Evidence map›Paper›PMID 16595800›Full record

ArticleNucleic acids research2006

Biochemical analysis of human Dna2.

Taro Masuda-Sasa, Osamu Imamura, Judith L Campbell

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 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. CtIP promotes the motor activity of DNA2 to accelerate long-range DNA end resection.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Assembling the Human Resectosome on DNA Curtains.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Taro Masuda-SasaBraun Laboratories, 147-75, California Institute of Technology, Pasadena, CA 91125, USA.
Osamu Imamura
Judith L Campbell
California Institute of Technology · US

Funding

ENZYMATIC MECHANISMS OF DNA REPLICATIONR01GM025508 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 1985 to 2006
$2.5M
NIGMS NIH HHS GM25508NIGMS NIH HHS R01 GM025508
6 · The paper itself

Abstract

Yeast Dna2 helicase/nuclease is essential for DNA replication and assists FEN1 nuclease in processing a subset of Okazaki fragments that have long single-stranded 5' flaps. It is also involved in the maintenance of telomeres. DNA2 is a gene conserved in eukaryotes, and a putative human ortholog of yeast DNA2 (ScDNA2) has been identified. Little is known about the role of human DNA2 (hDNA2), although complementation experiments have shown that it can function in yeast to replace ScDNA2. We have now characterized the biochemical properties of hDna2. Recombinant hDna2 has single-stranded DNA-dependent ATPase and DNA helicase activity. It also has 5'-3' nuclease activity with preference for single-stranded 5' flaps adjacent to a duplex DNA region. The nuclease activity is stimulated by RPA and suppressed by steric hindrance at the 5' end. Moreover, hDna2 shows strong 3'-5' nuclease activity. This activity cleaves single-stranded DNA in a fork structure and, like the 5'-3' activity, is suppressed by steric hindrance at the 3'-end, suggesting that the 3'-5' nuclease requires a 3' single-stranded end for activation. These biochemical specificities are very similar to those of the ScDna2 protein, but suggest that the 3'-5' nuclease activity may be more important than previously thought.

Indexed as

Adenosine TriphosphatasesAnimalsBaculoviridaeCell LineDeoxyribonucleasesDNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesExodeoxyribonucleasesHeLa CellsHumansInsectaRecombinant ProteinsSubstrate SpecificityAdenosine TriphosphatasesDeoxyribonucleasesDNA2 protein, humanDNA HelicasesDNA, Single-StrandedEndodeoxyribonucleasesExodeoxyribonucleasesRecombinant Proteins

Identifiers

PMID16595800
PMCPMC1428797
OpenAlexW2165336005

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.