ArticleThe Journal of biological chemistry2011
Mechanism of AMPA receptor activation by partial agonists: disulfide trapping of closed lobe conformations.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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
27 citing papers in PubMed, 38 citations in OpenAlex.
- Pre-activation and gating pathway of AMPA receptors revealed by full and partial agonists.Nature structural & molecular biology · 2026Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Kainate Receptor Antagonists: Recent Advances and Therapeutic Perspective.International journal of molecular sciences · 2023Review
- Structure, Function, and Regulation of the Kainate Receptor.Sub-cellular biochemistry · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Allosteric coupling of sub-millisecond clamshell motions in ionotropic glutamate receptor ligand-binding domains.Communications biology · 2021Article
- Measurements of the Timescale and Conformational Space of AMPA Receptor Desensitization.Biophysical journal · 2020Article
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Population Shift Mechanism for Partial Agonism of AMPA Receptor.Biophysical journal · 2019Article
- Structural Mechanisms of Gating in Ionotropic Glutamate Receptors.Biochemistry · 2018Article
- The Challenge of Interpreting Glutamate-Receptor Ion-Channel Structures.Biophysical journal · 2017Review
- R/G editing in GluA2RScientific reports · 2017Article
- Mechanism of partial agonism in AMPA-type glutamate receptors.Nature communications · 2017Article
- Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels.Nature structural & molecular biology · 2016Review
- Kinetic contributions to gating by interactions unique to N-methyl-D-aspartate (NMDA) receptors.The Journal of biological chemistry · 2015Article
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
- Article
- Structure of an agonist-bound ionotropic glutamate receptor.Science (New York, N.Y.) · 2014Article
- X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism.Science (New York, N.Y.) · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The mechanism by which agonist binding to an ionotropic glutamate receptor leads to channel opening is a central issue in molecular neurobiology. Partial agonists are useful tools for studying the activation mechanism because they produce full channel activation with lower probability than full agonists. Structural transitions that determine the efficacy of partial agonists can provide information on the trigger that begins the channel-opening process. The ligand-binding domain of AMPA receptors is a bilobed structure, and the closure of the lobes is associated with channel activation. One possibility is that partial agonists sterically block full lobe closure but that partial degrees of closure trigger the channel with a lower probability. Alternatively, full lobe closure may be required for activation, and the stability of the fully closed state could determine efficacy with the fully closed state having a lower stability when bound to partial relative to full agonists. Disulfide-trapping experiments demonstrated that even extremely low efficacy ligands such as 6-cyano-7-nitroquinoxaline-2,3-dione can produce a full lobe closure, presumably with low probability. The results are consistent the hypothesis that the efficacy is determined at least in part by the stability of the state in which the lobes are fully closed.
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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.