Evidence map›Paper›PMID 21737531›Full record

ReviewPharmacological reviews2011

Activation and regulation of purinergic P2X receptor channels.

Claudio Coddou, Zonghe Yan, Tomas Obsil, J Pablo Huidobro-Toro, Stanko S Stojilkovic

Open access · bronzeAbstract readReview
In one paragraph

Review in Pharmacological reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 273 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
273citing papers in PubMed, 1 pooled it
32.3field-weighted citation impact, top 1% 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

273 citing papers in PubMed, 1 synthesis or guideline pooled it, 487 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. The pathogenesis of liver fibrosis in Wilson's disease: hepatocyte injury and regulation mediated by copper metabolism dysregulation.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Subtype-specific structural features of the hearing loss-associated human P2X2 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Purinergic Receptor P2Y2 Activity Prevents DNA Damage in CClJournal of cellular biochemistry · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Purinergic system in cancer stem cells.Purinergic signalling · 2025
    Review
  18. Article
  19. A shared mechanism for TNP-ATP recognition by members of the P2X receptor family.Computational and structural biotechnology journal · 2024
    Article
  20. Article

213 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 3 countries.

Claudio CoddouSection on Cellular Signaling, Program in Developmental Neuroscience, National Institute of Child Health and Human Developmant, National Institutes of Health, Bethesda, MD 20892-4510, USA.
Zonghe Yan
Tomas Obsil
J Pablo Huidobro-Toro
Stanko S Stojilkovic
Charles University · CZEunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · US

Funding

Intracellular Signaling In Endocrine CellsZIAHD000195 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI STOJILKOVIC, STANKO S. · 2009 to 2025
$18.8M
Intramural NIH HHS
6 · The paper itself

Abstract

Mammalian ATP-gated nonselective cation channels (P2XRs) can be composed of seven possible subunits, denoted P2X1 to P2X7. Each subunit contains a large ectodomain, two transmembrane domains, and intracellular N and C termini. Functional P2XRs are organized as homomeric and heteromeric trimers. This review focuses on the binding sites involved in the activation (orthosteric) and regulation (allosteric) of P2XRs. The ectodomains contain three ATP binding sites, presumably located between neighboring subunits and formed by highly conserved residues. The detection and coordination of three ATP phosphate residues by positively charged amino acids are likely to play a dominant role in determining agonist potency, whereas an AsnPheArg motif may contribute to binding by coordinating the adenine ring. Nonconserved ectodomain histidines provide the binding sites for trace metals, divalent cations, and protons. The transmembrane domains account not only for the formation of the channel pore but also for the binding of ivermectin (a specific P2X4R allosteric regulator) and alcohols. The N- and C- domains provide the structures that determine the kinetics of receptor desensitization and/or pore dilation and are critical for the regulation of receptor functions by intracellular messengers, kinases, reactive oxygen species and mercury. The recent publication of the crystal structure of the zebrafish P2X4.1R in a closed state provides a major advance in the understanding of this family of receptor channels. We will discuss data obtained from numerous site-directed mutagenesis experiments accumulated during the last 15 years with reference to the crystal structure, allowing a structural interpretation of the molecular basis of orthosteric and allosteric ligand actions.

Indexed as

AnimalsBinding SitesHumansMetalsNerve Tissue ProteinsProtein ConformationProtein IsoformsPurinergic P2X Receptor AgonistsPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2XMetalsNerve Tissue ProteinsProtein IsoformsPurinergic P2X Receptor AgonistsPurinergic P2X Receptor AntagonistsReceptors, Purinergic P2X

Identifiers

PMID21737531
PMCPMC3141880
OpenAlexW2095795382

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.