ArticleNature communications2022
Structural basis of adhesion GPCR GPR110 activation by stalk peptide and G-proteins coupling.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Review
- Tethered agonist- and GAIN domain-independent signaling of an adhesion GPCR.Science advances · 2026Article
- aGPCR-HEK: A Stable High-Expression Inducible Mammalian Cell Expression System for Adhesion GPCR Structural Biology Applications.Bio-protocol · 2026Article
- Constitutive activity among orphan G protein-coupled receptors: Molecular mechanisms and pharmacological perspectives.Molecular pharmacology · 2026Review
- Re-evaluating Gα protein-response element specificity in GPCR signaling.Communications biology · 2026Article
- Hepatic GPR110 contributes to sex disparity in the development of MASH through oestrogen receptor α-dependent signalling.Nature metabolism · 2026Article
- Structure of the GNature communications · 2025Article
- Structural basis of protease-activated receptor 2 activation and biased agonism.Cell discovery · 2025Article
- Molecular mechanism of ligand recognition and activation of lysophosphatidic acid receptor LPAR6.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- G protein-coupled receptor-mediated renal fibrosis: a key focus on kidney disease drug development.Frontiers in pharmacology · 2025Review
- Structural basis of tethered agonism and G protein coupling of protease-activated receptors.Cell research · 2024Article
- Structural basis of Frizzled 4 in recognition of Dishevelled 2 unveils mechanism of WNT signaling activation.Nature communications · 2024Article
- Structural basis for the ligand recognition and G protein subtype selectivity of kisspeptin receptor.Science advances · 2024Article
- Structural basis of ligand recognition and design of antihistamines targeting histamine HNature communications · 2024Article
- Unveiling Mechanical Activation: GAIN Domain Unfolding and Dissociation in Adhesion GPCRs.Nano letters · 2023Article
- Article
- Stickier G-protein conformations.Nature chemical biology · 2023Article
- Tethered agonist activated ADGRF1 structure and signalling analysis reveal basis for G protein coupling.Nature communications · 2023Article
- Interaction between GPR110 (ADGRF1) and tight junction protein occludin implicated in blood-brain barrier permeability.iScience · 2023Article
- Structural basis of lysophosphatidylserine receptor GPR174 ligand recognition and activation.Nature communications · 2023Article
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Adhesion G protein-coupled receptors (aGPCRs) are keys of many physiological events and attractive targets for various diseases. aGPCRs are also known to be capable of self-activation via an autoproteolysis process that removes the inhibitory GAIN domain on the extracellular side of receptor and releases a stalk peptide to bind and activate the transmembrane side of receptor. However, the detailed mechanism of aGPCR activation remains elusive. Here, we report the cryo-electron microscopy structures of GPR110 (ADGRF1), a member of aGPCR, in complex with G
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