Evidence map›Paper›PMID 36358861›Full record

ReviewCancers2022

Protein Arginine Methyltransferases as Therapeutic Targets in Hematological Malignancies.

Camille Sauter, John Simonet, Fabien Guidez, Baptiste Dumétier, Baptiste Pernon, Mary Callanan, Jean-Noël Bastie, Romain Aucagne, Laurent Delva

Open access · goldAbstract readReview
In one paragraph

Review in Cancers, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
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  7. Review
  8. Discovery of PRMT3 Degrader for the Treatment of Acute Leukemia.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  9. Review
  10. Article
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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

9 authors at 1 institution in 1 country.

Camille SauterInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.
John SimonetInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.
Fabien GuidezInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.ORCID 0000-0003-1380-4473
Baptiste DumétierInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.ORCID 0000-0001-9087-2344
Baptiste PernonInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.
Mary CallananInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.
Jean-Noël BastieInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.
Romain AucagneInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.ORCID 0000-0002-5644-3287
Laurent DelvaInserm U1231, Team Epi2THM, LipSTIC Labex, UFR des Sciences de Santé, Université de Bourgogne, Université Bourgogne Franche-Comté, 21000 Dijon, France.
Inserm · FR

Funding

Fondation ARC pour la recherche sur le cancer ARCDOC42022010004491Fondation pour la Recherche Médicale ECO201906009006
6 · The paper itself

Abstract

Arginine methylation is a common post-translational modification affecting protein activity and the transcription of target genes when methylation occurs on histone tails. There are nine protein arginine methyltransferases (PRMTs) in mammals, divided into subgroups depending on the methylation they form on a molecule of arginine. During the formation and maturation of the different types of blood cells, PRMTs play a central role by controlling cell differentiation at the transcriptional level. PRMT enzymatic activity is necessary for many cellular processes in hematological malignancies, such as the activation of cell cycle and proliferation, inhibition of apoptosis, DNA repair processes, RNA splicing, and transcription by methylating histone tails' arginine. Chemical tools have been developed to inhibit the activity of PRMTs and have been tested in several models of hematological malignancies, including primary samples from patients, xenografts into immunodeficient mice, mouse models, and human cell lines. They show a significant effect by reducing cell viability and increasing the overall survival of mice. PRMT5 inhibitors have a strong therapeutic potential, as phase I clinical trials in hematological malignancies that use these molecules show promising results, thus, underlining PRMT inhibitors as useful therapeutic tools for cancer treatment in the future.

Indexed as

arginine methylationclinical trialshematological malignanciesinhibitorsPRMT

Identifiers

PMID36358861
PMCPMC9657843
OpenAlexW4308453676

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.