What is he best known for?
The fields of study he is best known for:
Didier Fournier mainly focuses on Acetylcholinesterase, Biochemistry, Enzyme, Carbamate and Organophosphate.
His work deals with themes such as Propoxur, Cholinesterase, Active site, Wild type and Allele, which intersect with Acetylcholinesterase.
His Allele research incorporates themes from Mutation and Point mutation.
His Biochemistry study incorporates themes from Dichlorvos and Biophysics.
Didier Fournier has researched Enzyme in several fields, including Molecular biology, Corbicula and Corbicula fluminea.
His Carbamate research is multidisciplinary, incorporating perspectives in Carbaryl, Insect, Enzyme assay and Carbofuran.
His most cited work include:
- Resistance-associated point mutations in insecticide-insensitive acetylcholinesterase (357 citations)
- Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides. (262 citations)
- Modification of acetylcholinesterase as a mechanism of resistance to insecticides. (239 citations)
What are the main themes of his work throughout his whole career to date?
Didier Fournier mostly deals with Acetylcholinesterase, Biochemistry, Enzyme, Stereochemistry and Substrate.
Didier Fournier combines subjects such as Drosophila melanogaster, Carbamate, Biosensor, Organophosphate and Active site with his study of Acetylcholinesterase.
His Carbamate research incorporates elements of Mutation and Insect.
His work carried out in the field of Biochemistry brings together such families of science as Molecular biology and Cholinesterase.
His research integrates issues of Metabolite, Molecule and Metabolism in his study of Enzyme.
His Substrate course of study focuses on Biophysics and Liposome and Lipid bilayer.
He most often published in these fields:
- Acetylcholinesterase (42.69%)
- Biochemistry (38.60%)
- Enzyme (30.99%)
What were the highlights of his more recent work (between 2005-2011)?
- Acetylcholinesterase (42.69%)
- Biochemistry (38.60%)
- Substrate (11.70%)
In recent papers he was focusing on the following fields of study:
Didier Fournier mainly investigates Acetylcholinesterase, Biochemistry, Substrate, Biophysics and Stereochemistry.
His Acetylcholinesterase study is focused on Enzyme in general.
His work on Carboxylic Ester Hydrolases and Aché as part of general Enzyme study is frequently linked to Investigation methods and Hysteresis, bridging the gap between disciplines.
His studies in Substrate integrate themes in fields like Membrane channel, Lipid bilayer and Biological membrane.
The Biophysics study which covers Liposome that intersects with Oligonucleotide, Radical polymerization and Vesicle.
His work deals with themes such as Azide, Drosophila melanogaster, Choline binding and Group, which intersect with Stereochemistry.
Between 2005 and 2011, his most popular works were:
- Evidence for inhibition of cholinesterases in insect and mammalian nervous systems by the insect repellent deet (135 citations)
- Structural Insights Into Substrate Traffic and Inhibition in Acetylcholinesterase. (126 citations)
- Comparative toxicity of imidacloprid, of its commercial liquid formulation and of diazinon to a non-target arthropod, the microcrustacean Daphnia magna. (119 citations)
In his most recent research, the most cited papers focused on:
The scientist’s investigation covers issues in Biochemistry, Acetylcholinesterase, Carbamate, Acetylthiocholine and Cholinesterase.
His study in Biophysics extends to Biochemistry with its themes.
His research in Acetylcholinesterase intersects with topics in Propoxur, Hydrolase, Denaturation, Pharmacology and DEET.
His work is dedicated to discovering how Carbamate, Enzyme assay are connected with Carbaryl, Organophosphate, Esterase and Pirimicarb and other disciplines.
He has included themes like Thiocholine, Chromatography, Binding site and Enzymatic hydrolysis in his Acetylthiocholine study.
The Cholinesterase study combines topics in areas such as Mercury, Insect repellent, Butyrylcholinesterase and Enzyme.
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