Title : Overlapping and unique substrate specificities of ST3GAL1 and 2 during hematopoietic and megakaryocytic differentiation.

Pub. Date : 2022 May 4

PMID : 35507766






2 Functional Relationships(s)
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1 Although the sialyltransferases ST3GAL1 and ST3GAL2 are known to transfer sialic acid to the galactose residue of type III disaccharides (Galbeta1,3GalNAc) in vitro, sialylation of O-linked glycosylated proteins in living cells has been largely attributed to ST3GAL1. N-Acetylneuraminic Acid ST3 beta-galactoside alpha-2,3-sialyltransferase 1 Homo sapiens
2 Although the sialyltransferases ST3GAL1 and ST3GAL2 are known to transfer sialic acid to the galactose residue of type III disaccharides (Galbeta1,3GalNAc) in vitro, sialylation of O-linked glycosylated proteins in living cells has been largely attributed to ST3GAL1. N-Acetylneuraminic Acid ST3 beta-galactoside alpha-2,3-sialyltransferase 1 Homo sapiens