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

With the sequencing of the genome of over 150 organisms, the field of biology has been
revolutionised. Instead of studying one gene or protein at the time, it is now possible to study …

A comparative study on the three quantitative methods frequently used in proteomics, 2D
DIGE (difference gel electrophoresis), cICAT (cleavable isotope-coded affinity tags) and …

Metalloproteases (MPs) are a large and diverse class of enzymes implicated in numerous
physiological and pathological processes, including tissue remodeling, peptide hormone …

Stable isotope labelling in combination with mass spectrometry has emerged as a powerful
tool to identify and relatively quantify thousands of proteins within complex protein mixtures …

A general method for the quantification of proteins in human serum was developed using
mass spectrometry (MS) and stable isotope‐labeled synthetic peptides as internal …

Achieving information content of satisfactory breadth and depth remains a formidable
challenge for proteomics. This problem is particularly relevant to the study of primary human …

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 …

Cancer progresses through a series of histopathological stages. Progression is thought to
be driven by the accumulation of genetic alterations and consequently gene expression …

The recent sequencing of a number of genomes has raised the level of opportunities for
studies on proteins. This area of research has been described with the all-embracing term …