Evidence map›Paper›PMID 28525740›Full record

ArticleMolecular cell2017

RNF8- and Ube2S-Dependent Ubiquitin Lysine 11-Linkage Modification in Response to DNA Damage.

Atanu Paul, Bin Wang

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Ubiquitin-conjugating Enzymes in Cancer.International journal of biological sciences · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. DNA damage-induced proteasome phosphorylation controls substrate recognition and facilitates DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. The regulation of necroptosis by ubiquitylation.Apoptosis : an international journal on programmed cell death · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis.Frontiers in cell and developmental biology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Atanu PaulDepartment of Genetics, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA; Genes and Development Program, The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences, Houston, TX 77030, USA.
Bin WangDepartment of Genetics, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA; Genes and Development Program, The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences, Houston, TX 77030, USA. Electronic address: bwang3@mdanderson.org.
The University of Texas MD Anderson Cancer Center · US

Funding

The role of a novel BRCA1 associated complex in DNA damage response and tumor supR01CA155025 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI WANG, BIN · 2011 to 2020
$3.4M
NCI NIH HHS R01 CA155025
6 · The paper itself

Abstract

Ubiquitin modification of proteins plays pivotal roles in the cellular response to DNA damage. Given the complexity of ubiquitin conjugation due to the formation of poly-conjugates of different linkages, functional roles of linkage-specific ubiquitin modification at DNA damage sites are largely unclear. We identify that Lys11-linkage ubiquitin modification occurs at DNA damage sites in an ATM-dependent manner, and ubiquitin-modifying enzymes, including Ube2S E2-conjugating enzyme and RNF8 E3 ligase, are responsible for the assembly of Lys11-linkage conjugates on damaged chromatin, including histone H2A/H2AX. We show that RNF8- and Ube2S-dependent Lys11-linkage ubiquitin conjugation plays an important role in regulating DNA damage-induced transcriptional silencing, distinct from the role of Lys63-linkage ubiquitin in the recruitment of DNA damage repair proteins 53BP1 and BRCA1. Thus, our study highlights the importance of linkage-specific ubiquitination at DNA damage sites, and it reveals that Lys11-linkage ubiquitin modification plays a crucial role in the DNA damage response.

Indexed as

DNA DamageDNA RepairUbiquitinationAtaxia Telangiectasia Mutated ProteinsBinding SitesBRCA1 ProteinCell Line, TumorChromatinDNA-Binding ProteinsDown-RegulationHEK293 CellsHistonesHumansLysineMutationProtein BindingAtaxia Telangiectasia Mutated ProteinsATM protein, humanBRCA1 ProteinBRCA1 protein, humanChromatinDNA-Binding ProteinsH2AX protein, humanHistonesLysineRNF8 protein, humanTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1Ube2S protein, humanUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesDNA damage responsedouble strand breakshistone H2A/H2AXionizing radiationRNF8transcription inhibitionUbe2Subiquitinubiquitin lysine 11-linkageubiquitin lysine 63-linkage

Identifiers

PMID28525740
PMCPMC5642944
OpenAlexW2614941853

What OpenQuestion holds

Textmetadata
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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.