Evidence map›Paper›PMID 22272184›Full record

ArticlePLoS biology2012

Substrate specificity within a family of outer membrane carboxylate channels.

Elif Eren, Jagamya Vijayaraghavan, Jiaming Liu, Belete R Cheneke, Debra S Touw, Bryan W Lepore, Mridhu Indic, Liviu Movileanu, Bert van den Berg

Abstract read
In one paragraph

Article in PLoS biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
–field-weighted citation impact
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

64 citing papers in PubMed.

  1. Trial
  2. Article
  3. A periplasmic metallochaperone (PmcY) couples ZnAntimicrobial agents and chemotherapy · 2026
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  4. High stability of the genome ofMicrobiology spectrum · 2026
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  6. Understanding Drug Permeability inLife (Basel, Switzerland) · 2025
    Review
  7. Review
  8. Review
  9. Review
  10. Outer membrane permeability ofMicrobiology spectrum · 2025
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Review
  17. Article
  18. Review
  19. Anti-Adhesion and Antibiofilm Activity ofPlants (Basel, Switzerland) · 2022
    Article
  20. Article

4 more citing papers are in PubMed but not listed here.

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

9 authors.

Elif ErenUniversity of Massachusetts Medical School, Program in Molecular Medicine, Worcester, Massachusetts, United States of America.
Jagamya Vijayaraghavan
Jiaming Liu
Belete R Cheneke
Debra S Touw
Bryan W Lepore
Mridhu Indic
Liviu Movileanu
Bert van den Berg

Funding

Engineered Nanopores for Single-Molecule Stochastic SensingR01GM088403 · NIGMS · SYRACUSE UNIVERSITY · PI MOVILEANU, LIVIU · 2009 to 2022
$3.8M
Structural and biochemical characterization of the OprD membrane protein familyR01GM085785 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI VAN DEN BERG, BERT · 2008 to 2011
$1.3M
NIGMS NIH HHS R01 GM085785NIGMS NIH HHS R01 GM088403
6 · The paper itself

Abstract

Many Gram-negative bacteria, including human pathogens such as Pseudomonas aeruginosa, do not have large-channel porins. This results in an outer membrane (OM) that is highly impermeable to small polar molecules, making the bacteria intrinsically resistant towards many antibiotics. In such microorganisms, the majority of small molecules are taken up by members of the OprD outer membrane protein family. Here we show that OprD channels require a carboxyl group in the substrate for efficient transport, and based on this we have renamed the family Occ, for outer membrane carboxylate channels. We further show that Occ channels can be divided into two subfamilies, based on their very different substrate specificities. Our results rationalize how certain bacteria can efficiently take up a variety of substrates under nutrient-poor conditions without compromising membrane permeability. In addition, they explain how channel inactivation in response to antibiotics can cause resistance but does not lead to decreased fitness.

Indexed as

Multigene FamilyAnti-Bacterial AgentsBacterial Outer Membrane ProteinsConserved SequenceCrystallography, X-RayHumansIon Channel GatingIon ChannelsModels, BiologicalModels, MolecularPorinsPorosityProtein BindingProtein Structure, SecondaryProtein TransportPseudomonas aeruginosaAnti-Bacterial AgentsBacterial Outer Membrane ProteinsIon ChannelsOprD protein, Pseudomonas aeruginosaPorins

Identifiers

PMID22272184
PMCPMC3260308

What OpenQuestion holds

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LicenceCC BY
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.