ArticleBiochemistry2008
LRET investigations of conformational changes in the ligand binding domain of a functional AMPA receptor.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- Conformational equilibrium of an ABC transporter analyzed by luminescence resonance energy transfer.Biophysical journal · 2025Article
- CaCommunications biology · 2023Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Lanthanide-Based Optical Probes of Biological Systems.Cell chemical biology · 2020Review
- Mechanism of modulation of AMPA receptors by TARP-γ8.The Journal of general physiology · 2020Article
- Activation and desensitization of ionotropic glutamate receptors by selectively triggering pre-existing motions.Neuroscience letters · 2019Review
- Mapping the Conformational Landscape of Glutamate Receptors Using Single Molecule FRET.Trends in neurosciences · 2019Review
- Stargazin Modulation of AMPA Receptors.Cell reports · 2016Article
- Conformational Selection and Submillisecond Dynamics of the Ligand-binding Domain of the N-Methyl-d-aspartate Receptor.The Journal of biological chemistry · 2016Article
- Structural rearrangement of the intracellular domains during AMPA receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc.The Journal of general physiology · 2015Article
- Subtype-dependent N-methyl-D-aspartate receptor amino-terminal domain conformations and modulation by spermine.The Journal of biological chemistry · 2015Article
- Stargazin promotes closure of the AMPA receptor ligand-binding domain.The Journal of general physiology · 2014Article
- Luminescence resonance energy transfer to study conformational changes in membrane proteins expressed in mammalian cells.Journal of visualized experiments : JoVE · 2014Article
- Proton-mediated conformational changes in an acid-sensing ion channel.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
- Conformational changes at the agonist binding domain of the N-methyl-D-aspartic acid receptor.The Journal of biological chemistry · 2011Article
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The structural investigations using the soluble ligand binding domain of the AMPA subtype of the glutamate receptor have provided invaluable insight into the mechanistic pathway by which agonist binding to this extracellular domain mediates the formation of cation-selective channels in this protein. These structures, however, are in the absence of the transmembrane segments, the primary functional component of the protein. Here, we have used a modified luminescence resonance energy transfer based method to obtain distance changes due to agonist binding in the ligand binding domain in the presence of the transmembrane segments. These distance changes show that the cleft closure conformational change observed in the isolated ligand binding domain upon binding agonist is conserved in the receptor with the channel segments, thus establishing that the isolated ligand binding domain is a good model of the domain in the receptor containing the transmembrane segments.
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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.