ArticleProceedings of the National Academy of Sciences of the United States of America2008
Supralinear potentiation of NR1/NR3A excitatory glycine receptors by Zn2+ and NR1 antagonist.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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
23 citing papers in PubMed.
- The GluN3-containing NMDA receptors.Channels (Austin, Tex.) · 2025Review
- Structural prediction of GluN3 NMDA receptors.Frontiers in physiology · 2024Article
- Activation of excitatory glycine NMDA receptors: At the mercy of a whimsical GluN1 subunit.The Journal of general physiology · 2023Article
- Allosteric modulation of GluN1/GluN3 NMDA receptors by GluN1-selective competitive antagonists.The Journal of general physiology · 2023Article
- Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Negative allosteric modulation of GluN1/GluN3 NMDA receptors.Neuropharmacology · 2020Article
- Control of aversion by glycine-gated GluN1/GluN3A NMDA receptors in the adult medial habenula.Science (New York, N.Y.) · 2019Article
- Structural features in the glycine-binding sites of the GluN1 and GluN3A subunits regulate the surface delivery of NMDA receptors.Scientific reports · 2019Article
- Unmasking GluN1/GluN3A excitatory glycine NMDA receptors.Nature communications · 2018Article
- Residues in the GluN1 C-terminal domain control kinetics and pharmacology of GluN1/GluN3A N-methyl-d-aspartate receptors.Neuropharmacology · 2017Article
- Protons Potentiate GluN1/GluN3A Currents by Attenuating Their Desensitisation.Scientific reports · 2016Article
- Article
- The Concise Guide to PHARMACOLOGY 2013/14: ligand-gated ion channels.British journal of pharmacology · 2013Article
- Calcium in red blood cells-a perilous balance.International journal of molecular sciences · 2013Review
- GluN3A: an NMDA receptor subunit with exquisite properties and functions.Neural plasticity · 2013Review
- NMDA hypofunction as a convergence point for progression and symptoms of schizophrenia.Frontiers in cellular neuroscience · 2013Article
- Open-channel blockade is less effective on GluN3B than GluN3A subunit-containing NMDA receptors.European journal of pharmacology · 2012Article
- Upregulation of KCC2 activity by zinc-mediated neurotransmission via the mZnR/GPR39 receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- A novel family of negative and positive allosteric modulators of NMDA receptors.The Journal of pharmacology and experimental therapeutics · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coassembly of the glycine-binding NMDA receptor subunits NR1 and NR3A results in excitatory glycine receptors of low efficacy. Here, we report that micromolar concentrations of the divalent cation Zn(2+) produce a 10-fold potentiation of NR1/NR3A receptor responses, which resembles that seen upon antagonizing glycine binding to the NR1 subunit. Coapplication of both Zn(2+) and NR1 antagonist caused a supralinear potentiation, resulting in a >120-fold increase of glycine-activated currents. At concentrations >50 microM, Zn(2+) alone generated receptor currents with similar efficacy as glycine, implying that NR1/NR3A receptors can be activated by different agonists. Point mutations in the NR1 and NR3A glycine-binding sites revealed that both the potentiating and agonistic effects of Zn(2+) are mediated by the ligand-binding domain of the NR1 subunit. In conclusion, Zn(2+) acts as a potent positive modulator and agonist at the NR1 subunit of NR1/NR3A receptors. Our results suggest that this unconventional member of the NMDA receptor family may in vivo be gated by the combined action of glycine and Zn(2+) or a yet unknown second ligand.
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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.