ArticleNature communications2018
Dynamic tuneable G protein-coupled receptor monomer-dimer populations.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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
54 citing papers in PubMed, 126 citations in OpenAlex.
- μ-Opioid receptors negatively regulate striatal dopamine DResearch square · 2026Article
- Improved Method for Predicting GPCR-GPCR Interaction Pairs.Proteins · 2026Article
- An Improved Cysteine-Based Labeling Strategy for GPCR Structural Dynamics Studies.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Mechanistic and therapeutic insights into class A GPCR dimers in neuropsychiatric disorders.npj drug discovery · 2026Review
- A neurotensin receptor type 1-derived pepducin acts as a biased allosteric modulator to regulate target receptor function.Acta pharmaceutica Sinica. B · 2026Article
- Differential conservation analysis identifies residues defining constitutive internalization in beta-adrenergic receptors.iScience · 2026Article
- Allosteric activation of the glutamate receptor mGlu2 by the serotonin receptor 5-HTNature communications · 2026Article
- The molecular basis of μ-opioid receptor signaling plasticity.Cell research · 2025Article
- Single-molecule methods for characterizing receptor dimers reveal metastable opioid receptor homodimers that induce functional modulation.Nature communications · 2025Article
- Single-molecule characterization of opioid receptor heterodimers reveals soluble µ-δ dimer blocker peptide alleviates morphine tolerance.Nature communications · 2025Article
- Structural basis for ligand promiscuity and high signaling activity of Kaposi's Sarcoma-associated Herpesvirus-encoded GPCR.Nature communications · 2025Article
- Dimerization propensity of the βProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The Conformational Equilibria of a Human GPCR Compared between Lipid Vesicles and Aqueous Solutions by IntegrativeJournal of the American Chemical Society · 2025Article
- Single-molecule localization microscopy as a tool to quantify di/oligomerization of receptor tyrosine kinases and G protein-coupled receptors.Molecular pharmacology · 2025Review
- Higher-order transient membrane protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024Review
- Real-Time Determination of Intracellular cAMP Reveals Functional Coupling of GInternational journal of molecular sciences · 2024Article
- Structural basis of dimerization of chemokine receptors CCR5 and CXCR4.Nature communications · 2023Article
- Advances in the allostery of angiotensin II type 1 receptor.Cell & bioscience · 2023Review
- Sub-millisecond conformational dynamics of the ACommunications biology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-coupled receptors (GPCRs) are the largest class of membrane receptors, playing a key role in the regulation of processes as varied as neurotransmission and immune response. Evidence for GPCR oligomerisation has been accumulating that challenges the idea that GPCRs function solely as monomeric receptors; however, GPCR oligomerisation remains controversial primarily due to the difficulties in comparing evidence from very different types of structural and dynamic data. Using a combination of single-molecule and ensemble FRET, double electron-electron resonance spectroscopy, and simulations, we show that dimerisation of the GPCR neurotensin receptor 1 is regulated by receptor density and is dynamically tuneable over the physiological range. We propose a "rolling dimer" interface model in which multiple dimer conformations co-exist and interconvert. These findings unite previous seemingly conflicting observations, provide a compelling mechanism for regulating receptor signalling, and act as a guide for future physiological studies.
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.