ArticleNature communications2015
A pain-inducing centipede toxin targets the heat activation machinery of nociceptor TRPV1.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
72 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.
- Centipede Venom Peptides Acting on Ion Channels.Toxins · 2020Pooled it
- Distinct functional open states of the polymodal nociceptor TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A single-point mutation in TRPA1 drives heat resilience in oviparous embryos.Science advances · 2026Article
- Review
- Peptides derived from exocrine secretions of venomous animals used as traditional Chinese "worm" medicines.Zoological research · 2026Review
- Article
- Mechanism of capsaicin entry into buried vanilloid sites in TRPV1.Nature chemical biology · 2025Article
- Neurotoxins Acting on TRPV1-Building a Molecular Template for the Study of Pain and Thermal Dysfunctions.Toxins · 2025Review
- Deciphering Scorpion Toxin-Induced Pain: Molecular Mechanisms and Ion Channel Dynamics.International journal of biological sciences · 2025Review
- Article
- Tick-Derived Peptide Blocks Potassium Channel TREK-1.International journal of molecular sciences · 2024Article
- Genetic code expansion, click chemistry, and light-activated PI3K reveal details of membrane protein trafficking downstream of receptor tyrosine kinases.bioRxiv : the preprint server for biology · 2024Article
- 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
- Design, synthesis and functional validation of peptide inhibitors based on TRPV1 ion channel agonist RhTx.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024Article
- Article
- A thermal receptor for nonvisual sunlight detection in myriapods.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cannabidiol sensitizes TRPV2 channels to activation by 2-APB.bioRxiv : the preprint server for biology · 2023Article
- Article
- Structure-guided peptide engineering of a positive allosteric modulator targeting the outer pore of TRPV1 for long-lasting analgesia.Nature communications · 2023Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
The capsaicin receptor TRPV1 ion channel is a polymodal nociceptor that responds to heat with exquisite sensitivity through an unknown mechanism. Here we report the identification of a novel toxin, RhTx, from the venom of the Chinese red-headed centipede that potently activates TRPV1 to produce excruciating pain. RhTx is a 27-amino-acid small peptide that forms a compact polarized molecule with very rapid binding kinetics and high affinity for TRPV1. We show that RhTx targets the channel's heat activation machinery to cause powerful heat activation at body temperature. The RhTx-TRPV1 interaction is mediated by the toxin's highly charged C terminus, which associates tightly to the charge-rich outer pore region of the channel where it can directly interact with the pore helix and turret. These findings demonstrate that RhTx binding to the outer pore can induce TRPV1 heat activation, therefore providing crucial new structural information on the heat activation machinery.
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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.