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

Role of dimer interface in activation and desensitization in AMPA receptors.

Proceedings of the National Academy of Sciences of the United States of America - 25 May 2010

Gonzalez Jennifer, Du Mei, Parameshwaran Kodeeswaran, Suppiramaniam Vishnu, Jayaraman Vasanthi

Abstract excerpt

The conversion of chemical to electrical signals by the AMPA receptors is the key step by which these proteins control cognitive and motor responses. Here, we have used luminescence resonance energy transfer (LRET) to gain insight into the conformational changes induced by glutamate binding in th...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Fluorescence Resonance Energy Transfer
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oocytes

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Receptors, AMPA

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 20457909
DOI: 10.1073/pnas.0911854107
PMCID: PMC2906876

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20457909-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of dimer interface in activation and desensitization in AMPA receptors.PMID 20457909Read ↗

Mechanism of glutamate receptor desensitization.Semantic proximity Read ↗

Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.Semantic proximity Read ↗

Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Semantic proximity Read ↗

A domain linking the AMPA receptor agonist binding site to the ion pore controls gating and causes lurcher properties when mutated.Semantic proximity Read ↗

Configurational Preference of the Glutamate Receptor Ligand Binding Domain Dimers.Semantic proximity Read ↗

Steered Molecular Dynamics Simulations Predict Conformational Stability of Glutamate Receptors.Semantic proximity Read ↗

Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions.Semantic proximity Read ↗

Diversity in AMPA receptor complexes in the brain.Semantic proximity Read ↗

Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes.Semantic proximity Read ↗

Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.Semantic proximity Read ↗

Unitary Properties of AMPA Receptors with Reduced Desensitization.Semantic proximity Read ↗

Coupled control of desensitization and gating by the ligand binding domain of glutamate receptors.Semantic proximity Read ↗

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