ST8SIA6: Difference between revisions
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==Function== | ==Function== | ||
Sialic acid is a key determinate of oligosaccharide structures involved in cell-cell communication, cell-substrate interaction, adhesion, and protein targeting. ST8SIA6 belongs to a family of sialyltransferases (EC 2.4.99.8) that synthesize sialylglycoconjugates (Takashima et al., 2002 [PubMed 11980897]). | [[Sialic acid]] is a key determinate of [[oligosaccharide]] structures involved in cell-cell communication, cell-substrate interaction, [[Cell adhesion|adhesion]], and [[protein targeting]]. ST8SIA6 belongs to a family of [[Sialyltransferase|sialyltransferases]] (EC 2.4.99.8) that synthesize sialylglycoconjugates (Takashima et al., 2002 [PubMed 11980897]). | ||
== References == | == References == | ||
Latest revision as of 17:11, 16 June 2018
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
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ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 6 is a protein that in humans is encoded by the ST8SIA6 gene. [1]
Function
Sialic acid is a key determinate of oligosaccharide structures involved in cell-cell communication, cell-substrate interaction, adhesion, and protein targeting. ST8SIA6 belongs to a family of sialyltransferases (EC 2.4.99.8) that synthesize sialylglycoconjugates (Takashima et al., 2002 [PubMed 11980897]).
References
- ↑ "Entrez Gene: ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 6". Retrieved 2017-02-02.
Further reading
- Avril T, North SJ, Haslam SM, Willison HJ, Crocker PR (2006). "Probing the cis interactions of the inhibitory receptor Siglec-7 with alpha2,8-disialylated ligands on natural killer cells and other leukocytes using glycan-specific antibodies and by analysis of alpha2,8-sialyltransferase gene expression". J. Leukoc. Biol. 80 (4): 787–96. doi:10.1189/jlb.1005559. PMID 16857734.
- Szabo R, Skropeta D, et al. (2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Med. Res. Rev. 37: 210–270. doi:10.1002/med.21407.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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