Recent advances in analytical techniques provide the opportunity to quantify even low‐
abundance glycopeptides derived from complex biological mixtures, allowing for the …

Proteomics is defined as the large-scale study of proteins in particular for their structures and
functions (Anderson and Anderson 1998), and investigations of proteins have become very …

Metabolomics, the study of all the small molecules in and outside a cell and fluxomics,
comprising all conversion rates in a cell, are increasingly used in fundamental and applied …

In the last decade, the advancement of liquid chromatography mass spectrometry (LC/MS)
techniques has enabled their broad application in protein characterization, both …

In LC–MS based proteomics, several accelerating trypsination methods have been
introduced in order to speed up the protein digestion, which is often considered a bottleneck …

N-glycosylation alteration has been reported in liver diseases. Characterizing N-
glycopeptides that correspond to N-glycan structure with specific site information enables …

Recently, we introduced a novel approach for protein quantification based on isobaric
peptide termini labeling (IPTL). In IPTL, both peptide termini are dervatized in two separate …

Stable isotopic labeling coupled with mass spectrometry analysis is a promising method of
detecting quantitative variations in glycans, which may result in aberrant glycosylation in …

Proteomics continues to forge significant strides in the discovery of essential biological
processes, uncovering valuable information on the identity, global protein abundance …

Two-dimensional gel electrophoresis coupled with liquid chromatography/mass
spectrometry (2DE-LC/MS) is a classic and conventional approach to separate and identify …