Evidence map›Paper›PMID 41652114›Full record

ReviewCellular and molecular neurobiology2026

Advances in Research on Endoplasmic Reticulum-Associated Degradation Mechanisms in Neurodegenerative Diseases.

Bing Kong, Weiyi Huang, Yiming Zhong, Yuenan Liu, Hao Wang, Yilin Shen, Jinju Xu, Mingliang Xiang, Bin Ye

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cellular and molecular neurobiology, 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.

Bing Kong *Department of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Weiyi Huang *Department of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Yiming Zhong *Department of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Yuenan LiuDepartment of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Hao WangDepartment of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Yilin ShenDepartment of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Jinju XuDepartment of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Mingliang XiangDepartment of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. xml12128@rjh.com.cn.
Bin YeDepartment of Otolaryngology & Head and Neck Surgery, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China. yb12237@rjh.com.cn.

Funding

National Natural Science Foundation of China 82471165,82301296,82301297Science and Technology Commission of Shanghai Municipality 23ZR1440200Scientific research project of Health and Family Planning Commission of Huangpu District HLM202502
6 · The paper itself

Abstract

The endoplasmic reticulum protein quality control system-comprising endoplasmic reticulum-associated degradation (ERAD), the unfolded protein response (UPR), and ER-phagy-serves as a crucial mechanism for maintaining protein homeostasis within the endoplasmic reticulum (ER) of eukaryotic cells. As a crucial pathway of recognition, transport, and degradation of misfolded proteins, ERAD dysfunction results in the excessive accumulation of aberrant proteins, thereby disrupting normal cellular physiology and ultimately leading to necrosis or apoptosis. It is reported that the occurrence and development of central and peripheral neurodegenerative diseases are closely related to the dysfunction of misfolded protein degradation. Many components within the ERAD pathway may play essential roles in these pathological processes. This review provides an overview of the ERAD processes, its regulatory mechanisms, and its involvement in the pathogenesis and potential treatment of neurodegenerative diseases, aiming to offer theoretical insight for future research on the specific roles of ERAD in different neurodegenerative diseases.

Indexed as

Biomedical ResearchEndoplasmic ReticulumEndoplasmic Reticulum-Associated DegradationNeurodegenerative DiseasesAnimalsHumansUnfolded Protein ResponseERADNeurodegenerative diseasesPharmacological therapyProtein homeostasis

Identifiers

PMID41652114
PMCPMC12921081

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.