ArticleJournal of neurochemistry2008
Contribution of extracellular negatively charged residues to ATP action and zinc modulation of rat P2X2 receptors.
Article in Journal of neurochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 12 citations in OpenAlex.
- Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins.Antioxidants & redox signaling · 2014Review
- Article
- Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating.Frontiers in cellular neuroscience · 2014Article
- Multiple roles of the extracellular vestibule amino acid residues in the function of the rat P2X4 receptor.PloS one · 2013Article
- Conserved ectodomain cysteines are essential for rat P2X7 receptor trafficking.Purinergic signalling · 2012Article
- Tightening of the ATP-binding sites induces the opening of P2X receptor channels.The EMBO journal · 2012Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- Allosteric modulation of ATP-gated P2X receptor channels.Reviews in the neurosciences · 2011Review
- Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating.Physiological research · 2010Article
- Opposite effects of zinc on human and rat P2X2 receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Two histidines are known to be essential for zinc potentiation of rat P2X2 receptors, but the chemistry of zinc coordination would suggest that other residues also participate in this zinc-binding site. There is also a second lower affinity zinc-binding site in P2X2 receptors whose constituents are unknown. To assess whether the extracellular acidic residues of the P2X2 receptor contribute to zinc potentiation or inhibition, site-directed mutagenesis was used to produce alanine substitutions at each extracellular glutamate or aspartate. Two electrode voltage clamp recordings from Xenopus oocytes indicated that 7 of the 34 mutants (D82A, E85A, E91A, E115A, D136A, D209A, and D281A) were deficient in zinc potentiation and one mutant (E84A) was deficient in zinc inhibition. Additional tests on cysteine mutants at these eight positions indicated that D136 is the only residue that is a strong candidate to be at the potentiating zinc-binding site, and that E84 is unlikely to be at the inhibitory zinc-binding site.
Indexed as
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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.