Evidence map›Paper›PMID 33361816›Full record

ArticleNature2021

Molecular basis of nucleosomal H3K36 methylation by NSD methyltransferases.

Wanqiu Li, Wei Tian, Gang Yuan, Pujuan Deng, Deepanwita Sengupta, Zhongjun Cheng, Yinghua Cao, Jiahao Ren, Yan Qin, Yuqiao Zhou and 4 more

Open access · greenAbstract read
In one paragraph

Article in Nature, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed, 1 pooled it
6.4field-weighted citation impact, top 2% 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

89 citing papers in PubMed, 1 synthesis or guideline pooled it, 147 citations in OpenAlex.

  1. Pooled it
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  5. Article
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  8. Article
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  11. Many faces of mammalian NSD methyltransferases.Cellular & molecular biology letters · 2026
    Review
  12. Article
  13. Article
  14. Article
  15. Article
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  18. Article
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29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 2 countries.

Wanqiu Li *Department of Biology, Cryo-EM Centre, Southern University of Science and Technology, Shenzhen, China.
Wei Tian *Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Gang Yuan *Department of Biology, Stanford University, Stanford, CA, USA.
Pujuan Deng *Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Deepanwita SenguptaDepartment of Biology, Stanford University, Stanford, CA, USA.
Zhongjun ChengStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
Yinghua CaoKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Jiahao RenKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Yan QinKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Yuqiao ZhouKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Yulin JiaKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China.
Or GozaniDepartment of Biology, Stanford University, Stanford, CA, USA. ogozani@stanford.edu.ORCID http://orcid.org/0000-0002-1365-4463
Dinshaw J PatelStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY, USA. pateld@mskcc.org.ORCID http://orcid.org/0000-0002-9779-7778
Zhanxin WangKey Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Sciences, Beijing Normal University, Beijing, China. wangz@bnu.edu.cn.ORCID http://orcid.org/0000-0001-9956-9376
Beijing Normal University · CNMemorial Sloan Kettering Cancer Center · USStanford University · USSouthern University of Science and Technology · CNStanford Medicine · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Function of PHD Domain Proteins in Chromatin RegulationR01GM079641 · NIGMS · STANFORD UNIVERSITY · PI GOZANI, OR P. · 2007 to 2020
$4.5M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM079641
6 · The paper itself

Abstract

Histone methyltransferases of the nuclear receptor-binding SET domain protein (NSD) family, including NSD1, NSD2 and NSD3, have crucial roles in chromatin regulation and are implicated in oncogenesis

Indexed as

Binding SitesBiocatalysisCell Line, TumorCell ProliferationCryoelectron MicroscopyHeterograftsHistone-Lysine N-MethyltransferaseHistonesHumansMethylationModels, MolecularMultiprotein ComplexesMutationNeoplasmsNeoplasm TransplantationNuclear ProteinsHistone-Lysine N-MethyltransferaseHistonesMultiprotein ComplexesNSD2 protein, humanNSD3 protein, humanNuclear ProteinsNucleosomesRepressor Proteins

Identifiers

PMID33361816
PMCPMC7889650
OpenAlexW3115301926

What OpenQuestion holds

Textmetadata
LicenceTDM
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.