Evidence map›Paper›PMID 31582846›Full record

ReviewNature structural & molecular biology2019

Histone lysine methyltransferases in biology and disease.

Dylan Husmann, Or Gozani

Open access · greenAbstract readReview
In one paragraph

Review in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 281 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
281citing papers in PubMed, 1 pooled it
15.6field-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

281 citing papers in PubMed, 1 synthesis or guideline pooled it, 468 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Epigenetic regulation of transgenes.Journal of biotechnology · 2026
    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. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

221 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 at 2 institutions in 1 country.

Dylan HusmannDepartment of Biology, Stanford University, Stanford, CA, USA.
Or GozaniDepartment of Biology, Stanford University, Stanford, CA, USA. ogozani@stanford.edu.ORCID http://orcid.org/0000-0002-1365-4463
Stanford Medicine · USStanford University · US

Funding

Function of PHD Domain Proteins in Chromatin RegulationR01GM079641 · NIGMS · STANFORD UNIVERSITY · PI GOZANI, OR P. · 2007 to 2020
$4.5M
Stanford Training Program in Aging ResearchT32AG047126 · NIA · STANFORD UNIVERSITY · PI VYJEYANTHI S PERIYAKOIL, TONY WYSS-CORAY · 2014 to 2026
$4.3M
Role of the METTL13 Lysine Methyltransferase in Signaling and CancerR01CA236118 · NCI · STANFORD UNIVERSITY · PI GOZANI, OR P., MAZUR, PAWEL K. · 2019 to 2023
$2.4M
NCI NIH HHS R01 CA236118NIA NIH HHS T32 AG047126NIGMS NIH HHS R01 GM079641
6 · The paper itself

Abstract

The precise temporal and spatial coordination of histone lysine methylation dynamics across the epigenome regulates virtually all DNA-templated processes. A large number of histone lysine methyltransferase (KMT) enzymes catalyze the various lysine methylation events decorating the core histone proteins. Mutations, genetic translocations and altered gene expression involving these KMTs are frequently observed in cancer, developmental disorders and other pathologies. Therapeutic compounds targeting specific KMTs are currently being tested in the clinic, although overall drug discovery in the field is relatively underdeveloped. Here we review the biochemical and biological activities of histone KMTs and their connections to human diseases, focusing on cancer. We also discuss the scientific and clinical challenges and opportunities in studying KMTs.

Indexed as

AnimalsGene Expression Regulation, DevelopmentalGene Expression Regulation, NeoplasticHistone-Lysine N-MethyltransferaseHistonesHumansMutationNeoplasmsHistone-Lysine N-MethyltransferaseHistones

Identifiers

PMID31582846
PMCPMC6951022
OpenAlexW2979183639

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.