Evidence map›Paper›PMID 25575121›Full record

ArticleACS nano2015

Resolved single-molecule detection of individual species within a mixture of anti-biotin antibodies using an engineered monomeric nanopore.

Monifa Fahie, Christina Chisholm, Min Chen

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

59 citing papers in PubMed, 97 citations in OpenAlex.

  1. The Ion Permeability of DNA Nanotube Channels.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Protein Analyte Sensing with an Outer Membrane Protein G (OmpG) Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Simulation of pH-Dependent, Loop-Based Membrane Protein Gating Using Pretzel.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Specific ATP Detection Using Molecule-Responsive DNA Nanopores.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  11. Article
  12. Graphene Nanopore Fabrication and Applications.International journal of molecular sciences · 2025
    Review
  13. Review
  14. Review
  15. Review
  16. Real-time label-free detection of dynamic aptamer-small molecule interactions using a nanopore nucleic acid conformational sensor.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. 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

3 authors at 1 institution in 1 country.

Monifa FahieMolecular and Cellular Biology Program and Department of Chemistry, University of Massachusetts , Amherst, Massachusetts 01003, United States.
Christina Chisholm
Min Chen
University of Massachusetts Amherst · US

Funding

CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NIGMS NIH HHS T32 GM008515NIGMS NIH HHS T32 GM08515
6 · The paper itself

Abstract

Oligomeric protein nanopores with rigid structures have been engineered for the purpose of sensing a wide range of analytes including small molecules and biological species such as proteins and DNA. We chose a monomeric β-barrel porin, OmpG, as the platform from which to derive the nanopore sensor. OmpG is decorated with seven flexible loops that move dynamically to create a distinct gating pattern when ionic current passes through the pore. Biotin was chemically tethered to the most flexible one of these loops. The gating characteristic of the loop's movement in and out of the porin was substantially altered by analyte protein binding. The gating characteristics of the pore with bound targets were remarkably sensitive to molecular identity, even providing the ability to distinguish between homologues within an antibody mixture. A total of five gating parameters were analyzed for each analyte to create a unique fingerprint for each biotin-binding protein. Our exploitation of gating noise as a molecular identifier may allow more sophisticated sensor design, while OmpG's monomeric structure greatly simplifies nanopore production.

Indexed as

EngineeringNanoporesAnimalsAntibodies, MonoclonalBacterial Outer Membrane ProteinsBiosensing TechniquesBiotinElectricityEscherichia coli ProteinsLigandsModels, MolecularNanotechnologyPolyethylene GlycolsPorinsProtein Structure, SecondaryStreptavidinAntibodies, MonoclonalBacterial Outer Membrane ProteinsBiotinEscherichia coli ProteinsLigandsOmpG protein, E coliPolyethylene GlycolsPorinsStreptavidinnanoporeOmpGprotein sensorsingle-molecule detection

Identifiers

PMID25575121
PMCPMC4958048
OpenAlexW2335366719

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.