Evidence map›Paper›PMID 22160858›Full record

ArticleMolecular and cellular biochemistry2012

Endonuclease G interacts with histone H2B and DNA topoisomerase II alpha during apoptosis.

Miroslav Vařecha, Michaela Potěšilová, Pavel Matula, Michal Kozubek

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Apoptosis: Activation and Inhibition in Health and Disease.Medical sciences (Basel, Switzerland) · 2018
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Killing of cancer cells through the use of eukaryotic expression vectors harbouring genes encoding nucleases and ribonuclease inhibitor.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Review
  12. Article
  13. Review
  14. Therapeutic advances in infectious disease
    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

4 authors at 1 institution in 1 country.

Miroslav VařechaCentre for Biomedical Image Analysis, Faculty of Informatics, Masaryk University, Botanická 68a, 602 00 Brno, Czech Republic. mvara@fi.muni.cz
Michaela Potěšilová
Pavel Matula
Michal Kozubek
Masaryk University · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apoptosis is a natural form of cell death involved in many physiological changes in the cell. Defects in the process of apoptosis can lead to serious diseases. During some apoptotic pathways, proteins apoptosis-inducing factor (AIF) and endonuclease G (EndoG) are released from the mitochondria and they translocate into the cell nuclei, where they probably participate in chromatin degradation together with other nuclear proteins. Exact mechanism of EndoG activity in cell nucleus is still unknown. Some interacting partners like flap endonuclease 1, DNase I, and exonuclease III were already suggested, but also other interacting partners were proposed. We conducted a living-cell confocal fluorescence microscopy followed by an image analysis of fluorescence resonance energy transfer to analyze the possibility of protein interactions of EndoG with histone H2B and human DNA topoisomerase II alpha (TOPO2a). Our results show that EndoG interacts with both these proteins during apoptotic cell death. Therefore, we can conclude that EndoG and TOPO2a may actively participate in apoptotic chromatin degradation. The possible existence of a degradation complex consisting of EndoG and TOPO2a and possibly other proteins like AIF and cyclophilin A have yet to be investigated.

Indexed as

ApoptosisChromatin Assembly and DisassemblyAntigens, NeoplasmCell NucleusDNA-Binding ProteinsDNA Topoisomerases, Type IIEndodeoxyribonucleasesFluorescence Resonance Energy TransferHeLa CellsHistonesHumansMicroscopy, ConfocalModels, MolecularProtein ConformationProtein Interaction Domains and MotifsProtein Interaction MappingAntigens, NeoplasmDNA-Binding ProteinsDNA Topoisomerases, Type IIEndodeoxyribonucleasesendonuclease GHistonesRecombinant Fusion Proteins

Identifiers

PMID22160858
OpenAlexW2006199380

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.