This review focuses specifically on O-phosphorylation and Lys-N(ε)-acetylation, the two best-characterized and most extensively crosstalking PTMs in plants, and integrates four perspectives: the historical development of proteomic and bioinformatics approaches to these modifications; current mass spectrometry-based wor...
A. I. Uba, Betül Subaşı, S. Usman· Computational biology and ch...· 0 citations
Improvements enabling quantification of site-specific modifications, including post-translational modifications and covalent compound-protein interactions spanning diverse pathways are described.
Steven R. Shuken, Geordon A. Frere, Charlotte R. Beard et al.· Nature Communications· 0 citations
Mass spectrometry-based chemical proteomics is a powerful method to analyze proteins labelled by small molecules to identify protein targets of active compounds and to profile protein post-translational modifications. The throughput and high protein input for chemical proteomics workflows has been often a limiting fact...
Liu Zang, Jonas Grandke, Jana Richter et al.· bioRxiv· 0 citations
This chapter provides an overview of the biological roles and structural diversity of SUMOylation, and presents an MS-based workflow designed to identify SUMOylation sites with high specificity and depth.
Chongyang Li, P. Thibault· Methods in molecular biology· 0 citations
Generic procedures to analyze PTMs with MS methods are summarized and an update with the latest development in sample preparation, MS analysis, and database search that advanced the way for PTM analysis is provided, improving knowledge of PTMs and understanding of their roles in various diseases.
How to build DDA PTM spectral libraries using various software tools, specifically Spectronaut, SpectroMine, and MSFragger are described, which were imported into Skyline for the analysis of previously published DIA succinylome data of Sirtuin-5 knocked-out vs wild-type mouse brains.
Alice Zhang, B. Schilling, J. Bons· Methods in molecular biology· 0 citations
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