Evidence map›Paper›PMID 36875494›Full record

ReviewFrontiers in endocrinology2023

Structure, activity and function of the lysine methyltransferase SETD5.

Mingyang Li, Yanan Hou, Ziwei Zhang, Bowen Zhang, Ting Huang, Aiqin Sun, Genbao Shao, Qiong Lin

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in endocrinology, 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
2.5field-weighted citation impact, top 11% 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, 16 citations in OpenAlex.

  1. Integrative Analysis UncoversCurrent issues in molecular biology · 2026
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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

8 authors at 1 institution in 1 country.

Mingyang LiDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Yanan HouDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Ziwei ZhangDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Bowen ZhangDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Ting HuangDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Aiqin SunDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Genbao ShaoDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Qiong LinDepartment of Basic Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.
Jiangsu University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SET domain-containing 5 (SETD5) is an uncharacterized member of the protein lysine methyltransferase family and is best known for its transcription machinery by methylating histone H3 on lysine 36 (H3K36). These well-characterized functions of SETD5 are transcription regulation, euchromatin formation, and RNA elongation and splicing. SETD5 is frequently mutated and hyperactive in both human neurodevelopmental disorders and cancer, and could be down-regulated by degradation through the ubiquitin-proteasome pathway, but the biochemical mechanisms underlying such dysregulation are rarely understood. Herein, we provide an update on the particularities of SETD5 enzymatic activity and substrate specificity concerning its biological importance, as well as its molecular and cellular impact on normal physiology and disease, with potential therapeutic options.

Indexed as

MethyltransferasesNeurodevelopmental DisordersHistonesHumansLysineHistonesLysineMethyltransferasesSETD5 protein, humancancerlysine methyltransferasemethylationneurodevelopmental disorder (NDD)posttranslational modificationsSETD5

Identifiers

PMID36875494
PMCPMC9982096
OpenAlexW4321252960

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.