ArticleeLife2022
Structural motifs for subtype-specific pH-sensitive gating of vertebrate otopetrin proton channels.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Human OTOP3 requires strong acidification for activation and exhibits mixed proton-anion permeation.The Journal of biological chemistry · 2026Article
- BEST4⁺ cells: a potential hub of intestinal ion transport and diarrhea manipulation.Advanced biotechnology · 2026Review
- OTOP2 proton channel couples luminal pH sensing to intestinal immune homeostasis.The Journal of biological chemistry · 2026Article
- Proton channels govern vesicular carbonate chemistry in mineralizing cells of a marine calcifier.Nature communications · 2026Article
- Developmental regulation of intestinalbioRxiv : the preprint server for biology · 2025Article
- Structure-guided discovery of Otopetrin 1 inhibitors reveals druggable binding sites at the intrasubunit interface.Nature communications · 2025Article
- Paramutation-Like Behavior of Genic piRNA-Producing Loci inInternational journal of molecular sciences · 2025Article
- Preferential allosteric modulation of Otop1 channels by small molecule compounds.Communications biology · 2025Article
- Epitope Tagging with Genome Editing in Mice Reveals That the Proton Channel OTOP1 Is Apically Localized and Not Restricted to Type III "Sour" Taste Receptor Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Receptors and signaling for sour and salty: the ionic taste qualities.Chemical senses · 2025Review
- Genetic analysis of non-syndromic peg lateralis using whole-exome sequencing.Frontiers in genetics · 2025Article
- Zinc inhibits the voltage-gated proton channel HCNL1.Biophysical journal · 2024Article
- Structural mechanism of proton conduction in otopetrin proton channel.Nature communications · 2024Article
- The ion channels of endomembranes.Physiological reviews · 2024Review
- Neuroendocrine cells initiate protective upper airway reflexes.Science (New York, N.Y.) · 2024Article
- Transcendent Aspects of Proton Channels.Annual review of physiology · 2024Review
- Determination of the Immunomodulatory Role of OTOP2 in Colon Adenocarcinoma.Journal of Cancer · 2024Article
- The proton channel OTOP1 is a sensor for the taste of ammonium chloride.Nature communications · 2023Article
- Zinc activation of OTOP proton channels identifies structural elements of the gating apparatus.eLife · 2023Article
- Vertebrate OTOP1 is also an alkali-activated channel.Nature communications · 2023Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Otopetrin (OTOP) channels are proton-selective ion channels conserved among vertebrates and invertebrates, with no structural similarity to other ion channels. There are three vertebrate OTOP channels (OTOP1, OTOP2, and OTOP3), of which one (OTOP1) functions as a sour taste receptor. Whether extracellular protons gate OTOP channels, in addition to permeating them, was not known. Here, we compare the functional properties of the three murine OTOP channels using patch-clamp recording and cytosolic pH microfluorimetry. We find that OTOP1 and OTOP3 are both steeply activated by extracellular protons, with thresholds of pH
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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.