What is he best known for?
The fields of study he is best known for:
- Enzyme
- Biochemistry
- Amino acid
His primary areas of study are Biochemistry, Oxidoreductase, Succinate dehydrogenase, Fumarate reductase and Electron Transport Complex II.
His Biochemistry course of study focuses on Gene mutation and Plasma protein binding and Bacterial adhesin.
His Oxidoreductase study combines topics in areas such as Protein structure, Enzyme complex and Flavoprotein.
His research in Succinate dehydrogenase intersects with topics in Stereochemistry and Site-directed mutagenesis.
Gary Cecchini interconnects Cofactor, Flavin group and Active site in the investigation of issues within Fumarate reductase.
Gary Cecchini focuses mostly in the field of Electron Transport Complex II, narrowing it down to matters related to Flavin adenine dinucleotide and, in some cases, Reactive oxygen species, Cellular respiration and Electron Transport Pathway.
His most cited work include:
- Architecture of succinate dehydrogenase and reactive oxygen species generation. (641 citations)
- Structure of the Escherichia coli fumarate reductase respiratory complex. (381 citations)
- Function and structure of complex II of the respiratory chain (316 citations)
What are the main themes of his work throughout his whole career to date?
The scientist’s investigation covers issues in Biochemistry, Fumarate reductase, Oxidoreductase, Succinate dehydrogenase and Stereochemistry.
His Biochemistry study frequently draws parallels with other fields, such as Quinone binding.
His studies in Fumarate reductase integrate themes in fields like Reductase, Site-directed mutagenesis, Active site, Photochemistry and Substrate.
His Oxidoreductase research includes themes of Submitochondrial particle, Respiratory chain, Mitochondrion, Electron transfer and Protein structure.
The Succinate dehydrogenase study combines topics in areas such as Cytochrome, Citrate synthase, Mitochondrial respiratory chain and Heme.
His Electron Transport Complex II study integrates concerns from other disciplines, such as Electron transport chain and Quinone oxidoreductase.
He most often published in these fields:
- Biochemistry (110.83%)
- Fumarate reductase (69.43%)
- Oxidoreductase (75.80%)
What were the highlights of his more recent work (between 2010-2020)?
- Biochemistry (110.83%)
- Fumarate reductase (69.43%)
- Stereochemistry (55.41%)
In recent papers he was focusing on the following fields of study:
His main research concerns Biochemistry, Fumarate reductase, Stereochemistry, Oxidoreductase and Flavoprotein.
His Biochemistry study frequently draws connections to adjacent fields such as Covalent bond.
His Fumarate reductase research incorporates themes from Biophysics and Respiratory chain.
His research integrates issues of Catalysis and Competitive inhibitor in his study of Stereochemistry.
His Oxidoreductase research is multidisciplinary, relying on both Electron Transport Complex II, Electron transport chain, Quinone binding, Hydrogen peroxide and ATP synthase.
Gary Cecchini has researched Flavoprotein in several fields, including SDHA, Cofactor and Flavin group.
Between 2010 and 2020, his most popular works were:
- A Structural Model for Binding of the Serine-Rich Repeat Adhesin GspB to Host Carbohydrate Receptors (69 citations)
- A Structural Model for Binding of the Serine-Rich Repeat Adhesin GspB to Host Carbohydrate Receptors (69 citations)
- A novel intracellular isoform of matrix metalloproteinase-2 induced by oxidative stress activates innate immunity. (68 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Amino acid
- Biochemistry
His primary scientific interests are in Biochemistry, Mitochondrion, Fumarate reductase, Oxidoreductase and Electron transport chain.
His Biochemistry research is multidisciplinary, incorporating perspectives in Bacterial adhesin and Gene mutation.
Enzyme and Succinate dehydrogenase are the areas that his Fumarate reductase study falls under.
The various areas that he examines in his Oxidoreductase study include Molecular mass and Hydrogen peroxide.
His Electron transport chain research incorporates elements of Electron Transport Complex II, Iron–sulfur cluster, Electron Transport Complex I and Adenosine triphosphate.
His Iron–sulfur cluster study incorporates themes from Flavoprotein, Quinone binding, Stereochemistry, Electron transfer and Redox.
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