Evidence map›Paper›PMID 19361419›Full record

ArticleJournal of molecular biology2009

Oligomeric structure and functional characterization of the urea transporter from Actinobacillus pleuropneumoniae.

Stefan Raunser, John C Mathai, Priyanka D Abeyrathne, Amanda J Rice, Mark L Zeidel, Thomas Walz

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Microbial conversion of biodiesel waste for carotenoid production.Frontiers in bioengineering and biotechnology · 2026
    Article
  2. Protein Structures of Urea Transporters.Sub-cellular biochemistry · 2025
    Review
  3. Article
  4. Urea-aromatic interactions in biology.Biophysical reviews · 2020
    Review
  5. Article
  6. Structure of urea transporters.Sub-cellular biochemistry · 2014
    Review
  7. Article
  8. Article
  9. Structure and permeation mechanism of a mammalian urea transporter.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  10. Review
  11. Article
  12. 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

6 authors at 2 institutions in 1 country.

Stefan RaunserDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
John C Mathai
Priyanka D Abeyrathne
Amanda J Rice
Mark L Zeidel
Thomas Walz
Harvard University · USBeth Israel Deaconess Medical Center · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
MECHANISMS OF WATER FLOW ACROSS BIOLOGICAL MEMBRANESR01DK043955 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZEIDEL, MARK L. · 1991 to 2009
$3.2M
Structural and functional studies of urea channelsR01GM082927 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALZ, THOMAS · 2008 to 2011
$923k
Howard Hughes Medical InstituteNIDDK NIH HHS DK43955NIDDK NIH HHS R01 DK043955NIGMS NIH HHS P01 GM062580NIGMS NIH HHS P01 GM62580NIGMS NIH HHS R01 GM082927
6 · The paper itself

Abstract

Urea transporters (UTs) facilitate urea permeation across cell membranes in prokaryotes and eukaryotes. Bacteria use urea as a means to survive in acidic environments and/or as a nitrogen source. The UT from Actinobacillus pleuropneumoniae, ApUT, the pathogen that causes porcine pleurisy and pneumonia, was expressed in Escherichia coli and purified. Analysis of the recombinant protein using cross-linking and blue-native gel electrophoresis established that ApUT is a dimer in detergent solution. Purified protein was reconstituted into proteoliposomes and urea efflux was measured by stopped-flow fluorometry to determine the urea transport kinetics of ApUT. The measured urea flux was saturable, could be inhibited by phloretin, and was not affected by pH. Two-dimensional crystals of the biologically active ApUT show that it is also dimeric in a lipid membrane and provide the first structural information on a member of the UT family.

Indexed as

Protein Structure, QuaternaryActinobacillus pleuropneumoniaeAnimalsBacterial ProteinsCrystallizationDetergentsDimerizationHumansMembrane Transport ProteinsPermeabilitySwineUreaUrea TransportersBacterial ProteinsDetergentsMembrane Transport ProteinsUreaUrea Transporters

Identifiers

PMID19361419
PMCPMC2682783
OpenAlexW2008229348

What OpenQuestion holds

Textmetadata
LicenceTDM
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.