Aberrant glycosylation is a key feature of malignant transformation. Hypersialylation, the
enhanced expression of sialic acid-terminated glycoconjugates on the cell surface, has …

Sialylation, or the covalent addition of sialic acid to the terminal end of glycoproteins, is a
biologically important modification that is involved in embryonic development …

The glycosyltransferase, ST6Gal-I, adds sialic acid in an α2–6 linkage to the N-glycans of
membrane and secreted glycoproteins. Up-regulation of ST6Gal-I occurs in many cancers …

Humans are genetically very similar to “great apes”,(chimpanzees, bonobos, gorillas and
orangutans), our closest evolutionary relatives. We have discovered multiple genetic and …

The complex multi-step process of glycosylation occurs in a single cell, yet current analytics
generally cannot measure the output (the glycome) of a single cell. Here, we addressed this …

Introduction 3. Survey of cancer-associated glycosylation changes 3.1. β1, 6 branching 3.2.
Sialyl Lewis antigens 3.3. α2, 6-sialylated lactosamine (Sia6LacNAc) 3.4. T, Tn and sialyl-Tn …

In the past decades, a large number of studies in mammalian cells have revealed that
processing of glycoproteins is compartmentalized into several subcellular organelles that …

Although it has been known for many years that β1 integrins undergo differential
glycosylation in accordance with changes in cell phenotype, the potential role of N …

Introduction 3. Human ST involved in the synthesis of sialylated TACA 3.1. The β-
galactoside α2, 3-sialyltransferases (ST3Gal) 3.2. The β-galactoside α2, 6-sialyltransferases …

All cells are decorated with complex carbohydrate structures called glycans that serve as
ligands for glycan-binding proteins (GBPs) to mediate a wide range of biological processes …