Evidence map›Paper›PMID 25493908›Full record

ArticleACS nano2014

Detection of two isomeric binding configurations in a protein-aptamer complex with a biological nanopore.

Veerle Van Meervelt, Misha Soskine, Giovanni Maglia

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Nanopore Technology for the Application of Protein Detection.Nanomaterials (Basel, Switzerland) · 2021
    Review
  7. A Biomimetic DNA-Based Membrane Gate for Protein-Controlled Transport of Cytotoxic Drugs.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  8. Article
  9. Article
  10. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  11. Sensing with Nanopores and Aptamers: A Way Forward.Sensors (Basel, Switzerland) · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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 2 countries.

Veerle Van MeerveltDepartment of Chemistry, KU Leuven , Leuven, B-3001, Belgium.
Misha Soskine
Giovanni Maglia
KU Leuven · BE

Funding

European Research Council 260884
6 · The paper itself

Abstract

Protein-DNA interactions play critical roles in biological systems, and they often involve complex mechanisms and dynamics that are not easily measured by ensemble experiments. Recently, we showed that folded proteins can be internalized inside ClyA nanopores and studied by ionic current recordings at the single-molecule level. Here, we use ClyA nanopores to sample the interaction between the G-quadruplex fold of the thrombin binding aptamer (TBA) and human thrombin (HT). Surprisingly, the internalization of the HT:TBA complex inside the nanopore induced two types of current blockades with distinguished residual current and lifetime. Using single nucleobase substitutions to TBA we showed that these two types of blockades originate from TBA binding to thrombin with two isomeric orientations. Voltage dependencies and the use of ClyA nanopores with two different diameters allowed assessing the effect of the applied potential and confinement and revealed that the two binding configurations of TBA to HT display different lifetimes. These results show that the ClyA nanopores can be used to probe conformational heterogeneity in protein:DNA interactions.

Indexed as

NanoporesAptamers, NucleotideHumansIsomerismKineticsModels, MolecularNanotechnologyProtein BindingProtein ConformationThrombinAptamers, NucleotideThrombinthrombin aptameraptamernanoporeprotein:DNA interactionssingle-moleculethrombin

Identifiers

PMID25493908
PMCPMC4410316
OpenAlexW2322999165

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.