Evidence map›Paper›PMID 21847359›Full record

ArticleNeoplasia (New York, N.Y.)2011

Enhanced expression of EHMT2 is involved in the proliferation of cancer cells through negative regulation of SIAH1.

Hyun-Soo Cho, John D Kelly, Shinya Hayami, Gouji Toyokawa, Masahi Takawa, Masanori Yoshimatsu, Tatsuhiko Tsunoda, Helen I Field, David E Neal, Bruce Aj Ponder and 2 more

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 6% 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

68 citing papers in PubMed, 1 synthesis or guideline pooled it, 123 citations in OpenAlex.

  1. Pooled it
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  8. mMolecular therapy. Nucleic acids · 2022
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8 more citing papers are in PubMed but not listed here.

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

12 authors at 3 institutions in 2 countries.

Hyun-Soo ChoHuman Genome Center, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
John D Kelly
Shinya Hayami
Gouji Toyokawa
Masahi Takawa
Masanori Yoshimatsu
Tatsuhiko Tsunoda
Helen I Field
David E Neal
Bruce Aj Ponder
Yusuke Nakamura
Ryuji Hamamoto
The University of Tokyo · JPUniversity of Cambridge · GBCancer Research UK · GB

Funding

Cancer Research UK 19275
6 · The paper itself

Abstract

EHMT2 is a histone lysine methyltransferase localized in euchromatin regions and acting as a corepressor for specific transcription factors. Although the role of EHMT2 in transcriptional regulation has been well documented, the pathologic consequences of its dysfunction in human disease have not been well understood. Here, we describe important roles of EHMT2 in human carcinogenesis. Expression levels of EHMT2 are significantly elevated in human bladder carcinomas compared with nonneoplastic bladder tissues (P < .0001) in real-time polymerase chain reaction analysis. Complementary DNA microarray analysis also revealed its overexpression in various types of cancer. The reduction of EHMT2 expression by small interfering RNAs resulted in the suppression of the growth of cancer cells and possibly caused apoptotic cell death in cancer cells. Importantly, we show that EHMT2 can suppress transcription of the SIAH1 gene by binding to its promoter region (-293 to +51) and by methylating lysine 9 of histone H3. Furthermore, an EHMT2-specific inhibitor, BIX-01294, significantly suppressed the growth of cancer cells. Our results suggest that dysregulation of EHMT2 plays an important role in the growth regulation of cancer cells, and further functional studies may affirm the importance of EHMT2 as a promising therapeutic target for various types of cancer.

Indexed as

Gene Expression Regulation, NeoplasticApoptosisAzepinesCell Line, TransformedCell Line, TumorCell ProliferationHEK293 CellsHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansNeoplasmsNuclear ProteinsQuinazolinesSeven in Absentia ProteinsUbiquitin-Protein LigasesAzepinesBIX 01294EHMT2 protein, humanHistocompatibility AntigensHistone-Lysine N-MethyltransferaseNuclear ProteinsQuinazolinesSeven in Absentia ProteinsUbiquitin-Protein Ligases

Identifiers

PMID21847359
PMCPMC3156658
OpenAlexW1921414899

What OpenQuestion holds

Textmetadata
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.