综述解读

去泛素化酶在 AD:从蛋白稳态到多条病理通路

来源:Biomolecules · PMID 42939748 · DOI 10.3390/biom16101494** · 来源:IMA 知识库《文献层·文献监控卡片》2026-10-29 期 · 全文级(file_id dGBunAeRiRlm,下载实测 692,872 B) · 全文已获取并通过归属校验

数据日期 2026-10-29 · 生成时间 2026-10-29 06:03

研究问题

Alzheimer’s disease (AD) is the most common neurodegenerative disease and the leading cause of dementia.

方法

In this review, we summarize the roles and molecular mechanisms of DUBs in Aβ and tau pathology, autophagic dysfunction, mitochondrial dysfunction, neuroinflammation, synaptic dysfunction, and other AD-related processes.;In this review, we summarize the roles of DUBs in these AD-related pathological processes.

核心结论

The defining pathological hallmarks of AD are extracellular amyloid plaques formed by amyloid-β (Aβ) deposition and intracellular neurofibrillary tangles composed of abnormally phosphorylated tau.;In addition, a cohort study of Chinese patients with AD and FTD identified four rare CYLD variants in approximately 1% of patients with AD, including three previously unreported variants, suggesting a potential association between rare CYLD variants and AD susceptibility [18].;However, whether these pathological improvements translate into cognitive or behavioral benefits remains unknown. ‖ 结论:Further work is needed to establish appropriate targets and determine whether individual DUBs should be inhibited or restored, while addressing drug selectivity, brain exposure, and long-term safety.

局限

全文未设独立 limitations 节;结构上为综述/二次研究,因果推断强度受限。

对本项目的价值

★★★☆☆ 脑老化是最大未满足需求,也是终点最难量化的领域;biomarker 与认知读数选择最敏感。命中核心 线粒体;队列:ADNI;设计 多组学。

全文来源

PMC JATS 全文(正文 46,043 字符,已过标题/DOI 逐字归属校验)

原文题录

  • 英文标题:Deubiquitinating Enzymes in Alzheimer's Disease: From Protein Homeostasis to Diverse Pathological Processes.
  • 期刊与标识:Biomolecules · PMID 42939748 · DOI 10.3390/biom16101494**

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