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- W72119908 abstract "Protein phosphorylation, principally on Ser, Thr and Tyr residues, is one of the most common cellular regulatory mechanisms [1–3] . Phosphorylation can modulate enzyme activity, alter affinity to other proteins, and transmit signals through kinase cascades that often are branched and interactive. To understand the molecular basis of these regulatory mechanisms, it is necessary to determine the sites that are phosphorylated in vivo. Mass spectrometry is becoming the method of choice for the identification of protein phosphorylation sites. This mass spectrometric approach offers at least three major advantages over the conventional biochemical and genetic approaches. First, it is accurate. There is no ambiguity once the phosphorylation site is identified through mass spectrometric sequencing of the phosphopeptide. Second, it is fast. The cycle of identifying phosphorylation sites is a few days. Third, it does not require 32P labeling. Many improvements in this mass spectrometry-based methodology have been in the area of improving sensitivity, selectivity and sample handling [4–13] ." @default.
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- W72119908 date "2000-01-01" @default.
- W72119908 modified "2023-09-23" @default.
- W72119908 title "Identification of in-vivo Phosphorylation Sites with Mass Spectrometry" @default.
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- W72119908 doi "https://doi.org/10.1007/978-1-59259-719-2_17" @default.
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