Evidence map›Paper›PMID 30990011›Full record

ArticleACS sensors2019

Quiet Outer Membrane Protein G (OmpG) Nanopore for Biosensing.

Raghavendar Reddy Sanganna Gari, Patrick Seelheim, Binyong Liang, Lukas K Tamm

Abstract read
In one paragraph

Article in ACS sensors, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Sculpting conducting nanopore size and shape throughbioRxiv : the preprint server for biology · 2023
    Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Structure and dynamics of nanoconfined water and aqueous solutions.The European physical journal. E, Soft matter · 2021
    Review
  15. Review
  16. Article
  17. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  18. Article
  19. Review
  20. Review
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.

Raghavendar Reddy Sanganna GariDepartment of Molecular Physiology and Biological Physics , Center for Cell and Membrane Physiology at the University of Virginia , Charlottesville , Virginia 22908 , United States.
Patrick SeelheimDepartment of Molecular Physiology and Biological Physics , Center for Cell and Membrane Physiology at the University of Virginia , Charlottesville , Virginia 22908 , United States.
Binyong LiangDepartment of Molecular Physiology and Biological Physics , Center for Cell and Membrane Physiology at the University of Virginia , Charlottesville , Virginia 22908 , United States.
Lukas K TammDepartment of Molecular Physiology and Biological Physics , Center for Cell and Membrane Physiology at the University of Virginia , Charlottesville , Virginia 22908 , United States.ORCID 0000-0002-1674-4464

Funding

Structure, Assembly, and Function of Outer Membrane ProteinsR01GM051329 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI TAMM, LUKAS K · 1997 to 2018
$6.4M
NIGMS NIH HHS R01 GM051329
6 · The paper itself

Abstract

Interest in nanopore technology has been growing due to nanopores' unique capabilities in small molecule sensing, measurement of protein folding, and low-cost DNA and RNA sequencing. The E. coli β-barrel outer membrane protein OmpG is an excellent alternative to other protein nanopores because of its single polypeptide chain. However, the flexibility of its extracellular loops ultimately limits applications in traditional biosensing. We deleted several residues in and near loop 6 of OmpG. The dynamic structure of the new construct determined by NMR shows that loops 1, 2, 6, and 7 have reduced flexibilities compared to those of wild-type. Electrophysiological measurements show that the new design virtually eliminates flickering between open and closed states across a wide pH range. Modification of the pore lumen with a copper chelating moiety facilitates detection of small molecules. As proof of concept, we demonstrate concurrent single-molecule biosensing of glutamate and adenosine triphosphate.

Indexed as

NanoporesAdenosine TriphosphateBacterial Outer Membrane ProteinsBiosensing TechniquesEscherichia coli ProteinsGlutamic AcidModels, MolecularPorinsProtein Conformation, beta-StrandAdenosine TriphosphateBacterial Outer Membrane ProteinsEscherichia coli ProteinsGlutamic AcidOmpG protein, E coliPorinsbiosensorblack lipid membraneelectrophysiologynanoporeNMROmpGouter membrane protein

Identifiers

PMID30990011
PMCPMC6596296

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.