ArticleStructure (London, England : 1993)2013
The role of a sodium ion binding site in the allosteric modulation of the A(2A) adenosine G protein-coupled receptor.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 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
74 citing papers in PubMed, 139 citations in OpenAlex.
- Protein Frustration Reveals Orthosteric and Allosteric Active Sites in GPCR:G Protein Complexes.Journal of chemical information and modeling · 2026Article
- The role of the tryptophan-rich allosteric network and sodium egress in GPCR activation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Binding pose depth modulates photoswitchable ligands' efficacy at the 5-HTCommunications chemistry · 2026Article
- Structural basis for ligand promiscuity and high signaling activity of Kaposi's Sarcoma-associated Herpesvirus-encoded GPCR.Nature communications · 2025Article
- Adiabatic-Bias Molecular Dynamics Simulations Reveal the Impact of Mutations on Muscarinic Antagonist Unbinding Kinetics.Journal of chemical information and modeling · 2025Article
- Molecular architecture of human LYCHOS involved in lysosomal cholesterol signaling.Nature structural & molecular biology · 2025Article
- Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery.Nature reviews. Drug discovery · 2025Review
- Single-Molecule Insights into GPCR Conformational Landscapes.The Journal of membrane biology · 2025Review
- Structure-guided design of partial agonists at an opioid receptor.Nature communications · 2025Article
- Ligand binding kinetics to evaluate the function and stability of ABiophysical journal · 2025Article
- Monitoring GPCR conformation with GFP-inspired dyes.iScience · 2024Article
- Structure-Guided Design of Partial Agonists at an Opioid Receptor.Research square · 2024Article
- Single-molecule visualization of human ACommunications biology · 2023Article
- An inverse agonist of orphan receptor GPR61 acts by a G protein-competitive allosteric mechanism.Nature communications · 2023Article
- The World of GPCR dimers - Mapping dopamine receptor DComputational and structural biotechnology journal · 2023Article
- Article
- Cancer-Associated Mutations of the Adenosine AMolecules (Basel, Switzerland) · 2022Article
- Activation and allosteric regulation of the orphan GPR88-Gi1 signaling complex.Nature communications · 2022Article
- Slow conformational dynamics of the human AStructure (London, England : 1993) · 2022Article
- Unique features of different classes of G-protein-coupled receptors revealed from sequence coevolutionary and structural analysis.Proteins · 2022Article
14 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
Abstract
The function of G protein-coupled receptors (GPCRs) can be modulated by a number of endogenous allosteric molecules. In this study, we used molecular dynamics, radioligand binding, and thermostability experiments to elucidate the role of the recently discovered sodium ion binding site in the allosteric modulation of the human A(2A) adenosine receptor, conserved among class A GPCRs. While the binding of antagonists and sodium ions to the receptor was noncompetitive in nature, the binding of agonists and sodium ions appears to require mutually exclusive conformational states of the receptor. Amiloride analogs can also bind to the sodium binding pocket, showing distinct patterns of agonist and antagonist modulation. These findings suggest that physiological concentrations of sodium ions affect functionally relevant conformational states of GPCRs and can help to design novel synthetic allosteric modulators or bitopic ligands exploiting the sodium ion binding pocket.
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.