |
|
| 1957 |
FRIDOVICH I, FARKAS W, SCHWERT GW, HANDLER P. Instrumental Artifacts in the Determination of Difference Spectra Science. 125: 1141-1142. DOI: 10.1126/Science.125.3258.1141-A |
0.443 |
|
| 1957 |
Fridovich I, Handler P. Colorimetric Assay for Reaction of Sulfhydryl Groups with Organic Mercurials Analytical Chemistry. 29: 1219-1220. DOI: 10.1021/Ac60128A034 |
0.478 |
|
| 1956 |
FRIDOVICH I, HANDLER P. The initial step in enzymatic sulfite oxidation. The Journal of Biological Chemistry. 223: 321-5. PMID 13376601 |
0.497 |
|
| 1956 |
FRIDOVICH I, HANDLER P. Hypoxanthine, cofactor for cysteine oxidation by liver preparations. Biochimica Et Biophysica Acta. 21: 173-4. PMID 13363878 DOI: 10.1016/0006-3002(56)90111-1 |
0.535 |
|
| 1956 |
FRIDOVICH I, HANDLER P. Hypoxanthine as a cofactor for the enzymatic oxidation of sulfite. The Journal of Biological Chemistry. 221: 323-31. PMID 13345822 |
0.509 |
|
| 1953 |
HEIMBERG M, FRIDOVICH I, HANDLER P. The enzymatic oxidation of sulfite. The Journal of Biological Chemistry. 204: 913-26. PMID 13117869 |
0.503 |
|
| Show low-probability matches. |
