Evidence map›Paper›PMID 34469566›Full record

ArticleNucleic acids research2021

YB-1 unwinds mRNA secondary structures in vitro and negatively regulates stress granule assembly in HeLa cells.

Karina Budkina, Krystel El Hage, Marie-Jeanne Clément, Bénédicte Desforges, Ahmed Bouhss, Vandana Joshi, Alexandre Maucuer, Loic Hamon, Lev P Ovchinnikov, Dmitry N Lyabin and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 28 citations in OpenAlex.

  1. A passive protein environment offsets RNA folding energetics in cells.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Article
  4. Y-box binding proteins in immunity and RNA virus infection.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  5. Unlocking the role of tRNA-derived fragments in shaping breast cancer signaling.Naunyn-Schmiedeberg's archives of pharmacology · 2025
    Review
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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

11 authors at 2 institutions in 2 countries.

Karina BudkinaSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.
Krystel El HageSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.ORCID 0000-0003-4837-3888
Marie-Jeanne ClémentSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.
Bénédicte DesforgesSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.
Ahmed BouhssSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.
Vandana JoshiSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.
Alexandre MaucuerSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.
Loic HamonSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.ORCID 0000-0003-2032-7994
Lev P OvchinnikovInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290, Russian Federation.
Dmitry N LyabinInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290, Russian Federation.ORCID 0000-0003-4605-8884
David PastréSABNP, Univ Evry, INSERM U1204, Université Paris-Saclay, 91025 Evry, France.ORCID 0000-0002-3348-9514
Inserm · FRInstitute of Protein Research · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the absence of the scanning ribosomes that unwind mRNA coding sequences and 5'UTRs, mRNAs are likely to form secondary structures and intermolecular bridges. Intermolecular base pairing of non polysomal mRNAs is involved in stress granule (SG) assembly when the pool of mRNAs freed from ribosomes increases during cellular stress. Here, we unravel the structural mechanisms by which a major partner of dormant mRNAs, YB-1 (YBX1), unwinds mRNA secondary structures without ATP consumption by using its conserved cold-shock domain to destabilize RNA stem/loops and its unstructured C-terminal domain to secure RNA unwinding. At endogenous levels, YB-1 facilitates SG disassembly during arsenite stress recovery. In addition, overexpression of wild-type YB-1 and to a lesser extent unwinding-defective mutants inhibit SG assembly in HeLa cells. Through its mRNA-unwinding activity, YB-1 may thus inhibit SG assembly in cancer cells and package dormant mRNA in an unfolded state, thus preparing mRNAs for translation initiation.

Indexed as

Adenosine TriphosphateArsenitesBase PairingCell Line, TumorHeLa CellsHumansInverted Repeat SequencesPeptide Chain Initiation, TranslationalRibosomesRNA, MessengerStress GranulesY-Box-Binding Protein 1Adenosine TriphosphatearseniteArsenitesRNA, MessengerY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID34469566
PMCPMC8464072
OpenAlexW3196964621

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.