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

Channel-opening kinetic mechanism of wild-type GluK1 kainate receptors and a C-terminal mutant.

Biochemistry - 24 Jan 2012

Han Yan, Wang Congzhou, Park Jae Seon, Niu Li

Abstract excerpt

GluK1 is a kainate receptor subunit in the ionotropic glutamate receptor family and can form functional channels when expressed, for instance, in HEK-293 cells. However, the channel-opening mechanism of GluK1 is poorly understood. One major challenge to studying the GluK1 channel is its apparent low level of surface expression, which results in a low whole-cell current response even to a saturating concentration...

Read the complete abstract on PubMed

Topics

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

Share to Alternative Splicing
Share to Endoplasmic Reticulum
Share to Glutamic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Isoenzymes

Share to Peptide Fragments

Share to Photolysis

Share to Receptors, Kainic Acid

Share to Up-Regulation

Source

Open in PubMed Open full text

Identifiers

PMID: 22191429
DOI: 10.1021/bi201446z
PMCID: PMC3272274

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Channel-opening kinetic mechanism of wild-type GluK1 kainate receptors and a C-terminal mutant.PMID 22191429Read ↗

Receptor occupancy and channel-opening kinetics: a study of GLUR1 L497Y AMPA receptor.Semantic proximity Read ↗

Functional Roles of the Edited Isoform of GluA2 in GluA2-Containing AMPA Receptor Channels.Semantic proximity Read ↗

Cell surface expression of GluR5 kainate receptors is regulated by an endoplasmic reticulum retention signal.Semantic proximity Read ↗

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

A binding site tyrosine shapes desensitization kinetics and agonist potency at GluR2. A mutagenic, kinetic, and crystallographic study.Semantic proximity Read ↗

Kinetic analysis of open- and closed-state inactivation transitions in human Kv4.2 A-type potassium channels.Semantic proximity Read ↗

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

Structure, Function, and Regulation of the Kainate Receptor.Semantic proximity Read ↗

Ligand binding is a critical requirement for plasma membrane expression of heteromeric kainate receptors.Semantic proximity Read ↗

Block of kainate receptor desensitization uncovers a key trafficking checkpoint.Semantic proximity Read ↗

Transmembrane topology of two kainate receptor subunits revealed by N-glycosylation.Semantic proximity Read ↗

Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization.Semantic proximity Read ↗

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