Evidence map›Paper›PMID 18559855›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation.

Elizabeth M Hearn, Dimki R Patel, Bert van den Berg

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Transcriptome ofMicroorganisms · 2024
    Article
  4. Review
  5. Review
  6. Microbial membrane transport proteins and their biotechnological applications.World journal of microbiology & biotechnology · 2024
    Review
  7. Article
  8. Review
  9. Microorganisms · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Passive membrane transport of lignin-related compounds.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. Toward engineeringProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. 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

3 authors at 1 institution in 1 country.

Elizabeth M HearnProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.
Dimki R Patel
Bert van den Berg
University of Massachusetts Chan Medical School · US

Funding

Hydrophobics transport across the outer membraneR01GM074824 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI VAN DEN BERG, BERT · 2005 to 2009
$1.5M
Transport of hydrophobic xenobiotics by gram-negative bacterial membrane proteinsF32GM079820 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI HEARN, ELIZABETH M · 2007 to 2008
$96k
NIGMS NIH HHS F32 GM079820NIGMS NIH HHS GM079820NIGMS NIH HHS R01 GM074824NIGMS NIH HHS R01GM074824
6 · The paper itself

Abstract

Bacterial biodegradation of hydrocarbons, an important process for environmental remediation, requires the passage of hydrophobic substrates across the cell membrane. Here, we report crystal structures of two outer membrane proteins, Pseudomonas putida TodX and Ralstonia pickettii TbuX, which have been implicated in hydrocarbon transport and are part of a subfamily of the FadL fatty acid transporter family. The structures of TodX and TbuX show significant differences with those previously determined for Escherichia coli FadL, which may provide an explanation for the substrate-specific transport of TodX and TbuX observed with in vivo transport assays. The TodX and TbuX structures revealed 14-stranded beta-barrels with an N-terminal hatch domain blocking the barrel interior. A hydrophobic channel with bound detergent molecules extends from the extracellular surface and is contiguous with a passageway through the hatch domain, lined by both hydrophobic and polar or charged residues. The TodX and TbuX structures support a mechanism for transport of hydrophobic substrates from the extracellular environment to the periplasm via a channel through the hatch domain.

Indexed as

Bacterial Outer Membrane ProteinsBinding SitesBiodegradation, EnvironmentalBiological TransportCrystallography, X-RayEscherichia coliHydrocarbons, AromaticModels, MolecularProtein Structure, TertiaryPseudomonas putidaRalstonia pickettiiSubstrate SpecificityBacterial Outer Membrane ProteinsHydrocarbons, Aromatic

Identifiers

PMID18559855
PMCPMC2438428
OpenAlexW2097999179

What OpenQuestion holds

Textmetadata
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.