ArticleScience (New York, N.Y.)2018
Structure of the human TRPM4 ion channel in a lipid nanodisc.
Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 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.
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.
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Who cites it
174 citing papers in PubMed, 1 synthesis or guideline pooled it, 277 citations in OpenAlex.
- Pooled it
- A Postzygotic TRPM4 Variant in a Patient with Inflammatory Linear Verrucous Epidermal Nevus.Acta dermato-venereologica · 2026Article
- Temperature-dependent ligand relocation reveals plasticity of TRPM4 inhibition.bioRxiv : the preprint server for biology · 2026Article
- Role of TRPM4 ion channel in pediatric arrhythmic syndromes.World journal of clinical pediatrics · 2026Review
- Temperature and intrinsic CaNature structural & molecular biology · 2026Article
- Evolution in metazoans of the TRPM channel family involves multiple gains and losses of genes and domains.Molecular biology and evolution · 2026Article
- Deep mutational scan of the pore of the cold-sensing TRPM8 channel.bioRxiv : the preprint server for biology · 2026Article
- Potent Anthranilic Anilide-Based TRPM4 Channel Inhibitors Identified by a Structure-Activity Relationship Study.Journal of medicinal chemistry · 2026Article
- A single allosteric site merges activation, modulation and inhibition in TRPM5.Nature chemical biology · 2026Article
- Noncanonical calcium-independent TRPM4 activation governs intestinal fluid homeostasis.Nature communications · 2026Article
- Structural landscape of activation, desensitization and inhibition in the human TRPM4 channel.Nature structural & molecular biology · 2026Article
- Temperature-induced structural changes in thermosensitive transient receptor potential channels (thermoTRPs).Frontiers in molecular neuroscience · 2026Review
- Structural biology of the TRPM4 channel: architecture, modulation, and therapeutic opportunities.Frontiers in pharmacology · 2026Review
- Integrate single-cell and transcriptome analyses to explore the prognostic genes related to TRPM4 in bladder cancer.Frontiers in bioengineering and biotechnology · 2026Article
- Exploiting metabolic cell death for cancer therapy.Nature reviews. Cancer · 2026Review
- MAASTY: a (dis)ordered copolymer for structural determination of human membrane proteins in native nanodiscs.Nature communications · 2025Article
- Transient receptor melastatin channel in colorectal cancer: pathophysiological mechanisms and a promising drug target.Cancer chemotherapy and pharmacology · 2025Review
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Multidimensional pan cancer analysis of the sodium induced cell death gene TRPM4.Scientific reports · 2025Article
- Probabilistic single-particle cryo-EM ab initio 3D reconstruction in SIMPLE.Acta crystallographica. Section D, Structural biology · 2025Article
114 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular calcium in a voltage-dependent manner but, unlike many other TRP channels, is permeable to monovalent cations only. Here we present two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo-electron microscopy. These structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain. The structures correspond to two distinct closed states. Calcium binding induces conformational changes that likely prime the channel for voltage-dependent opening.
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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.