Glycosylation is the most abundant and diverse form of post-translational modification of
proteins that is common to all eukaryotic cells. Enzymatic glycosylation of proteins involves a …

Despite recent progress in understanding the cancer genome, there is still a relative delay in
understanding the full aspects of the glycome and glycoproteome of cancer. Glycobiology …

Glycosylation is catalyzed by various glycosyltransferase enzymes which are mostly located
in the Golgi apparatus in cells. These enzymes glycosylate various complex carbohydrates …

Tumour metastasis is the main cause of cancer related deaths. Metastasis is an intricate
multi-step process that requires the acquisition of several cancer cell features, including the …

Glycosylation is one of the most common post‐translational modification reactions and
nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in …

α1, 6-Fucosyltransferase (Fut8) catalyzes the transfer of a fucose residue to N-linked
oligosaccharides on glycoproteins via an α1, 6-linkage to form core fucosylation in …

Among the various posttranslational modification reactions, glycosylation is the most
common, and nearly 50% of all known proteins are thought to be glycosylated. In particular …

Cancer cells depend on altered metabolism and nutrient uptake to generate and keep the
malignant phenotype. The hexosamine biosynthetic pathway is a branch of glucose …

N-glycan, a fundamental and versatile protein modification in mammals, plays critical roles
in various physiological and pathological events including cancer progression. The …

BACKGROUND: Cell migration is an essential process in organ homeostasis, in
inflammation, and also in metastasis, the main cause of death from cancer. The extracellular …