Decoding the SUMO Proteome: A Mass Spectrometry Workflow for Site-Specific Identification.

UbiSite Approach: Global Site-Specific Profiling of Canonical and Non-Canonical Ubiquitination in Cells and Tissues.

The UbiSite approach, a refined strategy for site-specific mapping of global ubiquitination using mass spectrometry-based proteomics, offers a robust and versatile platform for comprehensive ubiquitinome profiling with enhanced specificity and depth, enabling new insights into the regulatory roles of ubiquitin across d...

Identification of Protein Cysteine Modifications Using Unbiased Mass Spectrometry-Based Proteomics.

Mass spectrometry-based mapping of the ubiquitin chaperone code.

This chapter outlines experimental and computational strategies for MS-based analysis of the ubiquitin chaperone code, including di-glycine peptide enrichment, site identification, quantitative analysis, and validation.

STEP-PTMs: Sequential TMT-based Enrichment and Profiling of Post-Translational Modifications

Application of STEP-PTM to TMT16-plex cerebral brain organoids enabled the quantification of 10,413 proteins, 2,969 metabolites, 19,655 phosphopeptides, 28,876 peptides containing reversibly modified cysteines, 9,723 peptides containing free cysteines, 1,716 intact sialylated N-linked glycopeptides and 771 lysine-acety...

On the Impact of Post-Translational Succination on Small Ubiquitin-like Modifier 1 Structure: A Dual Approach combining Gas-Phase and Solution Studies

A Scalable and Robust Workflow for Cost-Effective Post-Translational Modifications Profiling by Chemical Proteomics

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...