ReviewBritish journal of pharmacology2008
G-protein-coupled receptor phosphorylation: where, when and by whom.
Review in British journal of pharmacology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 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
105 citing papers in PubMed, 229 citations in OpenAlex.
- Steric control of signaling bias in the immunometabolic receptor GPR84.Nature communications · 2026Article
- Evaluating Force Matching as a Parametrization Strategy for the CHARMM36m Force Field Using Phosphorylation.The journal of physical chemistry. B · 2026Article
- Article
- Conformational dynamics of the active state of β-arrestin 1.bioRxiv : the preprint server for biology · 2025Article
- GHRH and the prostate.Reviews in endocrine & metabolic disorders · 2025Review
- Capillary Zone Electrophoresis-Mass Spectrometry of Intact G Protein-Coupled Receptors Enables Proteoform Profiling.Analytical chemistry · 2025Article
- Functional profiling of serine, threonine and tyrosine sites.Nature chemical biology · 2025Article
- How Ligands Achieve Biased Signaling toward Arrestins.Biochemistry · 2025Review
- Proteome-wide analysis reveals G protein-coupled receptor-like proteins in rice (Plant signaling & behavior · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lysophosphatidic Acid Receptor 3 (LPA3): Signaling and Phosphorylation Sites.International journal of molecular sciences · 2024Article
- LPAInternational journal of molecular sciences · 2024Article
- Control of G protein-coupled receptor function via membrane-interacting intrinsically disordered C-terminal domains.bioRxiv : the preprint server for biology · 2024Article
- Information Transmission in G Protein-Coupled Receptors.International journal of molecular sciences · 2024Review
- Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors.Science (New York, N.Y.) · 2024Article
- Structure, function and drug discovery of GPCR signaling.Molecular biomedicine · 2023Review
- Roles of the αInternational journal of molecular sciences · 2023Article
- Unraveling the Functional Significance of Unstructured Regions in G Protein-Coupled Receptors.Biomolecules · 2023Review
- Profiling of basal and ligand-dependent GPCR activities by means of a polyvalent cell-based high-throughput platform.Nature communications · 2023Article
- Structural snapshots uncover a key phosphorylation motif in GPCRs driving β-arrestin activation.Molecular cell · 2023Article
45 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
1 author at 1 institution in 1 country.
Funding
Abstract
Almost all G-protein coupled receptors (GPCRs) are regulated by phosphorylation and this process is a key event in determining the signalling properties of this receptor super-family. Receptors are multiply phosphorylated at sites that can occur throughout the intracellular regions of the receptor. This diversity of phospho-acceptor sites together with a lack of consensus phosphorylation sequences has led to the suggestion that the precise site of phosphorylation is not important in the phosphorylation-dependent regulation of GPCR function but rather it is the increase in bulk negative charge of the intracellular face of the receptor which is the significant factor. This review investigates the possibility that the multi-site nature of GPCR phosphorylation reflects the importance of specific phosphorylation events which mediate distinct signalling outcomes. In this way receptor phosphorylation may provide for a flexible regulatory mechanism that can be tailored in a tissue specific manner to regulate physiological processes. By understanding the flexible nature of GPCR phosphorylation if may be possible to develop agonists or allosteric modulators that promote a subset of phosphorylation events on the target GPCR and thereby restrict the action of the drug to a particular receptor mediated signalling response.
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.