Evidence map›Paper›PMID 20350930›Full record

ArticleNucleic acids research2010

Visualizing helicases unwinding DNA at the single molecule level.

Natali Fili, Gregory I Mashanov, Christopher P Toseland, Christopher Batters, Mark I Wallace, Joseph T P Yeeles, Mark S Dillingham, Martin R Webb, Justin E Molloy

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. 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
2.3field-weighted citation impact, top 12% 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, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
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  5. Article
  6. Article
  7. Article
  8. Review
  9. Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Article
  12. Article
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  14. Review
  15. Article
  16. Article
  17. Application of the SSB biosensor to study in vitro transcription.Biochemical and biophysical research communications · 2018
    Article
  18. Article
  19. Article
  20. Probing DNA helicase kinetics with temperature-controlled magnetic tweezers.Small (Weinheim an der Bergstrasse, Germany) · 2015
    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

9 authors at 1 institution in 2 countries.

Natali FiliMRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.
Gregory I Mashanov
Christopher P Toseland
Christopher Batters
Mark I Wallace
Joseph T P Yeeles
Mark S Dillingham
Martin R Webb
Justin E Molloy
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_U117512742Medical Research Council MC_U117570592Wellcome Trust 061523Wellcome Trust 082960
6 · The paper itself

Abstract

DNA helicases are motor proteins that catalyze the unwinding of double-stranded DNA into single-stranded DNA using the free energy from ATP hydrolysis. Single molecule approaches enable us to address detailed mechanistic questions about how such enzymes move processively along DNA. Here, an optical method has been developed to follow the unwinding of multiple DNA molecules simultaneously in real time. This was achieved by measuring the accumulation of fluorescent single-stranded DNA-binding protein on the single-stranded DNA product of the helicase, using total internal reflection fluorescence microscopy. By immobilizing either the DNA or helicase, localized increase in fluorescence provides information about the rate of unwinding and the processivity of individual enzymes. In addition, it reveals details of the unwinding process, such as pauses and bursts of activity. The generic and versatile nature of the assay makes it applicable to a variety of DNA helicases and DNA templates. The method is an important addition to the single-molecule toolbox available for studying DNA processing enzymes.

Indexed as

Adenosine TriphosphateDNADNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedExodeoxyribonucleasesImmobilized ProteinsMicroscopy, FluorescenceAddAB enzymeAdenosine TriphosphateDNADNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedExodeoxyribonucleasesImmobilized Proteins

Identifiers

PMID20350930
PMCPMC2910053
OpenAlexW2113642908

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.