Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels

Burst kinetics of single NMDA receptor currents in cell‐attached patches from rat brain cortical neurons in culture.

Kleckner, N. W., & Pallotta, B. S. (1995) · The Journal of Physiology · doi:10.1113/jphysiol.1995.sp020822 · Cited by 27

α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Antagonists: From Bench to Bedside

Mattes, H., Carcache, D. A., Kalkman, H. O., & Koller, M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901688m · Cited by 27

Thiocyanate ions selectively antagonize AMPA‐evoked responses in Xenopus laevis oocytes microinjected with rat brain mRNA

Bowie, D., & Smart, T. G. (1993) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.1993.tb13642.x · Cited by 27

Cyclic benzamidines as orally efficacious NR2B-selective NMDA receptor antagonists

Nguyen, K. T., Claiborne, C. F., McCauley, J. A., et al. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.04.084 · Cited by 27

Structure–Activity Relationship Studies of Argiotoxins: Selective and Potent Inhibitors of Ionotropic Glutamate Receptors

Poulsen, M. H., Lucas, S., Bach, T. B., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301602d · Cited by 27

Neto2 Assembles with Kainate Receptors in DRG Neurons during Development and Modulates Neurite Outgrowth in Adult Sensory Neurons

Vernon, C. G., & Swanson, G. T. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2978-16.2017 · Cited by 27

Novel Mode of Antagonist Binding in NMDA Receptors Revealed by the Crystal Structure of the GluN1-GluN2A Ligand-Binding Domain Complexed to NVP-AAM077

Hernandez, A. R., & Furukawa, H. (2017) · Molecular Pharmacology · doi:10.1124/mol.116.107912 · Cited by 27

Development of Cortical Pyramidal Cell and Interneuronal Dendrites: a Role for Kainate Receptor Subunits and NETO1

Jäck, A., Hamad, M. I. K., Gonda, S., Gralla, S., Pahl, S., Hollmann, M., & Wahle, P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1414-0 · Cited by 27

Functional assessment of triheteromeric NMDA receptors containing a human variant associated with epilepsy

Marwick, K. F. M., Hansen, K. B., Skehel, P., Hardingham, G. E., & Wyllie, D. J. A. (2019) · The Journal of Physiology · doi:10.1113/jp277292 · Cited by 27

Cerebellar Stellate Cell Excitability Is Coordinated by Shifts in the Gating Behavior of Voltage-Gated Na + and A-Type K + Channels

Alexander, R. P. D., Mitry, J., Sareen, V., Khadra, A., & Bowie, D. (2019) · eNeuro · doi:10.1523/eneuro.0126-19.2019 · Cited by 27

Synaptic crosstalk conferred by a zone of differentially regulated Ca 2+ signaling in the dendritic shaft adjoining a potentiated spine

Dittmer, P. J., Dell’Acqua, M. L., & Sather, W. A. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902461116 · Cited by 27

Neuronal Glutamatergic Synaptic Clefts Alkalinize Rather Than Acidify during Neurotransmission

Stawarski, M., Hernandez, R. X., Feghhi, T., Borycz, J. A., Lu, Z., Agarwal, A. B., Reihl, K. D., Tavora, R., Lau, A. W. C., Meinertzhagen, I. A., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1774-19.2020 · Cited by 27

Discovery of Dihydropyrrolo[1,2-a]pyrazin-3(4H)-one-Based Second-Generation GluN2C- and GluN2D-Selective Positive Allosteric Modulators (PAMs) of the N-Methyl- d -Aspartate (NMDA) Receptor

Epplin, M. P., Mohan, A., Harris, L. D., Zhu, Z., Strong, K. L., Bacsa, J., Le, P., Menaldino, D. S., Traynelis, S. F., & Liotta, D. C. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01733 · Cited by 27

A Domain Linking the AMPA Receptor Agonist Binding Site to the Ion Pore Controls Gating and CauseslurcherProperties when Mutated

Schmid, S. M., Körber, C., Herrmann, S., Werner, M., & Hollmann, M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3175-07.2007 · Cited by 26

Enantiomeric Propanolamines as selectiveN-Methyl- d -aspartate 2B Receptor Antagonists

Tahirovic, Y. A., Geballe, M. T., Gruszecka‐Kowalik, E., Myers, S. J., Lyuboslavsky, P. N., Le, P., French, A. M., Irier, H. A., Choi, W., Easterling, K. W., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8002153 · Cited by 26

N-Methyl-D-Aspartate Receptors, Ketamine, and Rett Syndrome: Something Special on the Road to Treatments?

Katz, D. M., Menniti, F. S., & Mather, R. J. (2016) · Biological Psychiatry · doi:10.1016/j.biopsych.2016.03.1045 · Cited by 26

Physicochemical and biological properties of novel amide-based steroidal inhibitors of NMDA receptors

Adla, S. K., Slavı́ková, B., Šmídková, M., Tloušťová, E., Svoboda, M., Vyklický, V., Krausová, B. H., Hubálková, P., Nekardová, M., Holubová, K., et al. (2016) · Steroids · doi:10.1016/j.steroids.2016.08.010 · Cited by 26

Aberrant alternative splicing pattern of ADAR2 downregulates adenosine-to-inosine editing in glioma

LI, Z., Tian, Y., Tian, N., et al. (2015) · Oncology Reports · doi:10.3892/or.2015.3907 · Cited by 26

Increased Exon 5 Expression Alters Extrasynaptic NMDA Receptors in Cerebellar Neurons

Prybylowski, K., Rumbaugh, G., Wolfe, B. B., & Vicini, S. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751140.x · Cited by 26

Glutamate receptor antibodies directed against AMPA receptors subunit 3 peptide B (GluR3B) associate with some cognitive/psychiatric/behavioral abnormalities in epilepsy patients

Goldberg‐Stern, H., Ganor, Y., Cohen, R., Pollak, L., Teichberg, V. I., & Levite, M. (2013) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2013.11.007 · Cited by 26

Short-Term Plasticity of Kainate Receptor-Mediated EPSCs Induced by NMDA Receptors at Hippocampal Mossy Fiber Synapses

Rebola, N., Sachidhanandam, S., Perrais, D., Cunha, R. A., & Mulle, C. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5182-06.2007 · Cited by 26

Effect of Ifenprodil on GluN1/GluN2B N-Methyl-D-aspartate Receptor Gating

Bhatt, J. M., Prakash, A., Suryavanshi, P. S., & Dravid, S. M. (2012) · Molecular Pharmacology · doi:10.1124/mol.112.080952 · Cited by 26

Kinetic Contributions to Gating by Interactions Unique to N-methyl-d-aspartate (NMDA) Receptors

Borschel, W. F., Cummings, K. A., Tindell, L. K., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.678656 · Cited by 26

Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites

Maolanon, A. R., Risgaard, R., Wang, S., Snoep, Y., Papangelis, A., Yi, F., Holley, D. C., Barslund, A. F., Svenstrup, N., Hansen, K. B., et al. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00117 · Cited by 26

Identification of AICP as a GluN2C-Selective N-Methyl-d-Aspartate Receptor Superagonist at the GluN1 Glycine Site

Jessen, M., Frederiksen, K., Yi, F., Clausen, R. P., Hansen, K. B., Bräuner‐Osborne, H., Kilburn, P., & Damholt, A. B. (2017) · Molecular Pharmacology · doi:10.1124/mol.117.108944 · Cited by 26

Homozygous GRID2 missense mutation predicts a shift in the D-serine binding domain of GluD2 in a case with generalized brain atrophy and unusual clinical features

Ali, Z., Zulfiqar, S., Klar, J., et al. (2017) · BMC Medical Genetics · doi:10.1186/s12881-017-0504-6 · Cited by 26

NMDA receptors are altered in the substantia nigra pars reticulata and their blockade ameliorates motor deficits in experimental parkinsonism

Sitzia, G., Mantas, I., Zhang, X., Svenningsson, P., & Chergui, K. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108136 · Cited by 26

Activity Dependent Inhibition of AMPA Receptors by Zn 2+

Carrillo, E. C., Bhatia, N. K., Akimzhanov, A. M., & Jayaraman, V. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1481-20.2020 · Cited by 26

NMDA Receptors Require Multiple Pre-opening Gating Steps for Efficient Synaptic Activity

Amin, J. B., Gochman, A., He, M., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.11.009 · Cited by 26

Extracellular Vestibule Determinants of Ca2+ Influx in Ca2+‐Permeable AMPA Receptor Channels

Jatzke, C., Hernandez, M., & Wollmuth, L. P. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2002.034413 · Cited by 25

Altered Voltage Dependence of Fractional Ca2+ Current in N-Methyl-d-Aspartate Channel Pore Mutants with a Decreased Ca2+ Permeability

Schneggenburger, R. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77889-0 · Cited by 25

The NR2B subunit in NMDA receptors is functionally important during cerebellar granule cell migration

Mancini, J., & Atchison, W. D. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.09.079 · Cited by 25

Rescue of abnormal phenotypes in δ2 glutamate receptor‐deficient mice by the extracellular N‐terminal and intracellular C‐terminal domains of the δ2 glutamate receptor

Torashima, T., Iizuka, A., Horiuchi, H., Mitsumura, K., Yamasaki, M., Koyama, C., Takayama, K., Iino, M., Watanabe, M., & Hirai, H. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06841.x · Cited by 25

Glutamate delta-1 receptor regulates cocaine-induced plasticity in the nucleus accumbens

Liu, J., Gandhi, P. J., Pavuluri, R., Shelkar, G. P., & Dravid, S. M. (2018) · Translational Psychiatry · doi:10.1038/s41398-018-0273-9 · Cited by 25

Auxiliary Proteins are the Predominant Determinants of Differential Efficacy of Clinical Candidates Acting as AMPA Receptor Positive Allosteric Modulators

Ishii, T., Stolz, J. R., & Swanson, G. T. (2020) · Molecular Pharmacology · doi:10.1124/mol.119.118554 · Cited by 25

Characterizing the binding and function of TARP γ8-selective AMPA receptor modulators

Dohrke, J.-N., Watson, J. F., Birchall, K., & Greger, I. H. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014135 · Cited by 25

The auxiliary subunits Neto1 and Neto2 have distinct, subunit-dependent effects at recombinant GluK1- and GluK2-containing kainate receptors

Fisher, J. L. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.08.018 · Cited by 25

2,6-Disubstituted pyrazines and related analogs as NR2B site antagonists of the NMDA receptor with anti-depressant activity

Brown, D. G., Maier, D. L., Sylvester, M. A., Hoerter, T. N., Menhaji‐Klotz, E., Lasota, C. C., Hirata, L. T., Wilkins, D. E., Scott, C. W., Trivedi, S., et al. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.03.117 · Cited by 25

Binding site and ligand flexibility revealed by high resolution crystal structures of GluK1 competitive antagonists

Alushin, G. M., Jane, D. E., & Mayer, M. L. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.06.002 · Cited by 25

Global Scaling Down of Excitatory Postsynaptic Responses in Cerebellar Purkinje Cells Impairs Developmental Synapse Elimination

Kawata, S., Miyazaki, T., Yamazaki, M., Mikuni, T., Yamasaki, M., Hashimoto, K., Watanabe, M., Sakimura, K., & Kano, M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.014 · Cited by 25

Presynaptic AMPA receptors: more than just ion channels?

Schenk, U. (2004) · Biology of the Cell · doi:10.1016/j.biolcel.2004.01.008 · Cited by 25

Attenuated Plasticity of Postsynaptic Kainate Receptors in Hippocampal CA3 Pyramidal Neurons

Ito, K., Contractor, A., & Swanson, G. T. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1302-04.2004 · Cited by 25

Developmental profile of kainate receptor subunit KA1 revealed by Cre expression in YAC transgenic mice

Kask, K., Jerecı̀ć, J., Zamanillo, D., Wilbertz, J. H., Sprengel, R., & Seeburg, P. H. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02599-3 · Cited by 25

Glycine/NMDA Receptor Antagonists as Potential CNS Therapeutic Agents: ACEA-1021 and Related Compounds

Cai, S. X. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776894465 · Cited by 25

Disruption of cerebellar microzonal organization in GluD2 (GluRδ2) knockout mouse

Hashizume, M., Miyazaki, T., Sakimura, K., et al. (2013) · Frontiers in Neural Circuits · doi:10.3389/fncir.2013.00130 · Cited by 25

Ho15J—A new hotfoot allele in a hot spot in the gene encoding the δ2 glutamate receptor

Motohashi, J., Kakegawa, W., & Yuzaki, M. (2006) · Brain Research · doi:10.1016/j.brainres.2006.03.068 · Cited by 25

Quantifying Water-Mediated Protein–Ligand Interactions in a Glutamate Receptor: A DFT Study

Sahai, M., & Biggin, P. (2011) · Journal of Physical Chemistry B · doi:10.1021/jp200776t · Cited by 25

Gating reaction mechanism of neuronal NMDA receptors

Borschel, W. F., Myers, J. M., Kasperek, E. M., Smith, T. P., Graziane, N., Nowak, L. M., & Popescu, G. (2012) · Journal of Neurophysiology · doi:10.1152/jn.00551.2012 · Cited by 25

R/G editing in GluA2Rflop modulates the functional difference between GluA1 flip and flop variants in GluA1/2R heteromeric channels

Wen, W., Lin, C.-Y., & Niu, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-13233-2 · Cited by 25

Cerebellar Kainate Receptor-Mediated Facilitation of Glutamate Release Requires Ca2+-Calmodulin and PKA

Falcón‐Moya, R., Losada-Ruiz, P., Sihra, T. S., & Moreno, A. R. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00195 · Cited by 25

PTC-174, a positive allosteric modulator of NMDA receptors containing GluN2C or GluN2D subunits

Yi, F., Rouzbeh, N., Hansen, K. B., Xu, Y., Fanger, C. M., Gordon, E., Paschetto, K. A., Menniti, F. S., & Volkmann, R. A. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.107971 · Cited by 25

The "blue" side of glutamatergic neurotransmission: NMDA receptor antagonists as possible novel therapeutics for major depression.

Szakács, R., Janka, Z., & Kálmán, J. (2012) · PubMed · doi:10.5706/nph201203003 · Cited by 24

The Selective Activation of the Glutamate Receptor GluR5 by ATPA Is Controlled by Serine 741

Nielsen, M. M., Liljefors, T., Krogsgaard‐Larsen, P., & Egebjerg, J. (2003) · Molecular Pharmacology · doi:10.1124/mol.63.1.19 · Cited by 24

Expression of Btcl2, a novel member of Btcl gene family, during development of the central nervous system

Michishita, M., Ikeda, T., Nakashiba, T., Ogawa, M., Tashiro, K., Honjo, T., Doi, K., Itohara, S., & Endo, S. (2004) · Developmental Brain Research · doi:10.1016/j.devbrainres.2004.06.012 · Cited by 24

Two serine residues on GluN2A C-terminal tails control NMDA receptor current decay times

Maki, B. A., Cole, R., & Popescu, G. (2013) · Channels · doi:10.4161/chan.23968 · Cited by 24

Motoneuron-specificNR3Bgene

Niemann, S., Landers, J. E., Churchill, M., Hosler, B. A., Sapp, P. C., Speed, W. C., Lahn, B. T., Kídd, K. K., Brown, R. H., & Hayashi, Y. (2007) · Neurology · doi:10.1212/01.wnl.0000271078.51280.17 · Cited by 24

Modulation of ionotropic glutamate receptor function by vertebrate galectins

Copits, B. A., Vernon, C. G., Sakai, R., et al. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2013.269597 · Cited by 24

Partial deletion of GLRB and GRIA2 in a patient with intellectual disability

Hackmann, K., Matko, S., Gerlach, E., von der Hagen, M., Klink, B., Schröck, E., Rump, A., & Donato, N. D. (2012) · European Journal of Human Genetics · doi:10.1038/ejhg.2012.97 · Cited by 24

Discovery of 3-Substituted Aminocyclopentanes as Potent and Orally Bioavailable NR2B Subtype-Selective NMDA Antagonists

Layton, M. E., Kelly, M. J., Rodzinak, K. J., Sanderson, P. E. J., Young, S. D., Bednar, R. A., DiLella, A. G., McDonald, T. P., Wang, H., Mosser, S. D., et al. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200013d · Cited by 24

Exploring kainate receptor pharmacology using molecular dynamics simulations

Postila, P. A., Swanson, G. T., & Pentikäinen, O. T. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.08.019 · Cited by 24

Glutamate receptor agonist kainate enhances primary dendrite number and length from immature mouse cortical neurons in vitro

Monnerie, H., & Roux, P. D. L. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20805 · Cited by 24

Studies on an (S)-2-Amino-3-(3-hydroxy-5-methyl-4-isoxazolyl)propionic Acid (AMPA) Receptor Antagonist IKM-159: Asymmetric Synthesis, Neuroactivity, and Structural Characterization

Juknaitė, L., Sugamata, Y., Tokiwa, K., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm301590z · Cited by 24

Assessment of Structurally Diverse Philanthotoxin Analogues for Inhibitory Activity on Ionotropic Glutamate Receptor Subtypes: Discovery of Nanomolar, Nonselective, and Use-Dependent Antagonists

Frølund, S., Bella, A., Kristensen, A. S., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100886h · Cited by 24

All atom NMDA receptor transmembrane domain model development and simulations in lipid bilayers and water

Mesbahi‐Vasey, S., Veras, L., Yonkunas, M. J., Johnson, J. W., & Kurnikova, M. G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177686 · Cited by 24

A Phase Ib Randomized Controlled Study to Evaluate the Effectiveness of a Single-Dose of the NR2B Selective N-Methyl-d-Aspartate Antagonist MK-0657 on Levodopa-Induced Dyskinesias and Motor Symptoms in Patients With Parkinson Disease

Herring, W. J., Assaid, C. A., Budd, K., Vargo, R. C., Mazenko, R. S., Lines, C., Ellenbogen, A. L., & Metman, L. V. (2017) · Clinical Neuropharmacology · doi:10.1097/wnf.0000000000000241 · Cited by 24

RNAi-Based GluN3A Silencing Prevents and Reverses Disease Phenotypes Induced by Mutant huntingtin

Marco, S., Murillo, A., & Pérez‐Otaño, I. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.05.013 · Cited by 24

Mechanisms of CPT1C-Dependent AMPAR Trafficking Enhancement

Gratacòs‐Batlle, E., Olivella, M., Sánchez-Fernández, N., Yefimenko, N., Míguez‐Cabello, F., Fadó, R., Casals, N., Gasull, X., Ambrosio, S., & Soto, D. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00275 · Cited by 24

The NMDA receptor intracellular C-terminal domains reciprocally interact with allosteric modulators

Sapkota, K., Doré, K., Tang, K. L., Irvine, M. W., Fang, G., Burnell, E. S., Malinow, R., Jane, D. E., & Monaghan, D. T. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.11.018 · Cited by 24

Modulation of TARP γ8–Containing AMPA Receptors as a Novel Therapeutic Approach for Chronic Pain

Knopp, K. L., Simmons, R. M. A., Guo, W., Adams, B. L., Gardinier, K. M., Gernert, D. L., Ornstein, P. L., Porter, W. J., Reel, J. K., Ding, C., et al. (2019) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.250126 · Cited by 24

Mutational Analysis and Modeling of Negative Allosteric Modulator Binding Sites in AMPA Receptors

Stenum-Berg, C., Musgaard, M., Chavez-Abiega, S., et al. (2019) · Molecular Pharmacology · doi:10.1124/mol.119.116871 · Cited by 24

Hodgkin–Huxley–Katz Prize Lecture: Genetic and pharmacological control of glutamate receptor channel through a highly conserved gating motif

Perszyk, R. E., Myers, S. J., Yuan, H., Gibb, A. J., Furukawa, H., Sobolevsky, A. I., & Traynelis, S. F. (2020) · The Journal of Physiology · doi:10.1113/jp278086 · Cited by 24

AMPA Receptor Auxiliary Subunit GSG1L Suppresses Short-Term Facilitation in Corticothalamic Synapses and Determines Seizure Susceptibility

Kamalova, A., Futai, K., Delpire, E. J., & Nakagawa, T. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107921 · Cited by 24

Facilitation of GluN2C-containing NMDA receptors in the external globus pallidus increases firing of fast spiking neurons and improves motor function in a hemiparkinsonian mouse model

Liu, J., Shelkar, G. P., Sarode, L. P., Gawande, D. Y., Zhao, F., Clausen, R. P., Ugale, R. R., & Dravid, S. M. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105254 · Cited by 24

Pharmacology of NMDA receptors

JANE, D. (2001) · CRC Press eBooks · doi:10.1201/9780203299388-7 · Cited by 23

pH-Sensitive NMDA Inhibitors Improve Outcome in a Murine Model of SAH

Wang, H., James, M. L., Venkatraman, T. N., Wilson, L. J., Lyuboslavsky, P. N., Myers, S. J., Lascola, C. D., & Laskowitz, D. T. (2014) · Neurocritical Care · doi:10.1007/s12028-013-9944-9 · Cited by 23

A series of structurally novel heterotricyclic α‐amino‐3‐hydroxyl‐5‐methyl‐4‐isoxazole‐propionate receptor‐selective antagonists

Gill, M., Frausto, S. F., Ikoma, M., Sasaki, M., Oikawa, M., Sakai, R., & Swanson, G. T. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00784.x · Cited by 23

Crosslinking the ligand‐binding domain dimer interface locks kainate receptors out of the main open state

Daniels, B. A., Andrews, E. D., Aurousseau, M. R. P., et al. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.253666 · Cited by 23

Kainate receptor‐mediated depression of glutamatergic transmission involving protein kinase A in the lateral amygdala

Negrete‐Díaz, J. V., Duque‐Feria, P., Andrade‐Talavera, Y., Carrión, M., Flores, G., & Moreno, A. R. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07665.x · Cited by 23

Relative contribution of TARPs γ-2 and γ-7 to cerebellar excitatory synaptic transmission and motor behavior

Yamazaki, M., Pichon, C. E. L., Jackson, A. C., Cerpas, M., Sakimura, K., Scearce-Levie, K. A., & Nicoll, R. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1423670112 · Cited by 23

Selective Kainate Receptor (GluK1) Ligands Structurally Based upon 1H-Cyclopentapyrimidin-2,4(1H,3H)-dione: Synthesis, Molecular Modeling, and Pharmacological and Biostructural Characterization

Venskutonytė, R., Butini, S., Coccone, S. S., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm2004078 · Cited by 23

Expression of the N-methyl-d-aspartate receptor subunit NR3B regulates dendrite morphogenesis in spinal motor neurons

Prithviraj, R., & Inglis, F. M. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.03.089 · Cited by 23

N-Methyl- d -aspartic Acid Receptor Agonists: Resolution, Absolute Stereochemistry, and Pharmacology of the Enantiomers of 2-Amino-2-(3-hydroxy-5-methyl-4-isoxazolyl)acetic Acid

Madsen, U., Frydenvang, K., Ebert, B., et al. (1996) · Journal of Medicinal Chemistry · doi:10.1021/jm950393q · Cited by 23

Distribution of the NMDA receptor NR3A subunit in the adult pig-tail macaque brain

Mueller, H. T., & Meador‐Woodruff, J. H. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2004.11.002 · Cited by 23

Novel 3‐Carboxy‐ and 3‐Phosphonopyrazoline Amino Acids as Potent and Selective NMDA Receptor Antagonists: Design, Synthesis, and Pharmacological Characterization

Conti, P., Pinto, A., Tamborini, L., et al. (2010) · ChemMedChem · doi:10.1002/cmdc.201000184 · Cited by 23

Antibodies to glutamate receptor subtype 3 (GluR3) are found in some patients suffering from epilepsy as the main disease, but not in patients whose epilepsy accompanies antiphospholipid syndrome or Sneddon's syndrome

Ganor, Y., Goldberg‐Stern, H., Blank, M., Shoenfeld, Y., Добрынина, Л. А., Kalashnikova, L. A., & Levite, M. (2005) · Autoimmunity · doi:10.1080/08916930500246339 · Cited by 23

Axonal Kainate Receptors Modulate the Strength of Efferent Connectivity by Regulating Presynaptic Differentiation

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The C-terminus of NMDAR GluN1-1a Subunit Translocates to Nucleus and Regulates Synaptic Function

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Kainate Binding Proteins Possess Functional Ion Channel Domains

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