Evidence map›Paper›PMID 30590231›Full record

ArticleMutation research2019

Role of endonuclease III enzymes in uracil repair.

Ye Yang, Sung-Hyun Park, Maria Alford-Zappala, Hyun-Wook Lee, Jing Li, Richard P Cunningham, Weiguo Cao

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Mutation research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Ye YangDepartment of Genetics and Biochemistry, Clemson University, Room 049 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Sung-Hyun ParkDepartment of Genetics and Biochemistry, Clemson University, Room 049 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Maria Alford-ZappalaDepartment of Biological Sciences, The University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, USA.
Hyun-Wook LeeDepartment of Genetics and Biochemistry, Clemson University, Room 049 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Jing LiDepartment of Genetics and Biochemistry, Clemson University, Room 049 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA.
Richard P CunninghamDepartment of Biological Sciences, The University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, USA.
Weiguo CaoDepartment of Genetics and Biochemistry, Clemson University, Room 049 Life Sciences Facility, 190 Collings Street, Clemson, SC 29634, USA. Electronic address: wgc@clemson.edu.
Clemson University · USUniversity at Albany, State University of New York · US

Funding

STRUCTURE AND FUNCTION OF METALLOENZYMES FOR DNA REPAIRR01GM046312 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1991 to 2012
$5.9M
New Enzymes for DNA DemethylationR15GM121997 · NIGMS · CLEMSON UNIVERSITY · PI CAO, WEIGUO · 2017 to 2017
$457k
Xanthine DNA Glycosylase in Mammalian SystemsR15GM090141 · NIGMS · CLEMSON UNIVERSITY · PI CAO, WEIGUO · 2010 to 2010
$223k
NIGMS NIH HHS R01 GM046312NIGMS NIH HHS R15 GM090141NIGMS NIH HHS R15 GM121997
6 · The paper itself

Abstract

Endonuclease III is a DNA glycosylase previously known for its repair activity on oxidative pyrimidine damage. Uracil is a deamination product derived from cytosine. Uracil DNA N-glycosylase (UNG) and mismatch-specific uracil DNA glycosylase (MUG) are two known repair enzymes with enzymatic activity on uracil in E. coli. Here we report a G/U specific uracil DNA glycosylase activity in E. coli endonuclease III (endo III, Nth), which is comparable to MUG but significantly lower than its thymine glycol DNA glycosylase activity. The possibility that the novel activity is due to contamination is ruled out by expressing the wild type nth gene and an active site mutant in a uracil-repair-deficient genetic background. Consistent with the biochemical analysis, analyses of lac

Indexed as

DeaminationDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialDNA RepairEscherichia coli ProteinsHumansUracilUracil-DNA GlycosidaseDeoxyribonuclease (Pyrimidine Dimer)DNA, BacterialEscherichia coli ProteinsNTH protein, E coliUracilUracil-DNA GlycosidaseDeaminationEndonuclease IIINucleoside diphosphate kinaseUracilUracil DNA glycosylase

Identifiers

PMID30590231
PMCPMC6378108
OpenAlexW2905580319

What OpenQuestion holds

Textmetadata
LicenceTDM
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.