ReviewActa pharmacologica Sinica2016
Insights into the channel gating of P2X receptors from structures, dynamics and small molecules.
Review in Acta pharmacologica Sinica, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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Who cites it
29 citing papers in PubMed, 54 citations in OpenAlex.
- ATP-P2X3 Signaling as a Shared Neural Sensitization Pathway in Endometriosis and Irritable Bowel Syndrome: Mechanisms and Therapeutic Implications.Biomedicines · 2026Review
- Mitochondrial-endoplasmic reticulum interactions in lung diseases.Cell death & disease · 2026Review
- Structural basis for a central permeation pathway in the P2X1 receptor.Cell discovery · 2026Article
- Cell intrinsic versus cell extrinsic control of plasma cell longevity.Trends in immunology · 2026Review
- Damage-induced pyroptosis drives endogenous thymic regeneration by activating the purinergic receptor P2Y2.Cell death & disease · 2026Article
- Generalised Hodgkin-Huxley model captures human P2X and AMPA receptor currents.The Journal of physiology · 2026Article
- Endogenous forms of ATP-ATPProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The functional role of P2 purinergic receptors in the progression of gastric cancer.Purinergic signalling · 2025Review
- Implications of nociceptor receptors and immune modulation: emerging therapeutic targets for autoimmune diseases.Inflammopharmacology · 2025Review
- Progress on functions of intracellular domainZhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024Review
- Alcohol and e-cigarette damage alveolar-epithelial barrier by activation of P2X7r and provoke brain endothelial injury via extracellular vesicles.Cell communication and signaling : CCS · 2024Article
- Alcohol and e-cigarette damage alveolar-epithelial barrier by activation of P2X7r and provoke brain endothelial injury via extracellular vesicles.Research square · 2023Article
- Purinergic neurotransmission receptor P2X4 silencing alleviates intracerebral hemorrhage-induced neuroinflammation by blocking the NLRP1/Caspase-1 pathway.Scientific reports · 2023Article
- Modulation of P2X4 pore closure by magnesium, potassium, and ATP.Biophysical journal · 2022Article
- P2X3-selective mechanism of Gefapixant, a drug candidate for the treatment of refractory chronic cough.Computational and structural biotechnology journal · 2022Article
- How Structural Biology Has Directly Impacted Our Understanding of P2X Receptor Function and Gating.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- Pathophysiological Role of Purinergic P2X Receptors in Digestive System Diseases.Frontiers in physiology · 2021Review
- Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors.The Journal of biological chemistry · 2019Article
- P2X4 receptors, immunity, and sepsis.Current opinion in pharmacology · 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
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P2X receptors, as ATP-gated non-selective trimeric ion channels, are permeable to Na(+), K(+) and Ca(2+). Comparing with other ligand-gated ion channel families, P2X receptors are distinct in their unique gating properties and pathophysiological roles, and have attracted attention as promising drug targets for a variety of diseases, such as neuropathic pain, multiple sclerosis, rheumatoid arthritis and thrombus. Several small molecule inhibitors for distinct P2X subtypes have entered into clinical trials. However, many questions regarding the gating mechanism of P2X remain unsolved. The structural determinations of P2X receptors at the resting and ATP-bound open states revealed that P2X receptor gating is a cooperative allosteric process involving multiple domains, which marks the beginning of the post-structure era of P2X research at atomic level. Here, we review the current knowledge on the structure-function relationship of P2X receptors, depict the whole picture of allosteric changes during the channel gating, and summarize the active sites that may contribute to new strategies for developing novel allosteric drugs targeting P2X receptors.
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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.