Evidence map›Paper›PMID 30034588›Full record

ArticleACS medicinal chemistry letters2018

LLY-283, a Potent and Selective Inhibitor of Arginine Methyltransferase 5, PRMT5, with Antitumor Activity.

Zahid Q Bonday, Guillermo S Cortez, Michael J Grogan, Stephen Antonysamy, Ken Weichert, Wayne P Bocchinfuso, Fengling Li, Steven Kennedy, Binghui Li, Mary M Mader and 8 more

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

89 citing papers in PubMed, 179 citations in OpenAlex.

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  16. Exploiting Synthetic Lethality of PRMT5 for Precision Treatment of MTAP-Deficient Glioblastoma.International journal of translational medicine (Basel, Switzerland) · 2025
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29 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

18 authors at 3 institutions in 3 countries.

Zahid Q BondayLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Guillermo S CortezLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Michael J GroganLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Stephen AntonysamyLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Ken WeichertLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Wayne P BocchinfusoLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Fengling LiStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Steven KennedyStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Binghui LiLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Mary M MaderLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Cheryl H ArrowsmithStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Peter J BrownStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Mohammad S EramStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Magdalena M SzewczykStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Dalia Barsyte-LovejoyStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Masoud VedadiStructural Genomics Consortium, University of Toronto, Toronto, ON M5G 1L7, Canada.
Ernesto GuccioneInstitute of Molecular and Cell Biology, Singapore 138673.
Robert M CampbellLilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285, United States.
Eli Lilly (United States) · USUniversity of Toronto · CAInstitute of Molecular and Cell Biology · SG

Funding

Wellcome Trust
6 · The paper itself

Abstract

Protein arginine methyltransferase 5 (PRMT5) is a type II arginine methyltransferase that catalyzes the formation of symmetric dimethylarginine in a number of nuclear and cytoplasmic proteins. Although the cellular functions of PRMT5 have not been fully unraveled, it has been implicated in a number of cellular processes like RNA processing, signal transduction, and transcriptional regulation. PRMT5 is ubiquitously expressed in most tissues and its expression has been shown to be elevated in several cancers including breast cancer, gastric cancer, glioblastoma, and lymphoma. Here, we describe the identification and characterization of a novel and selective PRMT5 inhibitor with potent

Identifiers

PMID30034588
PMCPMC6047023
OpenAlexW2800877169

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.