Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitro by Phosphoproteomic and Bioinformatic tools.

ABSTRACT:

Background

The mitogen activated protein kinase (MAPK) pathways are known to be deregulated in many human malignancies. Phosphopeptide identification of protein-kinases and site determination are major challenges in biomedical mass spectrometry (MS). P38 and HuR protein kinases have been reported extensively in the general principles of signalling pathways modulated by phosphorylation, mainly by molecular biology and western blotting techniques. Thus, although it has been demonstrated they are phosphorylated in different stress/stimuli conditions, the phosphopeptides and specific amino acids in which the phosphate groups are located in those protein kinases have not been shown completely.

Methods

We have combined different resins: (a) IMAC (Immobilized Metal Affinity Capture

SUBMITTER: Lopez E 

PROVIDER: S-EPMC3164609 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature