Evidence map›Paper›PMID 33257899›Full record

ReviewNature genetics2020

Reevaluating the roles of histone-modifying enzymes and their associated chromatin modifications in transcriptional regulation.

Marc A J Morgan, Ali Shilatifard

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 206 papers.

0numbers the graph read from it
0cells of the map it votes in
206citing papers in PubMed
–field-weighted citation impact
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

206 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  5. Article
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  7. Article
  8. Review
  9. Discovery of a Highly Potent and Selective ENL Degrader.Journal of medicinal chemistry · 2026
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
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  18. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Review
  20. Review

146 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

2 authors.

Marc A J MorganSimpson Querrey Institute for Epigenetics, Department of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-0141-6273
Ali ShilatifardSimpson Querrey Institute for Epigenetics, Department of Biochemistry and Molecular Genetics, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA. ASH@Northwestern.edu.ORCID http://orcid.org/0000-0002-7490-2854

Funding

Mutations of Chromatin and its Modifying Machineries in MalignanciesR35CA197569 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Ali Shilatifard · 2015 to 2026
$10.7M
NCI NIH HHS R35 CA197569
6 · The paper itself

Abstract

Histone-modifying enzymes are implicated in the control of diverse DNA-templated processes including gene expression. Here, we outline historical and current thinking regarding the functions of histone modifications and their associated enzymes. One current viewpoint, based largely on correlative evidence, posits that histone modifications are instructive for transcriptional regulation and represent an epigenetic 'code'. Recent studies have challenged this model and suggest that histone marks previously associated with active genes do not directly cause transcriptional activation. Additionally, many histone-modifying proteins possess non-catalytic functions that overshadow their enzymatic activities. Given that much remains unknown regarding the functions of these proteins, the field should be cautious in interpreting loss-of-function phenotypes and must consider both cellular and developmental context. In this Perspective, we focus on recent progress relating to the catalytic and non-catalytic functions of the Trithorax-COMPASS complexes, Polycomb repressive complexes and Clr4/Suv39 histone-modifying machineries.

Indexed as

AnimalsChromatin Assembly and DisassemblyChromosomal Proteins, Non-HistoneDrosophilaDrosophila ProteinsGene Expression RegulationHistone CodeHistone-Lysine N-MethyltransferaseHistonesHumansMethyltransferasesPolycomb-Group ProteinsProtein Processing, Post-TranslationalRepressor ProteinsTranscriptional ActivationTranscription, GeneticChromosomal Proteins, Non-HistoneDrosophila ProteinsHistone-Lysine N-MethyltransferaseHistonesMethyltransferasesPolycomb-Group ProteinsRepressor ProteinsSUV39H1 protein, humantrx protein, Drosophila

Identifiers

What OpenQuestion holds

Textmetadata
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.