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
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 701–800 of 1,014
NADPH Oxidase-2: Linking Glucose, Acidosis, and Excitotoxicity in Stroke
Brennan, A., Won, S. J., & Swanson, R. A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5767 · Cited by 53
Vyklický, V., Krausová, B. H., Černý, J., Balík, A., Zapotocky, M., Novotný, M., Hemelíková, K., Smejkalová, T., Kaniaková, M., Kořı́nek, M., et al. (2015) · Scientific Reports · doi:10.1038/srep10935 · Cited by 53
Lessons from crystal structures of kainate receptors
Møllerud, S., Frydenvang, K., Pickering, D. S., & Kastrup, J. S. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.05.014 · Cited by 53
Sun, W., Hansen, K. B., & Jahr, C. E. (2017) · Neuron · doi:10.1016/j.neuron.2017.03.018 · Cited by 54
Self-citationXie, J., Chen, S.-R., Chen, H., & Pan, H. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.06.027 · Cited by 53
Camp, C. R., & Yuan, H. (2019) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2019.12.007 · Cited by 54
Self-citationNeurobiology of alcohol seeking behavior
Domi, E., Domi, A., Adermark, L., Heilig, M. A., & Augier, E. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15343 · Cited by 53
Scribble1/AP2 complex coordinates NMDA receptor endocytic recycling
Piguel, N. H., Fievre, S., Blanc, J.-M., Carta, M., Moreau, M. M., Moutin, E., Pinheiro, V. L., Medina, C., Ezan, J., Lasvaux, L., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.017 · Cited by 52
Encephalitis with Autoantibodies against the Glutamate Kainate Receptors GluK2
Landa, J., Guasp, M., Míguez‐Cabello, F., Guimarães, J., Mishima, T., Oda, F., Zipp, F., Krajinović, V., Fuhr, P., Honnorat, J., et al. (2021) · Annals of Neurology · doi:10.1002/ana.26098 · Cited by 52
Biotic and Abiotic Stresses Activate Different Ca2+ Permeable Channels in Arabidopsis
Cao, X., Jiang, Z., Yi, Y.-Y., Yang, Y., Ke, L., Pei, Z., & Zhu, S. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00083 · Cited by 52
Molecular Mechanism of AMPA Receptor Modulation by TARP/Stargazin
Ben-Yaacov, A., Gillor, M., Haham, T., Parsai, A., Qneibi, M., & Stern-Bach, Y. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.032 · Cited by 52
Xu, B., Liu, F., Liu, Q., Shi, T., Wang, Z., Wu, N., Xu, X., Li, L., Fan, X., Yu, L., et al. (2020) · Journal of Gastrointestinal Oncology · doi:10.21037/jgo-20-344 · Cited by 52
Role of GluK1 Kainate Receptors in Seizures, Epileptic Discharges, and Epileptogenesis
Fritsch, B., Reis, J., Ga̧sior, M., Kaminski, R. M., & Rogawski, M. A. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.5307-13.2014 · Cited by 52
PKC phosphorylates GluA1-Ser831 to enhance AMPA receptor conductance
Jenkins, M. A., & Traynelis, S. F. (2012) · Channels · doi:10.4161/chan.18648 · Cited by 52
Self-citationLutzu, S., & Castillo, P. E. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.02.019 · Cited by 54
Regulation of microglia by glutamate and its signal pathway in neurodegenerative diseases
Zhang, X., Wang, D., Zhang, B., Zhu, J., Zhou, Z., & Cui, L. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.04.001 · Cited by 53
Ismail, V., Zachariassen, L. G., Godwin, A., Sahakian, M., Ellard, S., Stals, K. L., Baple, E. L., Brown, K. T., Foulds, N. C., Wheway, G., et al. (2022) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2022.05.009 · Cited by 53
The unique contribution of ion channels to platelet and megakaryocyte function
Mahaut‐Smith, M. P. (2012) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2012.04837.x · Cited by 51
Asynchronous Movements Prior to Pore Opening in NMDA Receptors
Kazi, R., Gan, Q., Talukder, I., Markowitz, M., Salussolia, C. L., & Wollmuth, L. P. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5780-12.2013 · Cited by 51
Self-citationCottone, P., Iemolo, A., Narayan, A. R., Kwak, J., Momaney, D., & Sabino, V. (2012) · Psychopharmacology · doi:10.1007/s00213-012-2898-3 · Cited by 51
Pedrazzi, M., Averna, M., Sparatore, B., Patrone, M., Salamino, F., Marcoli, M., Maura, G., Cervetto, C., Frattaroli, D., Pontremoli, S., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044518 · Cited by 51
Pannexin channels and ischaemia
Thompson, R. J. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.282426 · Cited by 51
Cervelli, M., Bellavia, G., D’Amelio, M., Cavallucci, V., Moreno, S., Berger, J., Nardacci, R., Marcoli, M., Maura, G., Piacentini, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064810 · Cited by 51
Lind, G. E., Mou, T., Tamborini, L., Pomper, M. G., Micheli, C. D., Conti, P., Pinto, A., & Hansen, K. B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707752114 · Cited by 51
Self-citationEnhancing Action of Positive Allosteric Modulators through the Design of Dimeric Compounds
Drapier, T., Geubelle, P., Bouckaert, C., Nielsen, L., Laulumaa, S., Goffin, E., Dilly, S., Francotte, P., Hanson, J., Pochet, L., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00250 · Cited by 51
Okada, M., Fukuyama, K., Kawano, Y., Shiroyama, T., & Ueda, Y. (2019) · Pharmacology Research & Perspectives · doi:10.1002/prp2.457 · Cited by 51
The role of melatonin in targeting cell signaling pathways in neurodegeneration
Shukla, M., Chinchalongporn, V., Govitrapong, P., & Reiter, R. J. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14005 · Cited by 53
Consequences of NMDA Receptor Deficiency Can Be Rescued in the Adult Brain
Mielnik, C. A., Binko, M. A., Chen, Y., Funk, A. J., Johansson, E. M., Intson, K., Sivananthan, N., Islam, R., Milenkovic, M., Horsfall, W., et al. (2018) · Molecular Psychiatry · doi:10.1038/s41380-020-00859-4 · Cited by 56
Eltokhi, A., Santuy, A., Merchán-Pérez, Á., & Sprengel, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010059 · Cited by 54
Glycine agonism in ionotropic glutamate receptors
Stroebel, D., Mony, L., & Paoletti, P. (2021) · Neuropharmacology · doi:10.1016/j.neuropharm.2021.108631 · Cited by 51
Zhou, M., Chen, S., Wang, L., Huang, Y., Deng, M., Zhang, J., Zhang, J., Chen, H., Yan, J., & Pan, H. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0757-21.2021 · Cited by 53
Structural biology of glutamate receptor ion channel complexes
Mayer, M. L. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.07.002 · Cited by 50
Lituma, P. J., Kwon, H., Alviña, K., Luján, R., & Castillo, P. E. (2021) · eLife · doi:10.7554/elife.66612 · Cited by 51
Guha, S., & Majumder, K. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c01712 · Cited by 50
Teng, L., Meng, Q., Lü, J., Xie, J., Wang, Z., Liu, Y., & Wang, D. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.2289 · Cited by 50
Wildburger, N. C., & Laezza, F. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00080 · Cited by 52
Analytical Approaches for Studying Transporters, Channels and Porins
Robertson, J. W. F., Kasianowicz, J. J., & Banerjee, S. (2012) · Chemical Reviews · doi:10.1021/cr300317z · Cited by 50
Homeostatic synaptic scaling: molecular regulators of synaptic AMPA-type glutamate receptors
Chowdhury, D., & Hell, J. W. (2018) · F1000Research · doi:10.12688/f1000research.13561.1 · Cited by 50
Amin, J. B., Leng, X., Gochman, A., Zhou, H., & Wollmuth, L. P. (2018) · Nature Communications · doi:10.1038/s41467-018-06145-w · Cited by 52
Self-citationModifications of Plasma Membrane Organization in Cancer Cells for Targeted Therapy
Choromańska, A., Chwiłkowska, A., Kulbacka, J., Baczyńska, D., Rembiałkowska, N., Szewczyk, A., Michel, O., Gajewska-Naryniecka, A., Przystupski, D., & Saczko, J. (2021) · Molecules · doi:10.3390/molecules26071850 · Cited by 53
Diversity in AMPA receptor complexes in the brain
Jacobi, E., & von Engelhardt, J. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.03.001 · Cited by 50
Hussein, Y., Tripathi, U., Choudhary, A., Nayak, R., Peles, D., Rosh, I., Rabinski, T., Djamus, J., Vatine, G. D., Spiegel, R., et al. (2023) · Translational Psychiatry · doi:10.1038/s41398-023-02535-x · Cited by 54
Jin, D., Guo, M., Xue, B., Mao, L., & Wang, J. Q. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12434 · Cited by 49
Ran, I., Gkogkas, C. G., Vasuta, C., Tartas, M., Khoutorsky, A., Laplante, I., Parsyan, A. E., Nevarko, T., Sonenberg, N., & Lacaille, J. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3264-12.2013 · Cited by 50
Mapping the Binding of GluN2B-Selective N-Methyl-d-aspartate Receptor Negative Allosteric Modulators
Burger, P. B., Yuan, H., Karakaş, E., Geballe, M. T., Furukawa, H., Liotta, D. C., Snyder, J. P., & Traynelis, S. F. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.078568 · Cited by 50
Self-citationMetabotropic Glutamate Receptors in Central Nervous System Diseases
Golubeva, A. V., Moloney, R. D., O’Connor, R. M., Dinan, T. G., & Cryan, J. F. (2016) · Current Drug Targets · doi:10.2174/1389450116666150316224011 · Cited by 51
Investigational NMDA receptor modulators for depression
Szewczyk, B., Pałucha-Poniewiera, A., Poleszak, E., Pilc, A., & Nowak, G. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2012.638916 · Cited by 50
Vyklický, V., Smejkalová, T., Krausová, B. H., Balík, A., Kořínek, M., Borovská, J., Hořák, M., Chvojková, M., Kletečková, L., Valeš, K., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3181-15.2016 · Cited by 49
Ionotropic glutamate receptors: Which ones, when, and where in the mammalian neocortex
Hadzic, M., Jack, A., & Wahle, P. (2017) · Journal of Comparative Neurology · doi:10.1002/cne.24103 · Cited by 53
Alsaad, H. A., DeKorver, N. W., Mao, Z., Dravid, S. M., Arikkath, J., & Monaghan, D. T. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2526-7 · Cited by 52
Grenzi, M., Bonza, M. C., Alfieri, A., & Costa, A. (2020) · New Phytologist · doi:10.1111/nph.17034 · Cited by 49
N-methyl-d-aspartate receptors amplify activation and aggregation of human platelets
Kalev‐Zylinska, M. L., Green, T. N., Morel‐Kopp, M., Sun, P. P., Park, Y. E., Lasham, A., During, M. J., & Wård, C. (2014) · Thrombosis Research · doi:10.1016/j.thromres.2014.02.011 · Cited by 52
Synapse‐specific expression of calcium‐permeable AMPA receptors in neocortical layer 5
Lalanne, T., Oyrer, J., Mancino, A. S., Gregor, E., Chung, A. J., Huynh, L., Burwell, S., Maheux, J., Farrant, M., & Sjöström, P. J. (2015) · The Journal of Physiology · doi:10.1113/jp271394 · Cited by 49
Perampanel Inhibition of AMPA Receptor Currents in Cultured Hippocampal Neurons
Chen, C.-Y., Matt, L., Hell, J. W., & Rogawski, M. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108021 · Cited by 48
Glutamate Transporters EAAT4 and EAAT5 Are Expressed in Vestibular Hair Cells and Calyx Endings
Dalet, A., Bonsacquet, J., Gaboyard-Niay, S., Calin‐Jageman, I. E., Chidavaenzi, R. L., Ventéo, S., Desmadryl, G., Goldberg, J. M., Lysakowski, A., & Chabbert, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046261 · Cited by 49
Glutamate Receptor Antagonists in the Management of Migraine
Chan, K. Y., & MaassenVanDenBrink, A. (2014) · Drugs · doi:10.1007/s40265-014-0262-0 · Cited by 48
Soto, D., Coombs, I. D., Gratacòs‐Batlle, E., Farrant, M., & Cull-Candy, S. G. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0383-14.2014 · Cited by 49
Assembly Stoichiometry of the GluK2/GluK5 Kainate Receptor Complex
Reiner, A., Arant, R. J., & Isacoff, E. Y. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.01.003 · Cited by 48
Local constraints in either the GluN1 or GluN2 subunit equally impair NMDA receptor pore opening
Talukder, I., & Wollmuth, L. P. (2011) · The Journal of General Physiology · doi:10.1085/jgp.201110623 · Cited by 48
Self-citationRegulation of GABAergic synapse development by postsynaptic membrane proteins
Lü, W., Bromley‐Coolidge, S., & Li, J. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.07.004 · Cited by 48
Blunted mGluR Activation Disinhibits Striatopallidal Transmission in Parkinsonian Mice
Cui, Q., Pitt, J. E., Pamukcu, A., Poulin, J.-F., Mabrouk, O. S., Fiske, M. P., Fan, I. B., Augustine, E. C., Young, K. A., Kennedy, R. T., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.087 · Cited by 50
Enhancing NMDA Receptor Function: Recent Progress on Allosteric Modulators
Yao, L., & Zhou, Q. (2017) · Neural Plasticity · doi:10.1155/2017/2875904 · Cited by 50
A gain-of-function mutation in the GRIK2 gene causes neurodevelopmental deficits
Guzmán, Y. F., Ramsey, K. M., Stolz, J. R., Craig, D. W., Huentelman, M., Narayanan, V., & Swanson, G. T. (2017) · Neurology Genetics · doi:10.1212/nxg.0000000000000129 · Cited by 48
From direct to indirect lithium targets: a comprehensive review of omics data
Roux-Rouquié, M., & Dosseto, A. (2017) · Metallomics · doi:10.1039/c7mt00203c · Cited by 50
Modulation of Glycine-Mediated Spinal Neurotransmission for the Treatment of Chronic Pain
Cioffi, C. L. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00956 · Cited by 52
From bedside‐to‐bench: What disease‐associated variants are teaching us about the NMDA receptor
Amin, J. B., Moody, G. R., & Wollmuth, L. P. (2020) · The Journal of Physiology · doi:10.1113/jp278705 · Cited by 52
Self-citationArchitecture and structural dynamics of the heteromeric GluK2/K5 kainate receptor
Khanra, N., Brown, P. M. G. E., Perozzo, A. M., Bowie, D., & Meyerson, J. R. (2021) · eLife · doi:10.7554/elife.66097 · Cited by 49
Anti-Alpha-Amino-3-Hydroxy-5-Methyl-4-Isoxazolepropionic Acid Receptor Encephalitis: A Review
Zhang, T., Cai, M., Zheng, Y., Lai, Q., Shen, C., Qiao, S., & Zhang, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.652820 · Cited by 50
Girault, J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00006-7 · Cited by 55
Vieira, M. M., Jeong, J., & Roche, K. W. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.03.001 · Cited by 51
Delaney, A., Sedlak, P. L., Autuori, E., Power, J., & Sah, P. (2012) · Journal of Neurophysiology · doi:10.1152/jn.00176.2012 · Cited by 48
Ionotropic Glutamate Receptors: Regulation by G-Protein-Coupled Receptors
Rojas, A., & Dingledine, R. J. (2013) · Molecular Pharmacology · doi:10.1124/mol.112.083352 · Cited by 47
Self-citationA Molecular Determinant of Subtype-Specific Desensitization in Ionotropic Glutamate Receptors
Alsaloum, M., Kazi, R., Gan, Q., Amin, J. B., & Wollmuth, L. P. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2667-15.2016 · Cited by 47
Self-citationZimmerman, S. S., Khatri, A., Garnier‐Amblard, E. C., Mullasseril, P., Kurtkaya, N. L., Gyoneva, S., Hansen, K. B., Traynelis, S. F., & Liotta, D. C. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401695d · Cited by 47
Self-citationGažová, Z., Soukup, O., Šepsová, V., Šipošová, K., Drtinová, L., Jost, P., Špilovská, K., Korábečný, J., Nepovimová, E., Fedunová, D., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.020 · Cited by 47
Breakthroughs in neuroactive steroid drug discovery
Blanco, M.-J., La, D. S., Coughlin, Q., Newman, C. A., Griffin, A. M., Harrison, B. L., & Salituro, F. G. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.11.043 · Cited by 47
Afonso, P. M., Luca, P. D., Carvalho, R. D. S., Cortes, L., Pinheiro, P. S., Oliveiros, B., Almeida, R. D., Mele, M., & Duarte, C. B. (2019) · Science Signaling · doi:10.1126/scisignal.aav3577 · Cited by 49
Dysregulation of AMPA receptor subunit expression in sporadic ALS post‐mortem brain
Gregory, J. M., Livesey, M. R., McDade, K., Selvaraj, B. T., Barton, S. K., Chandran, S., & Smith, C. (2019) · The Journal of Pathology · doi:10.1002/path.5351 · Cited by 47
Li, L., Chen, S., Zhou, M., Wang, L., Li, D., Chen, H., Lee, G., Jayaraman, V., & Pan, H. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109396 · Cited by 52
Balderas, P. M. D. O., & Aguilera, P. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126314 · Cited by 50
Wang, Y., Zhang, N., Liu, L., Jiang, H., Hu, D., Wang, Z., Chen, N., & Zhang, Y. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.01.024 · Cited by 50
Structural insights into NMDA receptor pharmacology
Zhou, C., & Tajima, N. (2023) · Biochemical Society Transactions · doi:10.1042/bst20230122 · Cited by 47
Folate, Homocysteine and the Cardiac Neural Crest
Rosenquist, T. H. (2013) · Developmental Dynamics · doi:10.1002/dvdy.23922 · Cited by 46
Targeting α-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate receptors in epilepsy
Citraro, R., Aiello, R., Franco, V., Sarro, G. D., & Russo, E. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.874416 · Cited by 47
NMDA receptors mediate contractile responses in human airway smooth muscle cells
Anaparti, V., Ilarraza, R., Orihara, K., Stelmack, G. L., Ojo, O. O., Mahood, T. H., Unruh, H. W., Halayko, A. J., & Moqbel, R. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00402.2014 · Cited by 46
Ramaswamy, S. S., Cooper, D. R., Poddar, N. K., MacLean, D. M., Rambhadran, A., Taylor, J., Uhm, H., Landes, C. F., & Jayaraman, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371815 · Cited by 46
Choi, U. B., Xiao, S., Wollmuth, L. P., & Bowen, M. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.258897 · Cited by 46
Self-citationHansen, K. B., Mullasseril, P., Dawit, S., Kurtkaya, N. L., Yuan, H., Vance, K. M., Orr, A. G., Kvist, T., Ogden, K. K., Le, P., et al. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.166256 · Cited by 46
Self-citationPossible role of hemichannels in cancer
Schalper, K. A., Carvajal‐Hausdorf, D., & Oyarzo, M. P. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00237 · Cited by 46
Modes of glutamate receptor gating
Popescu, G. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.223750 · Cited by 46
A Toolkit for Orthogonal and in vivo Optical Manipulation of Ionotropic Glutamate Receptors
Levitz, J., Popescu, A. T., Reiner, A., & Isacoff, E. Y. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00002 · Cited by 51
Acker, T. M., Khatri, A., Vance, K. M., Slabber, C. A., Bacsa, J., Snyder, J. P., Traynelis, S. F., & Liotta, D. C. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400652r · Cited by 46
Self-citationMotoneuron glutamatergic receptor expression following recovery from cervical spinal hemisection
Gransee, H. M., Porras, M. A. G., Zhan, W., Sieck, G. C., & Mantilla, C. B. (2016) · The Journal of Comparative Neurology · doi:10.1002/cne.24125 · Cited by 48
GluN2A Subunit-Containing NMDA Receptors Are the Preferential Neuronal Targets of Homocysteine
Sibarov, D. A., Abushik, P. A., Giniatullin, R. A., & Antonov, S. M. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00246 · Cited by 46
Goffin, E., Drapier, T., Larsen, A. P., Geubelle, P., Ptak, C. P., Laulumaa, S., Rovinskaja, K., Gilissen, J., Tullio, P. D., Olsen, L., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01323 · Cited by 46
A Friend or Foe: Calcineurin across the Gamut of Neurological Disorders
Saraf, J., Bhattacharya, P., Kalia, K., Borah, A., Sarmah, D., Kaur, H., Dave, K. R., & Yavagal, D. R. (2018) · ACS Central Science · doi:10.1021/acscentsci.8b00230 · Cited by 46
Hartmann, J., Münch, R. C., Freiling, R.-T., Schneider, I. C., Dreier, B., Samukange, W. T., Koch, J., Seeger, M. A., Plückthun, A., & Buchholz, C. J. (2018) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2018.07.001 · Cited by 49
Carmichael, K., Sullivan, B. T., Lopez, E., Sun, L., & Cai, H. (2021) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2021.07 · Cited by 48
Structural elements of a pH-sensitive inhibitor binding site in NMDA receptors
Regan, M. C., Zhu, Z., Yuan, H., Myers, S. J., Menaldino, D. S., Tahirovic, Y. A., Liotta, D. C., Traynelis, S. F., & Furukawa, H. (2019) · Nature Communications · doi:10.1038/s41467-019-08291-1 · Cited by 46
Self-citationKaniaková, M., Krausová, B. H., Vyklický, V., Kořı́nek, M., Hemelíková, K., Vyklický, L., & Hořák, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.339085 · Cited by 46
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
