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Recent Submissions

  • 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; ... (American Chemical Society, 2016)
    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 ...
  • Fornelli, Luca; Durbin, Kenneth R; Fellers, Ryan T; Early, Bryan P; Greer, Joseph B; LeDuc, Richard D; Compton, Phillip D; Kelleher, Neil L (Forthcoming, 2016-08)
    Over the past decade, developments in high resolution mass spectrometry have enabled the high throughput analysis of intact proteins from complex proteomes, leading to the identification of thousands of proteoforms. ...
  • Shams, Daniel P; Early, Bryan P; Fellers, Ryan T; Greer, Joseph B; Thomas, Paul M; Fornelli, Luca; LeDuc, Richard D; Schwab, David J; Kelleher, Neil L (Forthcoming, )
    Within the last five years, top down proteomics (TDP) has emerged as a high throughput technique for protein identification in addition to characterization and quantitation of thousands of modified proteoforms. Here, a ...
  • DeHart, Caroline J; Fellers, Ryan T; Fornelli, Luca; Kelleher, Neil L; Thomas, Paul M (Methods in Molecular Biology, Springer, )
    Traditional bottom-up mass spectrometry-based proteomics relies on the use of an enzyme, often trypsin, to generate small peptides (typically < 25 amino acids long). In top-down proteomics, proteins remain intact and are ...
  • De Hart, Caroline J; Fellers, Ryan T; Fornelli, Luca; Kelleher, Neil L; Thomas, Paul M (Methods in Molecular Biology, Springer, 2016)
    Traditional bottom-up mass spectrometry-based proteomics relies on the use of an enzyme, often trypsin, to generate small peptides (typically < 25 amino acids long). In top-down proteomics, proteins remain intact and are ...

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