The DOI matches its Crossref record; 86 of the 86 references it cites were found in a registry or an index.
Functional roles of N‐glycans in cell signaling and cell adhesion in cancer
Open accessAbstract
Glycosylation is one of the most common post‐translational modification reactions and nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in oligosaccharide structures are associated with many physiological and pathological events, including cell growth, migration, differentiation, tumor invasion, host–pathogen interactions, cell trafficking, and transmembrane signaling. Emerging roles of glycan functions have been highly attractive to scientists in various fields of life science as they open a field, “Functional Glycomics”, that is a comprehensive study of the glycan structures in relation to functions. In particular, the N‐glycans of signaling molecules including receptors or adhesion molecules are considered to be involved in cellular functions. This review will focus on the roles of glycosyltransferases involved in the biosynthesis of N‐glycan branching and identification of cell surface receptors as their target proteins. We also suggest that the modulation of N‐glycans of those receptors alters their important functions such as cell signaling and cell adhesion which are implicated in cancer invasion and metastasis. (Cancer Sci 2008; 99: 1304–1310)
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Cited by
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Cell surface protein glycosylation in cancer
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Over forty years of bladder cancer glycobiology: Where do glycans stand facing precision oncology?
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Metadata
- Authors
- Zhao, Y., Takahashi, M., Gu, J., Miyoshi, E., Matsumoto, A., Kitazume, S., & Taniguchi, N.
- Venue
- Cancer Science
- Publisher
- Wiley
- Published
- 2008-05-19
- Volume
- 99
- Issue
- 7
- Pages
- 1304-1310
- ISSN
- 1347-9032 (ISSN-L)
- 1349-7006
- OpenAlex
- W1979917701
- Cited by
- 405
- References
- 86
- FWCI
- 9.80
- 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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