ArticleChannels (Austin, Tex.)
Agonist-specific gating of NMDA receptors.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- The N-Methyl-D-Aspartate Receptor Blocker REL-1017 (Esmethadone) Reduces Calcium Influx Induced by Glutamate, Quinolinic Acid, and Gentamicin.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
- Heteromerization of ligand binding domains of N-methyl-D-aspartate receptor requires both coagonists, L-glutamate and glycine.Biochemistry · 2015Article
- Asynchronous movements prior to pore opening in NMDA receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Structural determinants of agonist efficacy at the glutamate binding site of N-methyl-D-aspartate receptors.Molecular pharmacology · 2013Article
- Functional insights from glutamate receptor ion channel structures.Annual review of physiology · 2013Review
- Role of cross-cleft contacts in NMDA receptor gating.PloS one · 2013Article
- Modes of glutamate receptor gating.The Journal of physiology · 2012Review
- Mechanisms of modal activation of GluA3 receptors.Molecular pharmacology · 2011Article
- Cations but not anions regulate the responsiveness of kainate receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- NMDA receptors with locked glutamate-binding clefts open with high efficacy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Characterizing single-channel behavior of GluA3 receptors.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The mechanism by which ligand binding at extracellular receptor domains gates a transmembrane ion-conducting pore is insufficiently understood. Examining a channel's activation reaction in the presence of agonists with distinct efficacies may inform this issue and may help identify agonist-dependent transitions. We have recently applied this approach to NMDA receptors composed of GluN1 and GluN2A subunits. Based on our results with several subunit-specific partial agonists we concluded that agonist effects were distributed over several of the multiple transitions that make up NMDA receptor gating and that these changes were subunit independent. Here we examine an additional GluN2A partial agonist, 4-fluoro-D, L-glutamic acid, and we summarize the observed kinetic changes of all nine partial agonists investigated. These results support the premise that regardless of the subunit-type to which they bind, agonists influence multiple equilibria within the NMDA receptor reaction and may stabilize a slightly different family of conformers.
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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.