Evidence map›Paper›PMID 14712236›Full record

ArticleOncogene2004

Proteasome-dependent dispersal of PML nuclear bodies in response to alkylating DNA damage.

Lindus A Conlan, Carolyn J McNees, Jörg Heierhorst

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Mitochondrial DNA: cellular genotoxic stress sentinel.Trends in biochemical sciences · 2021
    Review
  3. Article
  4. PML-like subnuclear bodies, containing XRCC1, juxtaposed to DNA replication-based single-strand breaks.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Identification of RING finger protein 4 (RNF4) as a modulator of DNA demethylation through a functional genomics screen.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  11. Review
  12. Telomeric DNA mediates de novo PML body formation.Molecular biology of the cell · 2009
    Article
  13. Review
  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Lindus A ConlanSt Vincent's Institute of Medical Research, 9 Princes Street, Fitzroy, Victoria 3065, Australia.
Carolyn J McNees
Jörg Heierhorst
St Vincents Institute of Medical Research · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Promyelocytic leukemia protein (PML) nuclear bodies (NBs) are present in variable number in most human cell types and have been linked to various cellular functions, including roles as depots for DNA repair proteins. Here, we show that treatment of human cells with DNA methylating agents leads to redistribution of PML from NBs to a diffuse nuclear localization. Biochemically, this correlates with a specific reduction of PML levels in the nuclear matrix fraction without affecting total PML levels. Similar results were obtained for the other major PML NB component, the Sp100 protein, indicating that DNA methylating agents lead to a general disassembly of PML NBs. Similar to the dispersal of PML NBs in response to some viral infections, PML redistribution after DNA damage was inhibited by the proteasome inhibitor MG132. We propose that the regulated dispersal of PML NBs may facilitate the enhanced release of DNA repair proteins from NB depots in order to respond adequately to extensive DNA damage.

Indexed as

DNA DamageDNA MethylationNuclear ProteinsCell NucleusCysteine EndopeptidasesHumansMultienzyme ComplexesNeoplasm ProteinsPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexTranscription FactorsTumor Suppressor ProteinsCysteine EndopeptidasesMultienzyme ComplexesNeoplasm ProteinsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinProteasome Endopeptidase ComplexTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID14712236
OpenAlexW2062379285

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.