Evidence map›Paper›PMID 17563742›Full record

ArticleOncogene2007

The proteasome is involved in determining differential utilization of double-strand break repair pathways.

K Gudmundsdottir, C J Lord, A Ashworth

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Regulatory elements inGenetics in medicine open · 2024
    Article
  4. Article
  5. Review
  6. Increased chemosensitivity via BRCA2-independent DNA damage in DSS1- and PCID2-depleted breast carcinomas.Laboratory investigation; a journal of technical methods and pathology · 2021
    Article
  7. Article
  8. Article
  9. Proteasome Structure and Assembly.Journal of molecular biology · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. BRCA2: one small step for DNA repair, one giant protein purified.The Yale journal of biology and medicine · 2013
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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 2 institutions in 1 country.

K GudmundsdottirGene Function Laboratory, The Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, UK.
C J Lord
A Ashworth
Institute of Cancer Research · GBBreast Cancer Now · GB

Funding

Breast Cancer Now BREAST CANCER NOW RESEARCH CENTRECancer Research UK A8363
6 · The paper itself

Abstract

The DSS1 protein interacts with the breast cancer susceptibility protein BRCA2 that plays an integral role in the repair of DNA double-strand breaks (DSBs). DSS1 has also been shown to interact with components of the 26S proteasome in Saccharomyces cerevisiae and in human tumour cells. This raises the possibility of functional interplay between the DNA repair machinery and the proteasome. We show here that human DSS1 interacts with the RPN3 and RPN7 proteasome subunits and define regions of DSS1 important for the interactions with RPN3, RPN7 and BRCA2. We also show that BRCA2 interacts with RPN3 and RPN7 and that the BRCA2/RPN7 interaction is independent of DSS1. Finally, and most significantly, we demonstrate that the proteolytic activity of the proteasome is a determinant of the choice of DSB repair pathway; inhibition of proteasome proteolytic activity results in an increase in the utilization of potentially mutagenic single-strand annealing at the expense of a reduction in the level of error-free gene conversion. This confirms a functional link between DSB repair and proteasomal activity.

Indexed as

DNA DamageDNA RepairApoptosis Regulatory ProteinsBRCA2 ProteinBreast NeoplasmsExoribonucleasesFemaleGenetic Predisposition to DiseaseHexosyltransferasesHumansKineticsProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsApoptosis Regulatory ProteinsBLID protein, humanBRCA2 ProteinBRCA2 protein, humanDSS1 protein, S cerevisiaeExoribonucleasesHexosyltransferasesProteasome Endopeptidase ComplexRPN2 protein, humanSaccharomyces cerevisiae ProteinsSEM1 protein, human

Identifiers

PMID17563742
OpenAlexW2086039159

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.