Evidence map›Paper›PMID 16595799›Full record

ArticleNucleic acids research2006

Isolation of human Dna2 endonuclease and characterization of its enzymatic properties.

Jeong-Hoon Kim, Hee-Dai Kim, Gi-Hyuck Ryu, Do-Hyung Kim, Jerard Hurwitz, Yeon-Soo Seo

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

40 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
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  4. Moving Mountains-The BRCA1 Promotion of DNA Resection.Frontiers in molecular biosciences · 2019
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  9. Mitochondrial DNA maintenance: an appraisal.Molecular and cellular biochemistry · 2015
    Review
  10. Review
  11. Borrowing nuclear DNA helicases to protect mitochondrial DNA.International journal of molecular sciences · 2015
    Review
  12. Article
  13. Nuclease activity of Saccharomyces cerevisiae Dna2 inhibits its potent DNA helicase activity.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors at 1 institution in 1 country.

Jeong-Hoon KimNational Creative Research Initiative Center for Cell Cycle Control, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 305-701, Korea.
Hee-Dai Kim
Gi-Hyuck Ryu
Do-Hyung Kim
Jerard Hurwitz
Yeon-Soo Seo
Korea Advanced Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, the creation of ligatable nicks in DNA from flap structures generated by DNA polymerase delta-catalyzed displacement DNA synthesis during Okazaki fragment processing depends on the combined action of Fen1 and Dna2. These two enzymes contain partially overlapping but distinct endonuclease activities. Dna2 is well-suited to process long flaps, which are converted to nicks by the subsequent action of Fen1. In this report, we purified human Dna2 as a recombinant protein from human cells transfected with the cDNA of the human homologue of Saccharomyces cerevisiae Dna2. We demonstrated that the purified human Dna2 enzyme contains intrinsic endonuclease and DNA-dependent ATPase activities, but is devoid of detectable DNA helicase activity. We determined a number of enzymatic properties of human Dna2 including its substrate specificity. When both 5' and 3' tailed ssDNAs were present in a substrate, such as a forked-structured one, both single-stranded regions were cleaved by human Dna2 (hDna2) with equal efficiency. Based on this and other properties of hDna2, it is likely that this enzyme facilitates the removal of 5' and 3' regions in equilibrating flaps that are likely to arise during the processing of Okazaki fragments in human cells.

Indexed as

Adenosine TriphosphatasesCell LineDNADNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesFlap EndonucleasesHumansRecombinant Fusion ProteinsSubstrate SpecificityAdenosine TriphosphatasesDNADNA2 protein, humanDNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesFlap EndonucleasesOkazaki fragmentsRecombinant Fusion Proteins

Identifiers

PMID16595799
PMCPMC1428795
OpenAlexW2171763930

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.