The DOI matches its Crossref record; 140 of the 140 references it cites were found in a registry or an index.
Update of P2X receptor properties and their pharmacology: IUPHAR Review 30
Open accessAbstract
The known seven mammalian receptor subunits (P2X1–7) form cationic channels gated by ATP. Three subunits compose a receptor channel. Each subunit is a polypeptide consisting of two transmembrane regions (TM1 and TM2), intracellular N‐ and C‐termini, and a bulky extracellular loop. Crystallization allowed the identification of the 3D structure and gating cycle of P2X receptors. The agonist‐binding pocket is located at the intersection of two neighbouring subunits. In addition to the mammalian P2X receptors, their primitive ligand‐gated counterparts with little structural similarity have also been cloned. Selective agonists for P2X receptor subtypes are not available, but medicinal chemistry supplied a range of subtype‐selective antagonists, as well as positive and negative allosteric modulators. Knockout mice and selective antagonists helped to identify pathological functions due to defective P2X receptors, such as male infertility (P2X1), hearing loss (P2X2), pain/cough (P2X3), neuropathic pain (P2X4), inflammatory bone loss (P2X5), and faulty immune reactions (P2X7).
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Cites
Molecular Physiology of P2X Receptors
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Self-citationThe P2X7 Receptor in Infection and Inflammation
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Altered Cytokine Production in Mice Lacking P2X7Receptors
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Cited by
Structural insights into the human P2X1 receptor and ligand interactions
Bennetts, F. M., Venugopal, H., Glukhova, A., Mobbs, J. I., Ventura, S., & Thal, D. M. (2024) · Nature Communications · doi:10.1038/s41467-024-52776-7 · Cited by 14
Structural insights into the orthosteric inhibition of P2X receptors by non-ATP analog antagonists
(2023) · doi:10.7554/elife.92829 · Cited by 14
Structural insights into the orthosteric inhibition of P2X receptors by non-ATP-analog antagonists
Sheng, D., Yue, C., Jin, F., Wang, Y., Ichikawa, M., Yu, Y., Guo, C.-R., & Hattori, M. (2023) · doi:10.1101/2023.09.15.558037 · Cited by 3
Structural insights into the orthosteric inhibition of P2X receptors by non-ATP-analog antagonists
Sheng, D., Yue, C., Jin, F., Wang, Y., Ichikawa, M., Yu, Y., Guo, C.-R., & Hattori, M. (2024) · doi:10.7554/elife.92829.2
Structural insights into the orthosteric inhibition of P2X receptors by non-ATP analog antagonists
Sheng, D., Yue, C.-X., Jin, F., Wang, Y., Ichikawa, M., Yu, Y., Guo, C.-R., & Hattori, M. (2024) · eLife · doi:10.7554/elife.92829.3
Metadata
- Authors
- Illes, P., Müller, C. E., Jacobson, K. A., Grutter, T., Nicke, A., Fountain, S. J., Kennedy, C., Schmalzing, G., Jarvis, M. F., Stojilkovic, S. S., King, B. F., & Di Virgilio, F.
- Venue
- British Journal of Pharmacology
- Publisher
- Wiley
- Published
- 2020-12-21
- Volume
- 178
- Issue
- 3
- Pages
- 489-514
- ISSN
- 0007-1188 (ISSN-L)
- 1476-5381
- OpenAlex
- W3097463406
- Cited by
- 313
- References
- 140
- FWCI
- 20.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Illes, P., Müller, C. E., Jacobson, K. A., Grutter, T., Nicke, A., Fountain, S. J., Kennedy, C., Schmalzing, G., Jarvis, M. F., Stojilkovic, S. S., King, B. F., & Di Virgilio, F. (2021). Update of P2X receptor properties and their pharmacology: IUPHAR Review 30. British Journal of Pharmacology. https://doi.org/10.1111/bph.15299
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