Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Screening of hepatocyte proteins binding to F protein of hepatitis C virus by yeast two-hybrid system.
Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells.
Universal phosphatase-coupled glycosyltransferase assay.
The structure of human α-2,6-sialyltransferase reveals the binding mode of complex glycans.
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Crystal structures of human ST6Gal-I define the GT-A variant fold, CMP product/inhibitor binding, complex-glycan binding mode, and an SN2 inversion, substrate-assisted catalytic mechanism.
Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity.
Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans.
Network inference from glycoproteomics data reveals new reactions in the IgG glycosylation pathway.
The incorrect use of CD75 as a synonym for ST6GAL1 has fostered the expansion of commercial 'ST6GAL1' antibodies that do not recognize ST6GAL1.
A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans.
Divergent Enzymatic Assembly of a Comprehensive 64-Membered IgG N-Glycan Library for Functional Glycomics.
ST6GAL1,2 transfer Neu5Ac to terminal Gal (alpha-2,6 link)
O-glycosylation of 3a is terminated
Maturation of spike protein
Addition of sialic acids on some Spike glycosyl sidechains
ST6GAL1 transfers Neu5Ac to terminal Gal of N-glycans
Termination of O-glycan biosynthesis
ST6GAL1 transfers sialic acid to Tn antigens to form sTn antigens