ArticleThe Journal of physiology2008
Zinc inhibition of rat NR1/NR2A N-methyl-D-aspartate receptors.
Article in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 63 citations in OpenAlex.
- Associations of Maternal Prenatal Zinc Consumption with Infant Brain Tissue Organization and Neurodevelopmental Outcomes.Nutrients · 2025Article
- EAR-20 peptide, a novel NMDA receptor positive allosteric modulator.Frontiers in pharmacology · 2025Article
- A Frameshift Variant of GluN2A Identified in an Epilepsy Patient Results in NMDA Receptor Mistargeting.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Functional effects of disease-associated variants reveal that the S1-M1 linker of the NMDA receptor critically controls channel opening.Cellular and molecular life sciences : CMLS · 2023Article
- Intracellular zinc signaling influences NMDA receptor function by enhancing the interaction of ZnT1 with GluN2A.Neuroscience letters · 2022Article
- Genetic removal of synaptic ZnFrontiers in neurology · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- The Function and Regulation of Zinc in the Brain.Neuroscience · 2021Review
- New Insights of the Zn(II)-Induced P2 × 4R Positive Allosteric Modulation: Role of Head Receptor Domain SS2/SS3, E160 and D170.International journal of molecular sciences · 2020Article
- Article
- A structurally derived model of subunit-dependent NMDA receptor function.The Journal of physiology · 2018Article
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
- Article
- Properties of TriheteromericMolecular pharmacology · 2018Article
- Functional Investigation of a GRIN2A Variant Associated with Rolandic Epilepsy.Neuroscience bulletin · 2018Article
- Supplementation with zinc in rats enhances memory and reverses an age-dependent increase in plasma copper.Behavioural brain research · 2017Article
- The Regulation of GluN2A by Endogenous and Exogenous Regulators in the Central Nervous System.Cellular and molecular neurobiology · 2017Review
- NMDA receptors: linking physiological output to biophysical operation.Nature reviews. Neuroscience · 2017Review
- A de novo loss-of-function GRIN2A mutation associated with childhood focal epilepsy and acquired epileptic aphasia.PloS one · 2017Article
- Molecular Mechanism of Disease-Associated Mutations in the Pre-M1 Helix of NMDA Receptors and Potential Rescue Pharmacology.PLoS genetics · 2017Article
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 1 institution in 1 country.
Funding
Abstract
Zinc ions (Zn(2+)) are localized in presynaptic vesicles at glutamatergic synapses and released in an activity-dependent manner. Modulation of NMDA-type glutamate receptors by extracellular Zn(2+) may play an important role under physiological conditions and during pathologies such as ischaemia or seizure. Zn(2+) inhibits NMDA receptors containing the NR2A subunit with an IC(50) value in the low nanomolar concentration range. Here we investigate at the single-channel level the mechanism of high affinity Zn(2+) inhibition of recombinant NR1/NR2A receptors expressed in HEK293 cells. Zn(2+) reversibly decreases the mean single-channel open duration and channel open probability determined in excised outside-out patches, but has no effect on single-channel current amplitude. A parallel series of experiments demonstrates that lowering extracellular pH (increasing proton concentration) has a similar effect on NR1/NR2A single-channel properties as Zn(2+). Fitting the sequence of single-channel events with kinetic models suggests that the association of Zn(2+) with its binding site enhances proton binding. Modelling further suggests that protonated channels are capable of opening but with a lower open probability than unprotonated channels. These data and analyses are consistent with Zn(2+)-mediated inhibition of NMDA receptors primarily reflecting enhancement of proton inhibition.
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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.