ArticleCell2019
Assembly of a GPCR-G Protein Complex.
Article in Cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 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
123 citing papers in PubMed.
- Atomic, structural and molecular insights into GPCR ligand binding and signalling.Nature reviews. Molecular cell biology · 2026Review
- Ligand-dependent G protein dynamics underlying opioid efficacy.Nature structural & molecular biology · 2026Article
- G protein diffusion states reveal receptor binding dynamics at single-molecule scale.Cell chemical biology · 2026Article
- G Protein-Mediated Allosteric Modulation of Ligand Binding in Class A GPCRs: Receptor-Ligand-Transducer Ensembles in Disease and Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Kinetic model of partial agonism reveals cellular basis of ligand efficacy.The Journal of biological chemistry · 2026Article
- G protein-coupled receptor SmGPCR9 interacts with neuropeptides and controls spermatogenesis in Schistosoma mansoni.PLoS pathogens · 2026Article
- Nano-GAngewandte Chemie (International ed. in English) · 2026Article
- Tool antibody fragments reveal multiple conformations of the rhodopsin-Gi signaling complex.Biophysical journal · 2026Article
- Conformational Dynamics of Amylin Receptors Revealed by Hydrogen-Deuterium Exchange Mass Spectrometry.Journal of the American Chemical Society · 2026Article
- Article
- ABEL-FRET bridges the timescale gap in single-molecule measurements of the structural dynamics in the ACommunications chemistry · 2026Article
- Article
- Functional and structural insights into interactions between β-Arrestin 1 and Gαs or Gαi1.Nature communications · 2026Article
- Article
- Conformational Heterogeneity Underlying Divergent Signaling in Class A G Protein-Coupled Receptors.ACS pharmacology & translational science · 2025Review
- Conformational Signatures of Preassembled and Active Complexes of 5-HTJournal of chemical information and modeling · 2025Article
- Deciphering molecular determinants of GPBAR1-Gs protein interactions by HDX-MS and cryo-EM.Scientific reports · 2025Article
- Molecular mechanism of β-arrestin 2 interaction with phosphorylated intracellular loop 3 of dopamine receptor D2.Communications biology · 2025Article
- A high-sensitivity stopped-flow EPR system to monitor millisecond conformational kinetics in spin-labeled proteins.Protein science : a publication of the Protein Society · 2025Article
- Cryo-EM reveals an extrahelical allosteric binding site at the MNature communications · 2025Article
63 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
16 authors.
Funding
Abstract
The activation of G proteins by G protein-coupled receptors (GPCRs) underlies the majority of transmembrane signaling by hormones and neurotransmitters. Recent structures of GPCR-G protein complexes obtained by crystallography and cryoelectron microscopy (cryo-EM) reveal similar interactions between GPCRs and the alpha subunit of different G protein isoforms. While some G protein subtype-specific differences are observed, there is no clear structural explanation for G protein subtype-selectivity. All of these complexes are stabilized in the nucleotide-free state, a condition that does not exist in living cells. In an effort to better understand the structural basis of coupling specificity, we used time-resolved structural mass spectrometry techniques to investigate GPCR-G protein complex formation and G-protein activation. Our results suggest that coupling specificity is determined by one or more transient intermediate states that serve as selectivity filters and precede the formation of the stable nucleotide-free GPCR-G protein complexes observed in crystal and cryo-EM structures.
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.