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

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

The Journal of biological chemistry - 7 May 2004

Han Nian-Lin R, Clements John D, Lynch Joseph W

Abstract excerpt

In the ionotropic glutamate receptor, the global conformational changes induced by partial agonists are smaller than those induced by full agonists. However, in the pentameric ligand-gated ion channel receptor family, the structural basis of partial agonism is not understood. This study investigated whether full and partial agonists induce different conformation changes in the glycine receptor chloride channel...

Read the complete abstract on PubMed

Topics

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

Share to Electrophysiology
Share to Glycine
Share to Inhibitory Concentration 50

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysine

Share to Mesylates

Share to Receptors, Glycine

Share to Sulfhydryl Reagents

Share to Taurine

Source

Identifiers

PMID: 14981077
DOI: 10.1074/jbc.M400548200

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

Comparison of taurine- and glycine-induced conformational changes in the M2-M3 domain of the glycine receptor.PMID 14981077Read ↗

A picrotoxin-specific conformational change in the glycine receptor M2-M3 loop.Semantic proximity Read ↗

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

Mechanism of gating and partial agonist action in 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 ↗

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

Distinct conformational changes in activated agonist-bound and agonist-free glycine receptor subunits.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 ↗

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

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

Building new function into glycine receptors: a structural model for the activation of the glycine-gated chloride channel.Semantic proximity Read ↗

A novel hyperekplexia-causing mutation in the pre-transmembrane segment 1 of the human glycine receptor alpha1 subunit reduces membrane expression and impairs gating by agonists.Semantic proximity Read ↗

Agonist-specific conformational changes in the α1-γ2 subunit interface of the GABA A receptor.Semantic proximity Read ↗

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