Evidence map›Paper›PMID 18443290›Full record

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

Outer membrane protein G: Engineering a quiet pore for biosensing.

Min Chen, Syma Khalid, Mark S P Sansom, Hagan Bayley

Abstract 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 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing 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

82 citing papers in PubMed.

  1. Article
  2. Generative design of programmable asymmetric β-barrel nanopores.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Simulation of pH-Dependent, Loop-Based Membrane Protein Gating Using Pretzel.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023
    Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Min ChenChemistry Research Laboratory, Department of Chemistry, University of Oxford, Mansfield Road, Oxford OX1 3TA, United Kingdom.
Syma Khalid
Mark S P Sansom
Hagan Bayley

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032Medical Research Council G0300122
6 · The paper itself

Abstract

Bacterial outer membrane porins have a robust beta-barrel structure and therefore show potential for use as stochastic sensors based on single-molecule detection. The monomeric porin OmpG is especially attractive compared with multisubunit proteins because appropriate modifications of the pore can be easily achieved by mutagenesis. However, the gating of OmpG causes transient current blockades in single-channel recordings that would interfere with analyte detection. To eliminate this spontaneous gating activity, we used molecular dynamics simulations to identify regions of OmpG implicated in the gating. Based on our findings, two approaches were used to enhance the stability of the open conformation by site-directed mutagenesis. First, the mobility of loop 6 was reduced by introducing a disulfide bond between the extracellular ends of strands beta12 and beta13. Second, the interstrand hydrogen bonding between strands beta11 and beta12 was optimized by deletion of residue D215. The OmpG porin with both stabilizing mutations exhibited a 95% reduction in gating activity. We used this mutant for the detection of adenosine diphosphate at the single-molecule level, after equipping the porin with a cyclodextrin molecular adapter, thereby demonstrating its potential for use in stochastic sensing applications.

Indexed as

Biosensing TechniquesProtein EngineeringAdenosine DiphosphateBacterial Outer Membrane Proteinsbeta-CyclodextrinsComputer SimulationEscherichia coli ProteinsHydrogen BondingIon Channel GatingModels, MolecularMutant ProteinsPorinsPrincipal Component AnalysisProtein ConformationStochastic ProcessesAdenosine DiphosphateBacterial Outer Membrane Proteinsbeta-CyclodextrinsbetadexEscherichia coli ProteinsMutant ProteinsOmpG protein, E coliPorins

Identifiers

PMID18443290
PMCPMC2359795

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.