ArticleNature2013
Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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.
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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
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 107 citations in OpenAlex.
- Vaginal metatranscriptome meta-analysis reveals functional BV subgroups and novel colonisation strategies.Microbiome · 2024Pooled it
- ModifiedWorld journal of gastroenterology · 2017Trial
- Revisiting gut microbiota-driven ammonia metabolism: from disease burden to physiological adaptation.Gut microbes · 2026Review
- Article
- Berberine and Berberine-Derived Compounds as Promising Weapons AgainstPharmaceuticals (Basel, Switzerland) · 2026Review
- When can AlphaFold predict the oligomeric states of proteins?Protein science : a publication of the Protein Society · 2026Article
- Clear Native Gel Electrophoresis for the Purification of Fluorescently Labeled Membrane Proteins in Native Nanodiscs.Analytical chemistry · 2025Article
- Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified bySmall science · 2025Article
- Enhanced Site-Specific Fluorescent Labeling of Membrane Proteins Using Native Nanodiscs.Biomolecules · 2025Article
- Comprehensive multiomics analysis of the signatures of gastric mucosal bacteria and plasma metabolites across different stomach microhabitats in the development of gastric cancer.Cellular oncology (Dordrecht, Netherlands) · 2025Article
- Urea Transport Mediated by Membrane Proteins of Non-urea-Transporters.Sub-cellular biochemistry · 2025Review
- Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025Review
- New Directions inInfection and drug resistance · 2025Review
- Targeted nanotherapeutics for the treatment of Helicobacter pylori infection.Journal of biomedical science · 2024Review
- Structural characterization of human urea transporters UT-A and UT-B and their inhibition.Science advances · 2023Article
- Helicobacter pylori infection.Nature reviews. Disease primers · 2023Review
- Cryo-EM for Small Molecules.Current protocols · 2022Review
- Biomimetic Artificial Proton Channels.Biomolecules · 2022Review
- Protective immunity enhancedFrontiers in immunology · 2022Article
- Urea transport and hydrolysis in the rumen: A review.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2021Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Half the world's population is chronically infected with Helicobacter pylori, causing gastritis, gastric ulcers and an increased incidence of gastric adenocarcinoma. Its proton-gated inner-membrane urea channel, HpUreI, is essential for survival in the acidic environment of the stomach. The channel is closed at neutral pH and opens at acidic pH to allow the rapid access of urea to cytoplasmic urease. Urease produces NH(3) and CO(2), neutralizing entering protons and thus buffering the periplasm to a pH of roughly 6.1 even in gastric juice at a pH below 2.0. Here we report the structure of HpUreI, revealing six protomers assembled in a hexameric ring surrounding a central bilayer plug of ordered lipids. Each protomer encloses a channel formed by a twisted bundle of six transmembrane helices. The bundle defines a previously unobserved fold comprising a two-helix hairpin motif repeated three times around the central axis of the channel, without the inverted repeat of mammalian-type urea transporters. Both the channel and the protomer interface contain residues conserved in the AmiS/UreI superfamily, suggesting the preservation of channel architecture and oligomeric state in this superfamily. Predominantly aromatic or aliphatic side chains line the entire channel and define two consecutive constriction sites in the middle of the channel. Mutation of Trp 153 in the cytoplasmic constriction site to Ala or Phe decreases the selectivity for urea in comparison with thiourea, suggesting that solute interaction with Trp 153 contributes specificity. The previously unobserved hexameric channel structure described here provides a new model for the permeation of urea and other small amide solutes in prokaryotes and archaea.
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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.