What is he best known for?
The fields of study he is best known for:
- Enzyme
- Catalysis
- Amino acid
Stereochemistry, Flavin group, Substrate, Photochemistry and Flavoprotein are his primary areas of study.
David P. Ballou combines subjects such as Reductase, Cofactor, Steady state, Cytochrome and Hemeprotein with his study of Stereochemistry.
His Flavin group research entails a greater understanding of Enzyme.
His biological study spans a wide range of topics, including Active site, Dephosphorylation and Hydroxylation.
In Photochemistry, David P. Ballou works on issues like Xanthine oxidase, which are connected to Superoxide dismutase.
His work investigates the relationship between Flavoprotein and topics such as Redox that intersect with problems in Flavin reductase.
His most cited work include:
- Oxidative Protein Folding Is Driven by the Electron Transport System (337 citations)
- Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase. (290 citations)
- The Mechanism of Action of Xanthine Oxidase (266 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are Stereochemistry, Flavin group, Biochemistry, Enzyme and Flavoprotein.
His Stereochemistry research is multidisciplinary, relying on both Reductase, Hydroxylation, Cofactor, Active site and Substrate.
The concepts of his Flavin group study are interwoven with issues in Mutant, Photochemistry, Flavin adenine dinucleotide and Oxygen.
His Cytochrome, Microsome, Thioredoxin and Tryptophan study in the realm of Biochemistry connects with subjects such as Glutathione reductase.
His studies in Enzyme integrate themes in fields like Reactivity and Escherichia coli.
The Flavoprotein study combines topics in areas such as Oxidoreductase, Oxidative phosphorylation, Monooxygenase and Redox.
He most often published in these fields:
- Stereochemistry (52.45%)
- Flavin group (35.78%)
- Biochemistry (30.88%)
What were the highlights of his more recent work (between 2009-2021)?
- Biochemistry (30.88%)
- Flavin group (35.78%)
- Stereochemistry (52.45%)
In recent papers he was focusing on the following fields of study:
His scientific interests lie mostly in Biochemistry, Flavin group, Stereochemistry, Flavoprotein and Monooxygenase.
He has included themes like Photochemistry, Reductase and Substrate in his Flavin group study.
His studies deal with areas such as Residue, Liberation and Catalysis, Aldehyde as well as Photochemistry.
His Stereochemistry research includes elements of Hydroxylation, Cofactor, Peroxidase, Reaction rate constant and Steady state.
His study in Flavoprotein is interdisciplinary in nature, drawing from both Flavin adenine dinucleotide, Sulfur, Inorganic chemistry, Sulfite and Sulfide.
In his research, Oxidoreductase is intimately related to Flavin mononucleotide, which falls under the overarching field of Monooxygenase.
Between 2009 and 2021, his most popular works were:
- The biochemical mechanism of auxin biosynthesis by an arabidopsis YUCCA flavin-containing monooxygenase (129 citations)
- Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase (72 citations)
- Polymorphic Variants of Cytochrome P450 2B6 (CYP2B6.4–CYP2B6.9) Exhibit Altered Rates of Metabolism for Bupropion and Efavirenz: A Charge-Reversal Mutation in the K139E Variant (CYP2B6.8) Impairs Formation of a Functional Cytochrome P450-Reductase Complex (47 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Catalysis
- Amino acid
David P. Ballou mostly deals with Biochemistry, Flavin group, Stereochemistry, Flavoprotein and Glutaredoxin.
His work on Hydroxylation and Mutagenesis as part of general Biochemistry study is frequently connected to CYP2B6, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
His Flavin group research incorporates themes from Flavin adenine dinucleotide and Monooxygenase, Mixed Function Oxygenases.
His research in the fields of Circular dichroism overlaps with other disciplines such as Magnetic circular dichroism.
As a part of the same scientific study, David P. Ballou usually deals with the Flavoprotein, concentrating on Sulfide and frequently concerns with Combinatorial chemistry, Catalytic cycle, Photochemistry and Thiosulfate.
His Glutaredoxin research is multidisciplinary, incorporating elements of Protein disulfide-isomerase, Protein Data Bank and Active site.
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