The DOI matches its Crossref record; 2,576 of the 2,576 references it cites were found in a registry or an index.
Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels
Open accessAbstract
Many physiologic effects of l-glutamate, the major excitatory neurotransmitter in the mammalian central nervous system, are mediated via signaling by ionotropic glutamate receptors (iGluRs). These ligand-gated ion channels are critical to brain function and are centrally implicated in numerous psychiatric and neurologic disorders. There are different classes of iGluRs with a variety of receptor subtypes in each class that play distinct roles in neuronal functions. The diversity in iGluR subtypes, with their unique functional properties and physiologic roles, has motivated a large number of studies. Our understanding of receptor subtypes has advanced considerably since the first iGluR subunit gene was cloned in 1989, and the research focus has expanded to encompass facets of biology that have been recently discovered and to exploit experimental paradigms made possible by technological advances. Here, we review insights from more than 3 decades of iGluR studies with an emphasis on the progress that has occurred in the past decade. We cover structure, function, pharmacology, roles in neurophysiology, and therapeutic implications for all classes of receptors assembled from the subunits encoded by the 18 ionotropic glutamate receptor genes. SIGNIFICANCE STATEMENT: Glutamate receptors play important roles in virtually all aspects of brain function and are either involved in mediating some clinical features of neurological disease or represent a therapeutic target for treatment. Therefore, understanding the structure, function, and pharmacology of this class of receptors will advance our understanding of many aspects of brain function at molecular, cellular, and system levels and provide new opportunities to treat patients.
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 Hansen et al., 2021
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
Items 2,001–2,200 of 2,576
She, K., Ferreira, J. S., Carvalho, A. L., & Craig, A. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.345108 · Cited by 36
Zhang, X., Feng, Z., & Chergui, K. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12658 · Cited by 36
Takenouchi, T., Hashida, N., Torii, C., Kosaki, R., Takahashi, T., & Kosaki, K. (2013) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.36240 · Cited by 36
Presynaptic GluN2D receptors detect glutamate spillover and regulate cerebellar GABA release
Dubois, C., Lachamp, P. M., Sun, L., Mishina, M., & Liu, S. J. (2015) · Journal of Neurophysiology · doi:10.1152/jn.00687.2015 · Cited by 36
Presynaptic NMDA receptors: dynamics and distribution in developing axons in vitro and in vivo
Gill, I., Droubi, S., Giovedı̀, S., Fedder-Semmes, K. N., Bury, L. A. D., Bosco, F., Sceniak, M. P., Benfenati, F., & Sabo, S. L. (2014) · Journal of Cell Science · doi:10.1242/jcs.162362 · Cited by 36
Structural rearrangement of the intracellular domains during AMPA receptor activation
Zachariassen, L. G., Katchan, L., Jensen, A. G., Pickering, D. S., Plested, A. J. R., & Kristensen, A. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601747113 · Cited by 36
Wilding, T. J., Lopez, M. N., & Huettner, J. E. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0345-16.2016 · Cited by 36
Dawe, G. B., Kadir, M. F., Venskutonytė, R., Perozzo, A. M., Yan, Y., Alexander, R. P. D., Navarrete, C., Santander, E. A., Arsenault, M., Fuentes, C., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.03.046 · Cited by 36
Self-citationStructural and Functional Insights into GluK3-kainate Receptor Desensitization and Recovery
Kumari, J., Vinnakota, R., & Kumar, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-46770-z · Cited by 36
De novo partial deletion in GRID2 presenting with complicated spastic paraplegia
Maier, A., Klopocki, E., Horn, D., Tzschach, A., Holm, T., Meyer, R., & Meyer, T. (2013) · Muscle & Nerve · doi:10.1002/mus.24096 · Cited by 35
Na+/Cl- Dipole Couples Agonist Binding to Kainate Receptor Activation
Wong, A. Y. C., MacLean, D. M., & Bowie, D. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0284-07.2007 · Cited by 35
Self-citationInhibition of rat neuronal kainate receptors by cis‐unsaturated fatty acids
Wilding, T. J., Chai, Y. H., & Huettner, J. E. (1998) · The Journal of Physiology · doi:10.1111/j.1469-7793.1998.331bb.x · Cited by 35
Ahmed, A. H., Thompson, M. D., Fenwick, M. K., Romero, B., Loh, A. P., Jane, D. E., Sondermann, H., & Oswald, R. E. (2009) · Biochemistry · doi:10.1021/bi900107m · Cited by 35
Modulation of non‐NMDA receptor gating by auxiliary subunits
Howe, J. R. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.273904 · Cited by 35
Urwyler, S., Floersheim, P., Roy, B. L., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900363q · Cited by 35
Subunit Arrangement in N-Methyl-d-aspartate (NMDA) Receptors
Rambhadran, A., Gonzalez, J., & Jayaraman, V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.085035 · Cited by 35
Self-citationKvist, T., Steffensen, T. B., Greenwood, J. R., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.480210 · Cited by 35
Sirrieh, R. E., MacLean, D. M., & Jayaraman, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.649723 · Cited by 35
Self-citationBustos, F. J., Jury, N., Martínez, P., Ampuero, E., Campos, M., Abarzúa, S., Jaramillo, K., Ibing, S., Mardones, M. D., Haensgen, H., et al. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.25843 · Cited by 35
Kaniaková, M., Kletečková, L., Hemelíková, K., Holubová, K., Skřenková, K., Kořı́nek, M., Krůšek, J., Smejkalová, T., Korábečný, J., Valeš, K., et al. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.08.010 · Cited by 35
Structural and functional insights into transmembrane AMPA receptor regulatory protein complexes
Twomey, E. C., Yelshanskaya, M. V., & Sobolevsky, A. I. (2019) · The Journal of General Physiology · doi:10.1085/jgp.201812264 · Cited by 35
Self-citationConformational spread and dynamics in allostery of NMDA receptors
Durham, R. J., Paudyal, N., Carrillo, E. C., Bhatia, N. K., MacLean, D. M., Berka, V., Dolino, D. M., Gorfe, A. A., & Jayaraman, V. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1910950117 · Cited by 35
Self-citationGardoni, F., Stanic, J., Scheggia, D., Benussi, A., Borroni, B., & Luca, M. D. (2021) · Cells · doi:10.3390/cells10010077 · Cited by 35
Wild, A. R., Bollands, M., Morris, P. G., & Jones, S. (2015) · European Journal of Neuroscience · doi:10.1111/ejn.13075 · Cited by 34
Regulation of microglia by ionotropic glutamatergic and GABAergic neurotransmission
Wong, W. T., Wang, M., & Li, W. (2011) · Neuron Glia Biology · doi:10.1017/s1740925x11000123 · Cited by 34
Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation
Coombs, I. D., MacLean, D. M., Jayaraman, V., Farrant, M., & Cull-Candy, S. G. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.014 · Cited by 34
Self-citationCórdoba, M., Rodriguez, S. B., Morón, D. G., Medina, N., & Kauffman, M. (2014) · Clinical Genetics · doi:10.1111/cge.12423 · Cited by 34
Neto2-null mice have impaired GABAergic inhibition and are susceptible to seizures
Mahadevan, V., Dargaei, Z., Ivakine, E. A., Hartmann, A., Ng, D., Chevrier, J., Ormond, J., Nothwang, H. G., McInnes, R. R., & Woodin, M. A. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00368 · Cited by 34
Rossi, B., Ogden, D., Llano, I., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039983 · Cited by 34
Clarke, R. J., Glasgow, N. G., & Johnson, J. W. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3712-12.2013 · Cited by 34
Conformational Changes at the Agonist Binding Domain of the N-Methyl-d-Aspartic Acid Receptor
Rambhadran, A., Gonzalez, J., & Jayaraman, V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.224576 · Cited by 34
Self-citationPalmitoylation-dependent regulation of glutamate receptors and their PDZ domain-containing partners
Thomas, G. M., & Huganir, R. L. (2013) · Biochemical Society Transactions · doi:10.1042/bst20120223 · Cited by 34
The Role of NMDA Receptors in Neural Stem Cell Proliferation and Differentiation
Chakraborty, A., Murphy, S. K., & Coleman, N. (2017) · Stem Cells and Development · doi:10.1089/scd.2016.0325 · Cited by 34
Light‐induced regulation of ligand‐gated channel activity
Bregestovski, P. D., Maleeva, G., & Gorostiza, P. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14022 · Cited by 34
The 1980s: d-AP5, LTP and a Decade of NMDA Receptor Discoveries
Lodge, D., Watkins, J. C., Bortolotto, Z. A., Jane, D. E., & Volianskis, A. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2640-6 · Cited by 34
Regulation of glutamate receptors by striatal‐enriched tyrosine phosphatase 61 (STEP61)
Won, S., & Roche, K. W. (2021) · The Journal of Physiology · doi:10.1113/jp278703 · Cited by 34
Permeant Ion Effects on External Mg2+Block of NR1/2D NMDA Receptors
Qian, A., & Johnson, J. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3453-06.2006 · Cited by 33
Shinohara, Y. (2012) · Hippocampus · doi:10.1002/hipo.20950 · Cited by 33
Shaffer, C. L., Patel, N. C., Schwarz, J. B., Scialis, R. J., Wei, Y., Hou, X., Xie, L., Karki, K., Bryce, D. K., Osgood, S. M., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00300 · Cited by 33
Knight, H. M., WALKER, R. E., James, R., Porteous, D. J., Muir, W. J., Blackwood, D., & Pickard, B. S. (2011) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.31248 · Cited by 33
LTD expression is independent of glutamate receptor subtype
Granger, A. J., & Nicoll, R. A. (2014) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2014.00015 · Cited by 33
Gonzalez, J., Rambhadran, A., Du, M., & Jayaraman, V. (2008) · Biochemistry · doi:10.1021/bi800690b · Cited by 33
Self-citationThe role of hypernitrosylation in the pathogenesis and pathophysiology of neuroprogressive diseases
Morris, G., Walder, K. R., Carvalho, A. F., Tye, S. J., Lucas, K., Berk, M., & Maes, M. H. J. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.07.017 · Cited by 33
Influence of the intracellular GluN2 C-terminal domain on NMDA receptor function
Punnakkal, P., Jendritza, P., & Köhr, G. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.12.018 · Cited by 33
Birdsey-Benson, A., Gill, A., Henderson, L., & Madden, D. R. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4558-09.2010 · Cited by 33
Roles for short-term synaptic plasticity in behavior
Fortune, E. S., & Rose, G. J. (2002) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(03)00009-3 · Cited by 33
Ahmed, A. H., Ptak, C. P., & Oswald, R. E. (2010) · Biochemistry · doi:10.1021/bi1000678 · Cited by 33
Crabtree, J. W., Lodge, D., Bashir, Z. I., & Isaac, J. T. R. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12098 · Cited by 33
Kudová, E., Chodounská, H., Slavı́ková, B., Buděšı́nský, M., Nekardová, M., Vyklický, V., Krausová, B. H., Švehla, P., & Vyklický, L. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00570 · Cited by 33
The Good and the Bad of Glutamate Receptor RNA Editing
Filippini, A., Bonini, D., Via, L. L., & Barbon, A. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0201-z · Cited by 33
Orav, E., Atanasova, T., Shintyapina, A. B., Kesaf, S., Kokko, M., Partanen, J. M., Taira, T., & Lauri, S. E. (2017) · eNeuro · doi:10.1523/eneuro.0048-17.2017 · Cited by 33
A novel missense mutation in GRIN2A causes a nonepileptic neurodevelopmental disorder
Marmiesse, A. F., Kusumoto, H., Rekarte-García, S., Roca, I., Zhang, J., Myers, S. J., Traynelis, S. F., Couce, M. L., Gutiérrez-Solana, L. G., & Yuan, H. (2018) · Movement Disorders · doi:10.1002/mds.27315 · Cited by 33
Self-citationFredriksson, R., Sreedharan, S., Nordenankar, K., Alsiö, J., Lindberg, F. A., Hutchinson, A., Eriksson, A., Roshanbin, S., Ciuculete, D. M., Klockars, A., et al. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008455 · Cited by 33
Structural determinants of agonist-specific kinetics at the ionotropic glutamate receptor 2
Holm, M. M., Lunn, M.-L., Traynelis, S. F., Kastrup, J. S., & Egebjerg, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505522102 · Cited by 32
Self-citationLash, L. L., Sanders, J. M., Akiyama, N., Shoji, M., Postila, P. A., Pentikäinen, O. T., Sasaki, M., Sakai, R., & Swanson, G. T. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.129890 · Cited by 32
Self-citationFunctional Significance of the Kainate Receptor GluR6(M836I) Mutation that is Linked to Autism
Strutz-Seebohm, N., Korniychuk, G., Schwarz, R., Baltaev, R., Ureche, O., Mack, A., Ma, Z.-L., Hollmann, M., Lang, F., & Seebohm, G. (2006) · Cellular Physiology and Biochemistry · doi:10.1159/000097675 · Cited by 32
Mosley, C. A., Myers, S. J., Murray, E. E., Santangelo, R., Tahirovic, Y. A., Kurtkaya, N. L., Mullasseril, P., Yuan, H., Lyuboslavsky, P. N., Le, P., et al. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.05.085 · Cited by 32
Self-citationOn the role of NR3A in human NMDA receptors
Eriksson, M., Nilsson, A., Samuelsson, H., Samuelsson, E., Mo, L., Åkesson, E., Benedikz, E., & Sundström, E. (2007) · Physiology & Behavior · doi:10.1016/j.physbeh.2007.05.026 · Cited by 32
Campiani, G., Morelli, E., Nacci, V., Fattorusso, C., Ramunno, A., Novellino, E., Greenwood, J. R., Liljefors, T., Griffiths, R., Sinclair, C., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm015552m · Cited by 32
Sequerra, E. B., Goyal, R., Castro, P. A., Levin, J. B., & Borodinsky, L. N. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.2634-17.2018 · Cited by 32
Dose Timing of D -Cycloserine to Augment Exposure Therapy for Social Anxiety Disorder
Smits, J. A. J., Pollack, M. H., Rosenfield, D., Otto, M. W., Dowd, S. M., Carpenter, J. K., Dutcher, C. D., Lewis, E. M., Witcraft, S. M., Papini, S., et al. (2020) · JAMA Network Open · doi:10.1001/jamanetworkopen.2020.6777 · Cited by 32
Zhang, X.-Q., Feng, Z., & Chergui, K. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12758 · Cited by 32
Salussolia, C. L., Corrales, A., Talukder, I., Kazi, R., Akgül, G., Bowen, M. E., & Wollmuth, L. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.268839 · Cited by 32
Self-citationSaybaşılı, H., Stevens, D. R., & Haas, H. L. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12051-5 · Cited by 32
Two-component blocking kinetics of open NMDA channels by organic cations
Sobolevsky, A. I. (1999) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(98)00211-9 · Cited by 32
Self-citationLight-Induced Plasticity of Synaptic AMPA Receptor Composition in Retinal Ganglion Cells
Jones, R., Carroll, R. C., & Nawy, S. (2012) · Neuron · doi:10.1016/j.neuron.2012.05.030 · Cited by 32
Targeting AMPA Receptor Gating Processes with Allosteric Modulators and Mutations
Mitchell, N. A., & Fleck, M. W. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.095091 · Cited by 32
Malina, K. C.-K., Ganor, Y., Levite, M., & Teichberg, V. I. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9143-6 · Cited by 32
Inhibition of Presynaptic Release-Facilitatory Kainate Autoreceptors by Extracellular Cyclic GMP
Cervetto, C., Maura, G., & Marcoli, M. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.154955 · Cited by 32
Kristensen, A. S., Hansen, K. B., Naur, P., Olsen, L., Kurtkaya, N. L., Dravid, S. M., Kvist, T., Yi, F., Poehlsgaard, J., Clausen, R. P., et al. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.100909 · Cited by 32
Self-citationTamano, H., Koike, Y., Nakada, H., Shakushi, Y., & Takeda, A. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.03.003 · Cited by 32
Chue, P. S. (2012) · Current Pharmaceutical Design · doi:10.2174/138161213804805766 · Cited by 32
mGlu1 receptor canonical signaling pathway contributes to the opening of the orphan GluD2 receptor
Dadak, S., Bouquier, N., Goyet, E., Fagni, L., Lévénès, C., & Perroy, J. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.06.001 · Cited by 32
Identification and Structure-Function Study of Positive Allosteric Modulators of Kainate Receptors
Larsen, A. P., Fièvre, S., Frydenvang, K., Francotte, P., Pirotte, B., Kastrup, J. S., & Mulle, C. (2017) · Molecular Pharmacology · doi:10.1124/mol.116.107599 · Cited by 32
Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains
Zhao, H., Lomash, S., Chittori, S., et al. (2017) · eLife · doi:10.7554/elife.32056 · Cited by 32
Neurotransmitter Funneling Optimizes Glutamate Receptor Kinetics
Yu, A., Salazar, H., Plested, A. J. R., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.11.024 · Cited by 32
Stargazin and cornichon-3 relieve polyamine block of AMPA receptors by enhancing blocker permeation
Brown, P. M. G. E., McGuire, H., & Bowie, D. (2017) · The Journal of General Physiology · doi:10.1085/jgp.201711895 · Cited by 32
Self-citationRegan, M. C., & Furukawa, H. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6e7s/pdb · Cited by 32
Self-citationSchwarting, A., Möckel, T., Lütgendorf, F., et al. (2019) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2019-215098 · Cited by 32
Ca2+-Dependent Inactivation of GluN2A and GluN2B NMDA Receptors Occurs by a Common Kinetic Mechanism
Iacobucci, G. J., & Popescu, G. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.07.057 · Cited by 32
Homomeric GluA2(R) AMPA receptors can conduct when desensitized
Coombs, I. D., Soto, D., McGee, T. P., Gold, M. G., Farrant, M., & Cull-Candy, S. G. (2019) · Nature Communications · doi:10.1038/s41467-019-12280-9 · Cited by 32
Structural basis of subtype-selective competitive antagonism for GluN2C/2D-containing NMDA receptors
Wang, J. X., Irvine, M. W., Burnell, E. S., Sapkota, K., Thatcher, R. J., Li, M., Simorowski, N., Volianskis, A., Collingridge, G. L., Monaghan, D. T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14321-0 · Cited by 32
Self-citationGarst-Orozco, J., Malik, R., Lanz, T. A., Weber, M. L., Xi, H. S., Arion, D., Enwright, J. F., Lewis, D. A., O’Donnell, P., Sohal, V. S., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0233895 · Cited by 32
Silence Analysis of AMPA Receptor Mutated at the CaM-Kinase II Phosphorylation Site
Derkach, V. A. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74978-9 · Cited by 31
Distribution of Extracellular Glutamate in the Neuropil of Hippocampus
Herman, M. A., Nahir, B., & Jahr, C. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026501 · Cited by 31
Blockade of NMDA receptor channels by 9-aminoacridine and its derivatives
Barygin, O. I., Гмиро, В. Е., Kim, K. K., et al. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.12.036 · Cited by 31
A Subtype-Selective, Use-Dependent Inhibitor of Native AMPA Receptors
Nilsen, A. C., & England, P. M. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0705801 · Cited by 31
Gupta, S. C., Hillman, B. G., Prakash, A., Ugale, R. R., Stairs, D. J., & Dravid, S. M. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12197 · Cited by 31
Protons Potentiate GluN1/GluN3A Currents by Attenuating Their Desensitisation
Cummings, K. A., & Popescu, G. (2016) · Scientific Reports · doi:10.1038/srep23344 · Cited by 31
Michaëlsson, H., Andersson, M., Svensson, J., Karlsson, L., Ehn, J., Culley, G. R., Engström, A., Bergström, N., Savvidi, P., Kuhn, H. G., et al. (2018) · Acta Physiologica · doi:10.1111/apha.13211 · Cited by 31
Lee, J. H., Wei, L., Deveau, T. C., et al. (2015) · Brain Structure and Function · doi:10.1007/s00429-015-1099-3 · Cited by 31
Trafficking of Kainate Receptors
Pahl, S., Tapken, D., Haering, S., & Hollmann, M. (2014) · Membranes · doi:10.3390/membranes4030565 · Cited by 31
M�ller, E. H., Egebjerg, J., Brehm, L., Stensb�l, T. B., Johansen, T. N., Madsen, U., & Krogsgaard‐Larsen, P. (1999) · Chirality · doi:10.1002/(sici)1520-636x(1999)11:10 · Cited by 31
The unique properties of glutamate receptor channels
Sprengel, R., & Seeburg, P. H. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81420-5 · Cited by 31
Postila, P. A., Ylilauri, M., & Pentikäinen, O. T. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci2000055 · Cited by 31
A Eukaryotic Specific Transmembrane Segment is Required for Tetramerization in AMPA Receptors
Salussolia, C. L., Gan, Q., Kazi, R., Singh, P., Allopenna, J. J., Furukawa, H., & Wollmuth, L. P. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2626-12.2013 · Cited by 31
Self-citationGanor, Y., Goldberg‐Stern, H., Cohen, R., Teichberg, V. I., & Levite, M. (2014) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2014.01.005 · Cited by 31
Ward, S. E., Pennicott, L. E., & Beswick, P. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.4 · Cited by 31
Dai, J., & Zhou, H. (2014) · Structure · doi:10.1016/j.str.2014.11.012 · Cited by 31
Molecular Determinants Controlling NMDA Receptor Synaptic Incorporation
Storey, G. P., Opitz-Araya, X., & Barría, A. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5553-10.2011 · Cited by 31
Role of GluR1 in Activity-Dependent Motor System Development
Zhang, L., Schessl, J., Werner, M., Bönnemann, C. G., Xiong, G., Mojsilovic‐Petrovic, J., Zhou, W., Cohen, A. S., Seeburg, P. H., Misawa, H., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0880-08.2008 · Cited by 31
Extracellular Ca2+ ions reduce NMDA receptor conductance and gating
Maki, B. A., & Popescu, G. (2014) · The Journal of General Physiology · doi:10.1085/jgp.201411244 · Cited by 31
Smothers, C. T., & Woodward, J. J. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.109.158493 · Cited by 31
Constitutive Activation of the N-Methyl-d-aspartate Receptor via Cleft-spanning Disulfide Bonds
Blanke, M. L., & VanDongen, A. M. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709190200 · Cited by 31
Ligand-Binding Residues Integrate Affinity and Efficacy in the NMDA Receptor
Kalbaugh, T. L., VanDongen, H. M. A., & VanDongen, A. M. J. (2004) · Molecular Pharmacology · doi:10.1124/mol.66.2.209 · Cited by 31
Nayeem, N., Mayans, O. M., & Green, T. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4771-10.2011 · Cited by 31
A conserved structural mechanism of NMDA receptor inhibition: A comparison of ifenprodil and zinc
Sirrieh, R. E., MacLean, D. M., & Jayaraman, V. (2015) · The Journal of General Physiology · doi:10.1085/jgp.201511422 · Cited by 31
Self-citationMao, X., Gu, X., & Lü, W. (2016) · Journal of Neurophysiology · doi:10.1152/jn.00307.2016 · Cited by 31
Screening for AMPA receptor auxiliary subunit specific modulators
Azumaya, C. M., Days, E., Vinson, P. N., Stauffer, S. R., Sulikowski, G. A., Weaver, C. D., & Nakagawa, T. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174742 · Cited by 31
Self-citationRole of the Ion Channel Extracellular Collar in AMPA Receptor Gating
Yelshanskaya, M. V., Mesbahi‐Vasey, S., Kurnikova, M. G., & Sobolevsky, A. I. (2017) · Scientific Reports · doi:10.1038/s41598-017-01146-z · Cited by 31
Self-citationNeto1 associates with the NMDA receptor/amyloid precursor protein complex
Cousins, S. L., Innocent, N., & Stephenson, F. A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12280 · Cited by 30
A novel gene, Btcl1, encoding CUB and LDLa domains is expressed in restricted areas of mouse brain
Michishita, M., Ikeda, T., Nakashiba, T., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01035-0 · Cited by 30
Jenkins, M. A., Wells, G., Bachman, J., Snyder, J. P., Jenkins, A., Huganir, R. L., Oswald, R. E., & Traynelis, S. F. (2014) · Molecular Pharmacology · doi:10.1124/mol.113.091488 · Cited by 30
Self-citationThe NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain
Eriksson, M., Samuelsson, H., Samuelsson, E., Liu, L., McKeehan, W. L., Benedikz, E., & Sundström, E. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.179 · Cited by 30
Concanavalin‐A reports agonist‐induced conformational changes in the intact GluR6 kainate receptor
Fay, A.-M. L., & Bowie, D. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103580 · Cited by 30
Self-citationMenniti, F. S., Buchan, A. M., Chenard, B. L., Critchett, D. J., Ganong, A. H., Guanowsky, V., Seymour, P. A., & Welch, W. M. (2003) · Stroke · doi:10.1161/01.str.0000048216.90221.9c · Cited by 30
Self-citationGluN3A promotes NMDA spiking by enhancing synaptic transmission in Huntington's disease models
Mahfooz, K., Marco, S., Martínez-Turrillas, R., Raja, M. K., Pérez‐Otaño, I., & Wesseling, J. F. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.04.001 · Cited by 30
Advancing NMDA Receptor Physiology by Integrating Multiple Approaches
Zhou, H., & Wollmuth, L. P. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.001 · Cited by 30
Self-citationPochwat, B., Rafało-Ulińska, A., Domin, H., Misztak, P., Nowak, G., & Szewczyk, B. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.08.006 · Cited by 30
Glasgow, N. G., Wilcox, M. R., & Johnson, J. W. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.05.017 · Cited by 30
Kainate receptors regulate development of glutamatergic synaptic circuitry in the rodent amygdala
Ryazantseva, M., Englund, J., Shintyapina, A. B., Huupponen, J., Shteinikov, V., Pitkänen, A., Partanen, J. M., & Lauri, S. E. (2020) · eLife · doi:10.7554/elife.52798 · Cited by 30
Huettner, J. E. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.272724 · Cited by 30
Kostakis, E., Jang, M., Russek, S. J., Gibbs, T. T., & Farb, D. H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07442.x · Cited by 30
Joseph, D. J., Williams, D. J., & MacDermott, A. B. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20906 · Cited by 30
Ramos, C. I., Igiesuorobo, O., Wang, Q., & Serpe, M. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005191 · Cited by 30
Ganor, Y., Gottlieb, M., Eilam, R., et al. (2005) · Experimental Neurology · doi:10.1016/j.expneurol.2005.04.002 · Cited by 30
Ohno, T., Maeda, H., Murabe, N., Kamiyama, T., Yoshioka, N., Mishina, M., & Sakurai, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906551107 · Cited by 30
Möykkynen, T. P., Coleman, S. K., Semenov, A., & KEINÄNEN, K. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526301 · Cited by 30
CaMKII-Dependent Phosphorylation of the GTPase Rem2 Is Required to Restrict Dendritic Complexity
Ghiretti, A. E., Daman, K., Marr, M. T., & Paradis, S. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3861-12.2013 · Cited by 30
Trenité, D. G. A. K.-N., Brandt, C., Mayer, T., et al. (2015) · Epilepsia · doi:10.1111/epi.13008 · Cited by 30
GluD2 Endows Parallel Fiber–Purkinje Cell Synapses with a High Regenerative Capacity
Ichikawa, R., Sakimura, K., & Watanabe, M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0161-16.2016 · Cited by 30
Marshall, J. J., Xu, J., & Contractor, A. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.1788-17.2018 · Cited by 30
Autoantibodies against N-methyl-d-aspartate receptor 1 in health and disease
Ehrenreich, H. (2018) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000546 · Cited by 30
The LILI Motif of M3-S2 Linkers Is a Component of the NMDA Receptor Channel Gate
Ladislav, M., Černý, J., Krůšek, J., Hořák, M., Balík, A., & Vyklický, L. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00113 · Cited by 30
Salmi, M., Gallo, F. D., Minlebaev, M., Zakharov, A., Pauly, V., Perron, P., Pons-Bennaceur, A., Corby-Pellegrino, S., Aniksztejn, L., Lenck‐Santini, P., et al. (2019) · Epilepsia · doi:10.1111/epi.16060 · Cited by 30
NYX‐458 Improves Cognitive Performance in a Primate Parkinson's Disease Model
Barth, A., Schneider, J. S., Johnston, T. H., Hill, M. P., Brotchie, J. M., Moskal, J. R., & Cearley, C. N. (2020) · Movement Disorders · doi:10.1002/mds.27962 · Cited by 30
AMPA and NMDA Receptor Trafficking at Cocaine-Generated Synapses
Wang, Y. Q., Huang, Y. H., Balakrishnan, S., Liu, L., Wang, Y. T., Nestler, E. J., Schlüter, O. M., & Dong, Y. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.1918-20.2021 · Cited by 30
Sheng, Z., Dai, Q., Prorok, M., & Castellino, F. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.04.016 · Cited by 29
Organic blockers escape from trapping in the AMPA receptor channels by leaking into the cytoplasm
Tikhonova, T. B., Barygin, O. I., Гмиро, В. Е., Tikhonov, D. B., & Magazanik, L. G. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.11.014 · Cited by 29
Site within N-Methyl-D-aspartate Receptor Pore Modulates Channel Gating
Chen, N., Li, B., Murphy, T. H., & Raymond, L. A. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.1.157 · Cited by 29
Genomic organization, proposed alternative splicing mechanisms, and RNA editing structure of GRIK1
Barbon, A., & Barlati, S. (2000) · Cytogenetic and Genome Research · doi:10.1159/000015558 · Cited by 29
Midgett, C. R., & Madden, D. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.021 · Cited by 29
Liu, H.-P., Lin, W.-Y., Liu, S.-H., Wang, W.-F., Tsai, C.-H., Wu, B.-T., Wang, C.-K., & Tsai, F.-J. (2009) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000254757 · Cited by 29
Twede, V., Teichert, R. W., Walker, C. S., Gruszczyński, P., Kaźmierkiewicz, R., Bulaj, G. W., & Olivera, B. M. (2009) · Biochemistry · doi:10.1021/bi802259a · Cited by 29
Yamamoto, H., Kamegaya, E., Sawada, W., Hasegawa, R., Yamamoto, T., Hagino, Y., Takamatsu, Y., Imai, K., Koga, H., Mishina, M., et al. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-56 · Cited by 29
Nagy, D., Stoiljković, M., Menniti, F. S., & Hajós, M. (2015) · Neuropsychopharmacology · doi:10.1038/npp.2015.298 · Cited by 29
Self-citationPharmacological characterisation of S 47445, a novel positive allosteric modulator of AMPA receptors
Bretin, S., Louis, C., Seguin, L., Wagner, S., Thomas, J., Challal, S., Rogez, N., Albinet, K., Iop, F., Villain, N., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184429 · Cited by 29
Ren, H., Salous, A. K., Paul, J. M., Lamb, K., Dwyer, D. S., & Peoples, R. W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705933200 · Cited by 29
Molecular determinants of kainate receptor trafficking
Coussen, F. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2007.12.052 · Cited by 29
Effect of NMDA receptor antagonist on proliferation of neurospheres from embryonic brain
Mochizuki, N., Takagi, N., Kurokawa, K., Kawai, T., Besshoh, S., Tanonaka, K., & Takeo, S. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.02.066 · Cited by 29
Pregnenolone sulfate modulation of N-methyl-d-aspartate receptors is phosphorylation dependent
Petrovic, M., Sedlacek, M., Cais, O., Hořák, M., Chodounská, H., & Vyklický, L. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.02.052 · Cited by 29
Cerebellar Regulation Mechanisms Learned From Studies on GluRδ2
Hirano, T. (2005) · Molecular Neurobiology · doi:10.1385/mn:33:1:001 · Cited by 29
GluR‐ and TrkB‐mediated maturation of GABAA receptor function during the period of eye opening
Henneberger, C., Jüttner, R., Schmidt, S. A., Walter, J., Meier, J. C., Rothe, T., & Grantyn, R. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.03869.x · Cited by 29
NMDA receptor NR2B subunit over‐expression increases cerebellar granule cell migratory activity
Tárnok, K., Czöndör, K., Jelitai, M., Czirók, A., & Schlett, K. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05051.x · Cited by 29
C-Terminal Interactors of the AMPA Receptor Auxiliary Subunit Shisa9
Karataeva, A. R., Klaassen, R. V., Stroeder, J., Ruiperez‐Alonso, M., Hjorth, J. J. J., van Nierop, P., Spijker, S., Mansvelder, H. D., & Smit, A. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087360 · Cited by 29
Mechanisms of ischemic cerebral injury
Kaplan, J., Dimlich, R. V. W., Biros, M. H., et al. (1987) · Resuscitation · doi:10.1016/0300-9572(87)90012-8 · Cited by 29
Sanders, J. M., Pentikäinen, O. T., Settimo, L., et al. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.022772 · Cited by 29
Luchkina, N. V., Huupponen, J., Clarke, V. R. J., Coleman, S. K., KEINÄNEN, K. P., Taira, T., & Lauri, S. E. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315769111 · Cited by 29
Targeting glutamate to treat schizophrenia: lessons from recent clinical studies
Beck, K., Javitt, D. C., & Howes, O. D. (2016) · Psychopharmacology · doi:10.1007/s00213-016-4318-6 · Cited by 29
Steered Molecular Dynamics Simulations Predict Conformational Stability of Glutamate Receptors
Musgaard, M., & Biggin, P. C. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00297 · Cited by 29
Sheng, N., Shi, Y. S., & Nicoll, R. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619253114 · Cited by 29
Prius-Mengual, J., Pérez-Rodríguez, M., Andrade‐Talavera, Y., & Moreno, A. R. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1187-5 · Cited by 29
Modulation of AMPA Receptor Gating by the Anticonvulsant Drug, Perampanel
Yuan, C. L., Shi, E. Y., Srinivasan, J., Ptak, C. P., Oswald, R. E., & Nowak, L. M. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00322 · Cited by 29
Spatial Coupling Tunes NMDA Receptor Responses via Ca2+Diffusion
Iacobucci, G. J., & Popescu, G. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.0901-19.2019 · Cited by 29
NMDA receptor channel gating control by the pre-M1 helix
McDaniel, M. J., Ogden, K. K., Kell, S. A., Burger, P. B., Liotta, D. C., & Traynelis, S. F. (2020) · The Journal of General Physiology · doi:10.1085/jgp.201912362 · Cited by 29
Self-citationSite of Action of Brain Neurosteroid Pregnenolone Sulfate at the N-Methyl-D-Aspartate Receptor
Krausová, B. H., Kysilov, B., Černý, J., Vyklický, V., Smejkalová, T., Ladislav, M., Balík, A., Kořı́nek, M., Chodounská, H., Kudová, E., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.3010-19.2020 · Cited by 29
A Tetrazolyl-Substituted Subtype-Selective AMPA Receptor Agonist
Vogensen, S. B., Frydenvang, K., Greenwood, J. R., Postorino, G., Nielsen, B., Pickering, D. S., Ebert, B., Bølcho, U., Egebjerg, J., Gajhede, M., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061439q · Cited by 28
Antunes, F. M., Rubio, M. E., & Kandler, K. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.2573-19.2020 · Cited by 28
Effect of elevated homocysteine on cardiac neural crest migration in vitro
Brauer, P. R., & Rosenquist, T. H. (2002) · Developmental Dynamics · doi:10.1002/dvdy.10105 · Cited by 28
Regional analysis of developmental changes in the extent of GluR6 mRNA editing in rat brain
Schmitt, J., Dux, E., Gissel, C., & Paschen, W. (1996) · Developmental Brain Research · doi:10.1016/0165-3806(95)00175-1 · Cited by 28
Penn, A. C., Balík, A., & Greger, I. H. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1044 · Cited by 28
Self-citationNeuronal serine racemase regulates extracellular d-serine levels in the adult mouse hippocampus
Ishiwata, S., Umino, A., Balu, D. T., et al. (2015) · Journal of Neural Transmission · doi:10.1007/s00702-015-1388-2 · Cited by 28
Hald, H., Ahring, P. K., Timmermann, D. B., et al. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.002 · Cited by 28
Ahmed, A. H., Ptak, C. P., Fenwick, M. K., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.495564 · Cited by 28
AMPA Receptor Assembly: Atomic Determinants and Built-In Modulators
Sukumaran, M., Penn, A. C., & Greger, I. H. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-3-7091-0932-8_11 · Cited by 28
Self-citationKainate receptor pore‐forming and auxiliary subunits regulate channel block by a novel mechanism
Brown, P. M. G. E., Aurousseau, M. R. P., Musgaard, M., Biggin, P. C., & Bowie, D. (2015) · The Journal of Physiology · doi:10.1113/jp271690 · Cited by 28
Self-citationCell death cascade and molecular therapy in ADAR2-deficient motor neurons of ALS
Yamashita, T., & Kwak, S. (2018) · Neuroscience Research · doi:10.1016/j.neures.2018.06.004 · Cited by 28
Glycine Transporter Type I (GlyT1) Inhibitor, Bitopertin: A Journey from Lab to Patient
Pinard, E., Borroni, E., Koerner, A., et al. (2018) · CHIMIA International Journal for Chemistry · doi:10.2533/chimia.2018.477 · Cited by 28
Liu, J., Shelkar, G. P., Zhao, F., Clausen, R. P., & Dravid, S. M. (2019) · Molecular Pharmacology · doi:10.1124/mol.119.116780 · Cited by 28
Progressive neuroanatomical changes caused by Grin1 loss-of-function mutation
Intson, K., van Eede, M. C., Islam, R., Milenkovic, M., Yan, Y., Salahpour, A., Henkelman, R. M., & Ramsey, A. J. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104527 · Cited by 28
Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites
Li, Y., Duan, G., Sun, J., Wu, D., Ye, C., Zang, Y., Chen, G., Shi, Y., Wang, J., Zhang, W., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008631 · Cited by 28
The architecture of GluD2 ionotropic delta glutamate receptor elucidated by cryo-EM
Burada, A. P., Vinnakota, R., & Kumar, J. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2020.107546 · Cited by 28
Effect of the NR3 subunit on ethanol inhibition of recombinant NMDA receptors
Smothers, C. T., & Woodward, J. J. (2003) · Brain Research · doi:10.1016/s0006-8993(03)03315-8 · Cited by 27
Gill, A., Birdsey-Benson, A., Jones, B., Henderson, L., & Madden, D. R. (2008) · Biochemistry · doi:10.1021/bi8013196 · Cited by 27
Madden, D. R., Armstrong, N., Svergun, D. I., Pérez, J., & Vachette, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414523200 · Cited by 27
Brehm, L., Greenwood, J. R., Hansen, K. B., Nielsen, B., Egebjerg, J., Stensbøl, T. B., Bräuner‐Osborne, H., Sløk, F. A., Kronborg, T. T. A., & Krogsgaard‐Larsen, P. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm0204441 · Cited by 27
Self-citationLü, W., Gray, J. A., Granger, A. J., During, M. J., & Nicoll, R. A. (2010) · Journal of Neurophysiology · doi:10.1152/jn.00725.2010 · Cited by 27
Nicholson, K. L., Mansbach, R. S., Menniti, F. S., et al. (2007) · Behavioural Pharmacology · doi:10.1097/fbp.0b013e3282f14ed6 · Cited by 27
Self-citationThe Molecular Basis of Conantokin Antagonism of NMDA Receptor Function
Prorok, M., & Castellino, F. (2007) · Current Drug Targets · doi:10.2174/138945007780618481 · Cited by 27
Jin, L., Sugiyama, H., Takigawa, M., Katagiri, D., Tomitori, H., Nishimura, K., Kaur, N., Phanstiel, O., Kitajima, M., Takayama, H., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110528 · Cited by 27
Tweaking Agonist Efficacy at N-Methyl-d-aspartate Receptors by Site-Directed Mutagenesis
Hansen, K. B., Clausen, R. P., Bjerrum, E. J., Bechmann, C., Greenwood, J. R., Christensen, C. E., Kristensen, J. L., Egebjerg, J., & Bräuner‐Osborne, H. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.014795 · Cited by 27
Self-citationFernandez, L. M. J., Pellegrini, C., Vantomme, G., Béard, E., Lüthi, A., & Astori, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-12552-8 · Cited by 27
Hanania, T., Manfredi, P., Inturrisi, C., & Vitolo, O. V. (2020) · Experimental and Clinical Psychopharmacology · doi:10.1037/pha0000310 · Cited by 27
Pearlstein, É., Gouty‐Colomer, L., Michel, F. J., Cloarec, R., & Hammond, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00210 · Cited by 27
Gono, T., Takarada, T., Fukumori, R., Kawaguchi, Y., Kaneko, H., Hanaoka, M., Katsumata, Y., Yoneda, Y., & Yamanaka, H. (2011) · Arthritis & Rheumatism · doi:10.1002/art.30616 · Cited by 27
Beinat, C., Banister, S. D., Hoban, J., et al. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.12.087 · Cited by 27
Rutkowska-Włodarczyk, I., Aller, M. I., Valbuena, S., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5059-14.2015 · Cited by 27
Ionotropic glutamate receptor expression in human spinal cord during first trimester development
Åkesson, E., Kjældgaard, A., Samuelsson, E., et al. (2000) · Developmental Brain Research · doi:10.1016/s0165-3806(99)00158-3 · Cited by 27
An orphan ionotropic glutamate receptor: The δ2 subunit
Mandolesi, G., Cesa, R., Autuori, E., & Strata, P. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.02.050 · Cited by 27
Fenwick, M. K., & Oswald, R. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086371 · Cited by 27
Flagged first, then by citations
Cited by
Sorted by citations
Mechanisms of ketamine and its metabolites as antidepressants
Hess, E. M., Riggs, L. M., Michaelides, M., & Gould, T. D. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114892 · Cited by 175
Coombs, I. D., Ziobro, J., Krotov, V., Surtees, T., Cull‐Candy, S. G., & Farrant, M. (2022) · Epilepsia · doi:10.1111/epi.17419 · Cited by 32
Cryo-EM structure of the human Asc-1 transporter complex
Li, Y., Guo, Y., Bröer, A., Dai, L., Brӧer, S., & Yan, R. (2024) · Nature Communications · doi:10.1038/s41467-024-47468-1 · Cited by 12
Glutamate receptor 4 as a fluid biomarker for the diagnosis of psychiatric disorders
Gómez de San José, N., Goossens, J., Al Shweiki, M. R., Halbgebauer, S., Oeckl, P., Steinacker, P., Danzer, K. M., Graf, H., Schönfeldt-Lecuona, C., Belbin, O., et al. (2022) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2022.10.010 · Cited by 9
Metadata
- Authors
- Hansen, K. B., Wollmuth, L. P., Bowie, D., Furukawa, H., Menniti, F. S., Sobolevsky, A. I., Swanson, G. T., Swanger, S. A., Greger, I. H., Nakagawa, T., McBain, C. J., Jayaraman, V., Low, C.-M., Dell’Acqua, M. L., Diamond, J. S., Camp, C. R., Perszyk, R. E., Yuan, H., & Traynelis, S. F.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Traynelis, Stephen F.
- ORCID
- Hansen, Kasper B.
- Wollmuth, Lonnie P.
- Bowie, Derek
- Furukawa, Hiro
- Menniti, Frank S.
- Sobolevsky, Alexander I.
- Swanson, Geoffrey T.
- Swanger, Sharon A.
- Greger, Ingo H.
- Nakagawa, Terunaga
- McBain, Chris J.
- Jayaraman, Vasanthi
- Low, Chian-Ming
- Dell’Acqua, Mark L.
- Diamond, Jeffrey S.
- Camp, Chad R.
- Perszyk, Riley E.
- Yuan, Hongjie
- Traynelis, Stephen F.
- Venue
- Pharmacological Reviews
- Publisher
- Elsevier BV
- Published
- 2021-10
- Volume
- 73
- Issue
- 4
- Pages
- 1469-1658
- ISSN
- 0031-6997 (ISSN-L)
- PMC
- PMC8626789
- OpenAlex
- W3214054678
- Cited by
- 686
- References
- 2,576
- Citations by year
- 2026: 123 · 2025: 198 · 2024: 160 · 2023: 115 · 2022: 81 · 2021: 9
- FWCI
- 13.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Pharmacological Reviews (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Funders
- National Institutes of Health (5f31ns113530-02)
- Biotechnology and Biological Sciences Research Council (BB/N002113/1)
- National Institute of Mental Health (R56MH123474, R21MH127404, R01MH085926, R01MH123474)
- National Cancer Institute (R01CA206573)
- National Institute of General Medical Sciences (P20GM103546, R35GM122528)
- National Institute of Neurological Disorders and Stroke (F31‐NS113530, R01NS105804, R56NS040701, R01NS083660, R01NS040701, R01NS088479, R01NS111745, RF1NS113632, R01NS105502, R01NS107253, R35NS111619, R37NS083660, R01NS116055, R01NS097536)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R01HD082373)
- 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, glutamate, receptor subtypes, receptor structure, receptor pharmacology, excitatory neurotransmission, neurophysiology, neurological disorders, mental illness, therapeutic target
- MeSH terms
- Animals, Central Nervous System, Humans, Receptors, Glutamate, Neurotransmitter Agents, Glutamic Acid, Receptors, Ionotropic Glutamate
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