Evidence map›Paper›PMID 37503837›Full record

ArticleNucleic acids research2023

BLM helicase protein negatively regulates stress granule formation through unwinding RNA G-quadruplex structures.

Yehuda M Danino, Lena Molitor, Tamar Rosenbaum-Cohen, Sebastian Kaiser, Yahel Cohen, Ziv Porat, Hagai Marmor-Kollet, Corine Katina, Alon Savidor, Ron Rotkopf and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. G-Quadruplexes: Structural Diversity and Emerging Roles in Biomolecular Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

16 authors at 3 institutions in 3 countries.

Yehuda M DaninoDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0001-5295-0487
Lena MolitorDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Tamar Rosenbaum-CohenDepartment of Molecular Neuroscience, Weizmann Institute of Science, Rehovot 7610001, Israel.
Sebastian KaiserCenter for Chromosome Stability, Dept. of Cellular and Molecular Medicine, Panum Institute, Copenhagen Univ, 2200 København N., Denmark.
Yahel CohenDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ziv PoratFlow Cytometry Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot 7610001, Israel.
Hagai Marmor-KolletDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Corine Katinade Botton Institute for Protein Profiling, The Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
Alon Savidorde Botton Institute for Protein Profiling, The Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ron RotkopfBioinformatics Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0001-9503-7348
Eyal Ben-IsaacMICC Cell Observatory Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ofra GolaniMICC Cell Observatory Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot 7610001, Israel.
Yishai Levinde Botton Institute for Protein Profiling, The Nancy and Stephen Grand Israel National Center for Personalized Medicine, Weizmann Institute of Science, Rehovot 7610001, Israel.
David MonchaudInstitut de Chimie Moleculaire, ICMUB CNRS UMR 6302, uB Dijon, France.ORCID 0000-0002-3056-9295
Ian D HicksonCenter for Chromosome Stability, Dept. of Cellular and Molecular Medicine, Panum Institute, Copenhagen Univ, 2200 København N., Denmark.ORCID 0000-0002-0583-566X
Eran HornsteinDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Weizmann Institute of Science · ILUniversity of Copenhagen · DKCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bloom's syndrome (BLM) protein is a known nuclear helicase that is able to unwind DNA secondary structures such as G-quadruplexes (G4s). However, its role in the regulation of cytoplasmic processes that involve RNA G-quadruplexes (rG4s) has not been previously studied. Here, we demonstrate that BLM is recruited to stress granules (SGs), which are cytoplasmic biomolecular condensates composed of RNAs and RNA-binding proteins. BLM is enriched in SGs upon different stress conditions and in an rG4-dependent manner. Also, we show that BLM unwinds rG4s and acts as a negative regulator of SG formation. Altogether, our data expand the cellular activity of BLM and shed light on the function that helicases play in the dynamics of biomolecular condensates.

Indexed as

G-QuadruplexesStress GranulesDNAHumansRecQ HelicasesRNABloom syndrome proteinDNARecQ HelicasesRNA

Identifiers

PMID37503837
PMCPMC10516661
OpenAlexW4385330035

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.