ArticleeLife2019
Enzyme activity and selectivity filter stability of ancient TRPM2 channels were simultaneously lost in early vertebrates.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis 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
23 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Pooled it
- CaCommunications biology · 2026Article
- Evolution in metazoans of the TRPM channel family involves multiple gains and losses of genes and domains.Molecular biology and evolution · 2026Article
- Domain-Specific Agonist Binding Affinities Explain Structural and Functional Regulation of TRPM2.bioRxiv : the preprint server for biology · 2026Article
- Thermosensitive TRPM2: The regulatory mechanisms of its temperature sensitivity and physiological functions.The journal of physiological sciences : JPS · 2025Review
- A conserved mechanism couples cytosolic domain movements to pore gating in the TRPM2 channel.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Coupling enzymatic activity and gating in an ancient TRPM chanzyme and its molecular evolution.Nature structural & molecular biology · 2024Article
- Navigating the Controversies: Role of TRPM Channels in Pain States.International journal of molecular sciences · 2024Review
- Functional characterization of the transient receptor potential melastatin 2 (TRPM2) cation channel from Nematostella vectensis reconstituted into lipid bilayer.Scientific reports · 2023Article
- Cell death induction and protection by activation of ubiquitously expressed anion/cation channels. Part 3: the roles and properties of TRPM2 and TRPM7.Frontiers in cell and developmental biology · 2023Review
- Dual amplification strategy turns TRPM2 channels into supersensitive central heat detectors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Review
- TRP channels in health and disease at a glance.Journal of cell science · 2021Article
- Species-Specific Regulation of TRPM2 by PI(4,5)PInternational journal of molecular sciences · 2021Article
- Two Decades of Evolution of Our Understanding of the Transient Receptor Potential Melastatin 2 (TRPM2) Cation Channel.Life (Basel, Switzerland) · 2021Review
- Structure-Function Relationship of TRPM2: Recent Advances, Contradictions, and Open Questions.International journal of molecular sciences · 2020Review
- Simple binding of protein kinase A prior to phosphorylation allows CFTR anion channels to be opened by nucleotides.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The N-terminal domain in TRPM2 channel is a conserved nucleotide binding site.The Journal of general physiology · 2020Article
- Selective profiling of N- and C-terminal nucleotide-binding sites in a TRPM2 channel.The Journal of general physiology · 2020Article
- A structural overview of the ion channels of the TRPM family.Cell calcium · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Transient Receptor Potential Melastatin 2 (TRPM2) is a cation channel important for the immune response, insulin secretion, and body temperature regulation. It is activated by cytosolic ADP ribose (ADPR) and contains a nudix-type motif 9 (NUDT9)-homology (NUDT9-H) domain homologous to ADPR phosphohydrolases (ADPRases). Human TRPM2 (hsTRPM2) is catalytically inactive due to mutations in the conserved Nudix box sequence. Here, we show that TRPM2 Nudix motifs are canonical in all invertebrates but vestigial in vertebrates. Correspondingly, TRPM2 of the cnidarian
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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.