Evidence map›Paper›PMID 25283148›Full record

ArticleNature communications2014

ABRO1 suppresses tumourigenesis and regulates the DNA damage response by stabilizing p53.

Jianhong Zhang, Mengmeng Cao, Jiahong Dong, Changyan Li, Wangxiang Xu, Yiqun Zhan, Xiaohui Wang, Miao Yu, Changhui Ge, Zhiqiang Ge and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. MLF2 Negatively Regulates P53 and Promotes Colorectal Carcinogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  5. ABRO1 arrests cardiomyocyte proliferation and myocardial repair by suppressing PSPH.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  6. Review
  7. A review of deubiquitinases and thier roles in tumorigenesis and development.Frontiers in bioengineering and biotechnology · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. The multiple roles of deubiquitinases in liver cancer.American journal of cancer research · 2020
    Review
  18. USP7 Is a Master Regulator of Genome Stability.Frontiers in cell and developmental biology · 2020
    Review
  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

11 authors at 4 institutions in 1 country.

Jianhong ZhangState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Mengmeng CaoSchool of Chemical Engineering and Technology, TianJin University, Tianjin 300073, China.
Jiahong DongDepartment of Liver and Gallbladder Surgery, The General Hospital of Chinese People's Liberation Army, Beijing 100853, China.
Changyan LiState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Wangxiang XuState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Yiqun ZhanState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Xiaohui WangState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Miao YuState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Changhui GeState Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China.
Zhiqiang GeSchool of Chemical Engineering and Technology, TianJin University, Tianjin 300073, China.
Xiaoming Yang1] State Key Laboratory of Proteomics, Beijing Proteomics Research Center, Beijing Institute of Radiation Medicine, 27-Taiping Road, Beijing 100850, China [2] School of Chemical Engineering and Technology, TianJin University, Tianjin 300073, China.
Beijing Proteome Research Center · CNTianjin University · CNState Key Laboratory of ProteomicsPeople's Liberation Army No. 150 Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abraxas brother 1 (ABRO1) has been reported to be a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. However, current knowledge of the functions of ABRO1 is limited. Here we report that ABRO1 is frequently downregulated in human liver, kidney, breast and thyroid gland tumour tissues. Depletion of ABRO1 in cancer cells reduces p53 levels and enhances clone formation and cellular transformation. Conversely, overexpression of ABRO1 suppresses cell proliferation and tumour formation in a p53-dependent manner. We further show that ABRO1 stabilizes p53 by facilitating the interaction of p53 with USP7. DNA-damage induced accumulation of endogenous ABRO1 as well as translocation of ABRO1 to the nucleus, and the induction of p53 by DNA damage is almost completely attenuated by ABRO1 depletion. Our study shows that ABRO1 is a novel p53 regulator that plays an important role in tumour suppression and the DNA damage response.

Indexed as

DNA DamageGene Expression ProfilingApoptosisCarcinogenesisCell Line, TumorCell NucleusCell ProliferationDown-RegulationGene Expression Regulation, NeoplasticHumansNeoplasmsNuclear Matrix-Associated ProteinsRNA, MessengerTumor Suppressor Protein p53UbiquitinUbiquitin-Specific Peptidase 7ABRAXAS2 protein, humanNuclear Matrix-Associated ProteinsRNA, MessengerTP53 protein, humanTumor Suppressor Protein p53UbiquitinUbiquitin-Specific Peptidase 7Ubiquitin-Specific ProteasesUbiquitin ThiolesteraseUSP7 protein, human

Identifiers

PMID25283148
PMCPMC4205886
OpenAlexW1996286322

What OpenQuestion holds

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LicenceCC BY
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.