Evidence map›Paper›PMID 22334079›Full record

ArticleNature communications2012

Regulation of histone modification and chromatin structure by the p53-PADI4 pathway.

Chizu Tanikawa, Martha Espinosa, Akari Suzuki, Ken Masuda, Kazuhiko Yamamoto, Eiju Tsuchiya, Koji Ueda, Yataro Daigo, Yusuke Nakamura, Koichi Matsuda

Erratum issuedOpen access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 151 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Citrullination negatively regulates the functions of the p53 protein and opposes its ubiquitination and degradation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Citrullination in tumor immunity and therapy.The Journal of clinical investigation · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. The significant role of amino acid metabolic reprogramming in cancer.Cell communication and signaling : CCS · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Citrullination and the protein code: crosstalk between post-translational modifications in cancer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review

34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Chizu TanikawaLaboratory of Molecular Medicine, Human Genome Center, Institute of Medical Science, The University of Tokyo, Tokyo 1088639, Japan.
Martha Espinosa
Akari Suzuki
Ken Masuda
Kazuhiko Yamamoto
Eiju Tsuchiya
Koji Ueda
Yataro Daigo
Yusuke Nakamura
Koichi Matsuda
The University of Tokyo · JPRIKEN Center for Integrative Medical Sciences · JPSaitama Cancer Center · JPShiga University of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone proteins are modified in response to various external signals; however, their mechanisms are still not fully understood. Citrullination is a post-transcriptional modification that converts arginine in proteins into citrulline. Here we show in vivo and in vitro citrullination of the arginine 3 residue of histone H4 (cit-H4R3) in response to DNA damage through the p53-PADI4 pathway. We also show DNA damage-induced citrullination of Lamin C. Cit-H4R3 and citrullinated Lamin C localize around fragmented nuclei in apoptotic cells. Ectopic expression of PADI4 leads to chromatin decondensation and promotes DNA cleavage, whereas Padi4(-/-) mice exhibit resistance to radiation-induced apoptosis in the thymus. Furthermore, the level of cit-H4R3 is negatively correlated with p53 protein expression and with tumour size in non-small cell lung cancer tissues. Our findings reveal that cit-H4R3 may be an 'apoptotic histone code' to detect damaged cells and induce nuclear fragmentation, which has a crucial role in carcinogenesis.

Indexed as

Gene Expression RegulationAnimalsApoptosisArginineCell NucleusChromatinCitrullineDNADNA DamageHistonesHumansHydrolasesLamin Type AMiceMice, TransgenicModels, BiologicalArginineChromatinCitrullineDNAHistonesHydrolaseslamin CLamin Type APADI4 protein, humanpeptidylarginine deiminase 4, mouseProtein-Arginine DeiminasesProtein-Arginine Deiminase Type 4Tumor Suppressor Protein p53

Identifiers

PMID22334079
OpenAlexW2058443096

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.