ArticleMolecular pharmacology2018
Identifying Functional Hotspot Residues for Biased Ligand Design in G-Protein-Coupled Receptors.
Article in Molecular pharmacology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 57 citations in OpenAlex.
- Mechanistic insight into signal bias by the agonist-dependent conformational dynamics of GPR84.Nature communications · 2026Article
- Multiple intramolecular triggers converge to preferential G protein coupling in the CBNature communications · 2025Article
- Ligand-Induced Biased Activation of GPCRs: Recent Advances and New Directions from In Silico Approaches.Molecules (Basel, Switzerland) · 2025Review
- Agonist-selective activation of individual G-proteins by muscarinic receptors.Scientific reports · 2024Article
- Structure-guided engineering of biased-agonism in the human niacin receptor via single amino acid substitution.Nature communications · 2024Article
- Exploring TAS2R46 biomechanics through molecular dynamics and network analysis.Frontiers in molecular biosciences · 2024Article
- Quinazoline sulfonamide derivatives targeting MicroRNA-34a/MDM4/p53 apoptotic axis with radiosensitizing activity.Future medicinal chemistry · 2024Article
- Unraveling allostery within the angiotensin II type 1 receptor for GαScience signaling · 2023Article
- Computational design of dynamic receptor-peptide signaling complexes applied to chemotaxis.Nature communications · 2023Article
- Catalytic site mutations confer multiple states of G protein activation.Science signaling · 2023Article
- Ghrelin receptor signaling in health and disease: a biased view.Trends in endocrinology and metabolism: TEM · 2023Review
- Biased agonists differentially modulate the receptor conformation ensembles in Angiotensin II type 1 receptor.Journal of molecular graphics & modelling · 2023Article
- In Silico Study of Allosteric Communication Networks in GPCR Signaling Bias.International journal of molecular sciences · 2022Review
- Article
- Phenylalanine 193 in Extracellular Loop 2 of theMolecular pharmacology · 2022Article
- Deep learning approaches for conformational flexibility and switching properties in protein design.Frontiers in molecular biosciences · 2022Review
- Predicted Mode of Binding to and Allosteric Modulation of the μ-Opioid Receptor by Kratom's Alkaloids with Reported AntinociceptionBiochemistry · 2021Article
- Allosteric communication regulates ligand-specific GPCR activity.The FEBS journal · 2021Review
- Atomic-Level Characterization of the Methadone-Stabilized Active Conformation ofMolecular pharmacology · 2020Article
- How Do Molecular Dynamics Data Complement Static Structural Data of GPCRs.International journal of molecular sciences · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
G-protein-coupled receptors (GPCRs) mediate multiple signaling pathways in the cell, depending on the agonist that activates the receptor and multiple cellular factors. Agonists that show higher potency to specific signaling pathways over others are known as "biased agonists" and have been shown to have better therapeutic index. Although biased agonists are desirable, their design poses several challenges to date. The number of assays to identify biased agonists seems expensive and tedious. Therefore, computational methods that can reliably calculate the possible bias of various ligands ahead of experiments and provide guidance, will be both cost and time effective. In this work, using the mechanism of allosteric communication from the extracellular region to the intracellular transducer protein coupling region in GPCRs, we have developed a computational method to calculate ligand bias ahead of experiments. We have validated the method for several
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.