ArticleMethods in enzymology2021
Single molecule FRET methodology for investigating glutamate receptors.
Article in Methods in enzymology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor.Proteins · 2025Article
- Allosteric competition and inhibition in AMPA receptors.Nature structural & molecular biology · 2024Article
- Bi-directional allosteric pathway in NMDA receptor activation and modulation.Nature communications · 2024Article
- Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Allosteric Competition and Inhibition in AMPA Receptors.bioRxiv : the preprint server for biology · 2023Article
- Gating intermediates reveal inhibitory role of the voltage sensor in a cyclic nucleotide-modulated ion channel.Nature communications · 2022Article
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Authors and funding
3 authors.
Funding
Abstract
Single molecule Förster Resonance Energy Transfer (smFRET) allows us to measure variation in distances between donor and acceptor fluorophores attached to a protein, providing the conformational landscape of the protein with respect to this specific distance. smFRET can be performed on freely diffusing molecules or on tethered molecules. Here, we describe the tethered method used to study ionotropic glutamate receptors, which allows us to track the changes in FRET as a function of time, thus providing information on the conformations sampled and kinetics of conformational changes in the millisecond to second time scale. Strategies for attaching fluorophores to the proteins, methods for acquiring and analyzing the smFRET trajectories, and limitations are discussed.
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