Evidence map›Paper›PMID 22664237›Full record

ArticleMutation research2012

Human endonuclease V as a repair enzyme for DNA deamination.

Rongjuan Mi, Maria Alford-Zappala, Yoke W Kow, Richard P Cunningham, Weiguo Cao

Open access · greenAbstract read
In one paragraph

Article in Mutation research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

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  7. In vivo measurements of interindividual differences in DNA glycosylases and APE1 activities.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  18. Endonuclease V: an unusual enzyme for repair of DNA deamination.Cellular and molecular life sciences : CMLS · 2013
    Review
  19. Alternative excision repair pathways.Cold Spring Harbor perspectives in biology · 2013
    Review
  20. Article
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 3 institutions in 1 country.

Rongjuan MiDepartment of Genetics and Biochemistry, South Carolina Experiment Station, Clemson University, Room 219 Biosystems Research Complex, 105 Collings Street, Clemson, SC 29634, United States.
Maria Alford-Zappala
Yoke W Kow
Richard P Cunningham
Weiguo Cao
Clemson University · USUniversity at Albany, State University of New York · USEmory University · 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
Repair of Clustered DNA DamagesR01CA090860 · NCI · EMORY UNIVERSITY · PI KOW, YOKE W · 2002 to 2010
$1.3M
Repair of Clustered DNA DamagesR56CA090860 · NCI · EMORY UNIVERSITY · PI KOW, YOKE W · 2008 to 2008
$228k
Xanthine DNA Glycosylase in Mammalian SystemsR15GM090141 · NIGMS · CLEMSON UNIVERSITY · PI CAO, WEIGUO · 2010 to 2010
$223k
NCI NIH HHS CA90860NCI NIH HHS R01 CA090860NCI NIH HHS R56 CA090860NIGMS NIH HHS GM46312NIGMS NIH HHS R01 GM046312NIGMS NIH HHS R15 GM090141PHS HHS CRR1 C06RR0154464
6 · The paper itself

Abstract

The human endonuclease V gene is located in chromosome 17q25.3 and encodes a 282 amino acid protein that shares about 30% sequence identity with bacterial endonuclease V. This study reports biochemical properties of human endonuclease V with respect to repair of deaminated base lesions. Using soluble proteins fused to thioredoxin at the N-terminus, we determined repair activities of human endonuclease V on deoxyinosine (I)-, deoxyxanthosine (X)-, deoxyoxanosine (O)- and deoxyuridine (U)-containing DNA. Human endonuclease V is most active with deoxyinosine-containing DNA but with minor activity on deoxyxanthosine-containing DNA. Endonuclease activities on deoxyuridine and deoxyoxanosine were not detected. The endonuclease activity on deoxyinosine-containing DNA follows the order of single-stranded I>G/I>T/I>A/I>C/I. The preference of the catalytic activity correlates with the binding affinity of these deoxyinosine-containing DNAs. Mg(2+) and to a much less extent, Mn(2+), Ni(2+), Co(2+) can support the endonuclease activity. Introduction of human endonuclease V into Escherichia coli cells deficient in nfi, mug and ung genes caused three-fold reduction in mutation frequency. This is the first report of deaminated base repair activity for human endonuclease V. The relationship between the endonuclease activity and deaminated deoxyadenosine (deoxyinosine) repair is discussed.

Indexed as

DeaminationDNA RepairDeoxyribonuclease (Pyrimidine Dimer)DNADNA Repair EnzymesEscherichia coliGene Transfer TechniquesHumansInosineMutationThioredoxinsdeoxyinosineDeoxyribonuclease (Pyrimidine Dimer)DNADNA Repair EnzymesInosineThioredoxins

Identifiers

PMID22664237
PMCPMC3389188
OpenAlexW2158080837

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.