Evidence map›Paper›PMID 31104094›Full record

ReviewCellular and molecular life sciences : CMLS2019

Targeting protein methylation: from chemical tools to precision medicines.

David Dilworth, Dalia Barsyte-Lovejoy

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Special Issue "Protein Methyltransferases in Human Health and Diseases".International journal of molecular sciences · 2026
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  14. Protein Arginine Methyltransferase 5 FunctionsFrontiers in cell and developmental biology · 2021
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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.

David DilworthStructural Genomics Consortium, University of Toronto, Toronto, ON, M5G 1L7, Canada.
Dalia Barsyte-LovejoyStructural Genomics Consortium, University of Toronto, Toronto, ON, M5G 1L7, Canada. d.barsyte@utoronto.ca.
Structural Genomics Consortium · CAUniversity of Toronto · CA

Funding

Wellcome Trust
6 · The paper itself

Abstract

The methylation of proteins is integral to the execution of many important biological functions, including cell signalling and transcriptional regulation. Protein methyltransferases (PMTs) are a large class of enzymes that carry out the addition of methyl marks to a broad range of substrates. PMTs are critical for normal cellular physiology and their dysregulation is frequently observed in human disease. As such, PMTs have emerged as promising therapeutic targets with several inhibitors now in clinical trials for oncology indications. The discovery of chemical inhibitors and antagonists of protein methylation signalling has also profoundly impacted our general understanding of PMT biology and pharmacology. In this review, we present general principles for drugging protein methyltransferases or their downstream effectors containing methyl-binding modules, as well as best-in-class examples of the compounds discovered and their impact both at the bench and in the clinic.

Indexed as

Precision MedicineAllosteric RegulationBinding SitesCatalytic DomainEnzyme InhibitorsHistone-Lysine N-MethyltransferaseHumansNeoplasmsProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalEnzyme InhibitorsHistone-Lysine N-MethyltransferaseProtein-Arginine N-MethyltransferasesChemical biologyChemical probeChromatinDrug discoveryEpigeneticsMethyl-binder proteinOncologyProtein methyltransferase

Identifiers

PMID31104094
PMCPMC11105543
OpenAlexW2945168557

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.