Decreased antimicrobial efficiency has become a global public health issue. The paucity of
new antibacterial drugs is evident, and the arsenal against infectious diseases needs to be …

Sialidases, or neuraminidases, are enzymes that catalyze the hydrolysis of sialic acid (Sia)-
containing molecules, mostly removal of the terminal Sia (desialylation). By desialylation …

Sialic acids constitute a family of negatively charged structurally diverse monosaccharides
that are commonly presented on the termini of glycans in higher animals and some …

Sialidases (SAs) and sialyltransferases (STs), the enzymes responsible for removing and
adding sialic acid to other glycans, play essential roles in viruses, bacteria, parasites, and …

Inhibitors of human neuraminidase enzymes (NEU) are recognized as important tools for the
study of the biological functions of NEU and will be potent tools for elucidating the role of …

Human neuraminidases (NEU) are associated with human diseases including cancer,
atherosclerosis, and diabetes. To obtain small molecule inhibitors as research tools for the …

Sialic acids are commonly found on the terminal ends of biologically important
carbohydrates, including intestinal mucin O-linked glycans. Pathogens such as Clostridium …

This Perspective describes the classification, structures, substrates, mechanisms of action,
and implications of human neuraminidases (hNEUs) in various pathologies. Some inhibitors …

Neu1 is a sialidase enzyme that plays a crucial role in the regulation of glycosylation in a
variety of cellular processes, including cellular signaling and inflammation. In recent years …

In the past two decades, human neuraminidases (human sialidases, hNEUs) have been
found to be involved in numerous pathways in biology. The development of selective and …