The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Mucin‐type O ‐glycans in human colon and breast cancer: glycodynamics and functions
Open accessAbstract
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 the T and Tn antigens, and certain Lewis antigens. These structural changes can alter the function of the cell, and its antigenic and adhesive properties, as well as its potential to invade and metastasize. Cancer‐associated mucin antigens can be exploited in diagnosis and prognosis, and in the development of cancer vaccines. The activities and Golgi localization of glycosyltransferases are the basis for the glycodynamics of cancer cells, and determine the ranges and amounts of specific O ‐glycans produced. This review focuses on the glycosyltransferases of colon and breast cancer cells that determine the pathways of mucin‐type O ‐glycosylation, and the proposed functional and pathological consequences of altered O ‐glycans.
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Cites
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Self-citationSiglecs—the major subfamily of I-type lectins
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All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases
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Cited by
Glycosylation in cancer: mechanisms and clinical implications
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Mucin-bacterial interactions in the human oral cavity and digestive tract
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Loss of intestinal core 1–derived O-glycans causes spontaneous colitis in mice
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Metadata
- Authors
- Brockhausen, I.
- Venue
- EMBO reports
- Published
- 2006-06
- Volume
- 7
- Issue
- 6
- Pages
- 599-604
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- OpenAlex
- W2057049168
- Cited by
- 511
- References
- 52
- FWCI
- 6.14
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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