Notable

S.B. Ficarro et al., "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae," Nature Biotechnology, 20[3]:301-5, March 2002. "This is a long-awaited paper detailing more than 200 phosphorylation sites from Saccharomyces cerevisiae. The authors used immobilized metal affinity chromatography (IMAC) to selectively isolate phosphopeptides from nonphosphopeptides. The new advance is the selectivity of the IMAC column when utilized after methylation of aspartat

Jeffrey Perkel
Apr 28, 2002
S.B. Ficarro et al., "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae," Nature Biotechnology, 20[3]:301-5, March 2002.

"This is a long-awaited paper detailing more than 200 phosphorylation sites from Saccharomyces cerevisiae. The authors used immobilized metal affinity chromatography (IMAC) to selectively isolate phosphopeptides from nonphosphopeptides. The new advance is the selectivity of the IMAC column when utilized after methylation of aspartate and glutamate residues. These amino acids normally bind to IMAC columns as contaminating peptides. A finding that should be evaluated further is that 67% of the phosphopeptides detected were doubly phosphorylated, suggesting that the IMAC separation might need to be modified. This is the largest phosphoproteomics experiment to date, but it appears as a technical note. With only one figure and one table, I wished the authors had made a full paper out of it."

—Steven Gygi,
Harvard Medical School, US

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