Evidence map›Paper›PMID 30100186›Full record

ArticleCell2018

Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.

Qianhui Qu, Yoh-Hei Takahashi, Yidai Yang, Hongli Hu, Yan Zhang, Joseph S Brunzelle, Jean-Francois Couture, Ali Shilatifard, Georgios Skiniotis

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Probing the Cancer Mutational Landscape of KMT2 Regulatory Subunits.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Epigenetic remodeling during early embryonic development.Frontiers in cell and developmental biology · 2026
    Review
  13. Article
  14. Review
  15. Article
  16. The FBXW7-KMT2 axis in cancer-associated fibroblasts controls tumor growth via an epigenetic-paracrine mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

14 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

9 authors at 3 institutions in 2 countries.

Qianhui QuDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Yoh-Hei TakahashiDepartment of Biochemistry and Molecular Genetics, Simpson Querrey Center for Epigenetics, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Yidai YangDepartment of Biochemistry, Microbiology, and Immunology, Ottawa Institute of Systems Biology, University of Ottawa, Ottawa ON K1H 8M5, Canada.
Hongli HuDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Yan ZhangDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Joseph S BrunzelleNorthwestern Synchrotron Research Center, Life Sciences Collaborative Access Team, Northwestern University, Argonne, IL 60439, USA.
Jean-Francois CoutureDepartment of Biochemistry, Microbiology, and Immunology, Ottawa Institute of Systems Biology, University of Ottawa, Ottawa ON K1H 8M5, Canada.
Ali ShilatifardDepartment of Biochemistry and Molecular Genetics, Simpson Querrey Center for Epigenetics, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA. Electronic address: ash@northwestern.edu.
Georgios SkiniotisDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: yiorgo@stanford.edu.
Stanford University · USNorthwestern University · USUniversity of Ottawa · CA

Funding

Mutations of Chromatin and its Modifying Machineries in MalignanciesR35CA197569 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Ali Shilatifard · 2015 to 2026
$10.7M
Architectural Basis of Leptin Transmembrane SignalingR01DK090165 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SKINIOTIS, GEORGIOS · 2011 to 2017
$2.3M
CIHRNCI NIH HHS R35 CA197569NIDDK NIH HHS R01 DK090165
6 · The paper itself

Abstract

The methylation of histone 3 lysine 4 (H3K4) is carried out by an evolutionarily conserved family of methyltransferases referred to as complex of proteins associated with Set1 (COMPASS). The activity of the catalytic SET domain (su(var)3-9, enhancer-of-zeste, and trithorax) is endowed through forming a complex with a set of core proteins that are widely shared from yeast to humans. We obtained cryo-electron microscopy (cryo-EM) maps of the yeast Set1/COMPASS core complex at overall 4.0- to 4.4-Å resolution, providing insights into its structural organization and conformational dynamics. The Cps50 C-terminal tail weaves within the complex to provide a central scaffold for assembly. The SET domain, snugly positioned at the junction of the Y-shaped complex, is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3). The mobile SET-I motif of the SET domain is engaged by Cps30, explaining its key role in COMPASS catalytic activity toward higher H3K4 methylation states.

Indexed as

AnimalsCatalytic DomainChaetomiumChromatinCryoelectron MicroscopyDNA-Binding ProteinsEpigenesis, GeneticFungal ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansInsectaIntracellular Signaling Peptides and ProteinsMethylationProtein SubunitsChromatinDNA-Binding ProteinsFungal ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesIntracellular Signaling Peptides and ProteinsProtein SubunitsSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeWDR5 protein, humanCOMPASScryo-EMepigeneticshistone methylationMLL

Identifiers

PMID30100186
PMCPMC6108936
OpenAlexW2886127471

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.