ReviewMolecules (Basel, Switzerland)2017
The Formyl Peptide Receptors: Diversity of Ligands and Mechanism for Recognition.
Review in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.
What it found
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Who cites it
159 citing papers in PubMed, 270 citations in OpenAlex.
- The gut microbiome-bile acid-FXR interplay: a pivotal axis in metabolic and gastrointestinal diseases.Gut microbes · 2026Review
- Article
- The Transmembrane Envelope Protein of Porcine Endogenous Retroviruses Modulates Cytokine Release and Gene Expression in Human Immune Cells.International journal of molecular sciences · 2026Article
- TMAO Correlates with Transcriptomic Signatures of Leukocyte Activation and Systemic Inflammation Following Burn Injury.Journal of burn care & research : official publication of the American Burn Association · 2026Article
- Toward a Therapy for Autism Spectrum Disorder: The Formyl Peptide Receptor 2 Agonist MR-39 Supports Synaptic Health in the BTBR Mouse and Features a Favorable Safety Profile.ACS pharmacology & translational science · 2026Article
- Network Topology and Interactomic Analysis Reveal the Regulatory Framework of the Humanin Protein Family (MTRNR2Lx Class).Biomolecules · 2026Article
- Fully human antagonistic antibodies targeting FPR2 through dual extracellular-loop engagement for gastric cancer therapy.Antibody therapeutics · 2026Article
- Mechanisms and disease relevance of mitochondrial translation in humans.Nature reviews. Molecular cell biology · 2026Review
- Cell-based drug delivery for combating bacteria: focus on refractory infections.Journal of nanobiotechnology · 2026Review
- Agonist-specific FPR1 conformational change prevents receptor recycling and promotes targeted protein degradation.Acta pharmaceutica Sinica. B · 2026Article
- From data to discovery: The rise of information-theoretic predictive models in drug development.Scientific reports · 2026Article
- Clotting the Gap Between Mitochondria-Mediated Immunity and Mitochondrial Transfer.Circulation research · 2026Review
- Cross-Species Amyloid-like Features Shared by Mammalian andMicroorganisms · 2026Article
- Macrophages self-generate and refine chemotactic gradients during migration towards complement C5a.PLoS biology · 2026Article
- Parallel CRISPR screens reveal pathways controlling the cell surface levels of the attractant receptor FPR1.Communications biology · 2026Article
- Formyl peptide receptor 2 is a potential biomarker and therapeutic target for inflammatory bowel disease.Acta pharmacologica Sinica · 2026Article
- Bacterial vesicles from intratumoral L. salivarius enhance PD-1 blockade via FPR1-mediated macrophage polarization in gastric cancer.Cell reports. Medicine · 2026Article
- Crotoxin fromFrontiers in immunology · 2026Article
- Involvement of formyl peptide receptor 2 in canine coronavirus infection: in vitro and in Silico approaches.Virology journal · 2025Article
- Formyl peptide receptor 1 and its antagonist T0080 in atherosclerosis.Cell death and differentiation · 2025Article
99 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
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formyl peptide receptors (FPRs) are G protein-coupled receptors that transduce chemotactic signals in phagocytes and mediate host-defense as well as inflammatory responses including cell adhesion, directed migration, granule release and superoxide production. In recent years, the cellular distribution and biological functions of FPRs have expanded to include additional roles in homeostasis of organ functions and modulation of inflammation. In a prototype, FPRs recognize peptides containing N-formylated methionine such as those produced in bacteria and mitochondria, thereby serving as pattern recognition receptors. The repertoire of FPR ligands, however, has expanded rapidly to include not only N-formyl peptides from microbes but also non-formyl peptides of microbial and host origins, synthetic small molecules and an eicosanoid. How these chemically diverse ligands are recognized by the three human FPRs (FPR1, FPR2 and FPR3) and their murine equivalents is largely unclear. In the absence of crystal structures for the FPRs, site-directed mutagenesis, computer-aided ligand docking and structural simulation have led to the identification of amino acids within FPR1 and FPR2 that interact with several formyl peptides. This review article summarizes the progress made in the understanding of FPR ligand diversity as well as ligand recognition mechanisms used by these 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 Socratic graph.