Evidence map›Paper›PMID 27683219›Full record

ArticleNucleic acids research2016

Rev1 is a base excision repair enzyme with 5'-deoxyribose phosphate lyase activity.

Rajendra Prasad, Vladimir Poltoratsky, Esther W Hou, Samuel H Wilson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. The Catalytic Activity of Human REV1 on Undamaged and Damaged DNA.International journal of molecular sciences · 2024
    Article
  6. Article
  7. Article
  8. Involvement of Rev1 in alkylating agent-induced loss of heterozygosity in Oryzias latipes.Genes to cells : devoted to molecular & cellular mechanisms · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. 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

4 authors at 2 institutions in 1 country.

Rajendra PrasadGenome Integrity and Structural Biology Laboratory, National Institutes of Health, NIEHS, 111 T.W. Alexander Drive, PO Box 12233, MD F3-01, Research Triangle Park, NC 27709, USA.
Vladimir PoltoratskyGenome Integrity and Structural Biology Laboratory, National Institutes of Health, NIEHS, 111 T.W. Alexander Drive, PO Box 12233, MD F3-01, Research Triangle Park, NC 27709, USA.
Esther W HouGenome Integrity and Structural Biology Laboratory, National Institutes of Health, NIEHS, 111 T.W. Alexander Drive, PO Box 12233, MD F3-01, Research Triangle Park, NC 27709, USA.
Samuel H WilsonGenome Integrity and Structural Biology Laboratory, National Institutes of Health, NIEHS, 111 T.W. Alexander Drive, PO Box 12233, MD F3-01, Research Triangle Park, NC 27709, USA wilson5@niehs.nih.gov.
National Institute of Environmental Health Sciences · USNational Institutes of Health · US

Funding

BIOLOGY OF MAMMALIAN BASE EXCISION REPAIRZ01ES050159 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$4.5M
Nucleic Acid Enzymes--Pol Beta And Base Repair EnzymesZ01ES050158 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$2.8M
NIEHS NIH HHS Z01 ES050158NIEHS NIH HHS Z01 ES050159
6 · The paper itself

Abstract

Rev1 is a member of the Y-family of DNA polymerases and is known for its deoxycytidyl transferase activity that incorporates dCMP into DNA and its ability to function as a scaffold factor for other Y-family polymerases in translesion bypass events. Rev1 also is involved in mutagenic processes during somatic hypermutation of immunoglobulin genes. In light of the mutation pattern consistent with dCMP insertion observed earlier in mouse fibroblast cells treated with a base excision repair-inducing agent, we questioned whether Rev1 could also be involved in base excision repair (BER). Here, we uncovered a weak 5'-deoxyribose phosphate (5'-dRP) lyase activity in mouse Rev1 and demonstrated the enzyme can mediate BER in vitro The full-length Rev1 protein and its catalytic core domain are similar in their ability to support BER in vitro The dRP lyase activity in both of these proteins was confirmed by NaBH

Indexed as

DNA RepairAmino Acid SequenceAnimalsCatalytic DomainDNA-Directed DNA PolymeraseKineticsMiceNucleotidyltransferasesPeptide MappingPhosphorus-Oxygen LyasesProteolysisY-Family DNA Polymerases5'-deoxyribose phosphate lyaseDNA-Directed DNA PolymeraseNucleotidyltransferasesPhosphorus-Oxygen LyasesRev1 protein, mouseY-Family DNA Polymerases

Identifiers

PMID27683219
PMCPMC5159550
OpenAlexW2524679906

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.