Evidence map›Paper›PMID 41495810›Full record

ReviewCell communication and signaling : CCS2026

Physiological and pathological roles of ANXA11: a multifunctional regulator in neurodegeneration and other disorders.

Chenyang Liu, Yongting Lu, Honglin Zheng, Suying Duan, Hang Zhang, Yaochong Zhang, Han Liu, Haiyang Luo, Yuming Xu

Abstract readReview
In one paragraph

Review in Cell communication and signaling : CCS, 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

9 authors.

Chenyang Liu *Department of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Yongting Lu *Department of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Honglin Zheng *Department of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Suying DuanDepartment of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Hang ZhangDepartment of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Yaochong ZhangDepartment of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Han LiuDepartment of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China.
Haiyang LuoDepartment of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China. fccluohy@zzu.edu.cn.
Yuming XuDepartment of Neurology, the First Affiliated Hospital of Zhengzhou University, Zhengzhou University, Jian-She East Road, Zhengzhou, Henan, 450000, China. xuyuming@zzu.edu.cn.

Funding

China Postdoctoral Science Foundation 2022M722875Henan Provincial Science and Technology Research Project 232102311229National Natural Science Foundation of China 82301619
6 · The paper itself

Abstract

Annexin A11 (ANXA11) is a Ca²⁺-dependent phospholipid-binding protein of the annexin family, which has been traditionally studied for its established roles in tumor progression and autoimmune disorders. Recent studies have highlighted the roles of ANXA11 in newly discovered mechanisms related to neurodegenerative diseases, including liquid-liquid phase separation (LLPS), membrane lipid coupling, and function as a molecular tether linking membraneless organelles to lysosomal membranes. Recent landmark findings reveal that ANXA11 co-assembles with TAR DNA-binding protein 43(TDP-43) into heteromeric amyloid filaments, suggesting that these pathological amyloid structures may play a crucial role in neurodegeneration. In this review, we comprehensively explored the physiological and pathological roles of ANXA11 in neurodegeneration and other disorders, with a focus on LLPS, membrane dynamics, and amyloidogenesis. We discussed potential therapeutic strategies targeting the unique properties of ANXA11 and proposed several critical scientific questions that need to be explored.

Indexed as

AnnexinsNeurodegenerative DiseasesAmyloidAnimalsHumansAmyloidAnnexinsAmyloid filamentsANXA11Autoimmune diseasesCancerLLPSLysosomal tetheringNeurodegenerative diseases

Identifiers

PMID41495810
PMCPMC12870404

What OpenQuestion holds

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Registered trials

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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.