What is he best known for?
The fields of study he is best known for:
- Enzyme
- Organic chemistry
- Amino acid
His primary areas of investigation include Biochemistry, Flavin group, Dehydrogenase, Enzyme and Protein disulfide-isomerase.
His Redox research extends to Biochemistry, which is thematically connected.
His biological study spans a wide range of topics, including Oxidase test and Cofactor.
The Oxidase test study combines topics in areas such as Thiol, Cysteine, Egg white and Dithiothreitol.
The concepts of his Dehydrogenase study are interwoven with issues in Flavin adenine dinucleotide, Flavoprotein and Stereochemistry.
In his research, Reductase and Iodoacetamide is intimately related to Glutathione, which falls under the overarching field of Protein disulfide-isomerase.
His most cited work include:
- Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p (296 citations)
- Acyl-CoA dehydrogenases - a mechanistic overview (233 citations)
- An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion. (193 citations)
What are the main themes of his work throughout his whole career to date?
Biochemistry, Stereochemistry, Flavin group, Dehydrogenase and Enzyme are his primary areas of study.
All of his Biochemistry and Cysteine, Protein disulfide-isomerase, Protein folding, Oxidase test and Cofactor investigations are sub-components of the entire Biochemistry study.
His Stereochemistry study integrates concerns from other disciplines, such as Thioester, Adduct, Redox and Active center.
His Flavin group research is multidisciplinary, relying on both Flavin adenine dinucleotide, Flavoprotein, Semiquinone, Tris and Hydrogen peroxide.
His studies deal with areas such as Coenzyme A, Substrate and Active site as well as Dehydrogenase.
His research integrates issues of Molecular biology, Catalysis and Denaturation in his study of Enzyme.
He most often published in these fields:
- Biochemistry (57.66%)
- Stereochemistry (39.42%)
- Flavin group (39.42%)
What were the highlights of his more recent work (between 2008-2019)?
- Biochemistry (57.66%)
- Cysteine (18.25%)
- Protein folding (12.41%)
In recent papers he was focusing on the following fields of study:
The scientist’s investigation covers issues in Biochemistry, Cysteine, Protein folding, Protein disulfide-isomerase and Flavin group.
His study in Glutathione, Enzyme, Dithiothreitol, Cofactor and Thioredoxin are all subfields of Biochemistry.
The various areas that he examines in his Cysteine study include Amino acid, Oxidase test and Oxidoreductase.
His study in Protein folding is interdisciplinary in nature, drawing from both Oxidative phosphorylation and Intracellular.
His Protein disulfide-isomerase study combines topics in areas such as Flavin adenine dinucleotide, Arsenic trioxide and Arsenite.
His Flavin group research integrates issues from Flavoprotein, Selenocysteine, Selenium, Active site and Protein structure.
Between 2008 and 2019, his most popular works were:
- Quantification of Thiols and Disulfides (182 citations)
- Oxidative Protein Folding and the Quiescin–Sulfhydryl Oxidase Family of Flavoproteins (91 citations)
- Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum. (78 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Organic chemistry
- Amino acid
Colin Thorpe mainly investigates Biochemistry, Protein disulfide-isomerase, Protein folding, Cysteine and Endoplasmic reticulum.
His studies link Redox with Biochemistry.
In his work, Arsenite, Plasma protein binding and Arsenic trioxide is strongly intertwined with Glutathione, which is a subfield of Protein folding.
His Cysteine research is included under the broader classification of Enzyme.
His biological study deals with issues like Oxidative phosphorylation, which deal with fields such as Thioredoxin.
His study focuses on the intersection of Flavin group and fields such as Flavoprotein with connections in the field of Binding domain and Oxidative folding.
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