Evidence map›Paper›PMID 26027790›Full record

ReviewExperimental hematology2015

Targeting EZH2 and PRC2 dependence as novel anticancer therapy.

Bowen Xu, Kyle D Konze, Jian Jin, Gang Greg Wang

Open access · greenAbstract readReview
In one paragraph

Review in Experimental hematology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.0field-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

78 citing papers in PubMed, 119 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Unlocking Lung Cancer Cell Dormancy: An Epigenetic Perspective.International journal of molecular sciences · 2025
    Review
  10. Article
  11. Pharmacokinetics, metabolism, and excretion of [Cancer chemotherapy and pharmacology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

18 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

4 authors at 2 institutions in 1 country.

Bowen XuDepartment of Biochemistry and Biophysics, The Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Kyle D KonzeDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Jian JinDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Gang Greg WangDepartment of Biochemistry and Biophysics, The Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. Electronic address: greg_wang@med.unc.edu.
Icahn School of Medicine at Mount Sinai · USUniversity of North Carolina at Chapel Hill · US

Funding

Creating in vivo Chemical Probes for Lysine Methyltransferases G9a and GLPR01GM103893 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JIN, JIAN · 2013 to 2015
$1.1M
Cancer epigenetics: Understanding histone methylation in leukemia stem cellsR00CA151683 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WANG, G GREG · 2012 to 2014
$725k
Cancer epigenetics: Understanding histone methylation in leukemia stem cellsK99CA151683 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WANG, G GREG · 2010 to 2011
$276k
NCI NIH HHS CA130247NCI NIH HHS CA151683NCI NIH HHS K99 CA151683NCI NIH HHS R00 CA151683NIGMS NIH HHS R01 GM103893NIGMS NIH HHS R01GM103893
6 · The paper itself

Abstract

Distinctive patterns of chromatin modification control gene expression and define cellular identity during development and cell differentiation. Polycomb repressive complex 2 (PRC2), the sole mammalian enzymatic complex capable of establishing gene-repressive high-degree methylation of histone H3 at lysine 27 (H3K27), plays crucial roles in regulation of normal and malignant hematopoiesis. Recently, increasing evidence has indicated that recurrent gain-of-function mutation and overexpression of EZH2, the catalytic subunit of PRC2, drive and promote malignant transformation such as B-cell lymphomagenesis, providing a rationale for PRC2 inhibition as a novel anticancer strategy. Here, we summarize the recently developed strategies for inhibition of PRC2, which include a series of highly specific, highly potent, small-molecule inhibitors of EZH2 and EZH1, an EZH2-related methyltransferase. PRC2 establishes functional crosstalk with numerous epigenetic machineries during dynamic regulation of gene transcription. Perturbation of such functional crosstalk caused by genetic events observed in various hematologic cancers, such as inactivation of SNF5 and somatic mutation of UTX, confers PRC2 dependence, thus rendering an increased sensitivity to PRC2 inhibition. We discuss our current understanding of EZH2 somatic mutations frequently found in B-cell lymphomas and recurrent mutations in various other epigenetic regulators as novel molecular predictors and determinants of PRC2 sensitivity. As recent advances have indicated a critical developmental or tumor-suppressive role for PRC2 and EZH2 in various tissue types, we discuss concerns over potentially toxic or even adverse effects associated with EZH2/1 inhibition in certain biological contexts or on cancer genetic background. Collectively, inhibition of PRC2 catalytic activity has emerged as a promising therapeutic intervention for the precise treatment of a range of genetically defined hematologic malignancies and can be potentially applied to a broader spectrum of human cancers that bear similar genetic and epigenetic characteristics.

Indexed as

Lymphoma, B-CellPolycomb Repressive Complex 2AnimalsAntineoplastic AgentsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDrug Delivery SystemsEnhancer of Zeste Homolog 2 ProteinEnzyme InhibitorsEpigenesis, GeneticGene Expression Regulation, NeoplasticHistone DemethylasesHumansNuclear ProteinsSMARCB1 ProteinTranscription FactorsAntineoplastic AgentsChromosomal Proteins, Non-HistoneDNA-Binding ProteinsEnhancer of Zeste Homolog 2 ProteinEnzyme InhibitorsEZH2 protein, humanHistone DemethylasesKDM6A protein, humanNuclear ProteinsPolycomb Repressive Complex 2SMARCB1 ProteinSMARCB1 protein, humanTranscription Factors

Identifiers

PMID26027790
PMCPMC4706459
OpenAlexW1865495681

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.