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Updated: Jun 27, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
Published on: April 4, 2018
Analysis of protein lysine acetylation in vitro and in vivo
Nadine Pelletier1, Serge Grégoire1, Xiang-Jiao Yang1
1Rosalind and Morris Goodman Cancer Center and Department of Medicine, McGill University, Montreal, Canada.
Abstract:
Protein lysine acetylation, referring to acetylation of the epsilon-amino group of a lysine residue, has recently emerged as an important post-translational modification for regulating protein functions in various organisms. Like phosphorylation, lysine acetylation is a rapidly reversible and precisely controlled covalent modification that serves as a simple on/off switch or participates in a codified manner with other post-translational modifications to regulate protein functions in different cellular and developmental processes. This unit describes and discusses methods used for in vitro and in vivo determination of lysine acetylation.
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