Evidence map›Paper›PMID 41201471›Full record

ArticleRedox biology2025

3S-DB identifies an RNA repository facilitating stop codon readthrough for selenocysteine insertion and selenoproteome expansion.

Chenfang Si, Lu Zhang, Jing Gao, Kongyan Niu, Yunxia Li, Nan Liu, Bing Shan, Yaoyang Zhang

Abstract read
In one paragraph

Article in Redox biology, 2025. 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

8 authors.

Chenfang SiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China; The Core Facility Center, CAS Center for Excellence in Molecular Plant Sciences, Shanghai Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, 200032, China.
Lu ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Jing GaoInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China.
Kongyan NiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China.
Yunxia LiInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China.
Nan LiuInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China; Shanghai Key Laboratory of Aging Studies, 100 Haike Rd., Shanghai, 201210, China.
Bing ShanInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China. Electronic address: shanbing@sioc.ac.cn.
Yaoyang ZhangInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Haike Rd., Shanghai, 201210, China; Shanghai Key Laboratory of Aging Studies, 100 Haike Rd., Shanghai, 201210, China. Electronic address: zyy@sioc.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selenoproteins contain the selenocysteine (Sec, U), which is essential for redox regulation due to its reactive selenol group. The current set of 25 human selenoproteins was defined by the presence of SECIS elements in the 3' UTR coupled with in-frame UGA codons through a stop codon readthrough mechanism. However, the discovery of novel selenoproteins and SECIS elements remains limited by the constraints of SECIS prediction methods. In this study, we focus on SECISBP2, the core SECIS-binding protein, to analyze its binding RNAs using RNA immunoprecipitation sequencing (RIP-Seq) technology. We constructed the 3S-DB, a database of 1,333 SECISBP2-bound RNAs with potential SECIS functions for UGA recoding, including most known selenoprotein transcripts. Importantly, we validate that the 3' UTRs of PDF and ATP5MJ exhibit SECIS activity using luciferase assays and by fusing them to known selenoprotein RNAs. In summary, our results provide a valuable resource of mRNAs with potential for UGA recoding and previously unrecognized SECIS elements, with the potential to expand the known selenoproteome and advance our understanding of their roles in redox biology and beyond. Furthermore, this work offers new insights into non-canonical stop codon readthrough and the broader mechanisms governing translational regulation of the genetic code.

Indexed as

Codon, TerminatorProteomeRNA-Binding ProteinsSelenocysteineSelenoproteins3' Untranslated RegionsHumans3' Untranslated RegionsCodon, TerminatorProteomeRNA-Binding ProteinsSECISBP2 protein, humanSelenocysteineSelenoproteinsRedox biologySECISSecMSSelenoproteinStop codon readthrough

Identifiers

PMID41201471
PMCPMC12628022

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.