Evidence map›Paper›PMID 36669975›Full record

ArticleTrends in pharmacological sciences2023

Taming PRMT5-adaptor protein interactions.

Hunter S Sims, Mingji Dai

Abstract readComment
PubMed Full text at PMC Publisher
In one paragraph

Article in Trends in pharmacological sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Hunter S SimsDepartment of Chemistry, Emory University, Atlanta, GA 30322, USA; Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA. Electronic address: hunter.sims@emory.edu.
Mingji DaiDepartment of Chemistry, Emory University, Atlanta, GA 30322, USA. Electronic address: mingji.dai@emory.edu.

Funding

Synthesis and Study of Medicinally Important MoleculesR35GM128570 · NIGMS · PURDUE UNIVERSITY · PI Mingji Dai · 2018 to 2026
$3.7M
NIGMS NIH HHS R35 GM128570
6 · The paper itself

Abstract

Protein arginine methyltransferase (PRMT)-5 is a prominent epigenetic regulator and therapeutic target. Recently, Krzyzanowski et al. identified stapled peptides that inhibit the interaction of PRMT5 with two of its adaptor proteins. This discovery creates opportunities for novel therapeutic development by selectively modulating PRMT5 activity.

Indexed as

Protein-Arginine N-MethyltransferasesHumansPRMT5 protein, humanProtein-Arginine N-Methyltransferaseschloride channel nucleotide sensitive protein 1A (pICln)protein arginine methyltransferase 5 (PRMT5)protein-protein interaction (PPI) inhibitorRio domain-containing protein (RioK1)solid-phase peptide synthesis (SPPS)stapled peptide

Identifiers

PMID36669975
PMCPMC11167722

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.