pr050270m_si_006.xls (395 kB)
Quantitative Phosphoproteomic Analysis of the Tumor Necrosis Factor Pathway
dataset
posted on 2006-01-06, 00:00 authored by Greg T. Cantin, John D. Venable, Daniel Cociorva, John R. YatesProtein 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
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isoelectric145 phosphorylation sitesHeLa cells metabolicallyTNF pathwayLCTumor Necrosis Factor Pathway Protein phosphorylationPKAproteomic studiesmetal affinity chromatographyphosphorylation eventstumor necrosis factorphosphoproteomic analysisQuantitative Phosphoproteomic AnalysisIMACprotein samples
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