Evidence map›Paper›PMID 29262680›Full record

ArticleJournal of the American Chemical Society2018

Mechanism of OmpG pH-Dependent Gating from Loop Ensemble and Single Channel Studies.

Alan Perez-Rathke, Monifa A Fahie, Christina Chisholm, Jie Liang, Min Chen

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Simulation of pH-Dependent, Loop-Based Membrane Protein Gating Using Pretzel.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Cell-Free Expression ofACS nano · 2023
    Article
  10. Article
  11. Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Simulation of pH-Dependent, Loop-Based Membrane Protein Gating Using Pretzel.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  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

5 authors at 1 institution in 1 country.

Alan Perez-RathkeDepartment of Bioengineering, University of Illinois at Chicago , Chicago, Illinois 60607, United States.
Monifa A Fahie
Christina Chisholm
Jie LiangDepartment of Bioengineering, University of Illinois at Chicago , Chicago, Illinois 60607, United States.ORCID 0000-0002-2773-6427
University of Illinois Chicago · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Computational assembly of beta-barrel membrane proteinsR01GM079804 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LIANG, JIE · 2007 to 2016
$2.8M
Collaborative Research: Mathematical Framework for Biomolecules: From Protein to RNA to ChromosomesR01GM126558 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHANG, JINFENG · 2017 to 2021
$1.5M
OmpG nanopore for single molecule protein sensingR01GM115442 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, MIN · 2016 to 2020
$1.5M
NIGMS NIH HHS R01 GM079804NIGMS NIH HHS R01 GM115442NIGMS NIH HHS R01 GM126558NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

Outer membrane protein G (OmpG) from Escherichia coli has exhibited pH-dependent gating that can be employed by bacteria to alter the permeability of their outer membranes in response to environmental changes. We developed a computational model, Protein Topology of Zoetic Loops (Pretzel), to investigate the roles of OmpG extracellular loops implicated in gating. The key interactions predicted by our model were verified by single-channel recording data. Our results indicate that the gating equilibrium is primarily controlled by an electrostatic interaction network formed between the gating loop and charged residues in the lumen. The results shed light on the mechanism of OmpG gating and will provide a fundamental basis for the engineering of OmpG as a nanopore sensor. Our computational Pretzel model could be applied to other outer membrane proteins that contain intricate dynamic loops that are functionally important.

Indexed as

Bacterial Outer Membrane ProteinsEscherichia coli K12Escherichia coli ProteinsHydrogen-Ion ConcentrationIon Channel GatingModels, MolecularPorinsProtein ConformationStatic ElectricityBacterial Outer Membrane ProteinsEscherichia coli ProteinsOmpG protein, E coliPorins

Identifiers

PMID29262680
PMCPMC5831328
OpenAlexW2779720604

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.