Evidence map›Paper›PMID 40717130›Full record

ArticleScientific reports2025

A designer polyQ fusion protein modulates NF-κB signaling by sequestering P65/RelA into aggregates.

Xiang-Le Zhang, Lei-Lei Jiang, Heng-Tong Duan, Hong-Yu Hu

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

4 authors.

Xiang-Le ZhangKey Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China.
Lei-Lei JiangKey Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China.
Heng-Tong DuanKey Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China.
Hong-Yu HuKey Laboratory of RNA Innovation, Science and Engineering, Shanghai Institute of Biochemistry and Cell Biology, Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, 200031, People's Republic of China. hyhu@sibcb.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transcription factor P65 is a subunit of the NF-κB complex that regulates expression of pro-inflammatory cytokines, thereby controlling the innate immune response. Excessive activation of NF-κB is commonly associated with various chronic inflammatory conditions. We previously established a polyglutamine (polyQ) fusion strategy to modulate biological processes by sequestering the targeted proteins. Here, we report a designer polyQ fusion (Atx7

Indexed as

NF-kappa BPeptidesProtein AggregatesRecombinant Fusion ProteinsSignal TransductionTranscription Factor RelAAnimalsCell NucleusHEK293 CellsHumansInterleukin-6Tumor Necrosis Factor-alphaInterleukin-6NF-kappa BPeptidespolyglutamineProtein AggregatesRecombinant Fusion ProteinsRELA protein, humanTranscription Factor RelATumor Necrosis Factor-alphaAggregationLDEL peptideNF-κB pathway.P65 proteinPolyQ fusionSequestration

Identifiers

PMID40717130
PMCPMC12301440

What OpenQuestion holds

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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.