Show simple item record Anderson, Lissa C DeHart, Caroline J Kaiser, Nathan K Fellers, Ryan T Smith, Donald F Greer, Joseph B LeDuc, Richard D Blackney, Gregory T Thomas, Paul M Kelleher, Neil L Hendrickson, Christopher L 2016-07-18T18:03:43Z 2016-07-18T18:03:43Z 2016
dc.identifier.citation Forthcoming en
dc.description Collection of RAW files, .tdReport files, and search database information for the abovementioned research article. en
dc.description.abstract The National High Magnetic Field Laboratory (NHMFL) recently installed a 21T FT-ICR mass spectrometer, which is part of the NHMFL FT-ICR User Facility and available to all qualified users. Here, we demonstrate top-down LC-21 T FT-ICR MS/MS of intact proteins derived from human colorectal cancer cell lysate. We identify a combined total of 684 unique protein entries observed as 3,238 unique proteoforms at a 1% false discovery rate, based on rapid, data-dependent acquisition of collision-induced and electron-transfer dissociation tandem mass spectra from 40 LC-MS/MS experiments. en
dc.description.sponsorship This work was supported by the National Science Foundation Cooperative Agreement No. DMR-1157490 and the State of Florida as well as by the National Institute of General Medical Science (P41GM108569) for the National Resource for Translational and Developmental Proteomics (NRTDP) based at Northwestern University. en
dc.language.iso en_US en
dc.publisher American Chemical Society en
dc.relation.ispartofseries Forthcoming;Forthcoming
dc.relation.isversionof Forthcoming en
dc.rights Creative Commons Attribution 4.0 license ( en
dc.rights.uri en
dc.subject FT-ICR, 21 tesla, Top-down proteomics, ultra-high resolution, FTMS en
dc.title Identification and characterization of human proteoforms by top-down LC-21 tesla FT-ICR mass spectrometry en
dc.type Dataset en
dc.identifier.doi Forthcoming
dc.altmetrics.display true en

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