ArticleStructure (London, England : 1993)2012
Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 89 citations in OpenAlex.
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Membrane Protein Folding and Biogenesis: Insights from Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Conformational Heterogeneity Underlying Divergent Signaling in Class A G Protein-Coupled Receptors.ACS pharmacology & translational science · 2025Review
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- L-DOPA and Droxidopa: From Force Field Development to Molecular Docking into Human βLife (Basel, Switzerland) · 2022Article
- A cholesterol analog stabilizes the human βScience signaling · 2022Article
- Biophysical Approaches for Applying and Measuring Biological Forces.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Review
- Analysis of L-DOPA and droxidopa binding to human βBiophysical journal · 2021Article
- βDrug testing and analysis · 2021Review
- Structural Insight into G Protein-Coupled Receptor Signaling Efficacy and Bias between Gs and β-Arrestin.ACS pharmacology & translational science · 2019Article
- Differentiating between Inactive and Active States of Rhodopsin by Atomic Force Microscopy in Native Membranes.Analytical chemistry · 2019Article
- Seeing and sensing single G protein-coupled receptors by atomic force microscopy.Current opinion in cell biology · 2019Review
- Recent advances in computational studies of GPCR-G protein interactions.Advances in protein chemistry and structural biology · 2019Review
- Insertion and folding pathways of single membrane proteins guided by translocases and insertases.Science advances · 2019Article
- Applications of Single-Molecule Methods to Membrane Protein Folding Studies.Journal of molecular biology · 2018Review
- Bioluminescence resonance energy transfer-based biosensors allow monitoring of ligand- and transducer-mediated GPCR conformational changes.Communications biology · 2018Article
- Evolutionary action and structural basis of the allosteric switch controlling βNature communications · 2017Article
- G Protein-Coupled Receptors Contain Two Conserved Packing Clusters.Biophysical journal · 2017Article
- Effect of material flexibility on the thermodynamics and kinetics of hydrophobically induced evaporation of water.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
- Commented on by
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
G protein-coupled receptors (GPCRs) are a class of versatile proteins that transduce signals across membranes. Extracellular stimuli induce inter- and intramolecular interactions that change the functional state of GPCRs and activate intracellular messenger molecules. How these interactions are established and how they modulate the functional state of GPCRs remain to be understood. We used dynamic single-molecule force spectroscopy to investigate how ligand binding modulates the energy landscape of the human β2 adrenergic receptor (β2 AR). Five different ligands representing either agonists, inverse agonists or neutral antagonists established a complex network of interactions that tuned the kinetic, energetic, and mechanical properties of functionally important structural regions of β2 AR. These interactions were specific to the efficacy profile of the ligands investigated and suggest that the functional modulation of GPCRs follows structurally well-defined interaction patterns.
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.