Evidence map›Paper›PMID 37425931›Full record

ArticlebioRxiv : the preprint server for biology2023

Identification of small molecule inhibitors of G3BP-driven stress granule formation.

Brian D Freibaum, James Messing, Haruko Nakamura, Ugur Yurtsever, Jinjun Wu, Hong Joo Kim, Jeff Hixon, Rene Lemieux, Jay Duffner, Walter Huynh and 6 more

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 2 institutions in 1 country.

Brian D FreibaumDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
James MessingDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Haruko NakamuraDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Ugur YurtseverDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Jinjun WuDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Hong Joo KimDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
Jeff HixonFaze Medicines, Cambridge, Massachusetts, USA.
Rene LemieuxFaze Medicines, Cambridge, Massachusetts, USA.
Jay DuffnerFaze Medicines, Cambridge, Massachusetts, USA.
Walter HuynhFaze Medicines, Cambridge, Massachusetts, USA.
Kathy WongFaze Medicines, Cambridge, Massachusetts, USA.
Michael WhiteFaze Medicines, Cambridge, Massachusetts, USA.
Christia LeeFaze Medicines, Cambridge, Massachusetts, USA.
Rachel MeyersFaze Medicines, Cambridge, Massachusetts, USA.
Roy ParkerDepartment of Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado, USA.
J Paul TaylorDepartment of Cell and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee, USA.
St. Jude Children's Research Hospital · USHoward Hughes Medical Institute · US

Funding

Dynamic RNA-protein assemblies and neurological diseaseR35NS097974 · NINDS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI TAYLOR, JOSEPH PAUL · 2017 to 2024
$7.2M
NINDS NIH HHS R35 NS097974
6 · The paper itself

Abstract

Stress granule formation is triggered by the release of mRNAs from polysomes and is promoted by the action of the paralogs G3BP1 and G3BP2. G3BP1/2 proteins bind mRNAs and thereby promote the condensation of mRNPs into stress granules. Stress granules have been implicated in several disease states, including cancer and neurodegeneration. Consequently, compounds that limit stress granule formation or promote their dissolution have potential as both experimental tools and novel therapeutics. Herein, we describe two small molecules, referred to as G3BP inhibitor a and b (G3Ia and G3Ib), designed to bind to a specific pocket in G3BP1/2 that is known to be targeted by viral inhibitors of G3BP1/2 function. In addition to disrupting co-condensation of RNA, G3BP1, and caprin 1

Identifiers

PMID37425931
PMCPMC10327151
OpenAlexW4382363394

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.