Top-down Proteomic Characterization of Truncated Proteoforms
Links to Fileshttps://pubs.acs.org/doi/10.1021/acs.jproteome.9b00487
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Type of Work15 pages
journal articles postprints
Citation of Original PublicationChen, Dapeng; Geis-Asteggiante, Lucia; Gomes, Fabio; Ostrand-Rosenberg, Suzanne; Fenselau, Catherine; Top-down Proteomic Characterization of Truncated Proteoforms; Journal of Proteome Research 18,11 (2019); https://doi.org/10.1021/acs.jproteome.9b00487
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Access to this item will begin on 2020-09-23
This document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Journal of Proteome Research, copyright ©American Chemical Society after peer review. To access the final edited and published work see https://pubs.acs.org/doi/10.1021/acs.jproteome.9b00487.
top-down mass spectrometry
myeloid-derived suppressor cells
A top-down proteomic strategy with semi-automated analysis of data sets has proven successful for global identification of truncated proteins without the use of chemical derivatization, enzymatic manipulation, immunoprecipitation or other enrichment. This approach provides the reliable identification of internal polypeptides formed from precursor gene products by proteolytic cleavage of both the N- and C-termini, as well as truncated proteoforms that retain one or the other termini. The strategy has been evaluated by application to the immunosuppressive extracellular vesicles released by myeloid-derived suppressor cells. More than 1000 truncated proteoforms have been identified, from which binding motifs are derived to allow characterization of the putative proteases responsible for truncation.