What is he best known for?
The fields of study he is best known for:
Receptor, G protein-coupled receptor, Transmembrane domain, Biochemistry and Protein structure are his primary areas of study.
In the field of Receptor, his study on Ectodomain overlaps with subjects such as Human chorionic gonadotropin.
His G protein-coupled receptor research is multidisciplinary, relying on both Biophysics, Computational biology and Bioinformatics.
In his work, Conformational isomerism, Hydrogen bond and Transmembrane protein is strongly intertwined with Helix, which is a subfield of Transmembrane domain.
In his study, which falls under the umbrella issue of Protein structure, Structural motif is strongly linked to Peptide sequence.
His Pharmacology research is multidisciplinary, incorporating elements of Opioid receptor, JDTic, Opioid and Serotonin.
His most cited work include:
- Crystal structure of the µ-opioid receptor bound to a morphinan antagonist (950 citations)
- Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor (392 citations)
- A molecular dissection of the glycoprotein hormone receptors. (288 citations)
What are the main themes of his work throughout his whole career to date?
His scientific interests lie mostly in G protein-coupled receptor, Receptor, Stereochemistry, Biochemistry and Transmembrane domain.
His G protein-coupled receptor research integrates issues from Biophysics, Computational biology, Allosteric regulation and G protein.
He combines subjects such as Pharmacology and Cell biology with his study of Receptor.
Leonardo Pardo has included themes like Antagonist and Heteromer in his Pharmacology study.
His Stereochemistry study integrates concerns from other disciplines, such as Transmembrane protein, Hydrogen bond, Binding site and Ligand.
The various areas that Leonardo Pardo examines in his Transmembrane domain study include Protein structure, Peptide sequence, Helix and Mutant.
He most often published in these fields:
- G protein-coupled receptor (40.62%)
- Receptor (40.00%)
- Stereochemistry (33.12%)
What were the highlights of his more recent work (between 2016-2021)?
- G protein-coupled receptor (40.62%)
- Receptor (40.00%)
- Cell biology (15.00%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in G protein-coupled receptor, Receptor, Cell biology, Allosteric regulation and Adenosine.
His G protein-coupled receptor study is concerned with Biochemistry in general.
Leonardo Pardo combines topics linked to Amino acid with his work on Receptor.
His work in the fields of Cell biology, such as Signal transduction, G protein and Protein kinase A, overlaps with other areas such as Oncogenic signaling.
His Allosteric regulation study deals with Ligand intersecting with Effector and Macromolecular Complexes.
In Mutagenesis, Leonardo Pardo works on issues like Alanine, which are connected to Stereochemistry.
Between 2016 and 2021, his most popular works were:
- Evidence for functional pre-coupled complexes of receptor heteromers and adenylyl cyclase. (59 citations)
- Cross-communication between Gi and Gs in a G-protein-coupled receptor heterotetramer guided by a receptor C-terminal domain. (35 citations)
- Essential Control of the Function of the Striatopallidal Neuron by Pre-coupled Complexes of Adenosine A2A-Dopamine D2 Receptor Heterotetramers and Adenylyl Cyclase (32 citations)
In his most recent research, the most cited papers focused on:
Leonardo Pardo mainly investigates Receptor, G protein-coupled receptor, Adenosine A2A receptor, Cell biology and Adenosine.
His studies in Receptor integrate themes in fields like Plasma protein binding and Pharmacology.
His Plasma protein binding study incorporates themes from Amino acid, Ligand, Bivalent, Transmembrane protein and Stereochemistry.
His G protein-coupled receptor research is included under the broader classification of Biochemistry.
His Cell biology research includes themes of Adenosine A1 receptor and Endocannabinoid system.
In his study, Heteromer is inextricably linked to Adenosine receptor, which falls within the broad field of Adenosine.
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