This review provides insights on the impact of glycosylation in cancer biology and its
influence in the current approaches of targeted cancer therapies in the clinical setting. The …

Simple Summary All cells are covered in a thick layer of sugar molecules known as glycans.
Changes to this sugar coat are common in cancer, and in particular cancer cells often …

During oncogenesis, tumor cells present specific carbohydrate chains that are new targets
for cancer immunotherapy. Whereas these tumor-associated carbohydrates (TACA) can be …

Pancreatic ductal adenocarcinoma (PDAC) is an aggressive malignancy with a poor
prognosis. Gemcitabine, as a single agent or in combination therapy, remains the frontline …

While the importance of protein N‐glycosylation in cancer cell migration is well appreciated,
the precise mechanisms by which N‐acetylglucosaminyltransferase V (GnT‐V) regulates …

Abstract The α2, 3‐sialylation of N‐glycans is considered important but complicated
because the functions of the three β‐galactoside α2, 3‐sialyltransferases, ST3GAL3 …

N-glycosylations can regulate the adhesive function of integrins. Great variations in both the
number and distribution of N-glycosylation sites are found in the 18 α and 8 β integrin …

Sialylation is a terminal glycosylated modification of glycoproteins that regulates critical
biological events such as cell adhesion and immune response. Our previous study showed …

The ST6GAL1 sialyltransferase, which adds α2–6-linked sialic acids to N-glycosylated
proteins, is upregulated in many malignancies including ovarian cancer. Through its activity …

Abstract Upregulated β-galactoside α2, 6-sialyltransferase I (ST6Gal-I) expression
reportedly occurs in many cancers and is correlated with metastasis and poor prognosis …