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- W2443009416 abstract "Significance α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) are the main excitatory receptors in the brain. Although neurotransmitter binding to AMPARs is well understood, knowledge regarding their activation mechanisms remains incomplete. We exploited genetic insertion of fluorescent proteins to create AMPARs displaying fluorescence resonance energy transfer and allow optical monitoring of conformational changes in the receptor. Ligand-driven conformational changes are observed to occur in two intracellular domains of the receptor that are distant from the extracellular site where glutamate binds. The C terminus extends laterally from the receptor and remains relatively close to the plasma membrane. By measuring the activation of receptors electrically and optically at the same time, this study reveals AMPAR conformational changes occurring during receptor state transitions for a region not resolved in structural studies." @default.
- W2443009416 created "2016-06-24" @default.
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- W2443009416 date "2016-06-16" @default.
- W2443009416 modified "2023-10-10" @default.
- W2443009416 title "Structural rearrangement of the intracellular domains during AMPA receptor activation" @default.
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- W2443009416 doi "https://doi.org/10.1073/pnas.1601747113" @default.
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