ArticlePloS one2013
A novel inhibitor of α9α10 nicotinic acetylcholine receptors from Conus vexillum delineates a new conotoxin superfamily.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- Surface-Imprinted Acrylamide Polymer-Based Reduced Graphene-Gold Sensor in Rapid and Sensitive Electrochemical Determination of αB-Conotoxin.Sensors (Basel, Switzerland) · 2025Article
- Unravelling the allosteric binding mode of αD-VxXXB at nicotinic acetylcholine receptors.Frontiers in pharmacology · 2023Article
- Article
- Development of Immunochromatographic Strip for Detection of αB-VxXXIVA-Conotoxin Based on 5E4 Monoclonal Antibody.Toxins · 2022Article
- Detection of αB-Conotoxin VxXXIVA (αB-CTX) by ic-ELISA Based on an Epitope-Specific Monoclonal Antibody.Toxins · 2022Article
- Marine Origin Ligands of Nicotinic Receptors: Low Molecular Compounds, Peptides and Proteins for Fundamental Research and Practical Applications.Biomolecules · 2022Review
- Structural and Functional Diversity of Animal Toxins Interacting With GPCRs.Frontiers in molecular biosciences · 2022Review
- High-Throughput Prediction and Design of Novel Conopeptides for Biomedical Research and Development.Biodesign research · 2022Article
- DSPE-PEG Modification of α-Conotoxin TxID.Marine drugs · 2019Article
- Alanine-Scanning Mutagenesis of α-Conotoxin GI Reveals the Residues Crucial for Activity at the Muscle Acetylcholine Receptor.Marine drugs · 2018Article
- Neuronal Nicotinic Acetylcholine Receptor Modulators from Cone Snails.Marine drugs · 2018Review
- αO-Conotoxin GeXIVA disulfide bond isomers exhibit differential sensitivity for various nicotinic acetylcholine receptors but retain potency and selectivity for the human α9α10 subtype.Neuropharmacology · 2017Article
- Backbone cyclization of analgesic conotoxin GeXIVA facilitates direct folding of the ribbon isomer.The Journal of biological chemistry · 2017Article
- A Novel Lid-Covering Peptide Inhibitor of Nicotinic Acetylcholine Receptors Derived from αD-Conotoxin GeXXA.Marine drugs · 2017Article
- Inhibition of α9α10 nicotinic acetylcholine receptors prevents chemotherapy-induced neuropathic pain.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- High-throughput identification of novel conotoxins from the Chinese tubular cone snail (Conus betulinus) by multi-transcriptome sequencing.GigaScience · 2016Article
- Conotoxin αD-GeXXA utilizes a novel strategy to antagonize nicotinic acetylcholine receptors.Scientific reports · 2015Article
- αS-conotoxin GVIIIB potently and selectively blocks α9α10 nicotinic acetylcholine receptors.Biochemical pharmacology · 2015Article
- Cloning, synthesis, and characterization of αO-conotoxin GeXIVA, a potent α9α10 nicotinic acetylcholine receptor antagonist.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Optimized deep-targeted proteotranscriptomic profiling reveals unexplored Conus toxin diversity and novel cysteine frameworks.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Conotoxins (CTxs) selectively target a range of ion channels and receptors, making them widely used tools for probing nervous system function. Conotoxins have been previously grouped into superfamilies according to signal sequence and into families based on their cysteine framework and biological target. Here we describe the cloning and characterization of a new conotoxin, from Conus vexillum, named αB-conotoxin VxXXIVA. The peptide does not belong to any previously described conotoxin superfamily and its arrangement of Cys residues is unique among conopeptides. Moreover, in contrast to previously characterized conopeptide toxins, which are expressed initially as prepropeptide precursors with a signal sequence, a ''pro'' region, and the toxin-encoding region, the precursor sequence of αB-VxXXIVA lacks a ''pro'' region. The predicted 40-residue mature peptide, which contains four Cys, was synthesized in each of the three possible disulfide arrangements. Investigation of the mechanism of action of αB-VxXXIVA revealed that the peptide is a nicotinic acetylcholine receptor (nAChR) antagonist with greatest potency against the α9α10 subtype. (1)H nuclear magnetic resonance (NMR) spectra indicated that all three αB-VxXXIVA isomers were poorly structured in aqueous solution. This was consistent with circular dichroism (CD) results which showed that the peptides were unstructured in buffer, but adopted partially helical conformations in aqueous trifluoroethanol (TFE) solution. The α9α10 nAChR is an important target for the development of analgesics and cancer chemotherapeutics, and αB-VxXXIVA represents a novel ligand with which to probe the structure and function of this protein.
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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 OpenQuestion graph.