Evidence map›Paper›PMID 40276647›Full record

ArticleMedComm2025

DEAD-Box Helicase 6 Blockade in Brain-Derived Aβ Oligomers From Alzheimer's Disease Patients Attenuates Neurotoxicity.

Xiaoxu Wang, Lu Dai, Na Wu, Donghui Wu, Xinyuan Wang, Xia Meng, Qilei Zhang, Jing Lu, Xiaoxin Yan, Jing Zhang and 1 more

Abstract read
In one paragraph

Article in MedComm, 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

11 authors.

Xiaoxu WangDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.
Lu DaiDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.
Na WuLaboratory Animal Resource Center Capital Medical University Beijing China.
Donghui WuDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.
Xinyuan WangDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.
Xia MengLaboratory Animal Resource Center Capital Medical University Beijing China.
Qilei ZhangDepartment of Anatomy and Neurobiology Central South University Xiangya School of Medicine Changsha Hunan China.
Jing LuDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.
Xiaoxin YanDepartment of Anatomy and Neurobiology Central South University Xiangya School of Medicine Changsha Hunan China.
Jing ZhangDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.
Baian ChenDepartment of Laboratory Animal Sciences, School of Basic Medical Sciences Capital Medical University Beijing China.ORCID https://orcid.org/0000-0003-3038-4941

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There are no effective curative treatments for Alzheimer's disease (AD), the most prevalent form of dementia. Amyloid-beta (Aβ) oligomers are considered key neurotoxic molecules that trigger AD. Recent studies have shown that direct antibody targeting of Aβ oligomers is beneficial for early AD patients; however, serious side effects (e.g., brain hemorrhage, edema, and shrinkage) persist. Considering that Aβ oligomers readily bind to other proteins, contributing to neurotoxicity and AD onset, those proteins could represent alternative therapeutic targets. However, proteins that bind to Aβ oligomers in the brains of AD patients have not yet been identified. In this study, we identified four proteins (DDX6, DSP, JUP, and HRNR) that bind to Aβ oligomers derived from the brains of AD patients. Intriguingly, among these four proteins, only the blockade of DEAD-box helicase 6 (DDX6) in human-derived Aβ oligomers attenuated their neurotoxicity both in vitro and in vivo. Mechanistic analysis revealed that DDX6 promotes the formation of Aβ oligomers, likely due to DDX6 bind to Aβ oligomers at four distinct sites. These findings suggest that DDX6 could serve as a potential therapeutic target to reduce the neurotoxicity of Aβ oligomers in the brain and prevent the progression of AD.

Indexed as

Alzheimer's diseaseAβ oligomersDDX6neurotoxicity

Identifiers

PMID40276647
PMCPMC12018770

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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.