What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Stereochemistry, Biochemistry, Binding site, Active site and Peptide sequence.
The various areas that Richard A. Engh examines in his Stereochemistry study include Papain, Pterin, Aldehyde oxidase, Multiple isomorphous replacement and Peptide bond.
Richard A. Engh carries out multidisciplinary research, doing studies in Biochemistry and Serine Proteinase Inhibitors.
His research integrates issues of Factor Xa Inhibitor, Salt bridge, Hydrogen bond and Pyrrolidine in his study of Binding site.
Richard A. Engh has researched Active site in several fields, including Sequence alignment, Hydrolase and Matrix metalloproteinase, Batimastat, Matrix metalloproteinase inhibitor.
The study incorporates disciplines such as Molecular recognition, Substrate Interaction, Substrate, Protein structure and Peptide in addition to Peptide sequence.
His most cited work include:
- Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement (2270 citations)
- The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. (498 citations)
- The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. (484 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of investigation include Biochemistry, Stereochemistry, Protein kinase A, Kinase and Binding site.
His Stereochemistry research includes themes of Protein structure, Enzyme inhibitor, Hydrogen bond and Active site.
His Protein structure research is multidisciplinary, incorporating elements of Peptide sequence and Peptide.
Richard A. Engh interconnects Protein kinase C and Mutant in the investigation of issues within Protein kinase A.
His studies in Binding site integrate themes in fields like Crystallography and Protein kinase B.
His Molecule research is multidisciplinary, relying on both Crystal structure and Molecular dynamics.
He most often published in these fields:
- Biochemistry (44.12%)
- Stereochemistry (38.97%)
- Protein kinase A (33.09%)
What were the highlights of his more recent work (between 2013-2021)?
- Kinase (21.32%)
- Stereochemistry (38.97%)
- Protein kinase A (33.09%)
In recent papers he was focusing on the following fields of study:
His main research concerns Kinase, Stereochemistry, Protein kinase A, Biochemistry and ABL.
His Kinase research incorporates themes from Tyrosine, Mutant and Binding site.
He studied Binding site and Ribose that intersect with Drug discovery.
He has included themes like Crystallography, Phase and Small molecule in his Stereochemistry study.
In his study, which falls under the umbrella issue of Protein kinase A, Plasma protein binding and Protein structure is strongly linked to Transferase.
His work in the fields of Biochemistry, such as Cyclin-dependent kinase 2 and Cyclin-dependent kinase complex, intersects with other areas such as Firefly luciferin and Luciferin.
Between 2013 and 2021, his most popular works were:
- Luciferin and derivatives as a DYRK selective scaffold for the design of protein kinase inhibitors. (17 citations)
- Probing the ATP-Binding Pocket of Protein Kinase Dyrk1A with Benzothiazole Fragment Molecules (14 citations)
- The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A-PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine. (14 citations)
In his most recent research, the most cited papers focused on:
His main research concerns Kinase, Protein kinase A, Stereochemistry, Biochemistry and Transferase.
His work deals with themes such as Tyrosine, Arginine, Cysteine and Catalysis, which intersect with Kinase.
His Protein kinase A research is multidisciplinary, incorporating perspectives in Protein kinase B, Molecular recognition, Ribose, Binding site and Drug discovery.
Many of his studies on Stereochemistry apply to Small molecule as well.
His Cyclin-dependent kinase 2 and Cyclin-dependent kinase complex study, which is part of a larger body of work in Biochemistry, is frequently linked to Luciferin and Firefly luciferin, bridging the gap between disciplines.
His Transferase research integrates issues from Bifunctional, Plasma protein binding, Protein subunit, Protein–protein interaction and Protein structure.
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