蛋白质 S-亚硝基化:具有普遍生物活性的化学修饰

IF 1.9 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY The Protein Journal Pub Date : 2024-07-28 DOI:10.1007/s10930-024-10223-y
Adam A. Aboalroub, Khaldun M. Al Azzam
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引用次数: 0

摘要

一氧化氮(NO)可诱导蛋白质翻译后修饰(PTM),即 S-亚硝基化,它作为数千种底物蛋白质的关键调节因子已开始受到关注。然而,由于已鉴定的 S-亚硝基化蛋白质(S-NO 蛋白质)数量有限,我们对这一新兴 PTM 的生物学后果的了解还不全面。检测方法的最新进展有效地拓宽了已发现的 S-NO 蛋白的范围。本文简要回顾了 S-NO 蛋白检测方法的进展,并讨论了这些方法如何参与表征这种 PTM 的生物学后果。此外,我们还深入探讨了与 S-NO 蛋白相关的疾病,重点是这些蛋白质在减轻传染性疾病严重性方面的作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Protein S-Nitrosylation: A Chemical Modification with Ubiquitous Biological Activities

Nitric oxide (NO) induces protein posttranslational modification (PTM), known as S-nitrosylation, which has started to gain attention as a critical regulator of thousands of substrate proteins. However, our understanding of the biological consequences of this emerging PTM is incomplete because of the limited number of identified S-nitrosylated proteins (S–NO proteins). Recent advances in detection methods have effectively contributed to broadening the spectrum of discovered S–NO proteins. This article briefly reviews the progress in S–NO protein detection methods and discusses how these methods are involved in characterizing the biological consequences of this PTM. Additionally, we provide insight into S–NO protein-related diseases, focusing on the role of these proteins in mitigating the severity of infectious diseases.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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