Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks.

ABSTRACT: Although recent developments in MS have enabled the identification and quantification of hundreds of phosphorylation sites from a given biological sample, phosphoproteome analysis by MS has been plagued by inconsistent reproducibility arising from automated selection of precursor ions for fragmentation, identification, and quantification. To address this challenge, we have developed a new MS-based strategy, based on multiple reaction monitoring of stable isotope-labeled peptides, that enables highly reproducible quantification of hundreds of nodes (phosphorylation sites) within a signaling network and across multiple conditions simultaneously. We have applied this strategy to quantify temporal phosphorylation profiles of 222 tyrosine phosphorylated peptides across seven time points followi

SUBMITTER: Wolf-Yadlin A 

PROVIDER: S-EPMC1851582 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature