ArticlePflugers Archiv : European journal of physiology2006
Molecular cloning and functional characterization of the Aplysia FMRFamide-gated Na+ channel.
Article in Pflugers Archiv : European journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Flipped binding modes for the same agonist in closely related neuropeptide-gated ion channels.Biophysical journal · 2025Article
- Aromatic amino acids in the finger domain of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2023Article
- The FMRF-NH2 gated sodium channel of Biomphalaria glabrata: Localization and expression following infection by Schistosoma mansoni.PLoS neglected tropical diseases · 2023Article
- Comparative analysis defines a broader FMRFamide-gated sodium channel family and determinants of neuropeptide sensitivity.The Journal of biological chemistry · 2022Article
- Review: The evolution of peptidergic signaling in Cnidaria and Placozoa, including a comparison with Bilateria.Frontiers in endocrinology · 2022Review
- The chemical brain hypothesis for the origin of nervous systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- New techniques, applications and perspectives in neuropeptide research.The Journal of experimental biology · 2018Review
- The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide.The Journal of biological chemistry · 2017Article
- Modulation of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2017Article
- Identification of a cono-RFamide from the venom ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel.The Journal of biological chemistry · 2016Article
- Review
- Electrostatic charge at position 552 affects the activation and permeation of FMRFamide-gated Na+ channels.The journal of physiological sciences : JPS · 2014Article
- Diversity of the RFamide Peptide Family in Mollusks.Frontiers in endocrinology · 2014Review
- Parasite neuropeptide biology: Seeding rational drug target selection?International journal for parasitology. Drugs and drug resistance · 2012Review
- Heterologous expression of the invertebrate FMRFamide-gated sodium channel as a mechanism to selectively activate mammalian neurons.Neuroscience · 2008Article
- NMR analysis of Caenorhabditis elegans FLP-18 neuropeptides: implications for NPR-1 activation.Biochemistry · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FMRFamide-gated Na+ channel (FaNaC) is the only known peptide-gated ion channel, which belongs to the epithelial Na+ channel/degenerin (ENaC/DEG) family. We have cloned a putative FaNaC from the Aplysia kurodai CNS library using PCR, and examined its characteristics in Xenopus oocytes. A. kurodai FaNaC (AkFaNaC) comprised with 653 amino acids, and the sequence predicts two putative membrane domains and a large extracellular domain as in other members of the ENaC/DEG family. In oocytes expressing AkFaNaC, FMRFamide evoked amiloride-sensitive Na+ current. Different from the known FaNaCs (Helix and Helisoma FaNaCs), AkFaNaC was blocked by external Ca2+ but not by Mg2+. Also, desensitization of the current was enhanced by Mg2+ but not by Ca2+. The FMRFamide-gated current was depressed in both low and high pH. These results indicate that AkFaNaC is an FaNaC of Aplysia, and that the channel has Aplysia specific functional domains.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.