ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997
Baculovirus expression provides direct evidence for heteromeric assembly of P2X2 and P2X3 receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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Who cites it
30 citing papers in PubMed, 124 citations in OpenAlex.
- Cryo-EM structures of human P2X2/3 heteromer channel reveal the structural basis of ligand selectivity.Science advances · 2026Article
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- Purinergic signaling during Marek's disease in chickens.Scientific reports · 2023Article
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- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013Review
- Role of the ectonucleotidase NTPDase2 in taste bud function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA.Biochimica et biophysica acta · 2011Article
- Pharmacological properties and physiological function of a P2X-like current in single proximal tubule cells isolated from frog kidney.The Journal of membrane biology · 2010Article
- P2X receptors: dawn of the post-structure era.Trends in biochemical sciences · 2010Review
- Interaction of P2 purinergic receptors with cellular macromolecules.Naunyn-Schmiedeberg's archives of pharmacology · 2008Review
- Expression of multiple P2X receptors by glossopharyngeal neurons projecting to rat carotid body O2-chemoreceptors: role in nitric oxide-mediated efferent inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Pharmacology of P2X channels.Pflugers Archiv : European journal of physiology · 2006Review
- P2X receptor-mediated purinergic sensory pathways to the spinal cord dorsal horn.Purinergic signalling · 2004Article
- ATP analogues with modified phosphate chains and their selectivity for rat P2X2 and P2X2/3 receptors.British journal of pharmacology · 2003Article
- Subunit arrangement in P2X receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Heteromultimeric P2X(1/2) receptors show a novel sensitivity to extracellular pH.The Journal of pharmacology and experimental therapeutics · 2002Article
- Expression of P2X2 and P2X3 receptor subunits in rat carotid body afferent neurones: role in chemosensory signalling.The Journal of physiology · 2001Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
P2X2 and P2X3 are subunits of P2X receptors, cation channels opened by binding extracellular ATP. cDNAs encoding P2X2 and P2X3 receptor subunits, each with one of two C-terminal epitope tags, were cloned into baculovirus. Virally infected insect cells (Spodoptera frugiperda) expressed moderate to high levels of the corresponding proteins, as detected by Western blotting, by the specific binding of [35S]ATP and by whole-cell recordings of membrane current evoked by ATP or alphabetamethylene-ATP. In cells infected at the same time with two viruses encoding P2X2 and P2X3 receptors, the two proteins could be cross-immunoprecipitated with antibodies specific for either of the epitope tags. Whole-cell recordings from these cells showed that ATP and alphabetamethylene-ATP evoked currents with agonist sensitivity and desensitization quite distinct from those observed when P2X2 or P2X3 receptors were expressed alone. The results offer a method to express large amounts of P2X receptor protein, and they provide direct evidence that P2X2 and P2X3 subunits assemble to form heteromeric channels having distinct properties from those formed as homomers.
Indexed as
Identifiers
9254665PMC6573133W2048082309What 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.