Evidence map›Paper›PMID 26472914›Full record

ArticleScience (New York, N.Y.)2015

Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2.

Lianying Jiao, Xin Liu

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 251 papers.

0numbers the graph read from it
0cells of the map it votes in
251citing papers in PubMed
22.4field-weighted citation impact, top 1% 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

251 citing papers in PubMed, 396 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Structure and molecular function of the BCL7 proteins.Biochemical Society transactions · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Dual Effect ofBiology · 2026
    Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

191 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Lianying JiaoCecil H. and Ida Green Center for Reproductive Biology Sciences and Division of Basic Research, Department of Obstetrics and Gynecology and Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Xin LiuCecil H. and Ida Green Center for Reproductive Biology Sciences and Division of Basic Research, Department of Obstetrics and Gynecology and Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. xin.liu@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

Molecular Mechanisms of Promoter-Terminator Gene LoopingR01GM114576 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LIU, XIN · 2015 to 2019
$1.6M
NIGMS NIH HHS GM114576NIGMS NIH HHS R01 GM114576
6 · The paper itself

Abstract

Polycomb repressive complex 2 (PRC2) catalyzes histone H3K27 trimethylation (H3K27me3), a hallmark of gene silencing. Here we report the crystal structures of an active PRC2 complex of 170 kilodaltons from the yeast Chaetomium thermophilum in both basal and stimulated states, which contain Ezh2, Eed, and the VEFS domain of Suz12 and are bound to a cancer-associated inhibiting H3K27M peptide and a S-adenosyl-l-homocysteine cofactor. The stimulated complex also contains an additional stimulating H3K27me3 peptide. Eed is engulfed by a belt-like structure of Ezh2, and Suz12(VEFS) contacts both of these two subunits to confer an unusual split active SET domain for catalysis. Comparison of PRC2 in the basal and stimulated states reveals a mobile Ezh2 motif that responds to stimulation to allosterically regulate the active site.

Indexed as

Gene SilencingAllosteric RegulationAmino Acid SequenceCatalysisCatalytic DomainChaetomiumCrystallography, X-RayFungal ProteinsHistonesHumansJumonji Domain-Containing Histone DemethylasesMethylationMolecular Sequence DataMutationNeoplasmsPolycomb Repressive Complex 2Fungal ProteinsHistonesJumonji Domain-Containing Histone DemethylasesPolycomb Repressive Complex 2S-Adenosylhomocysteine

Identifiers

PMID26472914
PMCPMC5220110
OpenAlexW2145502498

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.