ArticleNature communications2019
Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 33 citations in OpenAlex.
- GluN2D NMDA Receptors: Bridging Physiology and Pathology.Biological psychiatry · 2026Review
- Central toxic effects of an antitumoral bufadienolide: In silico targets and in vivo findings.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Inhibition of GluN2B-containing N-methyl-D-aspartate receptors by radiprodil.Brain : a journal of neurology · 2026Article
- GluN2B-specific NMDAR positive allosteric modulation reverses cognitive and behavioral abnormalities inScience advances · 2026Article
- Dynamic control of NMDA receptor CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Accommodating Statistical and Physics-Based Computational Protocols for Molecular Glue Model and Evaluation.Journal of chemical information and modeling · 2025Article
- Reduced removal of waste products from energy metabolism takes center stage in human brain aging.Scientific reports · 2025Article
- Structural and functional mechanisms of anti-NMDAR autoimmune encephalitis.Nature structural & molecular biology · 2024Article
- Revealing the pH-dependent conformational changes in sol g 2.1 protein and potential ligands binding.Scientific reports · 2024Article
- Article
- Src dependency of the regulation of LTP by alternative splicing ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Article
- Structure and function of GluN1-3A NMDA receptor excitatory glycine receptor channel.Science advances · 2024Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
- Novel GluN2B-Selective NMDA Receptor Negative Allosteric Modulator Possesses Intrinsic Analgesic Properties and Enhances Analgesia of Morphine in a Rodent Tail Flick Pain Model.ACS chemical neuroscience · 2023Article
- Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs.Molecular cell · 2022Article
- Targeting NMDA Receptor Complex in Management of Epilepsy.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Neuronal Death Mechanisms and Therapeutic Strategy in Ischemic Stroke.Neuroscience bulletin · 2022Review
- Biphenyl scaffold for the design of NMDA-receptor negative modulators: molecular modeling, synthesis, and biological activity.RSC medicinal chemistry · 2022Article
- Inhibition of NMDA receptors through a membrane-to-channel path.Nature communications · 2022Article
- Structural insights into binding of therapeutic channel blockers in NMDA receptors.Nature structural & molecular biology · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Context-dependent inhibition of N-methyl-D-aspartate (NMDA) receptors has important therapeutic implications for the treatment of neurological diseases that are associated with altered neuronal firing and signaling. This is especially true in stroke, where the proton concentration in the afflicted area can increase by an order of magnitude. A class of allosteric inhibitors, the 93-series, shows greater potency against GluN1-GluN2B NMDA receptors in such low pH environments, allowing targeted therapy only within the ischemic region. Here we map the 93-series compound binding site in the GluN1-GluN2B NMDA receptor amino terminal domain and show that the interaction of the N-alkyl group with a hydrophobic cage of the binding site is critical for pH-dependent inhibition. Mutation of residues in the hydrophobic cage alters pH-dependent potency, and remarkably, can convert inhibitors into potentiators. Our study provides a foundation for the development of highly specific neuroprotective compounds for the treatment of neurological diseases.
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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.