ArticleNature communications2022
Structural basis for recognition of N-formyl peptides as pathogen-associated molecular patterns.
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 32 papers.
What it found
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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.
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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
32 citing papers in PubMed, 55 citations in OpenAlex.
- DAMP signaling networks: from receptors to diverse pathophysiological functions.Journal of advanced research · 2026Review
- Agonist-specific FPR1 conformational change prevents receptor recycling and promotes targeted protein degradation.Acta pharmaceutica Sinica. B · 2026Article
- CH25H-mediated cholesterol metabolism drives chondrogenic differentiation in adipose-derived stem cells and enhances cartilage repair.Communications biology · 2026Article
- N-formyl methionine peptide-driven neutrophil activation in idiopathic inflammatory myopathies.Rheumatology (Oxford, England) · 2026Article
- Investigation into ligand selectivity and bias at the formyl peptide receptor family.The Journal of pharmacology and experimental therapeutics · 2026Article
- Systemic neutrophil activation and N-formyl methionine-formyl peptide receptor-1 signaling define inflammatory endotypes in rheumatoid arthritis-associated lung involvement.Journal of internal medicine · 2025Article
- Formyl peptide receptor 1 and its antagonist T0080 in atherosclerosis.Cell death and differentiation · 2025Article
- Supramolecular assembly of novel achatin structurally similar peptide as potential G protein-coupled receptors anticancer ligands: focus on its pseudo-macrocycle nature.Royal Society open science · 2025Article
- Monoclonal Antibody 5F1 Modulates Formyl Peptide Receptor 1 Conformation for Transmembrane Signaling.FASEB bioAdvances · 2025Article
- Fragments of viral surface proteins modulate innate immune responses via formyl peptide receptors.iScience · 2025Article
- Bioactive Compounds as Modulators of N-Formyl Peptide Signaling in Chronic Diseases.Molecules (Basel, Switzerland) · 2025Review
- Chemosensory Receptors in Vertebrates: Structure and Computational Modeling Insights.International journal of molecular sciences · 2025Review
- Gene Regulation of Neutrophils Mediated Liver and Lung Injury through NETosis in Acute Pancreatitis.Inflammation · 2025Article
- P-Rex1 controls phagocytosis and the killing of bacteria by murine neutrophils independently of its catalytic activity.Frontiers in immunology · 2025Article
- A Novel Compound Ligusticum Cycloprolactam Alleviates Neuroinflammation After Ischemic Stroke via the FPR1/NLRP3 Signaling Axis.CNS neuroscience & therapeutics · 2024Article
- Turn-Adopting Peptidomimetic as a Formyl Peptide Receptor-1 Antagonist.ACS pharmacology & translational science · 2024Article
- Structure of G protein-coupled receptor GPR1 bound to full-length chemerin adipokine reveals a chemokine-like reverse binding mode.PLoS biology · 2024Article
- Reprogramming the myocardial infarction microenvironment with melanin-based composite nanomedicines in mice.Nature communications · 2024Article
- Sensory neurons: An integrated component of innate immunity.Immunity · 2024Review
- Article
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formyl peptide receptor 1 (FPR1) is primarily responsible for detection of short peptides bearing N-formylated methionine (fMet) that are characteristic of protein synthesis in bacteria and mitochondria. As a result, FPR1 is critical to phagocyte migration and activation in bacterial infection, tissue injury and inflammation. How FPR1 distinguishes between formyl peptides and non-formyl peptides remains elusive. Here we report cryo-EM structures of human FPR1-Gi protein complex bound to S. aureus-derived peptide fMet-Ile-Phe-Leu (fMIFL) and E. coli-derived peptide fMet-Leu-Phe (fMLF). Both structures of FPR1 adopt an active conformation and exhibit a binding pocket containing the R201
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What Socratic 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 Socratic graph.