Evidence map›Paper›PMID 31350521›Full record

ReviewNature reviews. Molecular cell biology2019

The regulation, functions and clinical relevance of arginine methylation.

Ernesto Guccione, Stéphane Richard

Erratum issuedAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Molecular cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 357 papers.

0numbers the graph read from it
0cells of the map it votes in
357citing papers in PubMed
22.2field-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

357 citing papers in PubMed, 630 citations in OpenAlex.

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297 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Ernesto GuccioneTisch Cancer Institute, Department of Oncological Sciences and Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York City, NY, USA. ernesto.guccione@mssm.edu.
Stéphane RichardSegal Cancer Center, Lady Davis Institute for Medical Research, SMBD Jewish General Hospital and Gerald Bronfman Department of Oncology and Departments of Medicine, Biochemistry and Human Genetics, McGill University, Montréal, Québec, Canada. stephane.richard@mcgill.ca.ORCID http://orcid.org/0000-0003-2665-4806
Icahn School of Medicine at Mount Sinai · USJewish General Hospital · CA

Funding

CIHR FDN-154303
6 · The paper itself

Abstract

Methylation of arginine residues by protein arginine methyltransferases (PRMTs) is involved in the regulation of fundamental cellular processes, including transcription, RNA processing, signal transduction cascades, the DNA damage response and liquid-liquid phase separation. Recent studies have provided considerable advances in the development of experimental tools and the identification of clinically relevant PRMT inhibitors. In this review, we discuss the regulation of PRMTs, their various cellular roles and the clinical relevance of PRMT inhibitors for the therapy of neurodegenerative diseases and cancer.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAnimalsArginineHumansMethylationNeoplasm ProteinsNeoplasmsProtein-Arginine N-MethyltransferasesArginineNeoplasm ProteinsProtein-Arginine N-Methyltransferases

Identifiers

PMID31350521
OpenAlexW2964804212

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.