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- W2478662014 endingPage "1286" @default.
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- W2478662014 abstract "Cell surface of eukaryotic cells is covered with a wide variety of sialylated molecules involved in diverse biological processes and taking part in cell–cell interactions. Although the physiological relevance of these sialylated glycoconjugates in vertebrates begins to be deciphered, the origin and evolution of the genetic machinery implicated in their biosynthetic pathway are poorly understood. Among the variety of actors involved in the sialylation machinery, sialyltransferases are key enzymes for the biosynthesis of sialylated molecules. This review focus on β-galactoside α2,3/6-sialyltransferases belonging to the ST3Gal and ST6Gal families. We propose here an outline of the evolutionary history of these two major ST families. Comparative genomics, molecular phylogeny and structural bioinformatics provided insights into the functional innovations in sialic acid metabolism and enabled to explore how ST-gene function evolved in vertebrates." @default.
- W2478662014 created "2016-08-23" @default.
- W2478662014 creator A5016090058 @default.
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- W2478662014 creator A5052282436 @default.
- W2478662014 creator A5063996071 @default.
- W2478662014 creator A5091449922 @default.
- W2478662014 date "2016-08-09" @default.
- W2478662014 modified "2023-09-27" @default.
- W2478662014 title "Phylogenetic-Derived Insights into the Evolution of Sialylation in Eukaryotes: Comprehensive Analysis of Vertebrate β-Galactoside α2,3/6-Sialyltransferases (ST3Gal and ST6Gal)" @default.
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- W2478662014 doi "https://doi.org/10.3390/ijms17081286" @default.
- W2478662014 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5000683" @default.
- W2478662014 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27517905" @default.
- W2478662014 hasPublicationYear "2016" @default.
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