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 …

The ST6GAL1 sialyltransferase, which adds α2–6 linked sialic acids to N-glycosylated
proteins, is overexpressed in a wide range of human malignancies. Recent studies have …

Abstract Background The ST6Gal-I sialyltransferase is upregulated in numerous cancers,
and high expression of this enzyme correlates with poor patient prognosis in various …

Activation of the tumor necrosis factor receptor 1 (TNFR1) death receptor by TNF induces
either cell survival or cell death. However, the mechanisms mediating these distinct …

The Golgi-sialyltransferase ST6Gal1 (βgalactosidase α2, 6 sialyltransferase 1), adds the
negatively charged sugar, sialic acid, to the terminal galactose of N-glycosylated proteins …

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

Hepatocellular carcinoma (HCC) is the third leading cause of cancer death worldwide.
Understanding the cancer mechanisms provides novel diagnostic, prognostic, and …

Aberrant cell surface glycosylation is prevalent in tumor cells, and there is ample evidence
that glycans have functional roles in carcinogenesis. Nonetheless, many molecular details …

ST6Gal-I, an enzyme upregulated in numerous malignancies, adds α2-6-linked sialic acids
to select membrane receptors, thereby modulating receptor signaling and cell phenotype. In …

ST6Gal-I sialyltransferase adds α2, 6-linked sialic acids to the terminal ends of glycan
chains of glycoproteins and glycolipids. ST6Gal-I is reportedly upregulated in many cancers …