Evidence map›Paper›PMID 20533493›Full record

ArticleChembiochem : a European journal of chemical biology2010

Going forward laterally: transmembrane passage of hydrophobic molecules through protein channel walls.

Bert van den Berg

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Lipid Transport Across Bacterial Membranes.Annual review of cell and developmental biology · 2022
    Review
  9. Review
  10. Article
  11. Article
  12. Passive membrane transport of lignin-related compounds.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  16. Article
  17. Review
  18. 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

1 author at 1 institution in 1 country.

Bert van den BergUniversity of Massachusetts Medical School, Program in Molecular Medicine, 373 Plantation Street, Worcester, MA 01606, USA. bert.vandenberg@umassmed.edu
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
NIGMS NIH HHS R01 GM074824PHS HHS 5R01M074824
6 · The paper itself

Abstract

Regular phospholipid bilayers do not pose efficient barriers for the transport of hydrophobic molecules. The outer membrane (OM) surrounding Gram-negative bacteria is a nontypical, asymmetric bilayer with an outer layer of lipopolysaccharide (LPS). The sugar molecules of the LPS layer prevent spontaneous diffusion of hydrophobic molecules across the OM. As regular OM channels such as porins do not allow passage of hydrophobic molecules, specialized OM transport proteins are required for their uptake. Such proteins, exemplified by channels of the FadL family, transport their substrates according to a lateral diffusion mechanism. Here, substrates diffuse from the lumen of the beta-barrel laterally into the OM, through a stable opening in the wall of the barrel. In this way, the lipopolysaccharide barrier is bypassed and, by depositing the substrates into the OM, a driving force for uptake is provided. Lateral diffusion through protein channel walls also occurs in alpha-helical inner membrane proteins, and could represent a widespread mechanism for proteins that transport and interact with hydrophobic substrates.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneCrystallography, X-RayEscherichia coli ProteinsFatty Acid Transport ProteinsGram-Negative BacteriaHydrophobic and Hydrophilic InteractionsLipopolysaccharidesMembrane Transport ProteinsPorinsProtein Structure, TertiaryBacterial Outer Membrane ProteinsEscherichia coli ProteinsfadL protein, E coliFatty Acid Transport ProteinsLipopolysaccharidesMembrane Transport ProteinsOmpF proteinPorins

Identifiers

PMID20533493
PMCPMC3013500
OpenAlexW2101969209

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.