Evidence map›Paper›PMID 24305683›Full record

ArticleNature communications2013

Mechanisms of molecular transport through the urea channel of Helicobacter pylori.

Reginald McNulty, Jakob P Ulmschneider, Hartmut Luecke, Martin B Ulmschneider

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.4field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Carbon dioxide regulatesInfection and immunity · 2025
    Article
  4. Article
  5. New Directions inInfection and drug resistance · 2025
    Review
  6. Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Cryo-EM for Small Molecules.Current protocols · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Urea-aromatic interactions in biology.Biophysical reviews · 2020
    Review
  16. Review
  17. pH-dependent gating mechanism of theScience advances · 2019
    Article
  18. Protection AgainstFrontiers in immunology · 2018
    Article
  19. Sodium butyrate mitigates in vitro ammonia generation in cecal content of laying hens.Environmental science and pollution research international · 2016
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 4 institutions in 2 countries.

Reginald McNulty1] Center for Biomembrane Systems & Department of Molecular Biology & Biochemistry, University of California, Irvine, California 92697, USA [2].
Jakob P Ulmschneider
Hartmut Luecke
Martin B Ulmschneider
Irvine University · USJohns Hopkins University · USScripps Research Institute · USShanghai Jiao Tong University · CN

Funding

Structure-Function Studies of the Proton-Gated Urea Channel from H. PyloriR01AI078000 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI LUECKE, HARTMUT · 2008 to 2016
$4.3M
Innovative Supercomputing for Breakthrough Molecular DynamicsRC2GM093307 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI DITTRICH, MARKUS · 2009 to 2010
$2.7M
NIAID NIH HHS R01 AI078000NIAID NIH HHS R01AI078000NIGMS NIH HHS RC2 GM093307NIGMS NIH HHS RC2GM093307
6 · The paper itself

Abstract

Helicobacter pylori survival in acidic environments relies on cytoplasmic hydrolysis of gastric urea into ammonia and carbon dioxide, which buffer the pathogen's periplasm. Urea uptake is greatly enhanced and regulated by HpUreI, a proton-gated inner membrane channel protein essential for gastric survival of H. pylori. The crystal structure of HpUreI describes a static snapshot of the channel with two constriction sites near the center of the bilayer that are too narrow to allow passage of urea or even water. Here we describe the urea transport mechanism at atomic resolution, revealed by unrestrained microsecond equilibrium molecular dynamics simulations of the hexameric channel assembly. Two consecutive constrictions open to allow conduction of urea, which is guided through the channel by interplay between conserved residues that determine proton rejection and solute selectivity. Remarkably, HpUreI conducts water at rates equivalent to aquaporins, which might be essential for efficient transport of urea at small concentration gradients.

Indexed as

Bacterial ProteinsBiological TransportHelicobacter pyloriMembrane Transport ProteinsMolecular Dynamics SimulationUreaWaterBacterial ProteinsMembrane Transport ProteinsUreaUreI protein, Helicobacter pyloriWater

Identifiers

PMID24305683
PMCPMC3863980
OpenAlexW2030119097

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.