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- W2095409870 abstract "Abstract Protein functions are often regulated by posttranslational modifications such as protein phosphorylation and fatty acylation. Once the identity of each protein is established, which is the first step in proteomics, the posttranslational modifications of proteins should be analyzed in a large proteomic scale to fully understand the cellular functions of proteins. Toward this goal, at least two steps in the analysis of the modified proteins should be improved. The first step is to isolate either modified proteins (or peptides) or proteins of interest such as the signaling proteins specifically. The second step is to analyze the modified proteins or peptides. In this paper, our effort in the analysis of brain-specific phosphoproteins will be described. Commercially available anti-phosphotyrosine antibody can be successfully used to isolate tyrosine-phosphorylated proteins. Proteins isolated in this way can be identified by the sequence tag method. Phosphopeptides are more specifically detected by precursor-scanning mode of triple–quadrupole mass spectrometer. The phosphorylated amino acid residues will be analyzed in a Q-TOF-type hybrid mass spectrometer. The application of these analytical methods to the analysis of phosphoproteins will be described." @default.
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- W2095409870 date "2002-12-01" @default.
- W2095409870 modified "2023-09-27" @default.
- W2095409870 title "Toward the global analysis of cellular signaling pathways" @default.
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- W2095409870 doi "https://doi.org/10.1016/s0531-5131(02)01139-1" @default.
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