ReviewMarine drugs2010
The tetrodotoxin receptor of voltage-gated sodium channels--perspectives from interactions with micro-conotoxins.
Review in Marine drugs, 2010. 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
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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.
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, 40 citations in OpenAlex.
- Tetrodotoxin (TTX): What do we currently know? The state of the art.Archives of toxicology · 2026Review
- Historical Perspective of the Characterization of Conotoxins Targeting Voltage-Gated Sodium Channels.Marine drugs · 2023Review
- Molecular determinants of μ-conotoxin KIIIA interaction with the human voltage-gated sodium channel NaFrontiers in pharmacology · 2023Article
- Computational Design of High-Affinity Blockers for Sodium Channel NaMarine drugs · 2022Article
- Article
- Small cyclic sodium channel inhibitors.Biochemical pharmacology · 2021Article
- Extremely Potent Block of Bacterial Voltage-Gated Sodium Channels by µ-Conotoxin PIIIA.Marine drugs · 2019Article
- Structural and Functional Analyses of Cone Snail Toxins.Marine drugs · 2019Review
- Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conotoxins That Could Provide Analgesia through Voltage Gated Sodium Channel Inhibition.Toxins · 2015Review
- Structure of membrane-active toxin from crab spider Heriaeus melloteei suggests parallel evolution of sodium channel gating modifiers in Araneomorphae and Mygalomorphae.The Journal of biological chemistry · 2015Article
- Recent progress in neuroactive marine natural products.Natural product reports · 2014Review
- Expanding chemical diversity of conotoxins: peptoid-peptide chimeras of the sodium channel blocker μ-KIIIA and its selenopeptide analogues.European journal of medicinal chemistry · 2013Article
- Mammalian neuronal sodium channel blocker μ-conotoxin BuIIIB has a structured N-terminus that influences potency.ACS chemical biology · 2013Article
- Design of bioactive peptides from naturally occurring μ-conotoxin structures.The Journal of biological chemistry · 2012Article
- Receptor-targeting mechanisms of pain-causing toxins: How ow?Toxicon : official journal of the International Society on Toxinology · 2012Review
- Neurotoxins and their binding areas on voltage-gated sodium channels.Frontiers in pharmacology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Neurotoxin receptor site 1, in the outer vestibule of the conducting pore of voltage-gated sodium channels (VGSCs), was first functionally defined by its ability to bind the guanidinium-containing agents, tetrodotoxin (TTX) and saxitoxin (STX). Subsequent studies showed that peptide micro-conotoxins competed for binding at site 1. All of these natural inhibitors block single sodium channels in an all-or-none manner on binding. With the discovery of an increasing variety of micro-conotoxins, and the synthesis of numerous derivatives, observed interactions between the channel and these different ligands have become more complex. Certain micro-conotoxin derivatives block single-channel currents partially, rather than completely, thus enabling the demonstration of interactions between the bound toxin and the channel's voltage sensor. Most recently, the relatively small micro-conotoxin KIIIA (16 amino acids) and its variants have been shown to bind simultaneously with TTX and exhibit both synergistic and antagonistic interactions with TTX. These interactions raise new pharmacological possibilities and place new constraints on the possible structures of the bound complexes of VGSCs with these toxins.
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.