Evidence map›Paper›PMID 33469207›Full record

ReviewNature reviews. Drug discovery2021

Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease.

Kamakoti P Bhat, H Ümit Kaniskan, Jian Jin, Or Gozani

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Drug discovery, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed, 1 pooled it
13.8field-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

150 citing papers in PubMed, 1 synthesis or guideline pooled it, 221 citations in OpenAlex.

  1. Pooled it
  2. Review
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  8. Article
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  17. Article
  18. Mapping Cellular Protein Lysine Methylation Using Targeted-Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  19. Review
  20. Article

90 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 4 institutions in 1 country.

Kamakoti P Bhat *Department of Biology, Stanford University, Stanford, CA, USA.ORCID http://orcid.org/0000-0001-7425-8336
H Ümit Kaniskan *Mount Sinai Center for Therapeutics Discovery, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Jian JinMount Sinai Center for Therapeutics Discovery, Icahn School of Medicine at Mount Sinai, New York, NY, USA. jian.jin@mssm.edu.ORCID http://orcid.org/0000-0002-2387-3862
Or GozaniDepartment of Biology, Stanford University, Stanford, CA, USA. ogozani@stanford.edu.ORCID http://orcid.org/0000-0002-1365-4463
Icahn School of Medicine at Mount Sinai · USStanford Medicine · USStanford University · USTisch Hospital · US

Funding

Epigenetic Therapy and Prader-Willi SyndromeR01HD088626 · NICHD · YALE UNIVERSITY · PI JIANG, YONG-HUI, JIN, JIAN · 2017 to 2021
$2.8M
Targeting Lysine Methyltransferases EZH2 and EZH1 for Treating MLL-rearranged LeukemiasR01CA218600 · NCI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI JIN, JIAN, WANG, G GREG · 2017 to 2021
$2.8M
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
(PQ9) Developing EZH2 Degraders for Treating Triple-Negative Breast CancerR01CA230854 · NCI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI JIN, JIAN, PARSONS, RAMON E · 2018 to 2022
$1.5M
Discovery of Selective Inhibitors for Histone MethyltransferasesR01GM122749 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI JIN, JIAN · 2017 to 2020
$1.3M
Molecular mechanisms of genome maintenance during DNA replication and repairK00CA212435 · NCI · STANFORD UNIVERSITY · PI BHAT, KAMAKOTI P. · 2018 to 2020
$255k
NCI NIH HHS K00 CA212435NCI NIH HHS R01 CA218600NCI NIH HHS R01 CA230854NCI NIH HHS R01 CA236118NICHD NIH HHS R01 HD088626NIGMS NIH HHS R01 GM122749
6 · The paper itself

Abstract

Protein lysine methylation is a crucial post-translational modification that regulates the functions of both histone and non-histone proteins. Deregulation of the enzymes or 'writers' of protein lysine methylation, lysine methyltransferases (KMTs), is implicated in the cause of many diseases, including cancer, mental health disorders and developmental disorders. Over the past decade, significant advances have been made in developing drugs to target KMTs that are involved in histone methylation and epigenetic regulation. The first of these inhibitors, tazemetostat, was recently approved for the treatment of epithelioid sarcoma and follicular lymphoma, and several more are in clinical and preclinical evaluation. Beyond chromatin, the many KMTs that regulate protein synthesis and other fundamental biological processes are emerging as promising new targets for drug development to treat diverse diseases.

Indexed as

Epigenesis, GeneticAnimalsAntineoplastic AgentsDrug DevelopmentHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansLysineMethylationProtein Processing, Post-TranslationalAntineoplastic AgentsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysine

Identifiers

PMID33469207
PMCPMC8035164
OpenAlexW3123990724

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.