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Cited by 511

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 access
Brockhausen, Inka·2006·EMBO reports

Abstract

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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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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CoChat. (2026). Citation check: Mucin‐type O ‐glycans in human colon and breast cancer: glycodynamics and functions. https://app.cochat.ai/papers/10.1038/sj.embor.7400705
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Brockhausen, I. (2006). Mucin‐type O ‐glycans in human colon and breast cancer: glycodynamics and functions. EMBO reports. https://doi.org/10.1038/sj.embor.7400705

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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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