Evidence map›Paper›PMID 17389648›Full record

ArticleNucleic acids research2007

Conserved interactions of the splicing factor Ntr1/Spp382 with proteins involved in DNA double-strand break repair and telomere metabolism.

Gernot Herrmann, Sanja Kais, Jan Hoffbauer, Kijwasch Shah-Hosseini, Nicole Brüggenolte, Heiko Schober, Margaret Fäsi, Primo Schär

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Dysfunction of Gpl1-Gih35-Wdr83 Complex inInternational journal of molecular sciences · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Regulation of DEAH/RHA helicases by G-patch proteins.BioMed research international · 2015
    Review
  9. Article
  10. RNA helicases in splicing.RNA biology · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. 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

8 authors at 4 institutions in 2 countries.

Gernot HerrmannDepartment of Dermatology, University of Cologne, Cologne, Germany. gernot.herrmann@uni-koeln.de
Sanja Kais
Jan Hoffbauer
Kijwasch Shah-Hosseini
Nicole Brüggenolte
Heiko Schober
Margaret Fäsi
Primo Schär
University of Basel · CHFriedrich Miescher Institute · CHUniversity of Cologne · DEUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ligation of DNA double-strand breaks in the process of non-homologous end-joining (NHEJ) is accomplished by a heterodimeric enzyme complex consisting of DNA ligase IV and an associated non-catalytic factor. This DNA ligase also accounts for the fatal joining of unprotected telomere ends. Hence, its activity must be tightly controlled. Here, we describe interactions of the DNA ligase IV-associated proteins Lif1p and XRCC4 of yeast and human with the putatively orthologous G-patch proteins Ntr1p/Spp382p and NTR1/TFIP11 that have recently been implicated in mRNA splicing. These conserved interactions occupy the DNA ligase IV-binding sites of Lif1p and XRCC4, thus preventing the formation of an active enzyme complex. Consistently, an excess of Ntr1p in yeast reduces NHEJ efficiency in a plasmid ligation assay as well as in a chromosomal double-strand break repair (DSBR) assay. Both yeast and human NTR1 also interact with PinX1, another G-patch protein that has dual functions in the regulation of telomerase activity and telomere stability, and in RNA processing. Like PinX1, NTR1 localizes to telomeres and associates with nucleoli in yeast and human cells, suggesting a function in localized control of DSBR.

Indexed as

DNA Breaks, Double-StrandedDNA RepairCell Cycle ProteinsDNA-Binding ProteinsHeLa CellsHumansNuclear ProteinsRNA Splicing FactorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTelomereTelomere-Binding ProteinsTumor Suppressor ProteinsTwo-Hybrid System TechniquesCell Cycle ProteinsDNA-Binding ProteinsLIF1 protein, S cerevisiaeNEJ1 protein, S cerevisiaeNuclear ProteinsPINX1 protein, humanRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSpp382 protein, S cerevisiaeTelomere-Binding ProteinsTFIP11 protein, humanTumor Suppressor Proteins

Identifiers

PMID17389648
PMCPMC1874655
OpenAlexW1994704295

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.