Evidence map›Paper›PMID 26691010›Full record

ArticleScientific reports2015

Directly interrogating single quantum dot labelled UvrA2 molecules on DNA tightropes using an optically trapped nanoprobe.

Michelle Simons, Mark R Pollard, Craig D Hughes, Andrew D Ward, Bennett Van Houten, Mike Towrie, Stan W Botchway, Anthony W Parker, Neil M Kad

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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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

9 authors.

Michelle SimonsSchool of Biological Sciences, University of Essex, Essex, CO4 3SQ, UK.
Mark R PollardCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, OX11 0FA, UK.
Craig D HughesSchool of Biological Sciences, University of Essex, Essex, CO4 3SQ, UK.
Andrew D WardCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, OX11 0FA, UK.
Bennett Van HoutenDepartment of Pharmacology and Chemical Biology, University of Pittsburgh Cancer Institute, Hillman Cancer Research Pavilion, 5117 Centre Ave, Pittsburgh, PA, USA 15213.
Mike TowrieCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, OX11 0FA, UK.
Stan W BotchwayCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, OX11 0FA, UK.
Anthony W ParkerCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, OX11 0FA, UK.
Neil M KadSchool of Biosciences, University of Kent, Canterbury, Kent, CT2 7NH, UK.

Funding

DNA damage recognition by nucleotide excision repair proteinsR01ES019566 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VAN HOUTEN, BENNETT · 2011 to 2020
$3.9M
Biotechnology and Biological Sciences Research Council BB/I003460/1NIEHS NIH HHS 1R01ES019566NIEHS NIH HHS R01 ES019566
6 · The paper itself

Abstract

In this study we describe a new methodology to physically probe individual complexes formed between proteins and DNA. By combining nanoscale, high speed physical force measurement with sensitive fluorescence imaging we investigate the complex formed between the prokaryotic DNA repair protein UvrA2 and DNA. This approach uses a triangular, optically-trapped "nanoprobe" with a nanometer scale tip protruding from one vertex. By scanning this tip along a single DNA strand suspended between surface-bound micron-scale beads, quantum-dot tagged UvrA2 molecules bound to these '"DNA tightropes" can be mechanically interrogated. Encounters with UvrA2 led to deflections of the whole nanoprobe structure, which were converted to resistive force. A force histogram from all 144 detected interactions generated a bimodal distribution centered on 2.6 and 8.1 pN, possibly reflecting the asymmetry of UvrA2's binding to DNA. These observations successfully demonstrate the use of a highly controllable purpose-designed and built synthetic nanoprobe combined with fluorescence imaging to study protein-DNA interactions at the single molecule level.

Indexed as

Optical TweezersStaining and LabelingDNADNA Repair EnzymesNanoparticlesQuantum DotsSolutionsDNADNA Repair EnzymesSolutions

Identifiers

PMID26691010
PMCPMC4686980

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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.