What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Active site, Stereochemistry, Biochemistry, Enzyme and Binding site.
The Active site study combines topics in areas such as Protein structure, Carbamoyl phosphate synthetase and Glutamine amidotransferase.
His Protein structure research is multidisciplinary, relying on both Crystallography and Ternary complex.
His studies deal with areas such as Hydrolase, Protein subunit, Isomerase, Substrate and NAD+ kinase as well as Stereochemistry.
James B. Thoden does research in Enzyme, focusing on Serine specifically.
His research in Binding site intersects with topics in Galactokinase deficiency, Mutant protein, Cofactor and Uridine diphosphate glucose.
His most cited work include:
- X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. (550 citations)
- Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism (364 citations)
- Structure of carbamoyl phosphate synthetase : a journey of 96 A from substrate to product (275 citations)
What are the main themes of his work throughout his whole career to date?
James B. Thoden focuses on Stereochemistry, Biochemistry, Enzyme, Active site and Protein structure.
James B. Thoden has researched Stereochemistry in several fields, including Protein subunit, Carbamoyl phosphate synthetase, Isomerase, Substrate and Binding site.
His biological study deals with issues like Campylobacter jejuni, which deal with fields such as Reductase and Microbiology.
His work deals with themes such as Mutant, Protein quaternary structure and Escherichia coli, which intersect with Enzyme.
His Active site research includes elements of Amino acid, Crystallography, Hydrolase, Nucleotide and Mutant protein.
His study explores the link between Crystallography and topics such as Hydrogen bond that cross with problems in Side chain.
He most often published in these fields:
- Stereochemistry (63.27%)
- Biochemistry (58.50%)
- Enzyme (40.82%)
What were the highlights of his more recent work (between 2014-2021)?
- Biochemistry (58.50%)
- Enzyme (40.82%)
- Stereochemistry (63.27%)
In recent papers he was focusing on the following fields of study:
Biochemistry, Enzyme, Stereochemistry, Transferase and Biosynthesis are his primary areas of study.
Biochemistry is represented through his Active site, NAD+ kinase, Phosphofructokinase 2, Dehydratase and Structure–activity relationship research.
His research integrates issues of Rhamnose, Protein subunit, Giant Virus and Mimivirus in his study of Active site.
He interconnects Escherichia coli, Campylobacter jejuni, Bacteria and Protein quaternary structure in the investigation of issues within Enzyme.
James B. Thoden performs integrative study on Stereochemistry and N-acetyltransferase in his works.
As a member of one scientific family, he mostly works in the field of Biosynthesis, focusing on Metabolic pathway and, on occasion, Streptomyces, Streptomyces fradiae and Protein tertiary structure.
Between 2014 and 2021, his most popular works were:
- Computational Redesign of Acyl-ACP Thioesterase with Improved Selectivity toward Medium-Chain-Length Fatty Acids (39 citations)
- New role for the ankyrin repeat revealed by a study of the N-formyltransferase from Providencia alcalifaciens. (16 citations)
- Structural and Biochemical Investigation of PglF from Campylobacter jejuni Reveals a New Mechanism for a Member of the Short Chain Dehydrogenase/Reductase Superfamily. (13 citations)
In his most recent research, the most cited papers focused on:
James B. Thoden focuses on Enzyme, Biochemistry, Transferase, Campylobacter jejuni and Bacteria.
The various areas that James B. Thoden examines in his Transferase study include Protein subunit, Pseudomonas aeruginosa, Stereochemistry, Glycoconjugate and Ankyrin repeat.
His Protein subunit research integrates issues from Amination, Moiety, Protein structure and Active site.
His research on Stereochemistry often connects related topics like Substrate.
His studies in Campylobacter jejuni integrate themes in fields like Pyridoxal, Reductase, Serotype, Microbiology and NAD+ kinase.
The concepts of his Bacteria study are interwoven with issues in Phosphofructokinase 2, Protein domain and Escherichia coli.
This overview was generated by a machine learning system which analysed the scientist’s
body of work. If you have any feedback, you can
contact us
here.
