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

Disruption of a putative intersubunit electrostatic bond enhances agonist efficacy at the human α1 glycine receptor.

Brain research - 15 Feb 2017

Welsh Brian T, Todorovic Jelena, Kirson Dean, Allen Hunter M, Bayly Michelle D, Mihic S John

Abstract excerpt

Partial agonists have lower efficacies than compounds considered 'full agonists', eliciting submaximal responses even at saturating concentrations. Taurine is a partial agonist at the glycine receptor (GlyR), a member of the cys-loop ligand-gated ion channel superfamily. The molecular mechanisms responsible for agonism are not fully understood but evidence suggests that efficacy at these receptors is determined...

Read the complete abstract on PubMed

Topics

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

Share to Aminobutyrates
Share to Aminoisobutyric Acids

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Membrane Potentials

Share to Neurotransmitter Agents

Share to Receptors, Glycine

Share to Static Electricity

Share to Taurine

Share to Xenopus laevis

Source

Open in PubMed Open full text

Identifiers

PMID: 27923639
DOI: 10.1016/j.brainres.2016.11.024
PMCID: PMC5303145

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disruption of a putative intersubunit electrostatic bond enhances agonist efficacy at the human α1 glycine receptor.PMID 27923639Read ↗

Disruption of an intersubunit electrostatic bond is a critical step in glycine receptor activation.Semantic proximity Read ↗

Comparison of taurine- and glycine-induced conformational changes in the M2-M3 domain of the glycine receptor.Semantic proximity Read ↗

Propofol modulation of α1 glycine receptors does not require a structural transition at adjacent subunits that is crucial to agonist-induced activation.Semantic proximity Read ↗

Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor.Semantic proximity Read ↗

Mechanism of gating and partial agonist action in the glycine receptor.Semantic proximity Read ↗

A highly conserved aspartic acid residue in the signature disulfide loop of the alpha 1 subunit is a determinant of gating in the glycine receptor.Semantic proximity Read ↗

Lack of positive allosteric modulation of mutated alpha(1)S267I glycine receptors by cannabinoids.Semantic proximity Read ↗

The M4 transmembrane segment contributes to agonist efficacy differences between alpha1 and alpha3 glycine receptors.Semantic proximity Read ↗

Correlating structural and energetic changes in glycine receptor activation.Semantic proximity Read ↗

Gating mechanism of the human α1β GlyR by glycineSemantic proximity Read ↗

A mutation in the glycine binding pocket of the N-methyl-D-aspartate receptor NR1 subunit alters agonist efficacy.Semantic proximity Read ↗

Exploring the Activation Process of the Glycine Receptor.Semantic proximity Read ↗

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