Evidence map›Paper›PMID 28668122›Full record

ArticleMethods in enzymology2017

Single-Molecule Methods for Nucleotide Excision Repair: Building a System to Watch Repair in Real Time.

Muwen Kong, Emily C Beckwitt, Luke Springall, Neil M Kad, Bennett Van Houten

Abstract read
In one paragraph

Article in Methods in enzymology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  15. Damage sensor role of UV-DDB during base excision repair.Nature structural & molecular biology · 2019
    Article
  16. Review
  17. Review
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.

Muwen KongUniversity of Pittsburgh School of Medicine, Pittsburgh, PA, United States; University of Pittsburgh Cancer Institute, Pittsburgh, PA, United States.
Emily C BeckwittUniversity of Pittsburgh School of Medicine, Pittsburgh, PA, United States; University of Pittsburgh Cancer Institute, Pittsburgh, PA, United States.
Luke SpringallSchool of Biosciences, University of Kent, Canterbury, United Kingdom.
Neil M KadSchool of Biosciences, University of Kent, Canterbury, United Kingdom.
Bennett Van HoutenUniversity of Pittsburgh School of Medicine, Pittsburgh, PA, United States; University of Pittsburgh Cancer Institute, Pittsburgh, PA, United States. Electronic address: vanhoutenb@upmc.edu.

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JOHN C. BYRD · 1988 to 2026
$158.0M
DNA damage recognition by nucleotide excision repair proteinsR01ES019566 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI VAN HOUTEN, BENNETT · 2011 to 2020
$3.9M
Training in the Molecular Biophysics and Structural BiologyT32GM088119 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HINCK, ANDREW P · 2011 to 2020
$1.6M
NCI NIH HHS P30 CA047904NIEHS NIH HHS R01 ES019566NIGMS NIH HHS T32 GM088119
6 · The paper itself

Abstract

Single-molecule approaches to solving biophysical problems are powerful tools that allow static and dynamic real-time observations of specific molecular interactions of interest in the absence of ensemble-averaging effects. Here, we provide detailed protocols for building an experimental system that employs atomic force microscopy and a single-molecule DNA tightrope assay based on oblique angle illumination fluorescence microscopy. Together with approaches for engineering site-specific lesions into DNA substrates, these complementary biophysical techniques are well suited for investigating protein-DNA interactions that involve target-specific DNA-binding proteins, such as those engaged in a variety of DNA repair pathways. In this chapter, we demonstrate the utility of the platform by applying these techniques in the studies of proteins participating in nucleotide excision repair.

Indexed as

DNA RepairAnimalsBase SequenceDNADNA-Binding ProteinsEquipment DesignHumansMicroscopy, Atomic ForceMicroscopy, FluorescenceProtein BindingDNADNA-Binding ProteinsAnomalous diffusion exponentAtomic force microscopyDiffusion coefficientDNA bend angleDNA damage arraysDNA tightrope assayFluorescence microscopyNucleotide excision repairOne-dimensional diffusionProtein–DNA interactionsProtein specificityProtein volumeQuantum dotSingle molecule

Identifiers

PMID28668122
PMCPMC5656006

What OpenQuestion holds

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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.