Evidence map›Paper›PMID 31541611›Full record

ArticleCancer science2019

Depletion of DNA damage binding protein 2 sensitizes triple-negative breast cancer cells to poly ADP-ribose polymerase inhibition by destabilizing Rad51.

Lin Zhao, Cheng-Shuai Si, Yue Yu, Jian-Wei Lu, Yan Zhuang

Open access · goldAbstract read
In one paragraph

Article in Cancer science, 2019. 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
0.8field-weighted citation impact, top 25% 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, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. International journal of oncology · 2025
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Emerging Roles of DDB2 in Cancer.International journal of molecular sciences · 2019
    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

5 authors at 2 institutions in 1 country.

Lin ZhaoDepartment of Neurosurgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.ORCID https://orcid.org/0000-0001-6929-8413
Cheng-Shuai SiDepartment of General Surgery, Jiangsu Institute of Cancer Research, Jiangsu Cancer Hospital, The Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, China.
Yue YuDepartment of Thoracic Surgery, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
Jian-Wei LuDepartment of Medical Oncology, Jiangsu Institute of Cancer Research, Jiangsu Cancer Hospital, The Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, China.
Yan ZhuangDepartment of Medical Oncology, Jiangsu Institute of Cancer Research, Jiangsu Cancer Hospital, The Affiliated Cancer Hospital of Nanjing Medical University, Nanjing, China.ORCID https://orcid.org/0000-0002-8269-7520
Jiangsu Cancer Hospital · CNJiangsu Province Hospital · CN

Funding

Jiangsu Cancer Hospital's Natural Science Foundation ZM201705National Natural Science Foundation of China No.81902453Natural Science Foundation of Jiangsu Province BK20181083
6 · The paper itself

Abstract

Poly ADP-ribose polymerase inhibitors (PARPi) have shown promising therapeutic efficacy in triple-negative breast cancer (TNBC) patients. However, resistance ultimately develops, preventing a curative effect from being attained. Extensive investigations have indicated the diversity in the mechanisms underlying the PARPi sensitivity of breast cancer. In this study, we found that DNA damage binding protein 2 (DDB2), a DNA damage-recognition factor, could protect TNBC cells from PARPi by regulating DNA double-strand break repair through the homologous recombination pathway, whereas the depletion of DDB2 sensitizes TNBC cells to PARPi. Furthermore, we found that DDB2 was able to stabilize Rad51 by physical association and disrupting its ubiquitination pathway-induced proteasomal degradation. These findings highlight an essential role of DDB2 in modulating homologous recombination pathway activity and suggest a promising therapeutic target for TNBC.

Indexed as

DNA Breaks, Double-StrandedRecombinational DNA RepairCell Line, TumorDNA-Binding ProteinsDNA RepairDrug Resistance, NeoplasmFemaleHumansNeoplasm ProteinsPoly(ADP-ribose) Polymerase InhibitorsRad51 RecombinaseTriple Negative Breast NeoplasmsUbiquitinationDDB2 protein, humanDNA-Binding ProteinsNeoplasm ProteinsPoly(ADP-ribose) Polymerase InhibitorsRAD51 protein, humanRad51 RecombinaseDDB2homologous recombinationPARPi sensitivityRad51triple-negative breast cancer

Identifiers

PMID31541611
PMCPMC6825009
OpenAlexW2973623440

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.