Evidence map›Paper›PMID 32003969›Full record

ArticleACS nano2020

Current Blockades of Proteins inside Nanopores for Real-Time Metabolome Analysis.

Sarah Zernia, Nieck Jordy van der Heide, Nicole Stéphanie Galenkamp, Giorgos Gouridis, Giovanni Maglia

Abstract read
In one paragraph

Article in ACS nano, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Purification and Oligomerization of YaxAB Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
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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.

Sarah ZerniaGroningen Biomolecular Sciences & Biotechnology Institute , University of Groningen , Nijenborgh 7 , 9747 AG Groningen , The Netherlands.ORCID 0000-0002-7513-5765
Nieck Jordy van der HeideGroningen Biomolecular Sciences & Biotechnology Institute , University of Groningen , Nijenborgh 7 , 9747 AG Groningen , The Netherlands.
Nicole Stéphanie GalenkampGroningen Biomolecular Sciences & Biotechnology Institute , University of Groningen , Nijenborgh 7 , 9747 AG Groningen , The Netherlands.
Giorgos GouridisRega Institute for Medical Research, Laboratory of Molecular Bacteriology , KU Leuven , Herestraat 49 , Box 1037, 3000 Leuven , Belgium.
Giovanni MagliaGroningen Biomolecular Sciences & Biotechnology Institute , University of Groningen , Nijenborgh 7 , 9747 AG Groningen , The Netherlands.ORCID 0000-0003-2784-0811

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological nanopores are emerging as powerful and low-cost sensors for real-time analysis of biological samples. Proteins can be incorporated inside the nanopore, and ligand binding to the protein adaptor yields changes in nanopore conductance. In order to understand the origin of these conductance changes and develop sensors for detecting metabolites, we tested the signal originating from 13 different protein adaptors. We found that the quality of the protein signal depended on both the size and charge of the protein. The engineering of a dipole within the surface of the adaptor reduced the current noise by slowing the protein dynamics within the nanopore. Further, the charge of the ligand and the induced conformational changes of the adaptor defined the conductance changes upon metabolite binding, suggesting that the protein resides in an electrokinetic minimum within the nanopore, the position of which is altered by the ligand. These results represent an important step toward understanding the dynamics of the electrophoretic trapping of proteins inside nanopores and will allow developing next-generation sensors for metabolome analysis.

Indexed as

NanoporesEscherichia coli ProteinsHemolysin ProteinsLipid BilayersNanotechnologyTime FactorsEscherichia coli ProteinsHemolysin ProteinshlyE protein, E coliLipid Bilayerscytolysin Aelectrochemistrymetabolite sensornanoporesubstrate-binding protein

Identifiers

PMID32003969
PMCPMC7045694

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.