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- W2034138130 abstract "Protein phosphorylation has become a focus of many proteomic studies due to the central role that it plays in biology. We combine peptide-based gel-free isoelectric focusing and immobilized metal affinity chromatography to enhance the detection of phosphorylation events within complex protein samples using LC−MS. This method is then used to carry out a quantitative phosphoproteomic analysis of the tumor necrosis factor (TNF) pathway using HeLa cells metabolically labeled with 15N-containing amino acids, where 145 phosphorylation sites were found to be up-regulated upon the activation of the TNF pathway. Keywords: isoelectric focusing • IMAC • phosphoproteome • metabolic labeling • TNF • PKA • apoptosis" @default.
- W2034138130 created "2016-06-24" @default.
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- W2034138130 date "2005-12-08" @default.
- W2034138130 modified "2023-10-11" @default.
- W2034138130 title "Quantitative Phosphoproteomic Analysis of the Tumor Necrosis Factor Pathway" @default.
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- W2034138130 doi "https://doi.org/10.1021/pr050270m" @default.
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