ArticleNature2015
Structure of the TRPA1 ion channel suggests regulatory mechanisms.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 308 papers, 2 of them syntheses that pooled it.
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
308 citing papers in PubMed, 2 syntheses or guidelines pooled it, 662 citations in OpenAlex.
- The Role of TRP Channels in Colitis and Inflammatory Bowel Disease: A Systematic Review.International journal of molecular sciences · 2025Pooled it
- A 10-year meta-analysis of membrane protein structural biology: Detergents, membrane mimetics, and structure determination techniques.Biochimica et biophysica acta. Biomembranes · 2021Pooled it
- Decay chemicals activate a pH-sensing pathway to initiate a persistent state.bioRxiv : the preprint server for biology · 2026Article
- Review
- Chemical Characterization and Pharmacological Activity of Byrsonima crassifolia (L.) Kunth (Murici): Antinociceptive Effects, Edema Reduction, and Molecular Docking.Chemistry & biodiversity · 2026Article
- TRPA1 Channels as Multimodal Environmental Sensors: Structure-Function Insights From Aquatic Organisms.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- Bidirectional crosstalk between TRP channels and Toll-like receptors in inflammation and host defense.Journal of neuroinflammation · 2026Review
- Schwann Cell TRPA1, a Proalgesic Ion Channel, Mediates Neuroinflammation and Fibromyalgia-Associated Behaviours in Mice.Journal of neurochemistry · 2026Review
- Methodological validation of a cryo-TEM-based detection method for empty capsid ratio in recombinant adeno-associated virus.Biochemistry and biophysics reports · 2026Article
- Europium Metal Complex [Eu(dbm)Chemistry & biodiversity · 2026Article
- Mechanostimulation of neuroendocrine cells and their clinical relevance.Molecular and cellular biochemistry · 2026Review
- Temperature-induced structural changes in thermosensitive transient receptor potential channels (thermoTRPs).Frontiers in molecular neuroscience · 2026Review
- TRP Channels from Sensory Coding to Physiology.Metabolites · 2025Review
- Molecular defense strategy of volatile organic compound-emitting plants (order Piperales) against herbivorous mammals.Communications biology · 2025Article
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Molecular mediators of cold adaptation in mammalian cells.Communications biology · 2025Review
- Calmodulin binding is required for calcium mediated TRPA1 desensitization.Nature communications · 2025Article
- Evolutionary adaptations of TRPA1 thermosensitivity and skin thermoregulation in vertebrates.iScience · 2025Article
- Identification of Phialomustin‑B (PHL-B) as a Novel Natural TRPA1 Channel Inhibitor.ACS omega · 2025Article
- The HIV-1 nuclear export complex reveals the role of RNA in CRM1 cargo recognition.Molecular cell · 2025Article
248 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The TRPA1 ion channel (also known as the wasabi receptor) is a detector of noxious chemical agents encountered in our environment or produced endogenously during tissue injury or drug metabolism. These include a broad class of electrophiles that activate the channel through covalent protein modification. TRPA1 antagonists hold potential for treating neurogenic inflammatory conditions provoked or exacerbated by irritant exposure. Despite compelling reasons to understand TRPA1 function, structural mechanisms underlying channel regulation remain obscure. Here we use single-particle electron cryo- microscopy to determine the structure of full-length human TRPA1 to ∼4 Å resolution in the presence of pharmacophores, including a potent antagonist. Several unexpected features are revealed, including an extensive coiled-coil assembly domain stabilized by polyphosphate co-factors and a highly integrated nexus that converges on an unpredicted transient receptor potential (TRP)-like allosteric domain. These findings provide new insights into the mechanisms of TRPA1 regulation, and establish a blueprint for structure-based design of analgesic and anti-inflammatory agents.
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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.