Journal
JOURNAL OF PROTEOME RESEARCH
Volume 5, Issue 1, Pages 127-134Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr050270m
Keywords
isoelectric focusing; IMAC; phosphoproteome; metabolic labeling; TNF; PKA; apoptosis
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Funding
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR011823] Funding Source: NIH RePORTER
- NATIONAL EYE INSTITUTE [R01EY013288] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF MENTAL HEALTH [R01MH067880] Funding Source: NIH RePORTER
- NCRR NIH HHS [RR11823-09, P41 RR011823, P41 RR011823-09] Funding Source: Medline
- NEI NIH HHS [EY13288, R01 EY013288-04, R01 EY013288] Funding Source: Medline
- NIMH NIH HHS [R01 MH067880, MH067880, R01 MH067880-03] Funding Source: Medline
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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 N-15-containing amino acids, where 145 phosphorylation sites were found to be up-regulated upon the activation of the TNF pathway.
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