Chen, DapengGeis-Asteggiante, LuciaGomes, FabioOstrand-Rosenberg, SuzanneFenselau, Catherine2019-11-142019-11-142019-09-10Chen, 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.9b00487https://doi.org/10.1021/acs.jproteome.9b00487http://hdl.handle.net/11603/16313A 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.15 pagesen-USThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.Access to this item will begin on 2020-09-23This 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.truncated proteoformstop-down mass spectrometrycleavage motifsprotease databaseextracellular vesiclesmyeloid-derived suppressor cellsText