Aberrant sialylation functions as an important modulator of all steps of malignant
transformation. Therefore, targeting sialylation regulators, such as sialyltransferases and …

Sialylation (the covalent addition of sialic acid to the terminal end of glycoproteins or
glycans), tightly regulated cell-and microenvironment-specific process and orchestrated by …

Altered glycosylation is a common feature of cancer cells and plays an important role in
tumor progression. β-Galactoside α2-6-sialyltransferase 1 (ST6Gal-I) is the critical …

Altered surface glycosylation is a key feature of cancers, including gynecologic
malignancies. Hypersialylation, the overexpression of sialic acid, is known to promote tumor …

Abstract The glycosyltransferase ST6Gal-I, which adds α2-6–linked sialic acids to substrate
glycoproteins, has been implicated in carcinogenesis; however, the nature of its pathogenic …

Sialyltransferases transfer sialic acid to nascent oligosaccharides and are upregulated in
cancer. The inhibition of sialyltransferases is emerging as a potential strategy to prevent …

Abstract Background The ST6Gal-I glycosyltransferase, which adds α2–6-linked sialic acids
to N-glycosylated proteins is upregulated in a wide range of malignancies including ovarian …

Aberrant sialylation of glycoproteins has been detected in many tumors, and upregulation of
the beta-galactosamide alpha-2, 6-sialyltransferase 1 (ST6GAL1) has been implicated with …

Abnormal sialylation due to overexpression of sialyltransferases has been associated with
tumorigenesis and tumor progression. Although ST6Gal-I influences cancer persistence and …

Simple Summary Tumor cells accumulate sialylation in tissues via the coordination of
sialyltransferases and sialidases. Tumor sialylation can block receptor and ligand binding at …