封面:病理二硫键交联:淀粉样蛋白发生和疾病进展的分子见解(ChemBioChem 18/2025)

IF 2.8 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
ChemBioChem Pub Date : 2025-09-19 DOI:10.1002/cbic.70050
Dong Min Kang, Nataliia Lukianenko, Ja-Hyun Baik, Yun Kyung Kim, Sungsu Lim
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引用次数: 0

摘要

这个封面说明了淀粉样蛋白之间的二硫交联在稳定错误折叠的蛋白寡聚物和促进它们聚集成纤维组装中起着关键作用。这些与二硫化物相连的物种逃避蛋白水解清除,破坏细胞蛋白质平衡,并在细胞间繁殖,从而驱动以异常蛋白质积累和聚集为特征的蛋白质病变,正如在各种神经退行性疾病中所观察到的那样。更多信息可以在Yun Kyung Kim, Sungsu Lim及其同事的评论文章中找到(DOI: 10.1002/cbic.202500316)。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Front Cover: Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression (ChemBioChem 18/2025)

Front Cover: Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression (ChemBioChem 18/2025)

Front Cover: Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression (ChemBioChem 18/2025)

Front Cover: Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression (ChemBioChem 18/2025)

Front Cover: Pathological Disulfide Bond Crosslinking: Molecular Insights into Amyloidogenesis and Diseases Progression (ChemBioChem 18/2025)

This cover illustrates that disulfide crosslinking between amyloidogenic proteins plays a critical role in stabilizing misfolded protein oligomers and facilitating their aggregation into fibrillar assemblies. These disulfide-linked species evade proteolytic clearance, disrupt cellular proteostasis, and propagate between cells—thereby driving proteinopathy characterized by aberrant protein accumulation and aggregation, as observed in various neurodegenerative disorders. More information can be found in the Review Article by Yun Kyung Kim, Sungsu Lim, and co-workers (DOI: 10.1002/cbic.202500316).

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来源期刊
ChemBioChem
ChemBioChem 生物-生化与分子生物学
CiteScore
6.10
自引率
3.10%
发文量
407
审稿时长
1 months
期刊介绍: ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).
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