Evidence map›Paper›PMID 28442573›Full record

ArticleThe Journal of biological chemistry2017

Cell cycle-dependent degradation of the methyltransferase SETD3 attenuates cell proliferation and liver tumorigenesis.

Xiaoqing Cheng, Yuan Hao, Wenjie Shu, Mengjie Zhao, Chen Zhao, Yuan Wu, Xiaodan Peng, Pinfang Yao, Daibiao Xiao, Guoliang Qing and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed, 55 citations in OpenAlex.

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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

14 authors at 5 institutions in 1 country.

Xiaoqing ChengFrom the Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072.
Yuan Haothe Department of General Surgery, Xinhua Hospital affiliated with Shanghai Jiaotong University School of Medicine, Shanghai 200092, haoyuan@medmail.com.cn.
Wenjie ShuFrom the Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072.
Mengjie ZhaoFrom the Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072.
Chen ZhaoFrom the Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072.
Yuan Wuthe Department of Radiotherapy, Hubei Cancer Hospital, Wuhan 430079.
Xiaodan Pengthe Department of Oncology, Shenzhen Hospital of Peking University, Shenzhen 518083.
Pinfang Yaothe Department of Radiotherapy, Hubei Cancer Hospital, Wuhan 430079.
Daibiao Xiaothe Medical Research Institute, Wuhan University, Wuhan 430071, and.
Guoliang Qingthe Medical Research Institute, Wuhan University, Wuhan 430071, and.
Zhengying Panthe Key Laboratory of Chemical Genomics, School of Chemical Biology and Biotechnology, Shenzhen Graduate School, Peking University, Shenzhen 518055, China.
Lei YinFrom the Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072.
Desheng Huthe Department of Radiotherapy, Hubei Cancer Hospital, Wuhan 430079, hds_05@163.com.
Hai-Ning DuFrom the Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan 430072, hainingdu@whu.edu.cn.
Wuhan University · CNHubei Cancer Hospital · CNPeking University · CNPeking University Shenzhen Hospital · CNXinHua Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone modifications, including lysine methylation, are epigenetic marks that influence many biological pathways. Accordingly, many methyltransferases have critical roles in various biological processes, and their dysregulation is often associated with cancer. However, the biological functions and regulation of many methyltransferases are unclear. Here, we report that a human homolog of the methyltransferase SET (

Indexed as

Cell ProliferationProteolysisAmino Acid SubstitutionAnimalsCell Cycle ProteinsCell Transformation, NeoplasticF-Box ProteinsF-Box-WD Repeat-Containing Protein 7Glycogen Synthase Kinase 3 betaHeLa CellsHeterograftsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansLiver Neoplasms, ExperimentalMiceCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanGlycogen Synthase Kinase 3 betaGSK3B protein, humanHistone-Lysine N-MethyltransferaseHistone MethyltransferasesNeoplasm ProteinsSETD3 protein, humanUbiquitin-Protein Ligasescell cyclecell proliferationliver cancermethyltransferaseprotein degradationprotein phosphorylationprotein stability

Identifiers

PMID28442573
PMCPMC5454089
OpenAlexW2608524463

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.