Evidence map›Paper›PMID 21666255›Full record

ArticleNucleic acids research2011

Single Qdot-labeled glycosylase molecules use a wedge amino acid to probe for lesions while scanning along DNA.

Andrew R Dunn, Neil M Kad, Shane R Nelson, David M Warshaw, Susan S Wallace

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

83 citing papers in PubMed, 114 citations in OpenAlex.

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23 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 2 countries.

Andrew R DunnThe Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Neil M Kad
Shane R Nelson
David M Warshaw
Susan S Wallace
University of Vermont · USUniversity of Essex · GB

Funding

Ventricular and Cardiac Fiber Characterization and Integration CoreP01HL059408 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 1999 to 2014
$26.4M
SUBSTRATE SPECIFICITY OF THE BER OXIDATIVE DNA GLYCOSYLASESP01CA098993 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LEE, ANDREA J · 2004 to 2021
$25.9M
NCI NIH HHS CA098993NCI NIH HHS P01 CA098993NHLBI NIH HHS HL059408NIEHS NIH HHS ES007122
6 · The paper itself

Abstract

Within the base excision repair (BER) pathway, the DNA N-glycosylases are responsible for locating and removing the majority of oxidative base damages. Endonuclease III (Nth), formamidopyrimidine DNA glycosylase (Fpg) and endonuclease VIII (Nei) are members of two glycosylase families: the helix-hairpin-helix (HhH) superfamily and the Fpg/Nei family. The search mechanisms employed by these two families of glycosylases were examined using a single molecule assay to image quantum dot (Qdot)-labeled glycosylases interacting with YOYO-1 stained λ-DNA molecules suspended between 5 µm silica beads. The HhH and Fpg/Nei families were found to have a similar diffusive search mechanism described as a continuum of motion, in keeping with rotational diffusion along the DNA molecule ranging from slow, sub-diffusive to faster, unrestricted diffusion. The search mechanism for an Fpg variant, F111A, lacking a phenylalanine wedge residue no longer displayed slow, sub-diffusive motion compared to wild type, suggesting that Fpg base interrogation may be accomplished by Phe(111) insertion.

Indexed as

Deoxyribonuclease (Pyrimidine Dimer)DiffusionDNADNA DamageDNA-Formamidopyrimidine GlycosylaseEscherichia coli ProteinsModels, MolecularOsmolar ConcentrationPhenylalanineQuantum DotsDeoxyribonuclease (Pyrimidine Dimer)DNADNA-Formamidopyrimidine GlycosylaseDNA-formamidopyrimidine glycosylase, E coliEscherichia coli ProteinsNei protein, E coliNTH protein, E coliPhenylalanine

Identifiers

PMID21666255
PMCPMC3177204
OpenAlexW1983898731

What OpenQuestion holds

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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.