Evidence map›Paper›PMID 24799677›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Two glycosylase families diffusively scan DNA using a wedge residue to probe for and identify oxidatively damaged bases.

Shane R Nelson, Andrew R Dunn, Scott D Kathe, David M Warshaw, Susan S Wallace

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
9.8field-weighted citation impact, top 2% 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

63 citing papers in PubMed, 104 citations in OpenAlex.

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3 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 1 institution in 1 country.

Shane R NelsonDepartment of Molecular Physiology and Biophysics, The University of Vermont, Burlington, VT 05405-0075; and.
Andrew R DunnDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, The University of Vermont, Burlington, VT 05405-0084.
Scott D KatheDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, The University of Vermont, Burlington, VT 05405-0084.
David M WarshawDepartment of Molecular Physiology and Biophysics, The University of Vermont, Burlington, VT 05405-0075; and susan.wallace@uvm.edu david.warshaw@uvm.edu.
Susan S WallaceDepartment of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, The University of Vermont, Burlington, VT 05405-0084 susan.wallace@uvm.edu david.warshaw@uvm.edu.
University of Vermont · US

Funding

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 CA P01098993NCI NIH HHS P01 CA098993
6 · The paper itself

Abstract

DNA glycosylases are enzymes that perform the initial steps of base excision repair, the principal repair mechanism that identifies and removes endogenous damages that occur in an organism's DNA. We characterized the motion of single molecules of three bacterial glycosylases that recognize oxidized bases, Fpg, Nei, and Nth, as they scan for damages on tightropes of λ DNA. We find that all three enzymes use a key "wedge residue" to scan for damage because mutation of this residue to an alanine results in faster diffusion. Moreover, all three enzymes bind longer and diffuse more slowly on DNA that contains the damages they recognize and remove. Using a sliding window approach to measure diffusion constants and a simple chemomechanical simulation, we demonstrate that these enzymes diffuse along DNA, pausing momentarily to interrogate random bases, and when a damaged base is recognized, they stop to evert and excise it.

Indexed as

DNA DamageAlanineCatalytic DomainDeoxyribonuclease (Pyrimidine Dimer)DiffusionDNA, BacterialDNA-Formamidopyrimidine GlycosylaseDNA Mutational AnalysisDNA RepairEscherichia coliEscherichia coli ProteinsMolecular ConformationMutationOxygenProtein BindingStress, MechanicalAlanineDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialDNA-Formamidopyrimidine GlycosylaseDNA-formamidopyrimidine glycosylase, E coliEscherichia coli ProteinsNei protein, E coliNTH protein, E coliOxygenDNA repairsearch mechanisms

Identifiers

PMID24799677
PMCPMC4034194
OpenAlexW2003447156

What OpenQuestion holds

Textmetadata
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.