Evidence map›Paper›PMID 38057834›Full record

ReviewEpigenetics & chromatin2023

The functions of SET domain bifurcated histone lysine methyltransferase 1 (SETDB1) in biological process and disease.

Hanshen Luo, Xingliang Wu, Xue-Hai Zhu, Xin Yi, Dunfeng Du, Ding-Sheng Jiang

Open access · goldAbstract readReview
In one paragraph

Review in Epigenetics & chromatin, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. The rebirth of repressive chromatin during early vertebrate development.Annals of the New York Academy of Sciences · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Genome-Wide Identification of theInternational journal of molecular sciences · 2024
    Article
  11. The Roles of H3K9me3 Writers, Readers, and Erasers in Cancer Immunotherapy.International journal of molecular sciences · 2024
    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.

Hanshen Luo *Division of Cardiovascular Surgery, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 1095 Jiefang Ave., Wuhan, 430030, China.
Xingliang Wu *Department of Cardiology, Renmin Hospital of Wuhan University, Wuhan, China.
Xue-Hai ZhuDivision of Cardiovascular Surgery, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 1095 Jiefang Ave., Wuhan, 430030, China.
Xin YiDepartment of Cardiology, Renmin Hospital of Wuhan University, Wuhan, China.
Dunfeng DuKey Laboratory of Organ Transplantation, Ministry of Education; NHC Key Laboratory of Organ Transplantation; Key Laboratory of Organ Transplantation, Chinese Academy of Medical Sciences, Wuhan, Hubei, China. dfdu@tjh.tjmu.edu.cn.
Ding-Sheng JiangDivision of Cardiovascular Surgery, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, 1095 Jiefang Ave., Wuhan, 430030, China. jds@hust.edu.cn.
Chinese Academy of Medical Sciences & Peking Union Medical College · CNRenmin Hospital of Wuhan University · CNMinistry of Education of the People's Republic of China · CNTongji Hospital · CN

Funding

National Natural Science Foundation of China 82070306National Natural Science Foundation of China 82170502
6 · The paper itself

Abstract

Histone methyltransferase SETDB1 (SET domain bifurcated histone lysine methyltransferase 1, also known as ESET or KMT1E) is known to be involved in the deposition of the di- and tri-methyl marks on H3K9 (H3K9me2 and H3K9me3), which are associated with transcription repression. SETDB1 exerts an essential role in the silencing of endogenous retroviruses (ERVs) in embryonic stem cells (mESCs) by tri-methylating H3K9 (H3K9me3) and interacting with DNA methyltransferases (DNMTs). Additionally, SETDB1 is engaged in regulating multiple biological processes and diseases, such as ageing, tumors, and inflammatory bowel disease (IBD), by methylating both histones and non-histone proteins. In this review, we provide an overview of the complex biology of SETDB1, review the upstream regulatory mechanisms of SETDB1 and its partners, discuss the functions and molecular mechanisms of SETDB1 in cell fate determination and stem cell, as well as in tumors and other diseases. Finally, we discuss the current challenges and prospects of targeting SETDB1 for the treatment of different diseases, and we also suggest some future research directions in the field of SETDB1 research.

Indexed as

NeoplasmsPR-SET DomainsDNA MethylationHistone-Lysine N-MethyltransferaseHistonesHumansHistone-Lysine N-MethyltransferaseHistonesSETDB1 protein, humanCancerHeterochromatinHistone methylationNon-histone proteins methylationProtein methylationSETDB1

Identifiers

PMID38057834
PMCPMC10702034
OpenAlexW4389410703

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.