Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural insights into competitive antagonism in NMDA receptors.

Neuron - 22 Jan 2014

Jespersen Annie, Tajima Nami, Fernandez-Cuervo Gabriela, Garnier-Amblard Ethel C, Furukawa Hiro

Abstract excerpt

There has been a great level of enthusiasm to downregulate overactive N-methyl-D-aspartate (NMDA) receptors to protect neurons from excitotoxicity. NMDA receptors play pivotal roles in basic brain development and functions as well as in neurological disorders and diseases. However, mechanistic understanding of antagonism in NMDA receptors is limited due to complete lack of antagonist-bound structures for the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Crystallography
Share to Excitatory Amino Acid Antagonists
Share to Glycine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microinjections

Share to Molecular Conformation

Share to Patch-Clamp Techniques

Share to Receptors, N-Methyl-D-Aspartate

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 24462099
DOI: 10.1016/j.neuron.2013.11.033
PMCID: PMC3997178

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural insights into competitive antagonism in NMDA receptors.PMID 24462099Read ↗

A Novel Binding Mode Reveals Two Distinct Classes of NMDA Receptor GluN2B-selective Antagonists.Semantic proximity Read ↗

Identification of novel allosteric modulator binding sites in NMDA receptors: A molecular modeling study.Semantic proximity Read ↗

Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition.Semantic proximity Read ↗

Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core.Semantic proximity Read ↗

An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.Semantic proximity Read ↗

Glutamate unbinding reveals new insights into NMDA receptor activation.Semantic proximity Read ↗

Downstream allosteric modulation of NMDA receptors by 3-benzazepine derivativesSemantic proximity Read ↗

Molecular and functional diversity of the NMDA receptor channel.Semantic proximity Read ↗

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain.Semantic proximity Read ↗

Disruption of interdomain interactions in the glutamate binding pocket affects differentially agonist affinity and efficacy of N-methyl-D-aspartate receptor activation.Semantic proximity Read ↗

Selective Negative Allosteric Modulation Of Metabotropic Glutamate Receptors – A Structural Perspective of Ligands and Mutants.Semantic proximity Read ↗

Mechanism of partial agonist action at the NR1 subunit of NMDA receptors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.