What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Receptor, G protein-coupled receptor, Stereochemistry, Agonist and Protein structure.
Biochemistry covers he research in Receptor.
His work deals with themes such as Hedgehog signaling pathway, Smoothened, Crystallography, Helix and Transmembrane domain, which intersect with G protein-coupled receptor.
His biological study spans a wide range of topics, including Metabotropic glutamate receptor 7, Metabotropic glutamate receptor, Dopamine receptor D2, Allosteric regulation and Binding site.
His studies deal with areas such as Biophysics, Neuroscience, Morphinan and Intracellular as well as Agonist.
Gye Won Han combines subjects such as Cutin, Salvinorin A, Norbinaltorphimine and JDTic with his study of Protein structure.
His most cited work include:
- Structure of the human dopamine d3 receptor in complex with a d2/d3 selective antagonist. (890 citations)
- Structure of an Agonist-Bound Human A2A Adenosine Receptor (676 citations)
- Structure of the human κ-opioid receptor in complex with JDTic (668 citations)
What are the main themes of his work throughout his whole career to date?
Gye Won Han spends much of his time researching Biochemistry, Stereochemistry, Receptor, G protein-coupled receptor and Protein structure.
Gye Won Han interconnects Helix, Crystal structure and Binding site in the investigation of issues within Stereochemistry.
Gye Won Han works mostly in the field of Receptor, limiting it down to topics relating to Docking and, in certain cases, Antagonist.
His study in G protein-coupled receptor is interdisciplinary in nature, drawing from both Biophysics, Allosteric regulation, Transmembrane domain and Ligand.
His Protein structure study integrates concerns from other disciplines, such as Conformational change, Transferase and Computational biology.
His studies in Agonist integrate themes in fields like Pharmacology and Peptide.
He most often published in these fields:
- Biochemistry (41.07%)
- Stereochemistry (23.81%)
- Receptor (22.62%)
What were the highlights of his more recent work (between 2015-2021)?
- Receptor (22.62%)
- G protein-coupled receptor (23.21%)
- Biophysics (11.31%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Receptor, G protein-coupled receptor, Biophysics, Agonist and Ligand.
His biological study spans a wide range of topics, including Protein structure, Membrane protein and Intracellular, Cell biology.
The various areas that he examines in his G protein-coupled receptor study include Inverse agonist, Frizzled, Allosteric regulation and Drug discovery.
His Biophysics research integrates issues from Glucagon-like peptide 1 receptor, Binding site and Transmembrane domain.
His Agonist study combines topics in areas such as Peptide sequence, Pharmacology and Peptide.
His Ligand research incorporates elements of Docking, Adrenergic receptor, Chemotaxis, Endogeny and Melatonin receptor.
Between 2015 and 2021, his most popular works were:
- Crystal Structure of the Human Cannabinoid Receptor CB2. (310 citations)
- Crystal structures of agonist-bound human cannabinoid receptor CB1 (209 citations)
- Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor (148 citations)
In his most recent research, the most cited papers focused on:
His primary areas of study are G protein-coupled receptor, Receptor, Biophysics, Allosteric regulation and Cell biology.
His G protein-coupled receptor research includes themes of Inverse agonist, Antagonist, Cannabinoid receptor type 2, Intracellular and Drug discovery.
His Drug discovery research includes elements of Protein structure and Structural biology.
The study incorporates disciplines such as Cannabinoid, Endocannabinoid system, Transmembrane domain, Partial agonist and Binding site in addition to Biophysics.
His Transmembrane domain study results in a more complete grasp of Biochemistry.
His research in Allosteric regulation intersects with topics in Plasma protein binding and Signal transduction.
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