The scientist’s investigation covers issues in Superoxide dismutase, Enzyme, Biochemistry, Inorganic chemistry and Superoxide. Superoxide dismutase is closely attributed to Reactive oxygen species in her study. Her Enzyme research incorporates elements of Redox, Manganese and Stereochemistry.
Her work deals with themes such as Wild type and Copper, which intersect with Biochemistry. Diane E. Cabelli has researched Inorganic chemistry in several fields, including Radiolysis, Aqueous solution and Catalysis. Her Radiolysis research includes themes of Radiation chemistry, Reactivity and Photochemistry.
Her main research concerns Superoxide dismutase, Superoxide, Biochemistry, Radiolysis and Inorganic chemistry. Her Superoxide dismutase study contributes to a more complete understanding of Enzyme. She has included themes like Oxidoreductase, Protonation, Product inhibition and Candida albicans in her Superoxide study.
Her Biochemistry research focuses on subjects like Zinc, which are linked to Copper and Mutagenesis. Her work carried out in the field of Radiolysis brings together such families of science as Photochemistry, Reactivity and Reaction mechanism. Her research in the fields of Thiocyanate overlaps with other disciplines such as Pulse.
Superoxide dismutase, Superoxide, Biochemistry, Candida albicans and Active site are her primary areas of study. Her study in Superoxide dismutase is interdisciplinary in nature, drawing from both Zinc, Reactive oxygen species, Stereochemistry, Hydrogen peroxide and Combinatorial chemistry. The subject of her Superoxide research is within the realm of Enzyme.
The various areas that Diane E. Cabelli examines in her Active site study include Ligand and Histidine. Her biological study spans a wide range of topics, including Radiation chemistry and Biophysics. Her Radiolysis research integrates issues from Stoichiometry, Carbonate and Nuclear chemistry.
Her primary scientific interests are in Superoxide, Superoxide dismutase, Biochemistry, Yeast and Saccharomyces cerevisiae. Her Superoxide study improves the overall literature in Enzyme. Her Enzyme study combines topics from a wide range of disciplines, such as Combinatorial chemistry, Protonation, Manganese and Stereochemistry.
Biochemistry connects with themes related to Candida albicans in her study. Her biological study deals with issues like Copper protein, which deal with fields such as Active site. In Oxidoreductase, she works on issues like Binding site, which are connected to Inorganic chemistry.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Reactivity of HO2/O−2 Radicals in Aqueous Solution
Benon H. J. Bielski;Diane E. Cabelli;Ravindra L. Arudi;Alberta B. Ross.
Journal of Physical and Chemical Reference Data (1985)
Superoxide dismutases and superoxide reductases
Yuewei Sheng;Isabel Alexandra Aguiar de Abreu;Diane E. Cabelli;Michael J. Maroney.
Chemical Reviews (2014)
Faster superoxide dismutase mutants designed by enhancing electrostatic guidance
Elizabeth D. Getzoff;Diane E. Cabelli;Cindy L. Fisher;Hans E. Parge.
Nature (1992)
Superoxide dismutases-a review of the metal-associated mechanistic variations.
Isabel A. Abreu;Diane E. Cabelli.
Biochimica et Biophysica Acta (2010)
Decreased Metallation and Activity in Subsets of Mutant Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis
Lawrence J. Hayward;Jorge A. Rodriguez;Ji W. Kim;Ashutosh Tiwari.
Journal of Biological Chemistry (2002)
Kinetics and mechanism for the oxidation of ascorbic acid/ascorbate by HO2/O2- (hydroperoxyl/superoxide) radicals. A pulse radiolysis and stopped-flow photolysis study
Diane E. Cabelli;Benon H. J. Bielski.
The Journal of Physical Chemistry (1983)
Human Mitochondrial Manganese Superoxide Dismutase Polymorphic Variant Ile58Thr Reduces Activity by Destabilizing the Tetrameric Interface
Gloria E.O. Borgstahl;Hans E. Parge;Hans E. Parge;Michael J. Hickey;Michael J. Johnson.
Biochemistry (1996)
Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis.
Joy J. Goto;Haining Zhu;Raylene J. Sanchez;Aram Nersissian.
Journal of Biological Chemistry (2000)
Examination of the nickel site structure and reaction mechanism in Streptomyces seoulensis superoxide dismutase
Suranjan B. Choudhury;Jin-Won Lee;Gerard Davidson;Yang In Yim.
Biochemistry (1999)
Nickel(II) macrocycles: highly efficient electrocatalysts for the selective reduction of CO2 to CO
Jacob Schneider;Hongfei Jia;Kazuya Kobiro;Diane E. Cabelli.
Energy and Environmental Science (2012)
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