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

Protonation controls ASIC1a activity via coordinated movements in multiple domains.

The Journal of general physiology - 1 Jan 2014

Bonifacio Gaetano, Lelli Cláudia Igutti Suenaga, Kellenberger Stephan

Abstract excerpt

Acid-sensing ion channels (ASICs) are neuronal Na(+)-conducting channels activated by extracellular acidification. ASICs are involved in pain sensation, expression of fear, and neurodegeneration after ischemic stroke. Functional ASICs are composed of three identical or homologous subunits, whose extracellular part has a handlike structure. Currently, it is unclear how protonation of residues in extracellular...

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 Amino Acid Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Ion Channel Gating

Share to Molecular Dynamics Simulation

Share to Protein Structure, Tertiary

Share to Protons

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 24344244
DOI: 10.1085/jgp.201311053
PMCID: PMC3874563

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protonation controls ASIC1a activity via coordinated movements in multiple domains.PMID 24344244Read ↗

Conformational dynamics and role of the acidic pocket in ASIC pH-dependent gating.Semantic proximity Read ↗

Gating transitions in the palm domain of ASIC1a.Semantic proximity Read ↗

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

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

Dynamic conformational changes of acid-sensing ion channels in different desensitizing conditions.Semantic proximity Read ↗

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

Conformational changes in the lower palm domain of ASIC1a contribute to desensitization and RFamide modulation.Semantic proximity Read ↗

Independent contribution of extracellular proton binding sites to ASIC1a activation.Semantic proximity Read ↗

The contact region between three domains of the extracellular loop of ASIC1a is critical for channel function.Semantic proximity Read ↗

Endogenous arginine-phenylalanine-amide-related peptides alter steady-state desensitization of ASIC1a.Semantic proximity Read ↗

Molecular mechanism and structural basis of small-molecule modulation of the gating of acid-sensing ion channel 1.Semantic proximity Read ↗

Extracellular chloride modulates the desensitization kinetics of acid-sensing ion channel 1a (ASIC1a).Semantic proximity Read ↗

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