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.
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.
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.
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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Generating disulfides enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
Einav Gross;Carolyn S. Sevier;Nimrod Heldman;Elvira Vitu.
Proceedings of the National Academy of Sciences of the United States of America (2006)
Acyl-CoA dehydrogenases - a mechanistic overview
Sandro Ghisla;Colin Thorpe.
FEBS Journal (2004)
Quantification of Thiols and Disulfides
Jakob R. Winther;Colin Thorpe.
Biochimica et Biophysica Acta (2014)
An acyl-coenzyme A dehydrogenase assay utilizing the ferricenium ion.
Thomas C. Lehman;Daniel E. Hale;Ajay Bhala;Colin Thorpe.
Analytical Biochemistry (1990)
Structure and mechanism of action of the acyl-CoA dehydrogenases.
Colin Thorpe;Jujng-Ja P. Kim.
The FASEB Journal (1995)
Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes.
Colin Thorpe;Karen L Hoober;Sonali Raje;Nicole M Glynn.
Archives of Biochemistry and Biophysics (2002)
New water-soluble phosphines as reductants of peptide and protein disulfide bonds: reactivity and membrane permeability.
Daniel J. Cline;Sarah E. Redding;Stephen G. Brohawn;James N. Psathas.
Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity.
Scott R. Farrell;Colin Thorpe.
Cyclic voltammetry and derivative cyclic voltabsorptometry of purified horse heart cytochrome c at tin-doped indium oxide optically transparent electrodes
Edmond F. Bowden;Fred M. Hawkridge;Jan F. Chlebowski;Eric E. Bancroft.
Journal of the American Chemical Society (1982)
Acyl-coenzyme A dehydrogenase from pig kidney. Purification and properties.
Colin Thorpe;Rowena G. Matthews;Charles H. Williams.
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