ReviewReviews in the neurosciences2011
Allosteric modulation of ATP-gated P2X receptor channels.
Review in Reviews in the neurosciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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
47 citing papers in PubMed, 78 citations in OpenAlex.
- Article
- Cell Type-Specific Expression of Purinergic P2X Receptors in the Hypothalamus.International journal of molecular sciences · 2025Review
- Preparation and preliminary evaluation of a tritium-labeled allosteric P2X4 receptor antagonist.Purinergic signalling · 2024Article
- Copper Increases the Cooperative Gating of Rat P2X2a Receptor Channels.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Cryo-EM structures of the human P2X1 receptor reveal subtype-specific architecture and antagonism by supramolecular ligand-binding.Nature communications · 2024Article
- Ivermectin increases striatal cholinergic activity to facilitate dopamine terminal function.Cell & bioscience · 2024Article
- Chronic cough relief by allosteric modulation of P2X3 without taste disturbance.Nature communications · 2023Article
- The Impact of Plasma Membrane Ion Channels on Bone Remodeling in Response to Mechanical Stress, Oxidative Imbalance, and Acidosis.Antioxidants (Basel, Switzerland) · 2023Review
- Article
- A novel definition and treatment of hyperinflammation in COVID-19 based on purinergic signalling.Purinergic signalling · 2022Review
- Agonists, Antagonists, and Modulators of P2X7 Receptors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Molecular Pharmacology of P2X Receptors: Exploring Druggable Domains Revealed by Structural Biology.Frontiers in pharmacology · 2022Review
- P2X3-selective mechanism of Gefapixant, a drug candidate for the treatment of refractory chronic cough.Computational and structural biotechnology journal · 2022Article
- Article
- Update of P2X receptor properties and their pharmacology: IUPHAR Review 30.British journal of pharmacology · 2021Review
- Targeting Neuroinflammation via Purinergic P2 Receptors for Disease Modification in Drug-Refractory Epilepsy.Journal of inflammation research · 2021Review
- Structural and Functional Basis for Understanding the Biological Significance of P2X7 Receptor.International journal of molecular sciences · 2020Review
- Resolving the Ionotropic P2X4 Receptor Mystery Points Towards a New Therapeutic Target for Cardiovascular Diseases.International journal of molecular sciences · 2020Review
- Article
- Evolution of acid nociception: ion channels and receptors for detecting acid.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Seven mammalian purinergic receptor subunits, denoted P2X1-P2X7, and several spliced forms of these subunits have been cloned. When heterologously expressed, these cDNAs encode ATP-gated non-selective cation channels organized as trimers. All activated receptors produce cell depolarization and promote Ca(2+) influx through their pores and indirectly by activating voltage-gated calcium channels. However, the biophysical and pharmacological properties of these receptors differ considerably, and the majority of these subunits are also capable of forming heterotrimers with other members of the P2X receptor family, which confers further different properties. These channels have three ATP binding domains, presumably located between neighboring subunits, and occupancy of at least two binding sites is needed for their activation. In addition to the orthosteric binding sites for ATP, these receptors have additional allosteric sites that modulate the agonist action at receptors, including sites for trace metals, protons, neurosteroids, reactive oxygen species and phosphoinositides. The allosteric regulation of P2X receptors is frequently receptor-specific and could be a useful tool to identify P2X members in native tissues and their roles in signaling. The focus of this review is on common and receptor-specific allosteric modulation of P2X receptors and the molecular base accounting for allosteric binding sites.
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.