Evidence map›Paper›PMID 42682010›Full record

ReviewBioscience reports2026

Ribosomal protein S3: a critical regulator of human disease mechanisms.

Joeline Dreik, Marwa Al Ali, Jalil Daher, Zeina Nasr

Abstract readReview
In one paragraph

Review in Bioscience reports, 2026. 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.

No citing paper in PubMed yet.

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

4 authors.

Joeline Dreik *Department of Biology, Faculty of Arts and Sciences, University of Balamand, Tripoli, Lebanon.
Marwa Al Ali *Department of Biology, Faculty of Arts and Sciences, University of Balamand, Tripoli, Lebanon.
Jalil Daher *Department of Biology, Faculty of Arts and Sciences, University of Balamand, Tripoli, Lebanon.
Zeina Nasr *Department of Biology, Faculty of Arts and Sciences, University of Balamand, Tripoli, Lebanon.ORCID 0000-0002-4369-5936

Funding

University of Balamand (UOB) RGA/FAS/19-20/014
6 · The paper itself

Abstract

Ribosomal protein S3 (RPS3) is an essential structural component of the 40S ribosomal subunit, yet growing evidence highlights crucial extraribosomal roles in genome maintenance, cell-cycle control, and immune signaling. Dysregulation of RPS3 contributes to diverse human disorders, including cancer, inflammatory diseases, neurodegeneration, and resistance to antimicrobial and anticancer therapies. As a cofactor of NF-κB and a participant in DNA damage responses, RPS3 occupies a node that integrates stress signaling with transcriptional reprogramming, enabling both protective and pathological outcomes. The present review critically evaluates mechanistic insights into RPS3 biology, emphasizing recent findings that delineate its context-dependent effects, discrepancies across models, and remaining gaps that restrict translational applications. Understanding these complexities is essential to assess RPS3's potential as a biomarker and therapeutic target.

Indexed as

NeoplasmsRibosomal ProteinsAnimalsDNA DamageHumansInflammationNF-kappa BSignal TransductionNF-kappa BRibosomal ProteinsRPS3 protein, humancancerDNA damage responseinflammationNF-κB signalingribosomal stressRPS3

Identifiers

PMID42682010
PMCPMC13538082

What Socratic 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 Socratic graph.