Evidence map›Paper›PMID 27757785›Full record

ArticlePurinergic signalling2017

2',3'-O-Substituted ATP derivatives as potent antagonists of purinergic P2X3 receptors and potential analgesic agents.

Diego Dal Ben, Anna Marchenkova, Ajiroghene Thomas, Catia Lambertucci, Andrea Spinaci, Gabriella Marucci, Andrea Nistri, Rosaria Volpini

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Purinergic signalling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 22% of its field
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

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. A shared mechanism for TNP-ATP recognition by members of the P2X receptor family.Computational and structural biotechnology journal · 2024
    Article
  2. Article
  3. Article
  4. Investigation on 2',3'-ACS medicinal chemistry letters · 2019
    Article
  5. Review
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

8 authors at 2 institutions in 1 country.

Diego Dal BenSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, via S. Agostino 1, 62032, Camerino, (MC), Italy.
Anna MarchenkovaNeuroscience Department, International School for Advanced Studies (SISSA), Via Bonomea 265, 34136, Trieste, Italy.
Ajiroghene ThomasSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, via S. Agostino 1, 62032, Camerino, (MC), Italy.
Catia LambertucciSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, via S. Agostino 1, 62032, Camerino, (MC), Italy.
Andrea SpinaciSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, via S. Agostino 1, 62032, Camerino, (MC), Italy.
Gabriella MarucciSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, via S. Agostino 1, 62032, Camerino, (MC), Italy.
Andrea NistriNeuroscience Department, International School for Advanced Studies (SISSA), Via Bonomea 265, 34136, Trieste, Italy.
Rosaria VolpiniSchool of Pharmacy, Medicinal Chemistry Unit, University of Camerino, via S. Agostino 1, 62032, Camerino, (MC), Italy. rosaria.volpini@unicam.it.ORCID 0000-0002-5304-5232
Università di Camerino · ITScuola Internazionale Superiore di Studi Avanzati · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Blocking membrane currents evoked by the activation of purinergic P2X3 receptors localized on nociceptive neurons represents a promising strategy for the development of agents useful for the treatment of chronic pain conditions. Among compounds endowed with such antagonistic action, 2',3'-O-(2,4,6-trinitrophenyl)-ATP (TNP-ATP) is an ATP analogue, whose inhibitory activity on P2X receptors has been previously reported. Based on the results of molecular modelling studies performed with homology models of the P2X3 receptor, novel adenosine nucleotide analogues bearing cycloalkyl or arylalkyl substituents replacing the trinitrophenyl moiety of TNP-ATP were designed and synthesized. These new compounds were functionally evaluated on native P2X3 receptors from mouse trigeminal ganglion (TG) sensory neurons using patch clamp recordings under voltage clamp configuration. Our data show that some of these molecules are potent (nanomolar range) and reversible inhibitors of P2X3 receptors, without any apparent effect on trigeminal GABA

Indexed as

Adenosine TriphosphateAnalgesicsAnimalsMiceModels, MolecularPatch-Clamp TechniquesPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X3Sensory Receptor CellsTrigeminal Ganglion2',3'-O-(2,4,6-trinitro-cyclohexadienylidine)adenosine 5'-triphosphateAdenosine TriphosphateAnalgesicsPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X3ATP derivativesMolecular modellingP2X3 receptor antagonistsPatch clampPurine derivativesPurinergic receptors

Identifiers

PMID27757785
PMCPMC5334199
OpenAlexW2533829256

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.