Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns.

By Martijn W. H. Pinkse, Pauliina M Uitto, M. Hilhorst, B. Ooms, Albert J. R. Heck. Analytical Chemistry, 2004

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Structural Characterization of the Human Eukaryotic Initiation Factor 3 Protein Complex by Mass Spectrometry*S (2007, methodology): “A total of 29 phosphorylation sites were identified within the eIF3a, eIF3b, eIF3c, eIF3f, eIF3g, eIF3h, and eIF3j subunits of which nine phosphorylation sites were identified only when selective enrichment of phosphopeptides by TiO2 and Ga(III) IMAC was carried out (see Tables I and II).”
Quantitative Phosphoproteomics of Early Elicitor Signaling in Arabidopsis*S (2007, methodology): “Subsequently each fraction was separately enriched for phosphopeptides using TiO2 affinity chromatography (23) in the presence of high concentrations of dihydroxybenzoic acid (36).”
Highly Selective Enrichment of Phosphorylated Peptides from Peptide Mixtures Using Titanium Dioxide Microcolumns* (2005, methodology): “The first procedure (A) was adopted from the method published previously (21).”
Proteomics by mass spectrometry: approaches, advances, and applications. (2009, methodology): “Other metal oxide affinity resins are TiO2 (116), Fe3O4 (117), and ZrO2 (118).”
A tissue-specific atlas of mouse protein phosphorylation and expression. (2010, positive): “Recently, phosphoproteomics has enabled large-scale identification of protein phosphorylation sites, benefiting from advances in phosphopeptide enrichment (Pinkse et al., 2004; Villen and Gygi, 2008) and improvements in mass spectrometry instrumentation and methods.”