This review focuses on techniques for quantification and identification in proteomics by
stable isotope coding. Methods are examined for analyzing expression, post-translational …

Proteomics has been defined as “the systematic analysis of the protein population in a
tissue, cell, or subcellular compartment.” Over the last 2 to 3 years, proteomics has …

Chemical derivatisation of functional groups has proved popular since the beginning of
organic mass spectrometry as a means to enhance the stability and volatility of the analytes …

We have previously shown that diabetogenic antibiotic streptozotocin (STZ), an analog of N-
acetylglucosamine (GlcNAc), inhibits the enzyme O-GlcNAc-selective N-acetyl-β-d …

Although mass spectrometry has become a powerful tool for the functional analysis of
biological systems, complete proteome characterization cannot yet be achieved. Instead, the …

Proteomic studies require efficient, robust, and practical methods of characterizing proteins
present in biological samples. Here we describe an integrated strategy for systematic …

Alcanivorax borkumensis is a ubiquitous marine petroleum oil-degrading bacterium with an
unusual physiology specialized for alkane metabolism. This “hydrocarbonoclastic” …

During the last decade, protein analysis and proteomics have been established as new tools
for understanding various biological problems. As the identification of proteins after classical …

Stable isotope-labeled proteotypic peptides are used as surrogate standards for absolute
quantification of proteins in proteomics. However, a stable isotope-labeled peptide has to be …

A procedure for reduction and alkylation of cysteine residues in proteins was developed
using the volatile reagents triethylphosphine and iodoethanol. These reagents may be used …