ArticleProceedings of the National Academy of Sciences of the United States of America2013
Discovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.
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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
79 citing papers in PubMed, 1 synthesis or guideline pooled it, 173 citations in OpenAlex.
- Centipede Venom Peptides Acting on Ion Channels.Toxins · 2020Pooled it
- Voltage-gated sodium channels in the nervous system: Molecular physiology to therapeutic interventions.Neural regeneration research · 2026Article
- Structural basis for inhibition of the voltage-gated sodium channel NaThe Journal of biological chemistry · 2026Article
- Molecular determinant of low-voltage dependence of human NaNature communications · 2026Article
- Exploring the Pain-Relieving Potential: Unveiling Antinociceptive Properties in Animal Venoms and Toxins.Toxins · 2026Review
- Peptides derived from exocrine secretions of venomous animals used as traditional Chinese "worm" medicines.Zoological research · 2026Review
- From Discovery to the Future Medical Applications of Venom-derived Analgesic Peptides for the Treatment of Peripheral Pains.Current pharmaceutical design · 2026Review
- Spider venom peptides with unique fold selectively block Shaker-type potassium channels.Cellular and molecular life sciences : CMLS · 2025Article
- Article
- Pathology of pain and its implications for therapeutic interventions.Signal transduction and targeted therapy · 2024Review
- Isolation and structural identification of a potassium ion channel Kv4.1 inhibitor SsTx-P2 from centipede venom.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024Article
- Coevolution with toxic prey produces functional trade-offs in sodium channels of predatory snakes.bioRxiv : the preprint server for biology · 2023Article
- Isolation and Characterization of Poeciguamerin, a Peptide with Dual Analgesic and Anti-Thrombotic Activity from theInternational journal of molecular sciences · 2023Article
- Antihepatoma peptide, scolopentide, derived from the centipede scolopendra subspinipes mutilans.World journal of gastroenterology · 2023Article
- General mechanism of spider toxin family I acting on sodium channel Nav1.7.Zoological research · 2022Article
- Bioactive Peptides and Proteins from Centipede Venoms.Molecules (Basel, Switzerland) · 2022Review
- Centipede Venom: A Potential Source of Ion Channel Modulators.International journal of molecular sciences · 2022Review
- Shrew's venom quickly causes circulation disorder, analgesia and hypokinesia.Cellular and molecular life sciences : CMLS · 2022Article
- An Apriori Algorithm-Based Association Analysis of Analgesic Drugs in Chinese Medicine Prescriptions Recorded From Patients With Rheumatoid Arthritis Pain.Frontiers in pain research (Lausanne, Switzerland) · 2022Article
- Antitussive effects of NaEuropean journal of pharmacology · 2021Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Loss-of-function mutations in the human voltage-gated sodium channel NaV1.7 result in a congenital indifference to pain. Selective inhibitors of NaV1.7 are therefore likely to be powerful analgesics for treating a broad range of pain conditions. Herein we describe the identification of µ-SLPTX-Ssm6a, a unique 46-residue peptide from centipede venom that potently inhibits NaV1.7 with an IC50 of ∼25 nM. µ-SLPTX-Ssm6a has more than 150-fold selectivity for NaV1.7 over all other human NaV subtypes, with the exception of NaV1.2, for which the selectivity is 32-fold. µ-SLPTX-Ssm6a contains three disulfide bonds with a unique connectivity pattern, and it has no significant sequence homology with any previously characterized peptide or protein. µ-SLPTX-Ssm6a proved to be a more potent analgesic than morphine in a rodent model of chemical-induced pain, and it was equipotent with morphine in rodent models of thermal and acid-induced pain. This study establishes µ-SPTX-Ssm6a as a promising lead molecule for the development of novel analgesics targeting NaV1.7, which might be suitable for treating a wide range of human pain pathologies.
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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.