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

Position 552 in a FMRFamide-gated Na(+) channel affects the gating properties and the potency of FMRFamide.

Zoological science - 1 May 2010

Kodani Yu, Furukawa Yasuo

Abstract excerpt

FMRFamide-gated Na(+) channel (FaNaC) is a peptide-gated sodium channel in the epithelial Na(+) channel/degenerin family. Although there are some data on the location of the putative peptide binding site, there is no structural information on the activation gating of FaNaC. Here, we addressed the function of a conserved aspartate residue in the second transmembrane domain of FaNaC. We used Aplysia kurodai FaNaC...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Conserved Sequence
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnesium

Share to Oocytes

Share to Protein Conformation

Share to Sodium Channels

Share to Xenopus

Source

Identifiers

PMID: 20443692
DOI: 10.2108/zsj.27.440

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

Position 552 in a FMRFamide-gated Na(+) channel affects the gating properties and the potency of FMRFamide.PMID 20443692Read ↗

Electrostatic charge at position 552 affects the activation and permeation of FMRFamide-gated Na+ channels.Semantic proximity Read ↗

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

Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complexSemantic proximity Read ↗

On the interaction between amiloride and its putative alpha-subunit epithelial Na+ channel binding site.Semantic proximity Read ↗

H(+)-gated cation channels.Semantic proximity Read ↗

The Pannexin-1 N-terminal Helix Gates a Switch between Ion Conductance and Anandamide TransportSemantic proximity Read ↗

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

Gating induces a conformational change in the outer vestibule of ENaC.Semantic proximity Read ↗

Amino acid substitutions in the FXYD motif enhance phospholemman-induced modulation of cardiac L-type calcium channels.Semantic proximity Read ↗

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

Gamma subunit second transmembrane domain contributes to epithelial sodium channel gating and amiloride block.Semantic proximity Read ↗

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

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