T
Tine E. Thingholm
Researcher at University of Southern Denmark
Publications - 22
Citations - 3960
Tine E. Thingholm is an academic researcher from University of Southern Denmark. The author has contributed to research in topics: Phosphopeptide & Phosphoproteomics. The author has an hindex of 17, co-authored 22 publications receiving 3723 citations. Previous affiliations of Tine E. Thingholm include Odense University Hospital & Lund University.
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Highly Selective Enrichment of Phosphorylated Peptides from Peptide Mixtures Using Titanium Dioxide Microcolumns
TL;DR: This work reports a highly selective enrichment procedure for phosphorylated peptides based on TiO2microcolumns and peptide loading in 2,5-dihydroxybenzoic acid (DHB), and demonstrates that this new procedure was more selective for binding phosphorylation peptides than IMAC using MALDI mass spectrometry.
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Highly selective enrichment of phosphorylated peptides using titanium dioxide
TL;DR: A protocol for selective phosphopeptide enrichment using titanium dioxide (TiO2) chromatography is described, well suited for the characterization of phosphoproteins from both in vitro and in vivo studies in combination with mass spectrometry (MS).
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Analytical strategies for phosphoproteomics
TL;DR: This review presents an overview of different analytical strategies for the characterization of phosphoproteins, focusing on the affinity methods utilized specifically for phosphoprotein and phosphopeptide enrichment prior to MS analysis, and on recent applications of these methods in cell biological applications.
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SIMAC (Sequential Elution from IMAC), a Phosphoproteomics Strategy for the Rapid Separation of Monophosphorylated from Multiply Phosphorylated Peptides
TL;DR: A simple and rapid strategy, SIMAC (sequential elution from IMAC), for sequential separation of monophosphorylation peptides and multiply phosphorylated peptides from highly complex biological samples is reported.
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Analysis of posttranslational modifications of proteins by tandem mass spectrometry
TL;DR: Large-scale, quantitative analysis of proteins by MS/MS is beginning to reveal novel patterns and functions of PTMs in cellular signaling networks and biomolecular structures.