Evidence map›Paper›PMID 16617058›Full record

ArticleThe Journal of biological chemistry2006

Pseudomonas aeruginosa porin OprF: properties of the channel.

Ekaterina M Nestorovich, Etsuko Sugawara, Hiroshi Nikaido, Sergey M Bezrukov

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. The Building Blocks of Antimicrobial Resistance inFrontiers in cellular and infection microbiology · 2021
    Review
  11. Article
  12. Engineering the Osmotic State ofFrontiers in bioengineering and biotechnology · 2020
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. OtopathogenicFrontiers in microbiology · 2016
    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

4 authors.

Ekaterina M NestorovichLaboratory of Physical and Structural Biology, NICHD/National Institutes of Health, 9 Memorial Drive, Bethesda, MD 20892-0924, USA.
Etsuko Sugawara
Hiroshi Nikaido
Sergey M Bezrukov

Funding

BIOCHEMISTRY OF BACTERIAL CELL MEMBRANESR01AI009644 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI NIKAIDO, HIROSHI · 1985 to 2015
$9.7M
Biophysics of Large Membrane ChannelsZ01HD000072 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BEZRUKOV, SERGEY M · 2004 to 2008
$1.6M
NIAID NIH HHS R01 AI009644
6 · The paper itself

Abstract

Using ion channel reconstitution in planar lipid bilayers, we examined the channel-forming activity of subfractions of Pseudomonas aeruginosa OprF, which was shown to exist in two different conformations: a minority single domain conformer and a majority two-domain conformer (Sugawara, E., Nestorovich, E. M., Bezrukov, S. M., and Nikaido, H. (2006) J. Biol. Chem. 281, 16220-16229). With the fraction depleted for the single domain conformer, we were unable to detect formation of any channels with well defined conductance levels. With the unfractionated OprF, we saw only rare channel formation. However, with the single domain-enriched fraction of OprF, we observed regular insertion of channels with highly reproducible conductances. Single OprF channels demonstrate rich kinetic behavior exhibiting spontaneous transitions between several subconformations that differ in ionic conductance and radius measured in polymer exclusion experiments. Although we showed that the effective radius of the most conductive conformation exceeds that of the general outer membrane porin of Escherichia coli, OmpF, we also found that a single OprF channel mainly exists in weakly conductive subconformations and switches to the fully open state for a short time only. Therefore, the low permeability of OprF reported earlier may be due to two factors: mainly to the paucity of the single domain conformer in the OprF population and secondly to the predominance of weakly conductive subconformations within the single domain conformer.

Indexed as

Bacterial Outer Membrane ProteinsIonsKineticsLipid BilayersLiposomesMolecular ConformationPolymersPorinsProtein ConformationProtein Structure, TertiaryPseudomonas aeruginosaVoltage-Dependent Anion ChannelsBacterial Outer Membrane ProteinsIonsLipid BilayersLiposomesPolymersPorinsVoltage-Dependent Anion Channels

Identifiers

PMID16617058
PMCPMC2846715

What OpenQuestion holds

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Registered trials

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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.