The DOI matches its Crossref record; 1,391 of the 1,399 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“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
The cited source says what the claim attributes to it.
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]
The cited source says what the claim attributes to it.
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]
The check wasn’t confident either way, so it gives no verdict — never disputed.
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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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
Flagged first, then by citations
8 of the 1399 references couldn’t be matched to a known paper.
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
Cited by
Sorted by citations
Items 301–400 of 1,014
Membrane Topology and Intracellular Processing of Cyclin M2 (CNNM2)
de Baaij, J. H. F., Stuiver, M., Meij, I. C., Laínez, S., Kopplin, K., Venselaar, H., Müller, D., Bindels, R. J. M., & Hoenderop, J. G. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.342204 · Cited by 102
Neuronal carbonic anhydrase VII provides GABAergic excitatory drive to exacerbate febrile seizures
Ruusuvuori, E., Huebner, A. K., Kirilkin, I., Yukin, A. Y., Blaesse, P., Helmy, M., Kang, H. J., Muayed, M. E., Hennings, J. C., Voipio, J., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.160 · Cited by 102
Ca2+ to the rescue – Ca2+channels and signaling in plant immunity
Moeder, W., Phan, V., & Yoshioka, K. (2018) · Plant Science · doi:10.1016/j.plantsci.2018.04.012 · Cited by 101
Alcohol and NMDA receptor: current research and future direction
Chandrasekar, R. (2013) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2013.00014 · Cited by 110
CRISPR/Cas9-Mediated Gene Knock-Down in Post-Mitotic Neurons
Straub, C., Granger, A. J., Saulnier, J. L., & Sabatini, B. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105584 · Cited by 100
Memantine and Ketamine Differentially Alter NMDA Receptor Desensitization
Glasgow, N. G., Povysheva, N. V., Azofeifa, A. M., & Johnson, J. W. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1173-17.2017 · Cited by 106
Heise, C., Gardoni, F., Culotta, L., di Luca, M., Verpelli, C., & Sala, C. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00035 · Cited by 99
Retchless, B. S., Gao, W., & Johnson, J. W. (2012) · Nature Neuroscience · doi:10.1038/nn.3025 · Cited by 99
Comparing plant and animal glutamate receptors: common traits but different fates?
Wudick, M. M., Michard, E., Nunes, C. O., & Feijó, J. A. (2018) · Journal of Experimental Botany · doi:10.1093/jxb/ery153 · Cited by 100
Ca 2+ ‐permeable AMPA receptors and their auxiliary subunits in synaptic plasticity and disease
Cull-Candy, S. G., & Farrant, M. (2021) · The Journal of Physiology · doi:10.1113/jp279029 · Cited by 103
Cholesterol modulates open probability and desensitization of NMDA receptors
Kořı́nek, M., Vyklický, V., Borovská, J., Hemelíková, K., Kaniaková, M., Krausová, B. H., Krůšek, J., Balík, A., Smejkalová, T., Hořák, M., et al. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.288209 · Cited by 99
Nimitvilai, S., Lopez, M. F., Mulholland, P. J., & Woodward, J. J. (2015) · Neuropsychopharmacology · doi:10.1038/npp.2015.250 · Cited by 99
Ligand-specific deactivation time course of GluN1/GluN2D NMDA receptors
Vance, K. M., Simorowski, N., Traynelis, S. F., & Furukawa, H. (2011) · Nature Communications · doi:10.1038/ncomms1295 · Cited by 99
Self-citationGlutamate as a Neurotransmitter
Mennerick, S. J., & Zorumski, C. F. (2012) · Wiley eBooks · doi:10.1002/9780470015902.a0000139.pub3 · Cited by 99
Wills, T. A., Klug, J. R., Silberman, Y., Baucum, A. J., Weitlauf, C., Colbran, R. J., Delpire, E., & Winder, D. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113820109 · Cited by 98
Time and space profiling of NMDA receptor co‐agonist functions
Mothet, J., Bail, M. L., & Billard, J. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13204 · Cited by 103
Advances in non-dopaminergic treatments for Parkinson's disease
Stayte, S., & Vissel, B. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00113 · Cited by 104
Structural basis of kainate subtype glutamate receptor desensitization
Meyerson, J. R., Chittori, S., Merk, A., Rao, P., Han, T. H., Serpe, M., Mayer, M. L., & Subramaniam, S. (2016) · Nature · doi:10.1038/nature19352 · Cited by 98
Carbonic Anhydrase Inhibitors and Epilepsy: State of the Art and Future Perspectives
Ciccone, L., Cerri, C., Nencetti, S., & Orlandini, E. (2021) · Molecules · doi:10.3390/molecules26216380 · Cited by 98
Dancing partners at the synapse: auxiliary subunits that shape kainate receptor function
Copits, B. A., & Swanson, G. T. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3335 · Cited by 97
Wang, X., & Zheng, W. (2019) · The FASEB Journal · doi:10.1096/fj.201801751r · Cited by 97
Neurosteroid Actions in Memory and Neurologic/Neuropsychiatric Disorders
Ratner, M. H., Kumaresan, V., & Farb, D. H. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00169 · Cited by 96
Modulation of Synaptic Plasticity by Glutamatergic Gliotransmission: A Modeling Study
Pittà, M. D., & Brunel, N. (2016) · Neural Plasticity · doi:10.1155/2016/7607924 · Cited by 98
Bal‐Price, A., Lein, P. J., Keil, K. P., Sethi, S., Shafer, T. J., Barenys, M., Fritsche, E., Sachana, M., & Meek, M. E. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.05.010 · Cited by 100
Role of Palmitoylation of Postsynaptic Proteins in Promoting Synaptic Plasticity
Matt, L., Kim, K., Chowdhury, D., & Hell, J. W. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00008 · Cited by 96
Glutamine Metabolism in Brain Tumors
Natarajan, S. K., & Venneti, S. (2019) · Cancers · doi:10.3390/cancers11111628 · Cited by 99
NMDARs in Cell Survival and Death: Implications in Stroke Pathogenesis and Treatment
Ge, Y., Chen, W., Axerio-Cilies, P., & Wang, Y. T. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.03.001 · Cited by 97
Mira, R. G., & Cerpa, W. F. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00924-0 · Cited by 98
Exciting Times for Pancreatic Islets: Glutamate Signaling in Endocrine Cells
Otter, S., & Lammert, E. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.12.004 · Cited by 103
The σ-1 Receptor Interacts Directly with GluN1 But Not GluN2A in the GluN1/GluN2A NMDA Receptor
Balasuriya, D., Stewart, A. P., & Edwardson, J. M. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3360-13.2013 · Cited by 95
Hansen, K. B., Tajima, N., Risgaard, R., Perszyk, R. E., Jørgensen, L. M., Vance, K. M., Ogden, K. K., Clausen, R. P., Furukawa, H., & Traynelis, S. F. (2013) · Molecular Pharmacology · doi:10.1124/mol.113.085803 · Cited by 95
Self-citationCalpains and neuronal damage in the ischemic brain: The swiss knife in synaptic injury
Curcio, M., Salazar, I. L., Mele, M., Canzoniero, L. M. T., & Duarte, C. B. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.001 · Cited by 99
Anti-NMDA Receptor Encephalitis: Clinical Features and Basic Mechanisms
Lynch, D. R., Rattelle, A., Dong, Y., Roslin, K., Gleichman, A. J., & Panzer, J. A. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.08.005 · Cited by 95
Torres, L., Robinson, S.-A., Kim, D.-G., Yan, A., Cleland, T. A., & Bynoe, M. S. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1086-8 · Cited by 97
A review on ferulic acid and analogs based scaffolds for the management of Alzheimer’s disease
Singh, Y. P., Rai, H., Singh, G., Singh, G. K., Mishra, S. K., Kumar, S., Srikrishna, S., & Modi, G. P. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113278 · Cited by 98
Interdomain movements in metabotropic glutamate receptor activation
Huang, S., Cao, J., Jiang, M., Labesse, G., Liu, J., Pin, J., & Rondard, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107775108 · Cited by 95
Glutamatergic Mechanisms in Glioblastoma and Tumor-Associated Epilepsy
Lange, F., Hörnschemeyer, M. F., & Kirschstein, T. (2021) · Cells · doi:10.3390/cells10051226 · Cited by 102
Martins, D., Giacomel, A., Williams, S., Turkheimer, F., Dipasquale, O., & Veronese, M. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110173 · Cited by 97
Cole, J., Sohn, M. N., Harris, A. D., Bray, S. L., Patten, S. B., & McGirr, A. (2022) · JAMA Psychiatry · doi:10.1001/jamapsychiatry.2022.3255 · Cited by 93
Frega, M., Pasquale, V., Tedesco, M., Marcoli, M., Contestabile, A., Nanni, M., Bonzano, L., Maura, G., & Chiappalone, M. (2011) · Neurotoxicology and Teratology · doi:10.1016/j.ntt.2011.08.001 · Cited by 93
Alfieri, A., Doccula, F. G., Pederzoli, R., Grenzi, M., Bonza, M. C., Luoni, L., Candeo, A., Romano-Armada, N., Barbiroli, A. G., Valentini, G., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905142117 · Cited by 93
AMPA receptor potentiators: from drug design to cognitive enhancement
Partin, K. M. (2014) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2014.11.002 · Cited by 93
Cahill, E., Pascoli, V., Trifilieff, P., Savoldi, D., Kappès, V., Lüscher, C., Caboche, J., & Vanhoutte, P. (2014) · Molecular Psychiatry · doi:10.1038/mp.2014.73 · Cited by 92
Ohba, C., Shiina, M., Tohyama, J., Haginoya, K., Lerman‐Sagie, T., Okamoto, N., Blumkin, L., Lev, D., Mukaida, S., Nozaki, F., et al. (2015) · Epilepsia · doi:10.1111/epi.12987 · Cited by 92
Mechanical coupling maintains the fidelity of NMDA receptor–mediated currents
Kazi, R., Dai, J., Sweeney, C., Zhou, H., & Wollmuth, L. P. (2014) · Nature Neuroscience · doi:10.1038/nn.3724 · Cited by 92
Self-citationA Cold-Sensing Receptor Encoded by a Glutamate Receptor Gene
Gong, J., Liu, J., Ronan, E. A., He, F., Cai, W., Fatima, M., Zhang, W., Lee, H. K., Li, Z., Kim, G.-H., et al. (2019) · Cell · doi:10.1016/j.cell.2019.07.034 · Cited by 92
Fossati, M., Assendorp, N., Gemin, O., Colasse, S., Dingli, F., Arras, G., Loew, D., & Charrier, C. (2019) · Neuron · doi:10.1016/j.neuron.2019.09.027 · Cited by 102
Fehrentz, T., Schönberger, M., & Trauner, D. H. (2011) · Angewandte Chemie · doi:10.1002/ange.201103236 · Cited by 92
Monaghan, D. T., Irvine, M. W., Costa, B. M., Fang, G., & Jane, D. E. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.01.004 · Cited by 97
Bøttger, P., Glerup, S., Gesslein, B., Illarionova, N. B., Isaksen, T. J., Heuck, A., Clausen, B. H., Füchtbauer, E., Gramsbergen, J. B., Gunnarson, E., et al. (2016) · Scientific Reports · doi:10.1038/srep22047 · Cited by 92
NMDA Receptor Internalization by Autoantibodies: A Reversible Mechanism Underlying Psychosis?
Masdeu, J. C., Dalmau, J. O., & Berman, K. F. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.006 · Cited by 92
Addis, L., Virdee, J. K., Vidler, L. R., Collier, D. A., Pal, D. K., & Ursu, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-00115-w · Cited by 92
Role of glia in developmental synapse formation
Allen, N. J. (2013) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.06.004 · Cited by 95
Ionic mechanisms in pancreatic β cell signaling
Yang, S. N., Shi, Y., Yang, G., Li, Y., Yu, J. H., & Berggren, P. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1680-6 · Cited by 92
24(S)-Hydroxycholesterol as a Modulator of Neuronal Signaling and Survival
Sun, M., Linsenbardt, A. J., Emnett, C. M., Eisenman, L. N., Izumi, Y., Zorumski, C. F., & Mennerick, S. J. (2015) · The Neuroscientist · doi:10.1177/1073858414568122 · Cited by 94
Roles of subunit phosphorylation in regulating glutamate receptor function
Wang, J. Q., Guo, M., Jin, D.-Z., Xue, B., Fibuch, E. E., & Mao, L. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.11.019 · Cited by 91
Diverse modes of NMDA receptor positive allosteric modulation: Mechanisms and consequences
Hackos, D. H., & Hanson, J. E. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.07.037 · Cited by 98
Amidfar, M., Woelfer, M., Réus, G. Z., Quevedo, J., Walter, M., & Kim, Y. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.109668 · Cited by 95
Cholesterol modulates presynaptic and postsynaptic properties of excitatory synaptic transmission
Korinek, M., Gonzalez-Gonzalez, I. M., Smejkalova, T., Hajdukovic, D., Skrenkova, K., Krusek, J., Horak, M., & Vyklicky, L. (2020) · Scientific Reports · doi:10.1038/s41598-020-69454-5 · Cited by 93
Therapeutic Targeting of α7 Nicotinic Acetylcholine Receptors
Papke, R. L., & Horenstein, N. A. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000097 · Cited by 92
Subsynaptic positioning of AMPARs by LRRTM2 controls synaptic strength
Ramsey, A. M., Tang, A., LeGates, T. A., Gou, X., Carbone, B. E., Thompson, S. M., Biederer, T., & Blanpied, T. A. (2021) · Science Advances · doi:10.1126/sciadv.abf3126 · Cited by 90
Structural Basis of the Proton Sensitivity of Human GluN1-GluN2A NMDA Receptors
Zhang, J., Chang, S., Xu, P., Miao, M., Wu, H., Zhang, Y., Zhang, T., Wang, H., Zhang, J., Xie, C., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.071 · Cited by 93
Roman, J. Y. M., & González, C. C. (2024) · Neuroprotection/Neuroprotection (Chichester, England. Print) · doi:10.1002/nep3.46 · Cited by 90
Assembly of AMPA receptors: mechanisms and regulation
Gan, Q., Salussolia, C. L., & Wollmuth, L. P. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.273755 · Cited by 97
Self-citationStructural Insights into Competitive Antagonism in NMDA Receptors
Jespersen, A., Tajima, N., Fernández‐Cuervo, G., Garnier‐Amblard, E. C., & Furukawa, H. (2014) · Neuron · doi:10.1016/j.neuron.2013.11.033 · Cited by 90
Novel treatment options for epilepsy: Focus on perampanel
Franco, V., Crema, F., Iudice, A., Zaccara, G., & Grillo, E. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.12.006 · Cited by 90
Reijntjes, D. O. J., & Pyott, S. J. (2016) · Hearing Research · doi:10.1016/j.heares.2016.03.011 · Cited by 90
Gu, X., Mao, X., Lussier, M. P., Hutchison, M. A., Zhou, L., Hamra, F. K., Roche, K. W., & Lü, W. (2016) · Nature Communications · doi:10.1038/ncomms10873 · Cited by 92
N-Glycosylation in Regulation of the Nervous System
Scott, H. A., & Panin, V. M. (2014) · Advances in neurobiology · doi:10.1007/978-1-4939-1154-7_17 · Cited by 92
An ER Assembly Line of AMPA-Receptors Controls Excitatory Neurotransmission and Its Plasticity
Schwenk, J., Boudkkazi, S., Kocylowski, M. K., Bréchet, A., Zolles, G., Bus, T., Costa, K. M., Kollewe, A., Jordan, J., Bank, J., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.08.033 · Cited by 93
Koh, W., Park, M., Chun, Y. E., Lee, J., Shim, H. S., Park, M. G., Kim, S., Sa, M., Joo, J., Kang, H., et al. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2021.10.012 · Cited by 91
Mignogna, M. L., Giannandrea, M., Gurgone, A., Fanelli, F., Raimondi, F., Mapelli, L., Bassani, S., Fang, H., van Anken, E., Alessio, M., et al. (2015) · Nature Communications · doi:10.1038/ncomms7504 · Cited by 92
Zinc in the Monoaminergic Theory of Depression: Its Relationship to Neural Plasticity
Doboszewska, U., Właź, P., Nowak, G., Radziwoń-Zaleska, M., Cui, R., & Młyniec, K. (2017) · Neural Plasticity · doi:10.1155/2017/3682752 · Cited by 90
Harvey, B. H., & Shahid, M. (2011) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2011.06.014 · Cited by 90
Nasir, M., Trujillo, D., Levine, J. L. S., Dwyer, J. B., Rupp, Z. W., & Bloch, M. H. (2020) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2020.548505 · Cited by 94
Controlling NMDA Receptor Subunit Composition Using Ectopic Retention Signals
Stroebel, D., Carvalho, S., Grand, T., Zhu, S., & Paoletti, P. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2736-14.2014 · Cited by 88
Structure and symmetry inform gating principles of ionotropic glutamate receptors
Zhu, S., & Gouaux, E. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.08.034 · Cited by 88
Disrupted Ionic Homeostasis in Ischemic Stroke and New Therapeutic Targets
Hu, H., & Song, M. (2017) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2017.09.011 · Cited by 88
Akgül, G., & McBain, C. J. (2016) · The Journal of Physiology · doi:10.1113/jp271764 · Cited by 87
Self-citationKetamine and the Future of Rapid-Acting Antidepressants
Riggs, L. M., & Gould, T. D. (2021) · Annual Review of Clinical Psychology · doi:10.1146/annurev-clinpsy-072120-014126 · Cited by 87
A structural biology perspective on NMDA receptor pharmacology and function
Regan, M. C., Hernandez, A. R., & Furukawa, H. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.07.012 · Cited by 92
Allosteric Modulators for the Treatment of Schizophrenia: Targeting Glutamatergic Networks
Menniti, F. S., Lindsley, C. W., Conn, P. J., Pandit, J., Zagouras, P., & Volkmann, R. A. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611313010005 · Cited by 87
Self-citationSex differences in the glutamate system: Implications for addiction
Giacometti, L. L., & Barker, J. M. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.03.010 · Cited by 92
Emerging structural insights into the function of ionotropic glutamate receptors
Karakaş, E., Regan, M. C., & Furukawa, H. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.04.002 · Cited by 94
Modulation of Central Synapses by Astrocyte-Released ATP and Postsynaptic P2X Receptors
Boué‐Grabot, É., & Pankratov, Y. (2017) · Neural Plasticity · doi:10.1155/2017/9454275 · Cited by 94
Hanson, J. E., Ma, K., Elstrott, J., Weber, M., Saillet, S., Khan, A. S., Simms, J. A., Liu, B., Kim, T. A., Yu, G.-Q., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.030 · Cited by 91
Pannexin‐1 in the CNS: Emerging concepts in health and disease
Yeung, A. K., Patil, C. S., & Jackson, M. F. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15004 · Cited by 90
Fyn Tyrosine Kinase as Harmonizing Factor in Neuronal Functions and Dysfunctions
Matrone, C., Petrillo, F., Nasso, R., & Ferretti, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124444 · Cited by 87
Ghatak, S., Talantova, M. V., McKercher, S. R., & Lipton, S. A. (2020) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-032320-015420 · Cited by 90
The tripartite glutamatergic synapse
Lalo, U., Koh, W., Lee, C. J., & Pankratov, Y. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108758 · Cited by 87
Mosley, C. A., Acker, T. M., Hansen, K. B., Mullasseril, P., Andersen, K. T., Le, P., Vellano, K. M., Bräuner‐Osborne, H., Liotta, D. C., & Traynelis, S. F. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100027p · Cited by 86
Self-citationMakhro, A., Hänggi, P., Goede, J. S., Wang, J., Brüggemann, A., Gassmann, M., Schmugge, M., Kaestner, L., Speer, O., & Bogdanova, A. Y. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00031.2013 · Cited by 86
Willard, S. S., & Koochekpour, S. (2013) · International Journal of Biological Sciences · doi:10.7150/ijbs.6475 · Cited by 86
Glutamate in peripheral organs: Biology and pharmacology
Du, J., Li, X., & Li, Y. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.05.009 · Cited by 86
GRIN1 mutation associated with intellectual disability alters NMDA receptor trafficking and function
Chen, W., Shieh, C., Swanger, S. A., Tankovic, A., Au, M., McGuire, M., Tagliati, M., Graham, J. M., Madan‐Khetarpal, S., Traynelis, S. F., et al. (2017) · Journal of Human Genetics · doi:10.1038/jhg.2017.19 · Cited by 86
Self-citationShi, Z., Zhu, L., Li, T., Tang, X., Xiang, Y., Han, X., Xia, L., Zeng, L., Nie, J., Huang, Y., et al. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00288 · Cited by 86
A comprehensive description of GluN2B-selective N-methyl-D-aspartate (NMDA) receptor antagonists
Liu, W., Jiang, X., Zu, Y., Yue, Y., Liu, Y., Sun, X., Xu, Z., Ding, H., & Zhao, Q. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112447 · Cited by 87
Cheng, Y., Lin, C., & Lane, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052283 · Cited by 89
Different oxysterols have opposing actions at N-methyl-d-aspartate receptors
Linsenbardt, A. J., Taylor, A., Emnett, C. M., Doherty, J., Krishnan, K., Covey, D. F., Paul, S. M., Zorumski, C. F., & Mennerick, S. J. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.05.027 · Cited by 85
Long-term potentiation in cultured hippocampal neurons
Molnár, E. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.07.017 · Cited by 95
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
