ArticleNature structural & molecular biology2018
Structural basis for signal recognition and transduction by platelet-activating-factor receptor.
Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.
- Platelet-activating factor receptor antagonists of natural origin for acute ischemic stroke: a systematic review of current evidence.Frontiers in pharmacology · 2022Pooled it
- Novel eugenol/limonene nanoplatform as a new remedy against bacterial lung infections.Scientific reports · 2026Article
- Adipose tissue-derived PRXL2A suppresses hepatic lipogenesis in a study with male mice.Nature communications · 2025Article
- Impact of targeting the platelet-activating factor and its receptor in cancer treatment.Military Medical Research · 2025Review
- PAFAH2 suppresses synchronized ferroptosis to ameliorate acute kidney injury.Nature chemical biology · 2024Article
- G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024Article
- Exploring GPCR conformational dynamics using single-molecule fluorescence.Methods (San Diego, Calif.) · 2024Review
- Non-IgE-Mediated Immediate Drug-Induced Hypersensitivity Reactions.The journal of allergy and clinical immunology. In practice · 2024Article
- Article
- Structural basis for ligand recognition and signaling of the lysophosphatidylserine receptors GPR34 and GPR174.PLoS biology · 2023Article
- Structural basis of hydroxycarboxylic acid receptor signaling mechanisms through ligand binding.Nature communications · 2023Article
- Insights into divalent cation regulation and GCell discovery · 2022Article
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- Structural identification of lysophosphatidylcholines as activating ligands for orphan receptor GPR119.Nature structural & molecular biology · 2022Article
- Structure Prediction, Evaluation, and Validation of GPR18 Lipid Receptor Using Free Programs.International journal of molecular sciences · 2022Article
- Structures of oxysterol sensor EBI2/GPR183, a key regulator of the immune response.Structure (London, England : 1993) · 2022Article
- Mapping the Binding Sites of UDP and Prostaglandin E2 Glyceryl Ester in the Nucleotide Receptor P2YChemMedChem · 2022Article
- Melanocortin-4 receptor complexity in energy homeostasis,obesity and drug development strategies.Diabetes, obesity & metabolism · 2022Review
- Universal platform for the generation of thermostabilized GPCRs that crystallize in LCP.Nature protocols · 2022Review
- In Silico, In Vitro, and In Vivo Analysis of Tanshinone IIA and Cryptotanshinone fromBiomolecules · 2022Article
Corrections and comments
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Authors and funding
22 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Platelet-activating-factor receptor (PAFR) responds to platelet-activating factor (PAF), a phospholipid mediator of cell-to-cell communication that exhibits diverse physiological effects. PAFR is considered an important drug target for treating asthma, inflammation and cardiovascular diseases. Here we report crystal structures of human PAFR in complex with the antagonist SR 27417 and the inverse agonist ABT-491 at 2.8-Å and 2.9-Å resolution, respectively. The structures, supported by molecular docking of PAF, provide insights into the signal-recognition mechanisms of PAFR. The PAFR-SR 27417 structure reveals an unusual conformation showing that the intracellular tips of helices II and IV shift outward by 13 Å and 4 Å, respectively, and helix VIII adopts an inward conformation. The PAFR structures, combined with single-molecule FRET and cell-based functional assays, suggest that the conformational change in the helical bundle is ligand dependent and plays a critical role in PAFR activation, thus greatly extending knowledge about signaling by G-protein-coupled receptors.
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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.