ArticleNeuropharmacology2015
Snake neurotoxin α-bungarotoxin is an antagonist at native GABA(A) receptors.
Article in Neuropharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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.
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Who cites it
29 citing papers in PubMed, 44 citations in OpenAlex.
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- Cyanidin-3-O-glucoside (C3G): A natural small-molecule compound for alleviating envenomation symptoms Induced by Bungarus multicinctus.PLoS neglected tropical diseases · 2026Article
- Early effects of α7nAChR regulation on maxillary expansion in mice : A study on osteogenesis and inflammatory factors.Journal of orofacial orthopedics = Fortschritte der Kieferorthopadie : Organ/official journal Deutsche Gesellschaft fur Kieferorthopadie · 2026Article
- Estimation of genome-wide coupling in rattlesnake hybrids provides insight into the process of speciation and its progress.Nature communications · 2025Article
- The Need for and Importance of Thorough and Comprehensive Studies on the Molecular Mechanisms of Action of Animal Toxins, Venoms, and Antivenoms.International journal of molecular sciences · 2025Article
- Molecular mechanism of human αCommunications biology · 2025Article
- A genetically engineered neuronal membrane-based nanotoxoid elicits protective immunity against neurotoxins.Bioactive materials · 2024Article
- Cholinergic Mechanisms in Gastrointestinal Neoplasia.International journal of molecular sciences · 2024Review
- The Cloning and Characterization of a Three-Finger Toxin Homolog (NXH8) from the CoralsnakeToxins · 2024Article
- Pharmacological Screening of Venoms from Five BrazilianInternational journal of molecular sciences · 2022Article
- Article
- Three-Finger Toxins from Brazilian Coral Snakes: From Molecular Framework to Insights in Biological Function.Toxins · 2021Article
- Novel Three-Finger Neurotoxins fromToxins · 2021Article
- Biomedical applications of snake venom: from basic science to autoimmunity and rheumatology.Journal of translational autoimmunity · 2021Review
- Interaction of α9α10 Nicotinic Receptors With Peptides and Proteins From Animal Venoms.Frontiers in cellular neuroscience · 2021Article
- Visualizing GABA A Receptor Trafficking Dynamics with Fluorogenic Protein Labeling.Current protocols in neuroscience · 2020Article
- Bipolar Cell Type-Specific Expression and Conductance of Alpha-7 Nicotinic Acetylcholine Receptors in the Mouse Retina.Investigative ophthalmology & visual science · 2019Article
- Last decade update for three-finger toxins: Newly emerging structures and biological activities.World journal of biological chemistry · 2019Review
- Proteomic Investigation of Murine Neuronal α7-Nicotinic Acetylcholine Receptor Interacting Proteins.Journal of proteome research · 2018Article
- Comparison of Strategies to Overcome Drug Resistance: Learning from Various Kingdoms.Molecules (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The snake neurotoxin α-bungarotoxin (α-Bgtx) is a competitive antagonist at nicotinic acetylcholine receptors (nAChRs) and is widely used to study their function and cell-surface expression. Increasingly, α-Bgtx is also used as an imaging tool for fluorophore-labelling studies, and given the structural conservation within the pentameric ligand-gated ion channel family, we assessed whether α-Bgtx could bind to recombinant and native γ-aminobutyric type-A receptors (GABAARs). Applying fluorophore-linked α-Bgtx to recombinant αxβ1/2γ2 GABAARs expressed in HEK-293 cells enabled clear cell-surface labelling of α2β1/2γ2 contrasting with the weaker staining of α1/4β1/2γ2, and no labelling for α3/5/6β1/2γ2. The labelling of α2β2γ2 was abolished by bicuculline, a competitive antagonist at GABAARs, and by d-tubocurarine (d-Tc), which acts in a similar manner at nAChRs and GABAARs. Labelling by α-Bgtx was also reduced by GABA, suggesting that the GABA binding site at the receptor β-α subunit interface forms part of the α-Bgtx binding site. Using whole-cell recording, high concentrations of α-Bgtx (20 μM) inhibited GABA-activated currents at all αxβ2γ2 receptors examined, but at lower concentrations (5 μM), α-Bgtx was selective for α2β2γ2. Using α-Bgtx, at low concentrations, permitted the selective inhibition of α2 subunit-containing GABAARs in hippocampal dentate gyrus granule cells, reducing synaptic current amplitudes without affecting the GABA-mediated tonic current. In conclusion, α-Bgtx can act as an inhibitor at recombinant and native GABAARs and may be used as a selective tool to inhibit phasic but not tonic currents in the hippocampus.
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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 Socratic graph.