Evidence map›Paper›PMID 23263163›Full record

ReviewCellular and molecular life sciences : CMLS2013

Endonuclease V: an unusual enzyme for repair of DNA deamination.

Weiguo Cao

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  7. Open biology · 2020
    Review
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  18. Determinants of spontaneous mutation in the bacterium Escherichia coli as revealed by whole-genome sequencing.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. 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

1 author at 1 institution in 1 country.

Weiguo CaoDepartment of Genetics and Biochemistry, South Carolina Experiment Station, Clemson University, Room 049 Life Science Building, 190 Collings Street, Clemson, SC, 29634, USA. wgc@clemson.edu
Clemson University · US

Funding

Xanthine DNA Glycosylase in Mammalian SystemsR15GM090141 · NIGMS · CLEMSON UNIVERSITY · PI CAO, WEIGUO · 2010 to 2010
$223k
NIGMS NIH HHS GM090141NIGMS NIH HHS R15 GM090141
6 · The paper itself

Abstract

Endonuclease V (endo V) was first discovered as the fifth endonuclease in Escherichia coli in 1977 and later rediscovered as a deoxyinosine 3' endonuclease. Decades of biochemical and genetic investigations have accumulated rich information on its role as a DNA repair enzyme for the removal of deaminated bases. Structural and biochemical analyses have offered invaluable insights on its recognition capacity, catalytic mechanism, and multitude of enzymatic activities. The roles of endo V in genome maintenance have been validated in both prokaryotic and eukaryotic organisms. The ubiquitous nature of endo V in the three domains of life: Bacteria, Archaea, and Eukaryotes, indicates its existence in the early evolutionary stage of cellular life. The application of endo V in mutation detection and DNA manipulation underscores its value beyond cellular DNA repair. This review is intended to provide a comprehensive account of the historic aspects, biochemical, structural biological, genetic and biotechnological studies of this unusual DNA repair enzyme.

Indexed as

DNA RepairAnimalsDeaminationDeoxyribonuclease (Pyrimidine Dimer)HumansDeoxyribonuclease (Pyrimidine Dimer)

Identifiers

PMID23263163
PMCPMC11114013
OpenAlexW1970811959

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.