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通过质谱法解码泛素修饰。

Decoding Ubiquitin Modifications by Mass Spectrometry.

机构信息

National Clinical Research Center for Geriatrics and Department of General Practice, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, China.

出版信息

Adv Exp Med Biol. 2024;1466:1-18. doi: 10.1007/978-981-97-7288-9_1.

Abstract

Protein ubiquitination is a critical and widely distributed post-translational modification (PTM) involved in the regulation of almost every cellular process and pathway in cells, such as proteostasis, DNA repair, trafficking, and immunity. Mass spectrometry (MS)-based proteomics is a robust tool to decode the complexity of ubiquitin networks by disclosing the proteome-wide ubiquitination sites, the length, linkage and topology of ubiquitin chains, the chemical modification of ubiquitin chains, and the crosstalk between ubiquitination and other PTMs. In this chapter, we discuss the application of MS in the interpretation of the ubiquitin code.

摘要

蛋白质泛素化是一种关键且广泛分布的翻译后修饰(PTM),参与调节细胞中的几乎每一个细胞过程和途径,如蛋白质稳态、DNA 修复、运输和免疫。基于质谱(MS)的蛋白质组学是一种强大的工具,通过揭示全蛋白质组的泛素化位点、泛素链的长度、连接和拓扑结构、泛素链的化学修饰以及泛素化与其他 PTM 之间的串扰,来解码泛素网络的复杂性。在本章中,我们讨论了 MS 在解释泛素密码中的应用。

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