Cabelli, Diane E.
Brookhaven National Laboratory
14 papers on CoChat
Most cited papers
- Verified
Reactivity of HO2/O− 2 radicals in aqueous solution
Bielski, B. H. J., Cabelli, D. E., Arudi, R. L., & Ross, A. B. (1985) · Journal of Physical and Chemical Reference Data
Advanced oxidation water treatmentFree Radicals and Antioxidants
Cited by 2,169
- Verified
Superoxide dismutases and superoxide reductases
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews
Metal-Catalyzed Oxygenation MechanismsRedox biology and oxidative stress
Cited by 1,081
- Verified
Superoxide dismutases—A review of the metal-associated mechanistic variations
Abreu, I. A., & Cabelli, D. E. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Metal-Catalyzed Oxygenation MechanismsGlutathione Transferases and Polymorphisms
Cited by 563
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Faster superoxide dismutase mutants designed by enhancing electrostatic guidance
Getzoff, E. D., Cabelli, D. E., Fisher, C. L., Parge, H. E., Viezzoli, M. S., Banci, L., & Hallewell, R. A. (1992) · Nature
Metal-Catalyzed Oxygenation MechanismsProtein Structure and Dynamics
Cited by 399
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Copper–zinc superoxide dismutase: Why not pH-dependent?
Ellerby, L. M., Cabelli, D. E., Graden, J. A., & Valentine, J. S. (1996) · Journal of the American Chemical Society
Metal-Catalyzed Oxygenation MechanismsGlutathione Transferases and Polymorphisms
Cited by 184
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Determination of Optimal Conditions for Synthesis of Peroxynitrite by Mixing Acidified Hydrogen Peroxide with Nitrite
Saha, A., Goldstein, S., Cabelli, D., & Czapski, G. (1998) · Free Radical Biology and Medicine
Physical Organic Chemistry and Reaction KineticsNitric Oxide and Endothelin Effects
Cited by 143
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The role of arginine 143 in the electrostatics and mechanism of Cu, Zn superoxide dismutase: Computational and experimental evaluation by mutational analysis
Fisher, C. L., Cabelli, D. E., Tainer, J. A., Hallewell, R. A., & Getzoff, E. D. (1994) · Proteins: Structure, Function, and Bioinformatics
Metal-Catalyzed Oxygenation MechanismsProtein Structure and Dynamics
Cited by 125
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Superoxide Reactivity of Rubredoxin Oxidoreductase (Desulfoferrodoxin) from Desulfovibrio vulgaris: A Pulse Radiolysis Study
Coulter, E. D., Emerson, J. P., Kurtz, D. M., & Cabelli, D. E. (2000) · Journal of the American Chemical Society
Metalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation Mechanisms
Cited by 101
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Kinetics and Mechanism of Superoxide Reduction by Two-Iron Superoxide Reductase from Desulfovibrio vulgaris
Emerson, J. P., Coulter, E. D., Cabelli, D. E., Phillips, R. S., & Kurtz, D. M. (2002) · Biochemistry
Metal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteins
Cited by 89
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Copper-only superoxide dismutase enzymes and iron starvation stress in Candida fungal pathogens
Schatzman, S. S., Peterson, R. L., Teka, M., He, B., Cabelli, D. E., Cormack, B. P., & Culotta, V. C. (2020) · Journal of Biological Chemistry
Fungal and yeast genetics researchMetal-Catalyzed Oxygenation Mechanisms
Cited by 54
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Superoxide Reduction Mechanism of Archaeoglobus fulgidus One-Iron Superoxide Reductase
Rodrigues, J. V., Abreu, I. A., Cabelli, D., & Teixeira, M. (2006) · Biochemistry
Metal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteins
Cited by 46
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Comparison of two yeast MnSODs: Mitochondrial Saccharomyces cerevisiae versus cytosolic Candida albicans
Sheng, Y., Stich, T. A., Barnese, K., Gralla, E. B., Cascio, D., Britt, R. D., Cabelli, D. E., & Valentine, J. S. (2011) · Journal of the American Chemical Society
Metal-Catalyzed Oxygenation MechanismsRedox biology and oxidative stress
Cited by 43
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Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: Comparison with neelaredoxin
Rodrigues, J. V., Saraiva, L. M., Abreu, I. A., Teixeira, M., & Cabelli, D. E. (2007) · JBIC Journal of Biological Inorganic Chemistry
Metal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteins
Cited by 40
- Verified
Superoxide reduction by Nanoarchaeum equitans neelaredoxin, an enzyme lacking the highly conserved glutamate iron ligand
Rodrigues, J. V., Victor, B. L., Huber, H., Saraiva, L. M., Soares, C. M., Cabelli, D. E., & Teixeira, M. (2008) · JBIC Journal of Biological Inorganic Chemistry
Metal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteins
Cited by 24
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