Abstract Two‐dimensional gel electrophoresis (2‐DE) with immobilized pH gradients (IPGs)
combined with protein identification by mass spectrometry (MS) is currently the workhorse …

Presently, phosphorylation of proteins is the most studied and best understood PTM.
However, the analysis of phosphoproteins and phosphopeptides is still one of the most …

The characterization of phosphorylated proteins is a challenging analytical task since many
of the proteins targeted for phosphorylation are low in abundance and phosphorylation is …

Recent advances in phosphopeptide enrichment prior to mass spectrometric analysis show
genuine promise for characterization of phosphoproteomes. Tandem mass spectrometry of …

Phosphorylation on serine, threonine and tyrosine residues is an extremely important
modulator of protein function. Therefore, there is a great need for methods capable of …

Detailed characterization of phosphoproteins as well as other post‐translationally modified
proteins is required to fully understand protein function and regulatory events in cells and …

Phosphorylation, the reversible addition of a phosphate group to amino acid side chains of
proteins, is a fundamental regulator of protein activity, stability, and molecular interactions …

2D gel electrophoresis is the technology that everyone loves to hate—it requires manual
dexterity and precision to reproduce precisely and is thus not well-suited as a high …

Phosphopeptides are often detected with low efficiency by MALDI MS analysis of peptide
mixtures. In an effort to improve the phosphopeptide ion response in MALDI MS, we …

This report describes an integrated and modular microsystem providing rapid analyses of
trace-level tryptic digests for proteomics applications. This microsystem includes an …