Evidence map›Paper›PMID 42490784›Full record

ArticleFrontiers in aging neuroscience2026

Novel proteomics and neuropathology of

Feixia Zhan, Jiaxin Zhu, Yang Wang, Yuwen Cao, Xiya Shen, Wenlu Lv, Jiewei Wei, Xiaojun Huang, Steven X Hou, Xinghua Luan and 1 more

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In one paragraph

Article in Frontiers in aging neuroscience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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.

Feixia Zhan *Department of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Jiaxin Zhu *State Key Laboratory of Genetic Engineering, Department of Cell and Developmental Biology at School of Life Sciences, Institute of Metabolism and Integrative Biology, Zhongshan Hospital, Fudan University, Shanghai, China.
Yang WangState Key Laboratory of Genetic Engineering, Department of Cell and Developmental Biology at School of Life Sciences, Institute of Metabolism and Integrative Biology, Zhongshan Hospital, Fudan University, Shanghai, China.
Yuwen CaoDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Xiya ShenDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Wenlu LvDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Jiewei WeiDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Xiaojun HuangDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Steven X HouState Key Laboratory of Genetic Engineering, Department of Cell and Developmental Biology at School of Life Sciences, Institute of Metabolism and Integrative Biology, Zhongshan Hospital, Fudan University, Shanghai, China.
Xinghua LuanDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Li CaoDepartment of Neurology, Shanghai Sixth People's Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Nucleotide repeat expansion disorders constitute a group of clinically and genetically heterogeneous diseases, pathologically characterized by the misfolding, aggregation, and accumulation of proteins. The expanded GGC repeats in the 5' untranslated region (5'UTR) of the Objectives: We aimed to investigate the proteomic profile of uN2CpolyG and explore the novel neuropathology in NIID patients, which may underlie the disease pathogenesis. Methods: Mass spectrometry analysis was performed on purified intranuclear inclusions to investigate the proteomic profile. Three patients with genetically confirmed NIID were enrolled; two participants underwent skin biopsy, and one underwent brain autopsy. Skin and brain tissues derived from these patients were used to examine Results: A group of enriched proteins interacting with uN2CpolyG were identified, characterized by significant intrinsically disordered regions (IDRs). Among these, we detected the co-localization of uN2CpolyG with PML and FUS in notably distinct patterns, causing significant DNA damage and impaired stress response. Furthermore, FUS- and PML-positive inclusions were confirmed in NIID patients' tissues. Conclusion: Our findings provide novel insights into the proteomic profile and neuropathology of NIID, potentially enlightening the pathogenesis and therapeutic strategies for protein aggregation-related neurodegenerative diseases.

Indexed as

neuronal intranuclear inclusion diseaseneuropathologyNOTCH2NLC geneprotein aggregationproteomic

Identifiers

PMID42490784
PMCPMC13375458

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