The quantification of differences between two or more physiological states of a biological
system is among the most important but also most challenging technical tasks in proteomics …

The evolution of mass spectrometry–based proteomic technologies has advanced our
understanding of the complex and dynamic nature of proteomes while concurrently …

A better understanding of proteostasis in health and disease requires robust methods to
determine protein half-lives. Here we improve the precision and accuracy of peptide ion …

Quantitative mass spectrometry methods offer near-comprehensive proteome coverage;
however, these methods still suffer with regards to sample throughput. Multiplex quantitation …

Accurate quantification of protein expression in biological systems is an increasingly
important part of proteomics research. Incorporation of differential stable isotopes in samples …

Proteolysis is a major protein posttranslational modification that, by altering protein structure,
affects protein function and, by truncating the protein sequence, alters peptide signatures of …

Herein, we describe the development and application of a set of novel N, N-dimethyl leucine
(DiLeu) 4-plex isobaric tandem mass (MS2) tagging reagents with high quantitation efficacy …

Stable isotope labeling is at present one of the most powerful methods in quantitative
proteomics. Stable isotope labeling has been performed at both the protein as well as the …

Edited by renowned protein scientist and bestselling author Roger L. Lundblad, with the
assistance of Fiona M. Macdonald of CRC Press, this fifth edition of the Handbook of …

Shotgun proteomics dominates the field of proteomics. The foundations of the strategy
consist of multiple rounds of peptide separation where chromatography provides the …