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Showing 1 to 5 of 5 for “"Top-Down Mass Spectrometry"”.

  1. Complex Proteoform Identification Using Top-Down Mass Spectrometry

    … exhibit different functional behaviors. Because top-down mass spectrometry directly analyzes intact proteoforms and provides complete sequence information of proteoforms, it has become the method of choice for the identification of complex proteoforms. Although instruments and experimental …

    iupui Repository record for Complex Proteoform Identification Using Top-Down Mass Spectrometry (opens in a new tab)

  2. Top Down Mass Spectrometry of Archaea and Human Tumor Cells

    A final study was performed applying the top down platform to human HeLa tumor cells. Thirty-four proteins in all were identified, and >90% of these were fully characterized. Several proteins harbored post-translational modifications including N-terminal and internal acetylations, methylations, …

    uiuc Repository record for Top Down Mass Spectrometry of Archaea and Human Tumor Cells (opens in a new tab)

  3. Direct Analysis of Intact Proteins From Microorganisms Using Top Down Mass Spectrometry

    We applied this top down proteomics platform to study proteins from Methanococcus jannaschii and Saccharomyces cerevisiae. From the whole cell lysate of yeast, ∼120 ion species were successfully identified with 100% sequence coverage, and we also detected several post-translational …

    uiuc Repository record for Direct Analysis of Intact Proteins From Microorganisms Using Top Down Mass Spectrometry (opens in a new tab)

  4. Bioinformatics of High Throughput Proteomics Using Tandem Mass Spectrometry of Intact Proteins

    Top down mass spectrometry is a unique approach to the problem of identifying and characterizing proteins with a DNA-predicted sequence. It would be desirable to move top down mass spectrometry in to the 'omic' sciences by developing a high throughput form that could be used to simultaneously …

    uiuc Repository record for Bioinformatics of High Throughput Proteomics Using Tandem Mass Spectrometry of Intact Proteins (opens in a new tab)

  5. Development of Surface Plasmon Resonance and Top-Down Mass Spectrometry Approaches to Monitor the Conformational Properties of Amyloidogenic Peptides and Their Enzymatic Cleavage: a Specific Application to Uncover the Mechanisms of Digestion of Branched Ubiquitin-Tau Proteoforms by the Human 20S Proteasome [Sviluppo di approcci di risonanza plasmonica di superficie e spettrometria di massa top-down per monitorare le proprietà conformazionali dei peptidi amiloidogenici e la loro digestione enzimatica: un'applicazione specifica per scoprire i meccanismi di digestione delle proteoforme ramificate di ubiquitina-tau da parte del proteasoma umano 20S]

    … esperimenti di SDS-PAGE e spettrometria di massa top-down (MS) per studiare il modello di degradazione delle proteoforme tau e per monitorare il rilascio dei frammenti di digestione. Lo sviluppo di un nuovo software chiamato SpectraSage è stato di fondamentale importanza per l'analisi, …

    catania Repository record for Development of Surface Plasmon Resonance and Top-Down Mass Spectrometry Approaches to Monitor the Conformational Properties of Amyloidogenic Peptides and Their Enzymatic Cleavage: a Specific Application to Uncover the Mechanisms of Digestion of Branched Ubiquitin-Tau Proteoforms by the Human 20S Proteasome [Sviluppo di approcci di risonanza plasmonica di superficie e spettrometria di massa top-down per monitorare le proprietà conformazionali dei peptidi amiloidogenici e la loro digestione enzimatica: un'applicazione specifica per scoprire i meccanismi di digestione delle proteoforme ramificate di ubiquitina-tau da parte del proteasoma umano 20S] (opens in a new tab)