DL-AP5 sodium salt, NMDA glutamate site antagonist
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(35 Publications)
- Cited in over 30 publications
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- Chemical Structure
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Chemical Structure - DL-AP5 sodium salt, NMDA glutamate site antagonist (AB120271)
2D chemical structure image of ab120271, DL-AP5 sodium salt, NMDA glutamate site antagonist
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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 (35)
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Molecular autism 16:26 PubMed40241211
2025
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Nature communications 15:8841 PubMed39396999
2024
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eLife 12: PubMed38470230
2024
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EMBO reports 25:351-377 PubMed38177913
2024
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Nature communications 14:5285 PubMed37648685
2023
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Cell reports 42:112699 PubMed37368752
2023
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Current protocols 3:e786 PubMed37272700
2023
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Journal of neurochemistry 166:248-264 PubMed37243578
2023
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Communications biology 6:267 PubMed36918719
2023
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The Journal of neuroscience : the official journal of the Society for Neuroscience 43:2002-2020 PubMed36759195
2023
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