Evidence map›Paper›PMID 18263876›Full record

ArticleThe Journal of biological chemistry2008

Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair.

Brian D Beck, Su-Jung Park, Young-Ju Lee, Yaritzabel Roman, Robert A Hromas, Suk-Hee Lee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Biomedicines · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Crystallization of and selenomethionine phasing strategy for a SETMAR-DNA complex.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  17. Review
  18. 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

6 authors at 3 institutions in 1 country.

Brian D BeckDepartment of Biochemistry & Molecular Biology and the Walther Cancer Institute, Indiana University School of Medicine, 1044 W. Walnut Street, Indianapolis, IN 46202, USA.
Su-Jung Park
Young-Ju Lee
Yaritzabel Roman
Robert A Hromas
Suk-Hee Lee
Indiana University School of MedicineUniversity of New Mexico · USWalther Cancer Foundation · US

Funding

Cancer Biology Training ProgramT32CA111198 · NCI · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI NAKSHATRI, HARIKRISHNA · 2005 to 2009
$1.8M
NCI NIH HHS CA 92111NCI NIH HHS T32 CA 111198-01NIDDK NIH HHS T32 DK 0075-20
6 · The paper itself

Abstract

Metnase, also known as SETMAR, is a SET and transposase fusion protein with an undefined role in mammalian DNA repair. The SET domain is responsible for histone lysine methyltransferase activity at histone 3 K4 and K36, whereas the transposase domain possesses 5'-terminal inverted repeat (TIR)-specific DNA binding, DNA looping, and DNA cleavage activities. Although the transposase domain is essential for Metnase function in DNA repair, it is not clear how a protein with sequence-specific DNA binding activity plays a role in DNA repair. Here, we show that human homolog of the ScPSO4/PRP19 (hPso4) forms a stable complex with Metnase on both TIR and non-TIR DNA. The transposase domain essential for Metnase-TIR interaction is not sufficient for its interaction with non-TIR DNA in the presence of hPso4. In vivo, hPso4 is induced and co-localized with Metnase following ionizing radiation treatment. Cells treated with hPso4-siRNA failed to show Metnase localization at DSB sites and Metnase-mediated stimulation of DNA end joining coupled to genomic integration, suggesting that hPso4 is necessary to bring Metnase to the DSB sites for its function(s) in DNA repair.

Indexed as

DNA Breaks, Double-StrandedCell LineDNA-Binding ProteinsDNA RepairDNA Repair EnzymesHistone-Lysine N-MethyltransferaseHistonesHumansNuclear ProteinsProtein Structure, TertiaryRNA, Small InterferingRNA Splicing FactorsTerminal Repeat SequencesDNA-Binding ProteinsDNA Repair EnzymesHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsPRPF19 protein, humanRNA, Small InterferingRNA Splicing FactorsSETMAR protein, human

Identifiers

PMID18263876
PMCPMC2431028
OpenAlexW2092718815

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.