Ma Junfeng, Hart Gerald W
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD, 21205-2185, USA.
Methods Mol Biol. 2016;1410:91-103. doi: 10.1007/978-1-4939-3524-6_6.
The dynamic co- and post-translational modification (PTM) of proteins, O-linked β-D-N-acetylglucosamine modification (O-GlcNAcylation) of serine/threonine residues is critical in many cellular processes, contributing to multiple physiological and pathological events. The term "O-GlcNAcome" refers to not only the complete set of proteins that undergo O-GlcNAcylation but also the O-GlcNAc status at individual residues, as well as the dynamics of O-GlcNAcylation in response to various stimuli. O-GlcNAcomic analyses have been a challenge for many years. In this chapter, we describe a recently developed approach for the identification and quantification of O-GlcNAc proteins/peptides from complex samples.
蛋白质的动态共翻译和翻译后修饰（PTM），即丝氨酸/苏氨酸残基的O-连接β-D-N-乙酰葡糖胺修饰（O-GlcNAcylation），在许多细胞过程中至关重要，参与多种生理和病理事件。术语“O-GlcNAcome”不仅指经历O-GlcNAcylation修饰的完整蛋白质组，还包括单个残基的O-GlcNAc状态，以及O-GlcNAcylation对各种刺激的响应动态。多年来，O-GlcNAcomic分析一直是一项挑战。在本章中，我们描述了一种最近开发的从复杂样品中鉴定和定量O-GlcNAc修饰蛋白质/肽的方法。
