Stable isotope labeling of phosphoproteins for large-scale phosphorylation rate determination.

ABSTRACT: Signals that control responses to stimuli and cellular function are transmitted through the dynamic phosphorylation of thousands of proteins by protein kinases. Many techniques have been developed to study phosphorylation dynamics, including several mass spectrometry (MS)-based methods. Over the past few decades, substantial developments have been made in MS techniques for the large-scale identification of proteins and their post-translational modifications. Nevertheless, all of the current MS-based techniques for quantifying protein phosphorylation dynamics rely on the measurement of changes in peptide abundance levels, and many methods suffer from low confidence in phosphopeptide identification due to poor fragmentation. Here we have optimized an approach for the stable isotope labeling

SUBMITTER: Molden RC 

PROVIDER: S-EPMC3977188 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature