ArticleThe Journal of biological chemistry2010
The annexin I sequence gln(9)-ala(10)-trp(11)-phe(12) is a core structure for interaction with the formyl peptide receptor 1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 37 citations in OpenAlex.
- Annexin-A1 tripeptide enhances functional recovery and mitigates brain damage in traumatic brain injury by inhibiting neuroinflammation and preventing ANXA1 nuclear translocation in mice.Metabolic brain disease · 2024Article
- Effects of Formyl Peptide Receptor Agonists AcCells · 2022Article
- Annexin-A1 Tripeptide Attenuates Surgery-Induced Neuroinflammation and Memory Deficits Through Regulation the NLRP3 Inflammasome.Frontiers in immunology · 2022Article
- 4-Aroyl-3-hydroxy-5-phenyl-1H-pyrrol-2(5H)-ones as N-formyl peptide receptor 1 (FPR1) antagonists.Biochemical pharmacology · 2017Article
- The Formyl Peptide Receptors: Diversity of Ligands and Mechanism for Recognition.Molecules (Basel, Switzerland) · 2017Review
- Neuroprotective Effects of Annexin A1 Tripeptide after Deep Hypothermic Circulatory Arrest in Rats.Frontiers in immunology · 2017Article
- 2-Arylacetamido-4-phenylamino-5-substituted pyridazinones as formyl peptide receptors agonists.Bioorganic & medicinal chemistry · 2016Article
- Formylated MHC Class Ib Binding Peptides Activate Both Human and Mouse Neutrophils Primarily through Formyl Peptide Receptor 1.PloS one · 2016Article
- Antagonism of human formyl peptide receptor 1 (FPR1) by chromones and related isoflavones.Biochemical pharmacology · 2014Article
- Development of small molecule non-peptide formyl peptide receptor (FPR) ligands and molecular modeling of their recognition.Current medicinal chemistry · 2014Review
- Further studies on 2-arylacetamide pyridazin-3(2H)-ones: design, synthesis and evaluation of 4,6-disubstituted analogs as formyl peptide receptors (FPRs) agonists.European journal of medicinal chemistry · 2013Article
- Distinct signaling cascades elicited by different formyl peptide receptor 2 (FPR2) agonists.International journal of molecular sciences · 2013Review
- Molecular docking of 2-(benzimidazol-2-ylthio)-N-phenylacetamide-derived small-molecule agonists of human formyl peptide receptor 1.Journal of molecular modeling · 2012Article
- Receptor-dependent and -independent immunomodulatory effects of phenol-soluble modulin peptides from Staphylococcus aureus on human neutrophils are abrogated through peptide inactivation by reactive oxygen species.Infection and immunity · 2012Article
- The role of water in activation mechanism of human N-formyl peptide receptor 1 (FPR1) based on molecular dynamics simulations.PloS one · 2012Article
- Gastrin-releasing peptide/neuromedin B receptor antagonists PD176252, PD168368, and related analogs are potent agonists of human formyl-peptide receptors.Molecular pharmacology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal part of the calcium-regulated and phospholipid-binding protein annexin AI contains peptide sequences with pro- and anti-inflammatory activities. We have earlier shown that a proinflammatory signal triggered by one of these peptides, Gln(9)-Lys(25), is mediated by FPR1, a member of the formyl peptide receptor family expressed in human neutrophils. To determine the core structure in Gln(9)-Lys(25), smaller peptides were generated, and their capacity to activate neutrophils was determined. A peptide spanning from amino acid Glu(14) to Lys(25) was inactive, whereas the activity was retained in the Gln(9)-Tyr(20) peptide. Removal of amino acids from the C and N terminus of Gln(9)-Tyr(20) revealed that the first amino acid (Gln(9)) was of the utmost importance for activity. The core structure that activated the neutrophil NADPH oxidase to release superoxide anions was Gln(9)-Ala(10)-Trp(11)-Phe(12). This peptide also inhibited the activity induced by N-formyl-Met-Leu-Phe and WKYMVM. A structural model of the peptide agonist-FPR1 complex suggests that the transmembrane part of the binding pocket of the receptor binds optimally to a tetrapeptide. According to the model and the results presented, the N-terminal amino acid glutamine in Gln(9)-Phe(12) is located close to the bottom of the binding cleft, leaving for steric reasons insufficient space to extend the peptide at the N terminus. The addition of amino acids at the C terminus will not affect binding. The model presented may be helpful in developing specific FPR1 ligands.
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.