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Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Open accessAbstract
The mammalian ionotropic glutamate receptor family encodes 18 gene products that coassemble to form ligand-gated ion channels containing an agonist recognition site, a transmembrane ion permeation pathway, and gating elements that couple agonist-induced conformational changes to the opening or closing of the permeation pore. Glutamate receptors mediate fast excitatory synaptic transmission in the central nervous system and are localized on neuronal and non-neuronal cells. These receptors regulate a broad spectrum of processes in the brain, spinal cord, retina, and peripheral nervous system. Glutamate receptors are postulated to play important roles in numerous neurological diseases and have attracted intense scrutiny. The description of glutamate receptor structure, including its transmembrane elements, reveals a complex assembly of multiple semiautonomous extracellular domains linked to a pore-forming element with striking resemblance to an inverted potassium channel. In this review we discuss International Union of Basic and Clinical Pharmacology glutamate receptor nomenclature, structure, assembly, accessory subunits, interacting proteins, gene expression and translation, post-translational modifications, agonist and antagonist pharmacology, allosteric modulation, mechanisms of gating and permeation, roles in normal physiological function, as well as the potential therapeutic use of pharmacological agents acting at glutamate receptors.
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“NMDARs are heterotetrameric ligand-gated ionotropic receptors”
From Mechanisms of ketamine and its metabolites as antidepressants (2022) · cites this paper as Traynelis et al., 2010
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In the citing paper
“The NMDAR ion channel is heteromeric, composed of two obligatory GluN1 subunits and two GluN2 or GluN3 subunits.”
From Lipid Nanoparticle Delivery of siRNA to Silence Neuronal Gene Expression in the Brain (2013) · cites this paper as [19]
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In the citing paper
“Expression of GluN1 is necessary for the formation of a functional NMDAR channel in the plasma membrane.19”
From Lipid Nanoparticle Delivery of siRNA to Silence Neuronal Gene Expression in the Brain (2013) · cites this paper as [19]
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In the citing paper
“The proposed role of glutamate as a signal molecule in ctenophores is supported by an unprecedented diversity of ionotropic glutamate receptors(iGluRs;ExtendedDataFig.7a,bandSupplementaryTable27)far exceeding the number of genes encoding iGluRs in other basal metazoans 28 .”
From The ctenophore genome and the evolutionary origins of neural systems (2014) · cites this paper as [28]
Experimental — accuracy not yet measuredIn the citing paper
“Throughout the central nervous system, the vast majority of fast synaptic neurotransmission arises via AMPARs (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“The M2 reentrant transmembrane loop of the AMPAR subunit forms the lining of the channel pore, and amino acids in the so-called “QRN” site determine the ion selectivity of the channel (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“Unlike GluA1, GluA3 and GluA4 subunits which contain an unedited glutamine (Q) most GluA2 subunits contain a fully edited arginine (R) at this site which has important consequences for single channel conductance, Ca2+-permeability, and channel block by polyamines (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“Of these subunits, incorporation of GluA2 is key to the overall biophysical properties of the receptor.”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“The TARP family comprises six isoforms, which differentially modify almost every function of native AMPARs (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“As described in section VA, CP-AMPARs are both Ca2+ permeable and blocked in a voltage-dependent manner by cytoplasmic polyamines, such as spermine and spermidine (1133).”
From Hippocampal GABAergic Inhibitory Interneurons (2017) · cites this paper as [1133]
In the citing paper
“NMDARs typically contain two GluN1 subunits and either two GluN2 subunits or a mixture of GluN2/GluN3 subunits 28, 29.”
From Mechanisms of ketamine action as an antidepressant (2018) · cites this paper as [29]
In the citing paper
“Both immunohistochemical and electrophysiological studies have confirmed the existence of extra-synaptic NMDARs, which are not located in the post-synaptic density 68, and are primarily comprised of GluN2B-containing heterotetramers 28, 29.”
From Mechanisms of ketamine action as an antidepressant (2018) · cites this paper as [29]
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Citations
Cites
Glutamate neurotoxicity and diseases of the nervous system
Choi, D. W. (1988) · Neuron · doi:10.1016/0896-6273(88)90162-6 · Cited by 8,188
Kessler, R. C., Berglund, P., Demler, O., Jin, R., Koretz, D., Merikangas, K. R., Rush, A. J., Walters, E. E., & Wang, P. S. (2003) · JAMA · doi:10.1001/jama.289.23.3095 · Cited by 7,988
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
Doyle, D., Morais-Cabral, J. H., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,851
Magnesium gates glutamate-activated channels in mouse central neurones
Nowak, L. M., Bregestovski, P. D., Ascher, P., Herbet, A., & Prochiantz, A. (1984) · Nature · doi:10.1038/307462a0 · Cited by 4,116
Ion Channels/Excitable Membranes
(2011) · Springer eBooks · doi:10.1007/springerreference_33998 · Cited by 4,066
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968
Pathobiology of ischaemic stroke: an integrated view
Dirnagl, U., Iadecola, C., & Moskowitz, M. A. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01401-0 · Cited by 3,943
Trivedi, M. H., Rush, A. J., Wisniewski, S. R., Nierenberg, A. A., Warden, D., Ritz, L., Norquist, G., Howland, R. H., Lebowitz, B., McGrath, P. J., et al. (2006) · American Journal of Psychiatry · doi:10.1176/appi.ajp.163.1.28 · Cited by 3,879
Antidepressant effects of ketamine in depressed patients
Berman, R. M., Cappiello, A., Anand, A., Oren, D. A., Heninger, G. R., Charney, D. S., & Krystal, J. H. (2000) · Biological Psychiatry · doi:10.1016/s0006-3223(99)00230-9 · Cited by 3,856
Neuronal plasticity: Increasing the gain in pain
Woolf, C. J., & Salter, M. W. (2000) · Science · doi:10.1126/science.288.5472.1765 · Cited by 3,781
Research works printed but not linked: 2
- Leung, 2007, Regulation of NR1/NR2B NMDA receptor function by thrombin, Soc Neuosci Abstr, 33
- Sang, 2003, The NR2B subunit-selective NMDA receptor antagonist CP-101,606 reduces pain intensity in patients with central and peripheral neuropathic pain, Soc Neurosci Abstr, 29, 814.9
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Strong, K. L., Jing, Y., Prosser, A. R., Traynelis, S. F., & Liotta, D. C. (2014) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2014.972938 · Cited by 43
Self-citationHiggins, G. A., Silenieks, L. B., MacMillan, C., Sevo, J., Zeeb, F. D., & Thevarkunnel, S. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.05.025 · Cited by 40
Li, D., Zhou, J., Zhang, J., & Pan, H. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2141-17.2017 · Cited by 40
Wu, M., Tian, H.-L., Liu, X., Lai, J. H. C., Du, S., & Xia, J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.015 · Cited by 42
Palmitoylation-mediated synaptic regulation of AMPA receptor trafficking and function
Sohn, H., & Park, M. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01134-z · Cited by 40
Zhang, T., Wu, C., Yang, X., Liu, Y., Yang, H., Yuan, L., Liu, Y., Sun, S., & Yang, J. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.05.030 · Cited by 40
Ketamine: The final frontier or another depressing end?
Sial, O. K., Parise, E. M., Parise, L. F., Gnecco, T., & Bolaños‐Guzmán, C. A. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.112508 · Cited by 41
Negative allosteric modulation of GluN1/GluN3 NMDA receptors
Zhu, Z., Yi, F., Epplin, M. P., Liu, D., Summer, S. L., Mizu, R. K., Shaulsky, G. H., XiangWei, W., Tang, W., Burger, P. B., et al. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108117 · Cited by 40
Self-citationTang, W., Liu, D., Traynelis, S. F., & Yuan, H. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108247 · Cited by 42
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Wang, J., & Swanson, R. A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00861 · Cited by 40
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Klykov, O. V., Gangwar, S. P., Yelshanskaya, M. V., Yen, L. Y., & Sobolevsky, A. I. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.030 · Cited by 40
Delta glutamate receptors are functional glycine- and ᴅ-serine–gated cation channels in situ
Carrillo, E. C., Gonzalez, C. U., Berka, V., & Jayaraman, V. (2021) · Science Advances · doi:10.1126/sciadv.abk2200 · Cited by 40
Colotta, V., Lenzi, O., Catarzi, D., Varano, F., Squarcialupi, L., Costagli, C., Galli, A., Ghelardini, C., Pugliese, A. M., Maraula, G., et al. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.05.036 · Cited by 40
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Ortinski, P. I. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8636-6 · Cited by 40
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García‐Nafría, J., Herguedas, B., Watson, J. F., & Greger, I. H. (2016) · The Journal of Physiology · doi:10.1113/jp271844 · Cited by 41
Sibarov, D. A., Abushik, P. A., Poguzhelskaya, E. E., Bolshakov, K. V., & Antonov, S. M. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.115.227173 · Cited by 40
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Zhang, J., Chang, S., Zhang, X., & Zhu, S. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6ira/pdb · Cited by 40
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Lambert, P. M., & Mennerick, S. J. (2020) · Wiley eBooks · doi:10.1002/9780470015902.a0029140 · Cited by 40
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Matsui, A., Spangler, C. J., Elferich, J., Shiozaki, M., Jean, N., Zhao, X., Qin, M., Zhong, H., Yu, Z., & Gouaux, E. (2024) · eLife · doi:10.7554/elife.98458.3 · Cited by 40
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Idle, J. R., & Beyoğlu, D. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108366 · Cited by 39
Distinct structure and gating mechanism in diverse NMDA receptors with GluN2C and GluN2D subunits
Zhang, J., Zhang, M., Wang, Q., Wen, H., Liu, Z., Wang, F., Wang, Y., Yao, F., Song, N., Kou, Z., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00959-z · Cited by 39
Jin, D., Chen, H., Zhou, M., Chen, S., & Pan, H. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0601-23.2023 · Cited by 39
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Tumdam, R., Hussein, Y., Garin-Shkolnik, T., & Stern, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252212366 · Cited by 45
Comparative Dynamics of NMDA- and AMPA-Glutamate Receptor N-Terminal Domains
Dutta, A., Shrivastava, I. H., Sukumaran, M., Greger, I. H., & Bahar, İ. (2012) · Structure · doi:10.1016/j.str.2012.08.012 · Cited by 43
Huang, L., Cichon, J., Ninan, I., & Yang, G. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf7151 · Cited by 39
Matsuda, K. (2017) · Neurosciences research · doi:10.1016/j.neures.2016.11.004 · Cited by 38
Glutamate Excitotoxicity Linked to Spermine Oxidase Overexpression
Pietropaoli, S., Leonetti, A., Cervetto, C., Venturini, A., Mastrantonio, R., Baroli, G., Persichini, T., Colasanti, M., Maura, G., Marcoli, M., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0864-0 · Cited by 39
Properties of Triheteromeric N-Methyl-d-Aspartate Receptors Containing Two Distinct GluN1 Isoforms
Yi, F., Zachariassen, L. G., Dorsett, K. N., & Hansen, K. B. (2018) · Molecular Pharmacology · doi:10.1124/mol.117.111427 · Cited by 39
Self-citationCause or compensation?—Altered neuronal Ca2+ handling in Huntington's disease
Mackay, J. P., Nassrallah, W. B., & Raymond, L. A. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12817 · Cited by 40
Kandel, M. B., Yamamoto, S., Midorikawa, R., Morise, J., Wakazono, Y., Oka, S., & Takamiya, K. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14565 · Cited by 39
Golovynska, I., Golovynskyi, S., Stepanov, Y. V., Garmanchuk, L., Stepanova, L. I., Qu, J., & Ohulchanskyy, T. Y. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28257 · Cited by 39
Skřenková, K., Hemelíková, K., Kolcheva, M., Kortus, Š., Kaniaková, M., Krausová, B. H., & Hořák, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-48845-3 · Cited by 39
Heterogeneous glutamatergic receptor mRNA expression across phrenic motor neurons in rats
Rana, S. D., Sieck, G. C., & Mantilla, C. B. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14881 · Cited by 38
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Valbuena, S., & Lerma, J. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.11.050 · Cited by 39
Striatal Kir2 K+ channel inhibition mediates the antidyskinetic effects of amantadine
Shen, W., Ren, W., Zhai, S., Yang, B., Vanoye, C. G., Mitra, A., George, A. L., & Surmeier, D. J. (2020) · Journal of Clinical Investigation · doi:10.1172/jci133398 · Cited by 40
Negri, S., Faris, P. S., Maniezzi, C., Pellavio, G., Spaiardi, P., Botta, L., Laforenza, U., Biella, G. R., & Moccia, F. D. (2021) · Cell Calcium · doi:10.1016/j.ceca.2021.102454 · Cited by 41
Contemporary advances in anti-NMDAR antibody (Ab)-mediated encephalitis
Seery, N., Butzkueven, H., O'Brien, T. J., & Monif, M. (2022) · Autoimmunity Reviews · doi:10.1016/j.autrev.2022.103057 · Cited by 39
Abulseoud, O. A., Alasmari, F. F., Hussein, A. M., & Sari, Y. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.841036 · Cited by 40
Gawande, D. Y., Narasimhan, K. K. S., Shelkar, G. P., Pavuluri, R., Stessman, H. A. F., & Dravid, S. M. (2023) · Biological Psychiatry · doi:10.1016/j.biopsych.2023.03.020 · Cited by 41
Choi, U. B., Kazi, R., Stenzoski, N. E., Wollmuth, L. P., Uversky, V. N., & Bowen, M. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.477810 · Cited by 39
Self-citationNedd4 is a specific E3 ubiquitin ligase for the NMDA receptor subunit GluN2D
Gautam, V., Trinidad, J. C., Rimerman, R. A., Costa, B. M., Burlingame, A. L., & Monaghan, D. T. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.04.035 · Cited by 39
Timm, D. E., Benveniste, M., Weeks, A. M., Nisenbaum, E. S., & Partin, K. M. (2011) · Molecular Pharmacology · doi:10.1124/mol.110.070243 · Cited by 39
den Hartog, C. R., Beckley, J. T., Smothers, C. T., Lench, D. H., Holseberg, Z. L., Fedarovich, H., Gilstrap, M. J., Homanics, G. E., & Woodward, J. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080541 · Cited by 39
Sasmal, D. K., & Lu, H. P. (2014) · Journal of the American Chemical Society · doi:10.1021/ja506231j · Cited by 39
Dziedzic, A., Miller, E., Saluk-Bijak, J., & Bijak, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051852 · Cited by 38
Doboszewska, U., Szewczyk, B., Sowa-Kućma, M., Młyniec, K., Rafało-Ulińska, A., Ostachowicz, B., Lankosz, M., & Nowak, G. (2015) · Behavioural Brain Research · doi:10.1016/j.bbr.2015.03.064 · Cited by 40
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Furukawa, H. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.213850 · Cited by 43
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Ribeiro, M. P. C., Custódio, J. B. A., & Santos, A. E. (2016) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-016-3129-0 · Cited by 38
Gong, B., Li, Y., Cheng, Z., Wang, P., Luo, L., Huang, H., Duan, S., & Liu, F. (2017) · Tumor Biology · doi:10.1177/1010428317704364 · Cited by 38
Wang, J., Lv, X., Wu, Y., Xu, T., Jiao, M., Yang, R., Li, X., Chen, M., Yan, Y.-G., Chen, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04672-0 · Cited by 38
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Wallach, J. V., & Brandt, S. D. (2018) · Handbook of experimental pharmacology · doi:10.1007/164_2018_124 · Cited by 39
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Lalanne, T., Oyrer, J., Farrant, M., & Sjöström, P. J. (2018) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2018.00034 · Cited by 38
Müller, M., Jacobi, E., Sakimura, K., Malinow, R., & von Engelhardt, J. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0611-4 · Cited by 40
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von Engelhardt, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061460 · Cited by 38
Savtchouk, I., Castro, M. A. D., Ali, R., Stubbe, H., Luján, R., & Volterra, A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1816013116 · Cited by 38
Rolland, M., Powell, R., Jacquier‐Sarlin, M. R., Boisseau, S., Reynaud-Dulaurier, R., Hernández, J. M., André, L., Borel, E., Buisson, A., & Lanté, F. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2501-19.2020 · Cited by 41
Modulation of information processing by AMPA receptor auxiliary subunits
Jacobi, E., & von Engelhardt, J. (2020) · The Journal of Physiology · doi:10.1113/jp276698 · Cited by 38
Herbrechter, R., Hube, N., Buchholz, R., & Reiner, A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03865-z · Cited by 41
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Xu, Y., Song, R., Chen, W., Strong, K. L., Shrey, D. W., Gedela, S., Traynelis, S. F., Zhang, G., & Yuan, H. (2021) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.51406 · Cited by 38
Self-citationChang, A., Chang, Y., & Wang, S. (2022) · Food & Function · doi:10.1039/d2fo01490d · Cited by 38
McKay, S., Griffiths, N., Butters, P., Thubron, E., Hardingham, G. E., & Wyllie, D. J. A. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01748.x · Cited by 38
Mattison, H. A., Hayashi, T., & Barría, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049089 · Cited by 38
Yuan, T., & Bellone, C. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.04.056 · Cited by 38
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Promising targets of cell death signaling of NR2B receptor subunit in stroke pathogenesis
Shu, S., Pei, L., & Lu, Y. (2014) · Regenerative Medicine Research · doi:10.1186/2050-490x-2-8 · Cited by 38
Golubeva, E. A., Lavrov, M. I., Radchenko, E. V., & Palyulin, V. A. (2022) · Biomolecules · doi:10.3390/biom13010056 · Cited by 36
Gautam, D., Naik, U. P., Naik, M. U., Yadav, S. K., Chaurasia, R. N., & Dash, D. (2023) · Biomolecules · doi:10.3390/biom13111609 · Cited by 38
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Lau, A. Y., Salazar, H., Blachowicz, L., Ghisi, V., Plested, A. J. R., & Roux, B. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.003 · Cited by 37
Sirrieh, R. E., MacLean, D. M., & Jayaraman, V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482356 · Cited by 37
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Via, L. L., Bonini, D., Russo, I., Orlandi, C., Barlati, S., & Barbon, A. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1223 · Cited by 37
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Berlin, S., & Isacoff, E. Y. (2017) · EMBO Reports · doi:10.15252/embr.201744010 · Cited by 38
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Suzuki, M., Imanishi, N., Mita, M., Hamase, K., Aiso, S., & Sasabe, J. (2017) · ASN NEURO · doi:10.1177/1759091417713905 · Cited by 37
Amakhin, D. V., Malkin, S. L., Ergina, J. L., Kryukov, K. A., Veniaminova, E. A., Zubareva, O. E., & Zaitsev, A. V. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00264 · Cited by 37
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John, A. S. P., Kundu, S., Pushpakumar, S. B., Amin, M., Tyagi, S. C., & Sen, U. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00251.2018 · Cited by 37
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Self-citationYamasaki, M., Aiba, A., Kano, M., & Watanabe, M. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108629 · Cited by 37
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Gómez, R. J., Maglio, L. E., Gonzalez-Hernandez, A. J., Rivero-Pérez, B., Bartolomé‐Martín, D., & Giráldez, T. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2107026118 · Cited by 37
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Seillier, C., Lesept, F., Toutirais, O., Potzeha, F., Blanc, M., & Vivien, D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810336 · Cited by 47
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Prole, D. L., & Taylor, C. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042404 · Cited by 37
Harms, J. E., Benveniste, M., Maclean, J. K. F., Partin, K. M., & Jamieson, C. J. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.06.008 · Cited by 37
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Fisher, J. L., & Mott, D. D. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.256776 · Cited by 36
Metadata
- Authors
- Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., & Dingledine, R.
- Affiliations
- Emory University (US)
- ORCID
- Venue
- Pharmacological Reviews
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 62
- Issue
- 3
- Pages
- 405-496
- ISSN
- 0031-6997 (ISSN-L)
- PMC
- PMC2964903
- OpenAlex
- W2037852973
- Cited by
- 3,568
- References
- 1,399
- Citations by year
- 2026: 151 · 2025: 181 · 2024: 216 · 2023: 201 · 2022: 247 · 2021: 279 · 2020: 269 · 2019: 272 · 2018: 235 · 2017: 268 · 2016: 242 · 2015: 221 · 2014: 257 · 2013: 221 · 2012: 162
- FWCI
- 15.66
- Type
- journal article
- Language
- en
- Update notices
- erratum (2014-10-01)
- Open access
- bronze
- doi.org
- Locations
- Pharmacological Reviews (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Michael J. Fox Foundation for Parkinson's Research
- Lundbeckfonden
- H. Lundbeck A/S
- National Institutes of Health (NS036654)
- National Institute of Mental Health (MH066892, R01MH066892)
- National Institute on Drug Abuse (T32-DA01504006, T32DA015040)
- National Eye Institute (R01EY016979, EY01697905)
- National Institute of General Medical Sciences (GM008602, T32GM008602)
- National Institute of Neurological Disorders and Stroke (R37NS036654, NS036604, NS068464, R01NS065371, NS065371, R01NS036654, NS036654, R01NS068464, R01NS036604)
- National Institute of Environmental Health Sciences (T32ES012870)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- ionotropic glutamate receptors, ligand-gated ion channels, receptor structure, receptor assembly, auxiliary subunits, receptor regulation, post-translational modification, allosteric modulation, gating mechanism, ion permeation, excitatory synaptic transmission, receptor nomenclature, neurological disorders, therapeutic agents
- MeSH terms
- Humans, Ion Channels, Synaptic Transmission, Terminology as Topic, Protein Processing, Post-Translational, Gene Expression, Receptors, Glutamate, Protein Subunits
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