ArticleBiochemistry2008
Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 39 citations in OpenAlex.
- Pre-activation and gating pathway of AMPA receptors revealed by full and partial agonists.Nature structural & molecular biology · 2026Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- Population Shift Mechanism for Partial Agonism of AMPA Receptor.Biophysical journal · 2019Article
- Structural Mechanisms of Gating in Ionotropic Glutamate Receptors.Biochemistry · 2018Article
- Mechanism of partial agonism in AMPA-type glutamate receptors.Nature communications · 2017Article
- Conformational Selection and Submillisecond Dynamics of the Ligand-binding Domain of the N-Methyl-d-aspartate Receptor.The Journal of biological chemistry · 2016Article
- Mechanism-Based Mathematical Model for Gating of Ionotropic Glutamate Receptors.The journal of physical chemistry. B · 2015Article
- Structural dynamics of the glycine-binding domain of the N-methyl-D-aspartate receptor.The Journal of biological chemistry · 2015Article
- Reduced curvature of ligand-binding domain free-energy surface underlies partial agonism at NMDA receptors.Structure (London, England : 1993) · 2015Article
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
- Structure of an agonist-bound ionotropic glutamate receptor.Science (New York, N.Y.) · 2014Article
- Thermodynamics and mechanism of the interaction of willardiine partial agonists with a glutamate receptor: implications for drug development.Biochemistry · 2014Article
- Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange.The Journal of biological chemistry · 2013Article
- Amino-terminal domain tetramer organization and structural effects of zinc binding in the N-methyl-D-aspartate (NMDA) receptor.The Journal of biological chemistry · 2013Article
- Functional insights from glutamate receptor ion channel structures.Annual review of physiology · 2013Review
- Role of conformational dynamics in α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor partial agonism.The Journal of biological chemistry · 2012Article
- Emerging models of glutamate receptor ion channel structure and function.Structure (London, England : 1993) · 2011Review
- Mechanism of AMPA receptor activation by partial agonists: disulfide trapping of closed lobe conformations.The Journal of biological chemistry · 2011Article
- Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?Journal of biomolecular NMR · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
The mechanism by which the binding of a neurotransmitter to a receptor leads to channel opening is a central issue in molecular neurobiology. The structure of the agonist binding domain of ionotropic glutamate receptors has led to an improved understanding of the changes in structure that accompany agonist binding and have provided important clues about the link between these structural changes and channel activation and desensitization. However, because the binding domain has exhibited different structures under different crystallization conditions, understanding the structure in the absence of crystal packing is of considerable importance. The orientation of the two lobes of the binding domain in the presence of a full agonist, an antagonist, and several partial agonists was measured using NMR spectroscopy by employing residual dipolar couplings. For some partial agonists, the solution conformation differs from that observed in the crystal. A model of channel activation based on the results is discussed.
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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.