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

N-glycosylation of acid-sensing ion channel 1a regulates its trafficking and acidosis-induced spine remodeling.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 21 Mar 2012

Jing Lan, Chu Xiang-Ping, Jiang Yu-Qing, Collier Daniel M, Wang Bin, Jiang Qian, Snyder Peter M, Zha Xiang-Ming

Abstract excerpt

Acid-sensing ion channel-1a (ASIC1a) is a potential therapeutic target for multiple neurological diseases. We studied here ASIC1a glycosylation and trafficking, two poorly understood processes pivotal in determining the functional outcome of an ion channel. We found that most ASIC1a in the mouse brain was fully glycosylated. Inhibiting glycosylation with tunicamycin reduced ASIC1a surface trafficking, dendritic...

Read the complete abstract on PubMed

Topics

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

Share to Acid Sensing Ion Channels
Share to Acidosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Asparagine

Share to Biotinylation

Share to Dendritic Spines

Share to Organ Culture Techniques

Share to Tunicamycin

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 22442073
DOI: 10.1523/JNEUROSCI.5021-11.2012
PMCID: PMC3322463

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

N-glycosylation of acid-sensing ion channel 1a regulates its trafficking and acidosis-induced spine remodeling.PMID 22442073Read ↗

Human ASIC1a mediates stronger acid-induced responses as compared with mouse ASIC1a.Semantic proximity Read ↗

Three distinct motifs within the C-terminus of acid-sensing ion channel 1a regulate its surface trafficking.Semantic proximity Read ↗

Two di-leucine motifs regulate trafficking and function of mouse ASIC2a.Semantic proximity Read ↗

Physiologic and pathophysiologic consequences of altered sialylation and glycosylation on ion channel function.Semantic proximity Read ↗

N-glycosylation of the AMPA-type glutamate receptor regulates cell surface expression and tetramer formation affecting channel function.Semantic proximity Read ↗

Dynamic conformational changes of acid-sensing ion channels in different desensitizing conditionsSemantic proximity Read ↗

Disruption of ER ion homeostasis maintained by an ER anion channel CLCC1 contributes to ALS-like pathologies.Semantic proximity Read ↗

Disruption of ER ion homeostasis maintained by an ER anion channel contributes to ALS-like pathologiesSemantic proximity Read ↗

Conformational plasticity of human acid-sensing ion channel 1aSemantic proximity Read ↗

Identification of the modulatory Ca2+-binding sites of acid-sensing ion channel 1a.Semantic proximity Read ↗

The Intracellular N-Terminal Domain of the Acid-Sensing Ion Channel 1a Participates in Channel Opening and Membrane Expression.Semantic proximity Read ↗

Protonation controls ASIC1a activity via coordinated movements in multiple domains.Semantic proximity Read ↗

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