Mucin-type O-glycans are a class of glycans initiated with N-acetylgalactosamine (GalNAc) α-
linked primarily to Ser/Thr residues within glycoproteins and often extended or branched by …

Protein glycosylation represents a nearly ubiquitous post-translational modification, and
altered glycosylation can result in clinically significant pathological consequences. Here we …

The glycoproteins of tumour cells are often abnormal, both in structure and in quantity. In
particular, the mucin‐type O‐glycans have several cancer‐associated structures, including …

Aberrant expression of immature truncated O-glycans is a characteristic feature observed on
virtually all epithelial cancer cells, and a very high frequency is observed in early epithelial …

Background While the underlying causes of cancer are genetic modifications, changes in
cellular states mediate cancer development. Tumor cells display markedly changed …

Glycosylation is a common post-translational modification process of proteins. Mucin-type O-
glycosylation is an O-glycosylation that starts from protein serine/threonine residues …

While only about ten percent of the databank entries are defined as glycoproteins, it has
been estimated recently that more than half of all proteins are glycoproteins. Mucintype …

Mucins are large glycoproteins expressed on the epithelia that provide a protective barrier
against harsh insults from toxins and pathogenic microbes. These glycoproteins are …

Glycans on proteins and lipids are known to alter with malignant transformation. The study of
these may contribute to the discovery of biomarkers and treatment targets as well as …

Changes in mucin-type O-linked glycosylation are seen in over 90% of breast cancers
where increased sialylation is often observed and a change from branched glycans to linear …