Evidence map›Paper›PMID 33199825›Full record

ReviewOncogene2021

Epigenetic modification and a role for the E3 ligase RNF40 in cancer development and metastasis.

Junjiang Fu, Li Liao, Kyathegowdanadoddi Srinivasa Balaji, Chunli Wei, Jaehoon Kim, Jiangzhou Peng

Open access · hybridAbstract readReview
In one paragraph

Review in Oncogene, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

31 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Article
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  11. Article
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  13. Article
  14. RNF20 contributes to epigenetic immunosuppression through CDK9-dependent LSD1 stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Review
  17. Article
  18. The RPA-RNF20-SNF2H cascade promotes proper chromosome segregation and homologous recombination repair.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. 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

6 authors at 4 institutions in 3 countries.

Junjiang FuKey Laboratory of Epigenetics and Oncology, The Research Center for Preclinical Medicine, Southwest Medical University, Luzhou, 646000, Sichuan, China. fujunjiang@hotmail.com.ORCID http://orcid.org/0000-0002-0708-2200
Li LiaoKey Laboratory of Epigenetics and Oncology, The Research Center for Preclinical Medicine, Southwest Medical University, Luzhou, 646000, Sichuan, China.
Kyathegowdanadoddi Srinivasa BalajiPost Graduation Department of Studies and Research in Biotechnology, Teresian Research Center, Teresian College (Affiliated to University of Mysore), Siddhartha Nagara, Mysore, Karnataka, 570011, India.ORCID http://orcid.org/0000-0002-7236-8993
Chunli WeiKey Laboratory of Epigenetics and Oncology, The Research Center for Preclinical Medicine, Southwest Medical University, Luzhou, 646000, Sichuan, China.
Jaehoon KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, 34141, South Korea. kimjaehoon@kaist.edu.ORCID http://orcid.org/0000-0003-4035-0438
Jiangzhou PengDepartment of Thoracic Surgery, The Third Affiliated Hospital of Southern Medical University, Guangzhou, 510500, Guangdong, China. jiangzhou83@163.com.ORCID http://orcid.org/0000-0002-8058-8988
Southwest Medical University · CNKorea Advanced Institute of Science and Technology · KRThird Affiliated Hospital of Southern Medical University · CNUniversity of Mysore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNF40 (OMIM: 607700) is a really interesting new gene (RING) finger E3 ubiquitin ligase containing multiple coiled-coil domains and a C-terminal RING finger motif, which engage in protein-DNA and protein-protein interactions. RNF40 encodes a polypeptide of 1001 amino acids with a predicted molecular mass of 113,678 Da. RNF40 and its paralog RNF20 form a stable heterodimer complex that can monoubiquitylate histone H2B at lysine 120 as well as other nonhistone proteins. Cancer is a major public health problem and the second leading cause of death. Through its protein ubiquitylation activity, RNF40 acts as a tumor suppressor or oncogene to play major epigenetic roles in cancer development, progression, and metastasis, highlighting the essential function of RNF40 and the importance of studying it. In this review, we summarize current knowledge about RNF40 gene structure and the role of RNF40 in histone H2B monoubiquitylation, DNA damage repair, apoptosis, cancer development, and metastasis. We also underscore challenges in applying this information to cancer prognosis and prevention and highlight the urgent need for additional investigations of RNF40 as a potential target for cancer therapeutics.

Indexed as

Epigenesis, GeneticGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticHumansNeoplasm MetastasisNeoplasm ProteinsNeoplasmsUbiquitin-Protein LigasesNeoplasm ProteinsRNF40 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID33199825
PMCPMC7819849
OpenAlexW3100829203

What OpenQuestion holds

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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.