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a cellular structure that is postulated to exist in order to mediate between a chemical agent that acts on nervous tissue and the physiological response
a salt or ester of glutamic acid

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=sense organ / 受信装置

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/08/14 23:57:01」(JST)

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Ionotropic glutamate receptors (iGluRs) are ligand-gated ion channels that are activated by the neurotransmitter glutamate.^[1] They mediate the majority of excitatory synaptic transmission throughout the central nervous system and are key players in synaptic plasticity, which is important for learning and memory. iGluRs have been divided into four subtypes on the basis of their ligand binding properties (pharmacology) and sequence similarity: AMPA receptors, kainate receptors, NMDA receptors and delta receptors (see below).^[2]

AMPA receptors are the main charge carriers during basal transmission, permitting influx of sodium ions to depolarise the postsynaptic membrane. NMDA receptors are blocked by magnesium ions and therefore only permit ion flux following prior depolarisation. This enables them to act as coincidence detectors for synaptic plasticity. Calcium influx through NMDA receptors leads to persistent modifications in the strength of synaptic transmission.^[3]^[4]

iGluRs are tetramers (they are formed of four subunits). All subunits have a shared architecture with four domain layers: two extracellular clamshell domains called the N-terminal domain (NTD) and ligand-binding domain (LBD; which binds glutamate), the transmembrane domain (TMD) that forms the ion channel, and an intracellular C-terminal domain (CTD).^[5]

Human proteins/genes encoding iGluR subunits

AMPA receptors: GluA1/GRIA1; GluA2/GRIA2; GluA3/GRIA3; GluA4/GRIA4;

delta receptors: GluD1/GRID1; GluD2/GRID2;

kainate receptors: GluK1/GRIK1; GluK2/GRIK2; GluK3/GRIK3; GluK4/GRIK4; GluK5/GRIK5;

NMDA receptors: GluN1/GRIN1; GluN2A/GRIN2A; GluN2B/GRIN2B; GluN2C/GRIN2C; GluN2D/GRIN2D; GluN3A/GRIN3A; GluN3B/GRIN3B;

References

^ Traynelis SF, Wollmuth LP, McBain CJ, Menniti FS, Vance KM, Ogden KK, Hansen KB, Yuan H, Myers SJ, Dingledine R (September 2010). "Glutamate receptor ion channels: structure, regulation, and function". Pharmacol. Rev. 62 (3): 405–496. doi:10.1124/pr.109.002451. PMC 2964903. PMID 20716669.
^ Collingridge GL, Olsen RW, Peters J, Spedding M (January 2009). "A nomenclature for ligand-gated ion channels". Neuropharmacology. 56 (1): 2–5. doi:10.1016/j.neuropharm.2008.06.063. PMC 2847504. PMID 18655795.
^ Bliss TV, Collingridge GL (January 1993). "A synaptic model of memory: long-term potentiation in the hippocampus". Nature. 361 (6407): 31–39. doi:10.1038/361031a0. PMID 8421494.
^ Citri A, Malenka RC (January 2008). "Synaptic plasticity: multiple forms, functions, and mechanisms". Neuropsychopharmacology. 33 (1): 18–41. doi:10.1038/sj.npp.1301559. PMID 17728696.
^ Traynelis SF, Wollmuth LP, McBain CJ, Menniti FS, Vance KM, Ogden KK, Hansen KB, Yuan H, Myers SJ, Dingledine R (September 2010). "Glutamate receptor ion channels: structure, regulation, and function". Pharmacol. Rev. 62 (3): 405–496. doi:10.1124/pr.109.002451. PMC 2964903. PMID 20716669.

This article incorporates text from the public domain Pfam and InterPro IPR001320

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Reduced extracellular zinc levels facilitate glutamate-mediated oligodendrocyte death after trauma.

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Presynaptic kainate receptor-mediated bidirectional modulatory actions: Mechanisms.

Sihra TS, Rodríguez-Moreno A.SourceDepartment of Neuroscience, Physiology and Pharmacology, University College London, London, United Kingdom. Electronic address: t.sihra@ucl.ac.uk.
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Kainate receptors (KARs) are members of the glutamate receptor family, which also includes two other ionotropic subtypes, i.e. NMDA- and AMPA-type receptors, and types I, II and III metabotropic glutamate receptors. KARs mediate synaptic transmission postynaptically through their ionotropic capacity
PMID 23538266

Japanese Journal

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NAID 110009966534

Error-based Extraction of States and Energy Landscapes from Experimental Single-Molecule Time-Series

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NAID 130004704766

「イオンチャネル内蔵型グルタミン酸受容体」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Lig_chan
	x-ray structure of the glur6 ligand binding core (s1s2a) in complex with glutamate at 1.65 a resolution
Identifiers
Symbol	Lig_chan
Pfam	PF00060
Pfam clan	CL0030
InterPro	IPR001320
SCOP	1gr2
SUPERFAMILY	1gr2
TCDB	1.A.10
OPM superfamily	231
OPM protein	3kg2
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary