Glycosylation of proteins is one of the most prevalent post-translational modifications
occurring in nature, with a wide repertoire of biological implications. Pathways for the main …

Humans have been increasingly recognized as being superorganisms, living in close
contact with a microbiota on all their mucosal surfaces. However, most studies on the human …

Over the last decade, studies on the virulence of the highly pathogenic intracellular bacterial
pathogen Francisella tularensis have increased dramatically. The organism produces an …

Glycosylation is one of the most abundant post-translational modifications (PTMs) required
for various structure/function modulations of proteins in a living cell. Although elucidated …

Bacterial protein glycosylation is an important post-translational modification that can
distinguish pathogenic bacteria from human cells. This review discusses recent findings in …

This review summarizes the analytical advances made during the last several years in the
structural and quantitative determinations of glycoproteins in complex biological mixtures …

Many endogenous proteins/peptides and proteins/peptides with post-translational
modifications (PTMs) are presented at extremely low abundance, and they usually suffer …

Background Francisella tularensis is a category-A select agent and is responsible for
tularemia in humans and animals. The surface components of F. tularensis that contribute to …

Staphylococcus aureus and Pseudomonas aeruginosa are primary pathogens in chronic
rhinosinusitis (CRS), and the presence of S. aureus and P. aeruginosa biofilms has been …

In this study, we sought to understand the selective pressures shaping the Ig-producing cell
repertoire in the parotid glands of primary Sjögren's syndrome (pSS) patients before and …