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

Hydrophobic interactions mediate binding of the glycine receptor beta-subunit to gephyrin.

Journal of neurochemistry - 1 Mar 1999

Kneussel M, Hermann A, Kirsch J, Betz H

Abstract excerpt

Glycine receptors (GlyRs) are ligand-gated chloride channel proteins composed of alpha- and beta-subunits. GlyRs are located to and anchored at postsynaptic sites by the receptor-associated protein gephyrin. Previous work from our laboratory has identified a core motif for gephyrin binding in the cytoplasmic loop of the GlyR beta-subunit. Here, we localized amino acid residues implicated in gephyrin binding by...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Monoclonal
Share to Carrier Proteins
Share to Green Fluorescent Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kidney

Share to Luminescent Proteins

Share to Mutagenesis, Site-Directed

Share to Receptors, Glycine

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 10037506
DOI: 10.1046/j.1471-4159.1999.0721323.x

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

Hydrophobic interactions mediate binding of the glycine receptor beta-subunit to gephyrin.PMID 10037506Read ↗

Gephyrin-mediated γ-aminobutyric acid type A and glycine receptor clustering relies on a common binding site.Semantic proximity Read ↗

Characterization of the effects of charged residues in the intracellular loop on ion permeation in alpha1 glycine receptor channels.Semantic proximity Read ↗

Structure and functions of inhibitory and excitatory glycine receptors.Semantic proximity Read ↗

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

A Novel Glycine Receptor Variant with Startle Disease Affects Syndapin I and Glycinergic Inhibition.Semantic proximity Read ↗

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

A critical role for glycine transporters in hyperexcitability disordersSemantic proximity Read ↗

Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.Semantic proximity Read ↗

Oligomerization of the {gamma}-aminobutyric acid transporter-1 is driven by an interplay of polar and hydrophobic interactions in transmembrane helix II.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 ↗

Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.Semantic proximity Read ↗

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

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