Evidence map›Paper›PMID 33058855›Full record

ArticleBiochimica et biophysica acta. Biomembranes2021

A pH-independent quiet OmpG pore with enhanced electrostatic repulsion among the extracellular loops.

Bach Pham, Christina M Chisholm, Joshua Foster, Emily Friis, Monifa A Fahie, Min Chen

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023
    Article
  8. Review
  9. 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

6 authors.

Bach PhamDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003, United States.
Christina M ChisholmMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA 01003, United States.
Joshua FosterMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA 01003, United States.
Emily FriisDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003, United States.
Monifa A FahieMolecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA 01003, United States.
Min ChenDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA 01003, United States; Molecular and Cellular Biology Program, University of Massachusetts Amherst, Amherst, MA 01003, United States. Electronic address: mchen1@umass.edu.

Funding

OmpG nanopore for single molecule protein sensingR01GM115442 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI CHEN, MIN · 2016 to 2020
$1.5M
NIGMS NIH HHS R01 GM115442
6 · The paper itself

Abstract

Membrane protein pores have emerged as powerful nanopore sensors for single-molecule detection. OmpG, a monomeric nanopore, is comprised of fourteen β-strands connected by seven flexible extracellular loops. The OmpG nanopore exhibits pH-dependent gating as revealed by planar lipid bilayer studies. Current evidence strongly suggests that the dynamic movement of loop 6 is responsible for the gating mechanism. In this work, we have shown that enhancing the electrostatic repulsion forces between extracellular loops suppressed the pH-dependent gating. Our mutant containing additional negative charges in loop 6 and loop 1 exhibited minimal spontaneous gating and reduced sensitivity to pH changes compared to the wild type OmpG. These results provide new evidence to support the mechanism of OmpG gating controlled by the complex electrostatic network around the gating loop 6. The pH-independent quiet OmpG pores could potentially be used as a sensing platform that operates at a broad range of pH conditions.

Indexed as

Ion Channel GatingBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsHydrogen-Ion ConcentrationLipid BilayersPorinsProtein Structure, SecondaryStatic ElectricityBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipid BilayersOmpG protein, E coliPorinsGating mechanismNanoporeOuter membrane protein GQuiet pore

Identifiers

PMID33058855
PMCPMC7704735

What OpenQuestion holds

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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.