Evidence map›Paper›PMID 28717873›Full record

ReviewCellular and molecular life sciences : CMLS2018

Orchestration of H3K27 methylation: mechanisms and therapeutic implication.

Mei-Ren Pan, Ming-Chuan Hsu, Li-Tzong Chen, Wen-Chun Hung

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

53 citing papers in PubMed, 91 citations in OpenAlex.

  1. Trial
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  8. Regulation of histones in thromboinflammation.Frontiers in immunology · 2026
    Review
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  12. Review
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  19. Dinochromosome Heterotermini with Telosomal Anchorages.International journal of molecular sciences · 2024
    Article
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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

4 authors at 2 institutions in 1 country.

Mei-Ren PanGraduate Institute of Clinical Medicine, College of Medicine, Kaohsiung Medical University, Kaohsiung, 807, Taiwan.
Ming-Chuan HsuNational Institute of Cancer Research, National Health Research Institutes, Tainan, 704, Taiwan.
Li-Tzong ChenNational Institute of Cancer Research, National Health Research Institutes, Tainan, 704, Taiwan.
Wen-Chun HungNational Institute of Cancer Research, National Health Research Institutes, Tainan, 704, Taiwan. hung1228@nhri.org.tw.
National Health Research Institutes · TWKaohsiung Medical University · TW

Funding

Ministry of Health and Welfare CA-106-PP-15Ministry of Health and Welfare MOHW105-TDU-B-212-134005Ministry of Science and Technology, Taiwan 104-2320-B-400 -010 -MY3Ministry of Science and Technology, Taiwan 105-2314-B-037-001Ministry of Science and Technology, Taiwan 105-2320-B-400-005
6 · The paper itself

Abstract

Histone proteins constitute the core component of the nucleosome, the basic unit of chromatin. Chemical modifications of histone proteins affect their interaction with genomic DNA, the accessibility of recognized proteins, and the recruitment of enzymatic complexes to activate or diminish specific transcriptional programs to modulate cellular response to extracellular stimuli or insults. Methylation of histone proteins was demonstrated 50 years ago; however, the biological significance of each methylated residue and the integration between these histone markers are still under intensive investigation. Methylation of histone H3 on lysine 27 (H3K27) is frequently found in the heterochromatin and conceives a repressive marker that is linked with gene silencing. The identification of enzymes that add or erase the methyl group of H3K27 provides novel insights as to how this histone marker is dynamically controlled under different circumstances. Here we summarize the methyltransferases and demethylases involved in the methylation of H3K27 and show the new evidence by which the H3K27 methylation can be established via an alternative mechanism. Finally, the progress of drug development targeting H3K27 methylation-modifying enzymes and their potential application in cancer therapy are discussed.

Indexed as

Gene SilencingAnimalsHeterochromatinHistone DemethylasesHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansLysineMethylationProtein Processing, Post-TranslationalHeterochromatinHistone DemethylasesHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineEpigenetic drugsGene mutationHistone modificationPolycomb repression complex 2

Identifiers

PMID28717873
PMCPMC5756243
OpenAlexW2735564610

What OpenQuestion holds

Textmetadata
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.