Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of <Emphasis Type="Italic">in vivo</Emphasis> protein phosphorylation sites |
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Authors: | Florian?Wolschin Email author" target="_blank">Wolfram?WeckwerthEmail author |
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Institution: | (1) Max Planck Institute of Molecular Plant Physiology, 14424 Potsdam, Germany |
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Abstract: | Background Protein phosphorylation is accepted as a major regulatory pathway in plants. More than 1000 protein kinases are predicted
in the Arabidopsis proteome, however, only a few studies look systematically for in vivo protein phosphorylation sites. Owing to the low stoichiometry and low abundance of phosphorylated proteins, phosphorylation
site identification using mass spectrometry imposes difficulties. Moreover, the often observed poor quality of mass spectra
derived from phosphopeptides results frequently in uncertain database hits. Thus, several lines of evidence have to be combined
for a precise phosphorylation site identification strategy. |
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Keywords: | |
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