Evidence map›Paper›PMID 41144700›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

Marginal Stability of the YB1 Cold-Shock Domain in Cells Enables Binding of Multiple Nucleic Acids.

Puja Shrestha, Sara S Ribeiro, Janne Aurich, Christian Herrmann, Simon Ebbinghaus

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

5 authors.

Puja ShresthaLehrstuhl für Biophysikalische Chemie and Research Center Chemical Sciences and Sustainability, Research Alliance Ruhr, Ruhr University Bochum, Universitätsstraße 150, 44801, Bochum, Germany.
Sara S RibeiroLehrstuhl für Biophysikalische Chemie and Research Center Chemical Sciences and Sustainability, Research Alliance Ruhr, Ruhr University Bochum, Universitätsstraße 150, 44801, Bochum, Germany.ORCID https://orcid.org/0000-0001-6033-8853
Janne AurichInstitute of Physical and Theoretical Chemistry, Technical University Braunschweig, Rebenring 56, 38106, Braunschweig, Germany.
Christian HerrmannDepartment of Physical Chemistry I, Ruhr University Bochum, Universitätsstraße 150, 44801, Bochum, Germany.
Simon EbbinghausLehrstuhl für Biophysikalische Chemie and Research Center Chemical Sciences and Sustainability, Research Alliance Ruhr, Ruhr University Bochum, Universitätsstraße 150, 44801, Bochum, Germany.ORCID https://orcid.org/0000-0001-9309-1279

Funding

Deutsche Forschungsgemeinschaft RESOLV: EXC 2033-390677874
6 · The paper itself

Abstract

YB1 is an intrinsically disordered protein with a folded cold shock domain (CSD) required for translation, transcription, and RNA metabolism. This multifunctionality and cancer involvement make it a therapeutically attractive target. YB1-CSD and nucleic acid interaction is essential for function. The CSD is marginally stable in vitro, with unknown implications for its function in the cell. In this study, the folding stability of the CSD in living cells is studied at the physiological levels of nucleic acids. The CSD is highly stabilized (increase in T

Indexed as

Nucleic AcidsY-Box-Binding Protein 1HumansProtein BindingProtein DomainsProtein FoldingProtein StabilityThermodynamicsNucleic AcidsY-Box-Binding Protein 1YBX1 protein, humanfolding and binding free‐energy landscapesin‐cell protein foldingnucleic acid bindingYB1‐cold shock domain

Identifiers

PMID41144700
PMCPMC12767080

What Socratic 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 Socratic graph.