Evidence map›Paper›PMID 19012294›Full record

ArticleChembiochem : a European journal of chemical biology2008

Orientation of the monomeric porin OmpG in planar lipid bilayers.

Min Chen, Qiu-Hong Li, Hagan Bayley

Open access · greenAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.7field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Protein Analyte Sensing with an Outer Membrane Protein G (OmpG) Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Article
  3. Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025
    Article
  4. Article
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  6. Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021
    Article
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  16. Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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.

Min ChenDepartment of Chemistry, University of Oxford, Oxford, UK.
Qiu-Hong Li
Hagan Bayley
University of Oxford · GB

Funding

Single-Molecule DNA Sequencing with Engineered NanoporesR01HG003709 · NHGRI · SCRIPPS RESEARCH INSTITUTE, THE · PI GHADIRI, M. REZA · 2005 to 2017
$13.2M
Medical Research Council G0300122NHGRI NIH HHS R01 HG003709
6 · The paper itself

Abstract

Outer membrane protein G (OmpG) is a non-selective porin from Escherichia coli. OmpG is a monomer, which makes it unusual among porins, and suggests that it may be useful in biotechnology. In planar lipid bilayers, individual OmpG pores reconstituted by insertion from detergent exhibit pronounced asymmetry in current-voltage relationships and voltage-dependent gating. Here, this asymmetry is used to deduce the orientation of OmpG in the bilayers. We introduced two cysteines into the extracellular loops of OmpG. Cleavage of the disulfide bond formed by these residues significantly increases spontaneous gating of the pore. By adding DTT to one side of the bilayer or the other, we demonstrated that pores showing a quiet trace at negative potentials have a "trans" conformation (extracellular loops on the trans side of the bilayer), while pores showing a quiet trace at positive potentials have a "cis" conformation (extracellular loops on the cis side). With this knowledge, we examined the binding of a cyclodextrin to OmpG. When the cyclodextrin was presented to the extracellular face of the pore, transient multisite interactions were observed. In contrast, when the cyclodextrin was presented to the periplasmic face, a more stable single-site interaction occurred. Because the cyclodextrin can act as a molecular adapter by binding analytes, this information serves to advance the use of OmpG as a biosensor.

Indexed as

Bacterial Outer Membrane ProteinsCyclodextrinsCysteineDithiothreitolEscherichia coli ProteinsLipid BilayersPorinsVoltage-Dependent Anion ChannelsBacterial Outer Membrane ProteinsCyclodextrinsCysteineDithiothreitolEscherichia coli ProteinsLipid BilayersOmpG protein, E coliPorinsVoltage-Dependent Anion Channels

Identifiers

PMID19012294
PMCPMC3498615
OpenAlexW2058411875

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.