Evidence map›Paper›PMID 39539264›Full record

ArticleACS pharmacology & translational science2024

Turn-Adopting Peptidomimetic as a Formyl Peptide Receptor-1 Antagonist.

Maria De Fenza, Filippo Locri, Flavia Plastino, Marco Chino, Ornella Maglio, Linda Leone, Giorgia Gazzaroli, Mirella Belleri, Arianna Giacomini, Anders Kvanta and 3 more

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Article in ACS pharmacology & translational science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Maria De FenzaDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126 Naples, Italy.ORCID https://orcid.org/0000-0002-2856-5615
Filippo LocriDepartment of Clinical Neuroscience, Division of Eye and Vision, St. Erik Eye Hospital, Karolinska Institutet, 17177 Stockholm, Sweden.
Flavia PlastinoDepartment of Clinical Neuroscience, Division of Eye and Vision, St. Erik Eye Hospital, Karolinska Institutet, 17177 Stockholm, Sweden.
Marco ChinoDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126 Naples, Italy.ORCID https://orcid.org/0000-0002-0436-3293
Ornella MaglioDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126 Naples, Italy.
Linda LeoneDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126 Naples, Italy.ORCID https://orcid.org/0000-0001-7293-1814
Giorgia GazzaroliUnit of Experimental Oncology and Immunology, Department of Molecular and Translational Medicine, University of Brescia, 25123 Brescia, Italy.
Mirella BelleriUnit of Experimental Oncology and Immunology, Department of Molecular and Translational Medicine, University of Brescia, 25123 Brescia, Italy.
Arianna GiacominiUnit of Experimental Oncology and Immunology, Department of Molecular and Translational Medicine, University of Brescia, 25123 Brescia, Italy.
Anders KvantaDepartment of Clinical Neuroscience, Division of Eye and Vision, St. Erik Eye Hospital, Karolinska Institutet, 17177 Stockholm, Sweden.
Helder AndréDepartment of Clinical Neuroscience, Division of Eye and Vision, St. Erik Eye Hospital, Karolinska Institutet, 17177 Stockholm, Sweden.
Vincenzo PavoneDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126 Naples, Italy.
Daniele D'AlonzoDepartment of Chemical Sciences, University of Naples Federico II, Via Cintia 21, 80126 Naples, Italy.ORCID https://orcid.org/0000-0002-2857-8600

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The design, synthesis, and characterization of a new peptidomimetic acting as a formyl peptide receptor (FPR1) antagonist (N-19004) are herein reported. The molecule has been identified with docking studies of the highly potent FPR1 antagonist UPARANT on human receptor. N-19004 recapitulates all pharmacophoric groups necessary for recognition into a minimal structure, with a crucial role of the 2,6-diamino-thiophenyl scaffold mimicking the positions of Cα atoms of Arg residues in the turned Arg-Aib-Arg segment of UPARANT. N-19004 demonstrated to interfere with the biological properties of FPR1 both

Identifiers

PMID39539264
PMCPMC11555506

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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.