Evidence map›Paper›PMID 26007651›Full record

ArticleNucleic acids research2015

Disturbance-free rapid solution exchange for magnetic tweezers single-molecule studies.

Shimin Le, Mingxi Yao, Jin Chen, Artem K Efremov, Sara Azimi, Jie Yan

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Single-molecule force spectroscopy reveals intra- and intermolecular interactions ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
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  7. APL bioengineering · 2024
    Article
  8. Review
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  19. Article
  20. Single-molecule Manipulation of G-quadruplexes by Magnetic Tweezers.Journal of visualized experiments : JoVE · 2017
    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.

Shimin LeMechanobiology Institute, National University of Singapore, 117411, Singapore.
Mingxi YaoMechanobiology Institute, National University of Singapore, 117411, Singapore.
Jin ChenMechanobiology Institute, National University of Singapore, 117411, Singapore.
Artem K EfremovMechanobiology Institute, National University of Singapore, 117411, Singapore.
Sara AzimiDepartment of Physics, National University of Singapore, 117542, Singapore.
Jie YanMechanobiology Institute, National University of Singapore, 117411, Singapore Department of Physics, National University of Singapore, 117542, Singapore Centre for Bioimaging Sciences, National University of Singapore, 117557, Singapore phyyj@nus.edu.sg.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule manipulation technologies have been extensively applied to studies of the structures and interactions of DNA and proteins. An important aspect of such studies is to obtain the dynamics of interactions; however the initial binding is often difficult to obtain due to large mechanical perturbation during solution introduction. Here, we report a simple disturbance-free rapid solution exchange method for magnetic tweezers single-molecule manipulation experiments, which is achieved by tethering the molecules inside microwells (typical dimensions-diameter (D): 40-50 μm, height (H): 100 μm; H:D∼2:1). Our simulations and experiments show that the flow speed can be reduced by several orders of magnitude near the bottom of the microwells from that in the flow chamber, effectively eliminating the flow disturbance to molecules tethered in the microwells. We demonstrate a wide scope of applications of this method by measuring the force dependent DNA structural transitions in response to solution condition change, and polymerization dynamics of RecA on ssDNA/SSB-coated ssDNA/dsDNA of various tether lengths under constant forces, as well as the dynamics of vinculin binding to α-catenin at a constant force (< 5 pN) applied to the α-catenin protein.

Indexed as

Microfluidic Analytical Techniquesalpha CateninDNADNA-Binding ProteinsDNA, Single-StrandedRec A RecombinasesSodium ChlorideVinculinalpha CateninDNADNA-Binding ProteinsDNA, Single-StrandedRec A RecombinasesSodium ChlorideVinculin

Identifiers

PMID26007651
PMCPMC4787821

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Registered trials

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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.