ArticleMethods in molecular biology (Clifton, N.J.)2026
Identification of Protein Cysteine Modifications Using Unbiased Mass Spectrometry-Based Proteomics.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Post-translational modifications (PTMs) can play vital roles in the protein's structure, function, localization, and interactions, enabling dynamic control of cellular processes. As such, understanding these modifications is essential to elucidate key biological mechanisms. This chapter discusses an unbiased, mass spectrometry-based approach using wildcard (open) searches in the Byonic platform to detect and identify nondisulfide cysteine PTMs. By targeting individual cysteines and scanning for mass shifts across a broad range, this strategy enables discovery of novel or unexpected modifications. The method is applicable to both new and existing datasets and can be extended to any amino acid, offering a versatile tool for redox and PTM-focused proteomics.
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