Terunaga Nakagawa
Affiliations: | Vanderbilt University, Nashville, TN |
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"Terunaga Nakagawa"Mean distance: 14.78 (cluster 11) | S | N | B | C | P |
Parents
Sign in to add mentorNobutaka Hirokawa | grad student | University of Tokyo | |
Morgan Sheng | post-doc |
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Publications
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Ivica J, Kejzar N, Ho H, et al. (2024) Proton-triggered rearrangement of the AMPA receptor N-terminal domains impacts receptor kinetics and synaptic localization. Nature Structural & Molecular Biology |
Perozzo AM, Schwenk J, Kamalova A, et al. (2023) GSG1L-containing AMPA receptor complexes are defined by their spatiotemporal expression, native interactome and allosteric sites. Nature Communications. 14: 6799 |
Zhang D, Lape R, Shaikh SA, et al. (2023) Modulatory mechanisms of TARP γ8-selective AMPA receptor therapeutics. Nature Communications. 14: 1659 |
Hansen KB, Wollmuth LP, Bowie D, et al. (2021) Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels. Pharmacological Reviews. 73: 298-487 |
Kamalova A, Futai K, Delpire E, et al. (2021) AMPA receptor auxiliary subunit GSG1L suppresses short-term facilitation in corticothalamic synapses and determines seizure susceptibility. Cell Reports. 34: 108732 |
Kamalova A, Futai K, Delpire E, et al. (2020) AMPA Receptor Auxiliary Subunit GSG1L Suppresses Short-Term Facilitation in Corticothalamic Synapses and Determines Seizure Susceptibility. Cell Reports. 32: 107921 |
Kendall AK, Xie B, Xu P, et al. (2020) Mammalian Retromer Is an Adaptable Scaffold for Cargo Sorting from Endosomes. Structure (London, England : 1993) |
Perfitt TL, Wang X, Dickerson MT, et al. (2020) Neuronal L-Type Calcium Channel Signaling to the Nucleus Requires a Novel CaMKIIα-Shank3 Interaction. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience |
Kamalova A, Nakagawa T. (2020) AMPA receptor structure and auxiliary subunits. The Journal of Physiology |
Azumaya CM, Linton EA, Risener CJ, et al. (2020) Cryo-EM structure of human type-3 inositol triphosphate receptor reveals the presence of a self-binding peptide that acts as an antagonist. The Journal of Biological Chemistry |