NBQX disodium salt, AMPA / kainate antagonist
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(74 Publications)
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- Cited in over 60 publications
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Chemical Structure - NBQX disodium salt, AMPA / kainate antagonist (AB120046)
2D chemical structure image of ab120046, NBQX disodium salt, AMPA / kainate antagonist
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Functional Studies - NBQX disodium salt, AMPA / kainate antagonist (AB120046)
ab96379 staining MEK1 (phospho S298) in SK-N-SH cells treated with NBQX disodium salt (ab120046), by ICC/IF. Decrease in MEK1 (phospho S298) expression correlates with increased concentration of NBQX disodium salt, as described in literature.
The cells were incubated at 37°C for 24h in media containing different concentrations of ab120046 (NBQX disodium salt) in DMSO, fixed with 4% formaldehyde for 10 minutes at room temperature and blocked with PBS containing 10% goat serum, 0.3 M glycine, 1% BSA and 0.1% tween for 2h at room temperature. Staining of the treated cells with ab96379 (1/100 dilution) was performed overnight at 4°C in PBS containing 1% BSA and 0.1% tween. A DyLight® 488 goat anti-rabbit polyclonal antibody (ab96899) at 1/250 dilution was used as the secondary antibody.
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Pathways
The GluR1-containing AMPA receptors participate significantly in the glutamatergic signaling pathway which is vital for fast excitatory synaptic transmission in the brain. This pathway also involves the NMDA receptors which work together with AMPA receptors to regulate synaptic plasticity and neuronal communication. Additionally the GluR1 interacts within the long-term potentiation (LTP) pathway contributing to the strengthening of synapses an essential mechanism underlying learning and memory.
Biological function summary
The GluR1 subunit is an essential component of the AMPA receptor complex which typically forms as a tetramer. This complex modulates synaptic strength and plasticity processes critical for learning and memory. The activity of AMPA receptors including those containing GluR1 is regulated by several auxiliary proteins and is essential for post-synaptic responses. The GluR1 subunit also interacts with other proteins such as TARPs which modulate its trafficking and channel properties.
Publications (74)
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Nature communications 16:5663 PubMed40595546
2025
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eLife 13: PubMed40013677
2025
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eLife 13: PubMed39819796
2025
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Science advances 11:eadq6663 PubMed39823338
2025
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The Journal of neuroscience : the official journal of the Society for Neuroscience 44: PubMed39147589
2024
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iScience 27:110145 PubMed38952682
2024
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Nature communications 15:5095 PubMed38876987
2024
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Nature neuroscience 27:484-496 PubMed38233682
2024
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eLife 12: PubMed37490401
2023
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Cell reports 40:111440 PubMed36170833
2022
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