Proteins > Glutamate receptor ionotropic, kainate 1
Page last updated: 2024-08-07 16:36:47
Glutamate receptor ionotropic, kainate 1
A glutamate receptor ionotropic, kainate 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P39086]
Synonyms
GluK1;
Excitatory amino acid receptor 3;
EAA3;
Glutamate receptor 5;
GluR-5;
GluR5
Research
Bioassay Publications (17)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (11.76) | 18.2507 |
| 2000's | 11 (64.71) | 29.6817 |
| 2010's | 4 (23.53) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Compounds (16)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| kainic acid | Homo sapiens (human) | EC50 | 16.2000 | 2 | 2 |
| glutamic acid | Homo sapiens (human) | EC50 | 57.3333 | 3 | 3 |
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| ly 293558 | Homo sapiens (human) | Kb | 0.2000 | 1 | 1 |
| ubp 310 | Homo sapiens (human) | Kb | 0.0090 | 2 | 2 |
| ubp 302 | Homo sapiens (human) | Kb | 0.8000 | 2 | 2 |
| ubp296 | Homo sapiens (human) | Kb | 0.6000 | 1 | 1 |
Design, synthesis, and pharmacology of a highly subtype-selective GluR1/2 agonist, (RS)-2-amino-3-(4-chloro-3-hydroxy-5-isoxazolyl)propionic acid (Cl-HIBO).Journal of medicinal chemistry, , May-22, Volume: 46, Issue:11, 2003
Heteroaryl analogues of AMPA. Synthesis and quantitative structure-activity relationships.Journal of medicinal chemistry, , Aug-29, Volume: 40, Issue:18, 1997
2-n-Butyl-9-methyl-8-[1,2,3]triazol-2-yl-9H-purin-6-ylamine and analogues as A2A adenosine receptor antagonists. Design, synthesis, and pharmacological characterization.Journal of medicinal chemistry, , Nov-03, Volume: 48, Issue:22, 2005
4-Alkylidenyl glutamic acids, potent and selective GluR5 agonists.Bioorganic & medicinal chemistry letters, , Aug-21, Volume: 10, Issue:16, 2000
4-Alkyl- and 4-cinnamylglutamic acid analogues are potent GluR5 kainate receptor agonists.Journal of medicinal chemistry, , May-18, Volume: 43, Issue:10, 2000
Structure-activity relationship studies on N3-substituted willardiine derivatives acting as AMPA or kainate receptor antagonists.Journal of medicinal chemistry, , Apr-20, Volume: 49, Issue:8, 2006
4-Alkylidenyl glutamic acids, potent and selective GluR5 agonists.Bioorganic & medicinal chemistry letters, , Aug-21, Volume: 10, Issue:16, 2000
4-Alkyl- and 4-cinnamylglutamic acid analogues are potent GluR5 kainate receptor agonists.Journal of medicinal chemistry, , May-18, Volume: 43, Issue:10, 2000
GluK1 antagonists from 6-(tetrazolyl)phenyl decahydroisoquinoline derivatives: in vitro profile and in vivo analgesic efficacy.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 23, Issue:23, 2013
Ion channels as therapeutic targets: a drug discovery perspective.Journal of medicinal chemistry, , Feb-14, Volume: 56, Issue:3, 2013
alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) antagonists: from bench to bedside.Journal of medicinal chemistry, , Aug-12, Volume: 53, Issue:15, 2010
Two prodrugs of potent and selective GluR5 kainate receptor antagonists actives in three animal models of pain.Journal of medicinal chemistry, , Jun-30, Volume: 48, Issue:13, 2005
(3SR,4aRS,6SR,8aRS)-6-(1H-tetrazol-5-yl)decahydroisoquinoline-3-carboxylic acid, a novel, competitive, systemically active NMDA and AMPA receptor antagonist.Journal of medicinal chemistry, , Dec-08, Volume: 38, Issue:25, 1995
Synthesis and pharmacological characterization of N3-substituted willardiine derivatives: role of the substituent at the 5-position of the uracil ring in the development of highly potent and selective GLUK5 kainate receptor antagonists.Journal of medicinal chemistry, , Apr-05, Volume: 50, Issue:7, 2007
Structure-activity relationship studies on N3-substituted willardiine derivatives acting as AMPA or kainate receptor antagonists.Journal of medicinal chemistry, , Apr-20, Volume: 49, Issue:8, 2006
Two prodrugs of potent and selective GluR5 kainate receptor antagonists actives in three animal models of pain.Journal of medicinal chemistry, , Jun-30, Volume: 48, Issue:13, 2005
Bioisosteric modifications of 2-arylureidobenzoic acids: selective noncompetitive antagonists for the homomeric kainate receptor subtype GluR5.Journal of medicinal chemistry, , Dec-30, Volume: 47, Issue:27, 2004
2-arylureidobenzoic acids: selective noncompetitive antagonists for the homomeric kainate receptor subtype GluR5.Journal of medicinal chemistry, , Dec-18, Volume: 46, Issue:26, 2003
Enables
This protein enables 4 target(s):
| Target | Category | Definition |
|---|
| glutamate-gated receptor activity | molecular function | Catalysis of the transmembrane transfer of an ion by a channel that opens when glutamate has been bound by the channel complex or one of its constituent parts. [ISBN:0198506732] |
| kainate selective glutamate receptor activity | molecular function | An ionotropic glutamate receptor activity that exhibits fast gating by glutamate, acts by opening a cation channel permeable to sodium and potassium, and for which kainate is an agonist. [GOC:mah, PMID:10049997, PMID:8804111] |
| glutamate-gated calcium ion channel activity | molecular function | Enables the transmembrane transfer of a calcium ion by a channel that opens when glutamate has been bound by the channel complex or one of its constituent parts. [GOC:mtg_transport, ISBN:0815340729] |
| transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | molecular function | Any transmitter-gated ion channel activity that is involved in regulation of postsynaptic membrane potential. [GO_REF:0000061, GOC:TermGenie, PMID:20200227] |
Located In
This protein is located in 2 target(s):
| Target | Category | Definition |
|---|
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
Active In
This protein is active in 3 target(s):
| Target | Category | Definition |
|---|
| plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
| presynaptic membrane | cellular component | A specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction; many synaptic junctions exhibit structural presynaptic characteristics, such as conical, electron-dense internal protrusions, that distinguish it from the remainder of the axon plasma membrane. [GOC:jl, ISBN:0815316194] |
| postsynaptic density membrane | cellular component | The membrane component of the postsynaptic density. This is the region of the postsynaptic membrane in which the population of neurotransmitter receptors involved in synaptic transmission are concentrated. [GOC:dos] |
Part Of
This protein is part of 1 target(s):
| Target | Category | Definition |
|---|
| kainate selective glutamate receptor complex | cellular component | An assembly of four or five subunits which form a structure with an extracellular N-terminus and a large loop that together form the ligand binding domain. The C-terminus is intracellular. The ionotropic glutamate receptor complex itself acts as a ligand gated ion channel; on binding glutamate, charged ions pass through a channel in the center of the receptor complex. Kainate receptors are multimeric assemblies of GluK1-3 (also called GluR5-7), GluK4 (KA1) and GluK5 (KA2) subunits. [GOC:bf, http://www.bris.ac.uk/Depts/Synaptic/info/glutamate.html, PMID:18655795] |
Involved In
This protein is involved in 11 target(s):
| Target | Category | Definition |
|---|
| glutamate receptor signaling pathway | biological process | The series of molecular signals initiated by the binding of glutamate to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling, PMID:9131252] |
| chemical synaptic transmission | biological process | The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse. [GOC:jl, MeSH:D009435] |
| nervous system development | biological process | The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state. [GOC:dgh] |
| central nervous system development | biological process | The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord. [GOC:bf, GOC:jid, ISBN:0582227089] |
| calcium-mediated signaling | biological process | Any intracellular signal transduction in which the signal is passed on within the cell via calcium ions. [GOC:signaling] |
| monoatomic ion transmembrane transport | biological process | A process in which a monoatomic ion is transported across a membrane. Monatomic ions (also called simple ions) are ions consisting of exactly one atom. [GOC:mah] |
| ionotropic glutamate receptor signaling pathway | biological process | The series of molecular signals initiated by glutamate binding to a glutamate receptor on the surface of the target cell, followed by the movement of ions through a channel in the receptor complex, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, ISBN:0198506732] |
| regulation of synaptic transmission, glutamatergic | biological process | Any process that modulates the frequency, rate or extent of glutamatergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter glutamate. [GOC:ai] |
| regulation of postsynaptic membrane potential | biological process | Any process that modulates the potential difference across a post-synaptic membrane. [GOC:dph, GOC:ef] |
| modulation of chemical synaptic transmission | biological process | Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission. [GOC:ai] |
| synaptic transmission, glutamatergic | biological process | The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse. [GOC:dos] |