Virtually all cell surface proteins and many cell membrane lipids are glycosylated, creating a
cell surface glycocalyx. The glycan chains attached to cell surface glycoproteins and …

Sialylation of glycoproteins and glycolipids is catalyzed by sialyltransferases in the Golgi of
mammalian cells, whereby sialic acid residues are added at the nonreducing ends of …

Glycosylation, a common modification of cellular proteins and lipids, is often altered in
diseases and pathophysiological states such as hypoxia, yet the underlying molecular …

The sialyltransferase family represents a group of enzymes that transfers sialic acid from its
common nucleotide sugar donor, CMP-NeuAc, to the terminal carbohydrates group of …

Eukaryotic sialyltransferases (SiaTs) comprise a superfamily of enzymes catalyzing the
transfer of sialic acid (Sia) from a common donor substrate to various acceptor substrates in …

Purpose Glycosylation has been demonstrated to be involved in tumorigenesis, progression,
and immunoregulation, and to present specific profiles in different tumors. In this study, we …

Breast cancer is the second leading cause of cancer-related death among women and a
major source of brain metastases. Despite the increasing incidence of brain metastasis from …

Although disialyl glycosphingolipids such as GD3 and GD2 have been considered to be
associated with malignant tumours, whether branched-type disialyl glycosphingolipids show …

Gangliogliomas, the most frequent neoplasms in patients with pharmacoresistant focal
epilepsies, are characterized by histological combinations of glial and dysplastic neuronal …

Fifty-one human glycosyltransferases were expressed in Saccharomyces cerevisiae as
immobilized enzymes and were assayed for enzymatic activities. The stem and catalytic …