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- W3137013588 abstract "Recent studies have revealed diverse amino acid, post-translational, and noncanonical modifications of proteins in diverse organisms and tissues. However, their unbiased detection and analysis remain hindered by technical limitations. Here, we present a spectral alignment method for the identification of protein modifications using high-resolution mass spectrometry proteomics. Termed SAMPEI for spectral alignment-based modified peptide identification, this open-source algorithm is designed for the discovery of functional protein and peptide signaling modifications, without prior knowledge of their identities. Using synthetic standards and controlled chemical labeling experiments, we demonstrate its high specificity and sensitivity for the discovery of substoichiometric protein modifications in complex cellular extracts. SAMPEI mapping of mouse macrophage differentiation revealed diverse post-translational protein modifications, including distinct forms of cysteine itaconatylation. SAMPEI’s robust parametrization and versatility are expected to facilitate the discovery of biological modifications of diverse macromolecules. SAMPEI is implemented as a Python package and is available open-source from BioConda and GitHub (https://github.com/FenyoLab/SAMPEI)." @default.
- W3137013588 created "2021-03-29" @default.
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- W3137013588 date "2021-03-22" @default.
- W3137013588 modified "2023-10-14" @default.
- W3137013588 title "Discovery of Protein Modifications Using Differential Tandem Mass Spectrometry Proteomics" @default.
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- W3137013588 doi "https://doi.org/10.1021/acs.jproteome.0c00638" @default.
- W3137013588 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8341206" @default.
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- W3137013588 hasPublicationYear "2021" @default.
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