ArticleScience (New York, N.Y.)2019
Structures of the AMPA receptor in complex with its auxiliary subunit cornichon.
Article in Science (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 2 of them syntheses that pooled it.
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.
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
56 citing papers in PubMed, 2 syntheses or guidelines pooled it, 88 citations in OpenAlex.
- Genome-wide association meta-analyses of drug-resistant epilepsy.EBioMedicine · 2025Pooled it
- Preclinical evidence and mechanistic insights of ligustilide in ischemic stroke: a systematic review and meta-analysis.Frontiers in pharmacology · 2025Pooled it
- Apoptin-Derived Peptide Alleviates Temporal Lobe Epilepsy (TLE) by Limiting Neuronal CaCNS neuroscience & therapeutics · 2026Article
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- Native AMPA receptor architecture reveals SynDIG4 engagement and auxiliary subunit heterogeneity.Science advances · 2026Article
- Assembly and gating mechanism of native AMPA receptors from the cerebellum.Cell research · 2026Article
- The Lack of a COPII Cargo Receptor Erv14 Impacts Physiological Functions of the Vacuole in Saccharomyces cerevisiae.Traffic (Copenhagen, Denmark) · 2026Article
- Auxiliary subunits reshape structural asymmetry and functional plasticity in heterotetrameric GluA1/A2 AMPA receptor core.Nature communications · 2026Article
- Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.Science (New York, N.Y.) · 2026Article
- Trafficking of the human NaProtein science : a publication of the Protein Society · 2026Article
- Sex differences in AMPA receptor trafficking proteins.Biology of sex differences · 2026Review
- Structural basis for activation and conformational plasticity of the GluA4 AMPA receptor.Nature communications · 2026Article
- Efficient and rapid isolation of native AMPA receptor complexes for cryo-EM.Protein science : a publication of the Protein Society · 2026Article
- GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins.Nature structural & molecular biology · 2025Article
- Dynamic extracellular interactions with AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Atomistic mechanisms of calcium permeation modulated by Q/R editing and selectivity filter mutations in GluA2 AMPA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Allosteric competition and inhibition in AMPA receptors.Nature structural & molecular biology · 2024Article
- Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization.Nature structural & molecular biology · 2024Article
- The Role of Cornichons in the Biogenesis and Functioning of Monovalent-Cation Transport Systems.Physiological research · 2024Review
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1 author at 1 institution in 1 country.
Funding
Abstract
In the brain, AMPA-type glutamate receptors (AMPARs) form complexes with their auxiliary subunits and mediate the majority of fast excitatory neurotransmission. Signals transduced by these complexes are critical for synaptic plasticity, learning, and memory. The two major categories of AMPAR auxiliary subunits are transmembrane AMPAR regulatory proteins (TARPs) and cornichon homologs (CNIHs); these subunits share little homology and play distinct roles in controlling ion channel gating and trafficking of AMPAR. Here, I report high-resolution cryo-electron microscopy structures of AMPAR in complex with CNIH3. Contrary to its predicted membrane topology, CNIH3 lacks an extracellular domain and instead contains four membrane-spanning helices. The protein-protein interaction interface that dictates channel modulation and the lipids surrounding the complex are revealed. These structures provide insights into the molecular mechanism for ion channel modulation and assembly of AMPAR/CNIH3 complexes.
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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.