ReviewFrontiers in cellular neuroscience2013
Exploring the ATP-binding site of P2X receptors.
Review in Frontiers in cellular neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 59 citations in OpenAlex.
- ATP and glutamate coordinate contractions in the freshwater sponge Ephydatia muelleri.The Journal of experimental biology · 2025Article
- Structural insights into the human P2X1 receptor and ligand interactions.Nature communications · 2024Article
- A current review on P2X7 receptor antagonist patents in the treatment of neuroinflammatory disorders: a patent review on antagonists.Naunyn-Schmiedeberg's archives of pharmacology · 2024Review
- Comparative Atomistic Insights on Apo and ATP-I1171N/S/T in Nonsmall-Cell Lung Cancer.ACS omega · 2023Article
- The P2X1 receptor as a therapeutic target.Purinergic signalling · 2022Review
- P2X2 receptor subunit interfaces are missense variant hotspots, where mutations tend to increase apparent ATP affinity.British journal of pharmacology · 2022Article
- Enlightening activation gating in P2X receptors.Purinergic signalling · 2022Review
- Modulation of P2X4 pore closure by magnesium, potassium, and ATP.Biophysical journal · 2022Article
- Molecular Pharmacology of P2X Receptors: Exploring Druggable Domains Revealed by Structural Biology.Frontiers in pharmacology · 2022Review
- Identification of a novel P2X7 antagonist using structure-based virtual screening.Frontiers in pharmacology · 2022Article
- Pharmacological and genetic characterisation of the canine P2X4 receptor.British journal of pharmacology · 2020Article
- Drosophila taste neurons as an agonist-screening platform for P2X receptors.Scientific reports · 2020Article
- Full-Length P2XCell · 2019Article
- Molecular determinants for agonist recognition and discrimination in P2X2 receptors.The Journal of general physiology · 2019Article
- Mapping the Allosteric Action of Antagonists A740003 and A438079 Reveals a Role for the Left Flipper in Ligand Sensitivity at P2X7 Receptors.Molecular pharmacology · 2018Article
- The Molecular Determinants of Small-Molecule Ligand Binding at P2X Receptors.Frontiers in pharmacology · 2018Article
- New Insights Into Permeation of Large Cations Through ATP-Gated P2X Receptors.Frontiers in molecular neuroscience · 2018Article
- Intersubunit physical couplings fostered by the left flipper domain facilitate channel opening of P2X4 receptors.The Journal of biological chemistry · 2017Article
- Regulation of Pannexin 1 Surface Expression by Extracellular ATP: Potential Implications for Nervous System Function in Health and Disease.Frontiers in cellular neuroscience · 2017Article
- P2X2 Dominant Deafness Mutations Have No Negative Effect on Wild-Type Isoform: Implications for Functional Rescue and in Deafness Mechanism.Frontiers in molecular neuroscience · 2017Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P2X receptors are ATP-gated non-selective cation channels involved in many different physiological processes, such as synaptic transmission, inflammation, and neuropathic pain. They form homo- or heterotrimeric complexes and contain three ATP-binding sites in their extracellular domain. The recent determination of X-ray structures of a P2X receptor solved in two states, a resting closed state and an ATP-bound, open-channel state, has provided unprecedented information not only regarding the three-dimensional shape of the receptor, but also on putative conformational changes that couple ATP binding to channel opening. These data provide a structural template for interpreting the huge amount of functional, mutagenesis, and biochemical data collected during more than fifteen years. In particular, the interfacial location of the ATP binding site and ATP orientation have been successfully confirmed by these structural studies. It appears that ATP binds to inter-subunit cavities shaped like open jaws, whose tightening induces the opening of the ion channel. These structural data thus represent a firm basis for understanding the activation mechanism of P2X receptors.
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.