What is he best known for?
The fields of study he is best known for:
- Enzyme
- Amino acid
- Biochemistry
His scientific interests lie mostly in Stereochemistry, Biochemistry, Chemical shift, Nuclear magnetic resonance spectroscopy and Crystallography.
His Stereochemistry study incorporates themes from Amino acid, Dihedral angle, Antibiotics, Dihydrofolate reductase and Conformational isomerism.
The various areas that James Feeney examines in his Biochemistry study include Cell biology and Mass spectrometry.
James Feeney interconnects Proton NMR, Polarization, Fluorine-19 NMR, Ligand and Molecule in the investigation of issues within Chemical shift.
His Nuclear magnetic resonance spectroscopy study deals with the bigger picture of Nuclear magnetic resonance.
His Crystallography study combines topics from a wide range of disciplines, such as Antiparallel, Protein tertiary structure, Nuclear Overhauser effect, Peptide bond and Protein structure.
His most cited work include:
- High Resolution Nuclear Magnetic Resonance Spectroscopy (949 citations)
- Structure revision of the antibiotic echinomycin. (262 citations)
- Binding of flexible ligands to macromolecules (179 citations)
What are the main themes of his work throughout his whole career to date?
James Feeney focuses on Stereochemistry, Dihydrofolate reductase, Biochemistry, Nuclear magnetic resonance spectroscopy and Enzyme.
His Stereochemistry research incorporates elements of Crystallography, Protein structure, Binding site and Chemical shift.
His research in Chemical shift tackles topics such as Hydrogen bond which are related to areas like Intramolecular force.
His research investigates the connection between Dihydrofolate reductase and topics such as Cofactor that intersect with problems in Nicotinamide.
The study incorporates disciplines such as Solution structure and Methotrexate in addition to Biochemistry.
His study in Nuclear magnetic resonance spectroscopy is interdisciplinary in nature, drawing from both Dihedral angle and Plasma protein binding.
He most often published in these fields:
- Stereochemistry (55.35%)
- Dihydrofolate reductase (41.40%)
- Biochemistry (22.33%)
What were the highlights of his more recent work (between 1997-2014)?
- Stereochemistry (55.35%)
- Dihydrofolate reductase (41.40%)
- Crystallography (13.95%)
In recent papers he was focusing on the following fields of study:
James Feeney mainly focuses on Stereochemistry, Dihydrofolate reductase, Crystallography, Biochemistry and Solution structure.
His Stereochemistry research is mostly focused on the topic Nuclear magnetic resonance spectroscopy.
The concepts of his Dihydrofolate reductase study are interwoven with issues in Ligand, Hydrogen bond and Trimethoprim.
His studies in Crystallography integrate themes in fields like Conformational change, Calmodulin and Ligand.
His Biochemistry research is multidisciplinary, incorporating perspectives in Isotopomers, Deuterated methanol and Mass spectrometry.
His Chemical shift research includes themes of Residue, Carboxylate and EF hand.
Between 1997 and 2014, his most popular works were:
- Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1. (137 citations)
- Inhibitory and blocking monoclonal antibody epitopes on merozoite surface protein 1 of the malaria parasite Plasmodium falciparum. (134 citations)
- High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3 (77 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Amino acid
- Biochemistry
Crystallography, Stereochemistry, Monomer, Biochemistry and Calmodulin are his primary areas of study.
He has included themes like Nuclear magnetic resonance spectroscopy and Conformational change in his Crystallography study.
The various areas that James Feeney examines in his Stereochemistry study include Dihedral angle, Mechanism of action, Ternary complex, Receptor and Dihydrofolate reductase.
His Dihydrofolate reductase study integrates concerns from other disciplines, such as Protein dynamics, Hydrogen bond, Substrate and NADPH binding.
His Biochemistry study frequently involves adjacent topics like Naphthylamine.
His Calmodulin research incorporates themes from Ion, Magnetic susceptibility and Chemical shift.
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