Evidence map›Paper›PMID 23394999›Full record

ArticleMolecular cell2013

RNF111-dependent neddylation activates DNA damage-induced ubiquitination.

Teng Ma, Yibin Chen, Feng Zhang, Chao-Yie Yang, Shaomeng Wang, Xiaochun Yu

Abstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
–field-weighted citation impact
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

80 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  13. Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

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

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

6 authors.

Teng MaDivision of Molecular Medicine and Genetics, Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Yibin Chen
Feng Zhang
Chao-Yie Yang
Shaomeng Wang
Xiaochun Yu

Funding

Regulation of Ionizing Radiation-Induced DNA Damage ResponseR01CA130899 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LIU, YILUN · 2009 to 2023
$5.5M
Molecular Mechanisms of BRCA1-Dependent DNA Damage Response and TumorogenesisR01CA132755 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHEN, BINGHUI · 2008 to 2019
$3.5M
NCI NIH HHS CA130899NCI NIH HHS CA132755NCI NIH HHS R01 CA130899NCI NIH HHS R01 CA132755
6 · The paper itself

Abstract

Ubiquitin-like proteins have been shown to be covalently conjugated to targets. However, the functions of these ubiquitin-like proteins are largely unknown. Here, we have screened most known ubiquitin-like proteins after DNA damage and found that NEDD8 is involved in the DNA damage response. Following various DNA damage stimuli, NEDD8 accumulated at DNA damage sites; this accumulation was dependent on an E2 enzyme (UBE2M) and an E3 ubiquitin ligase (RNF111). We further found that histone H4 was polyneddylated in response to DNA damage, and NEDD8 was conjugated to the N-terminal lysine residues of H4. Interestingly, the DNA damage-induced polyneddylation chain could be recognized by the MIU (motif interacting with ubiquitin) domain of RNF168. Loss of DNA damage-induced neddylation negatively regulated DNA damage-induced foci formation of RNF168 and its downstream functional partners, such as 53BP1 and BRCA1, thus affecting the normal DNA damage repair process.

Indexed as

DNA DamageBRCA1 ProteinCell LineCells, CulturedDNADNA RepairHistonesHumansIntracellular Signaling Peptides and ProteinsNEDD8 ProteinNuclear ProteinsPolyadenylationTumor Suppressor p53-Binding Protein 1UbiquitinationUbiquitin-Protein LigasesUbiquitinsBRCA1 ProteinBRCA1 protein, humanDNAHistonesIntracellular Signaling Peptides and ProteinsNEDD8 ProteinNEDD8 protein, humanNuclear ProteinsRNF111 protein, humanTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1Ubiquitin-Protein LigasesUbiquitins

Identifiers

PMID23394999
PMCPMC3595365

What OpenQuestion holds

Textmetadata
LicenceTDM
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.