PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27704662-2	2016	For example, alpha2,6-sialylation on terminal galactose, catalyzed by the sialyltransferase ST6GAL1, inhibits the binding of galectin-1, a beta-galactoside-binding lectin.	Galactose	46-55	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	92-99	
30959459-3	2019	This redox state change was accompanied by loss of two surface-exposed disulfide bonds in the catalytic domain of the alpha-2,6-sialyltransferase (ST6Gal-I) and its ability to functionally interact with B4GalT-I, an enzyme adding the preceding galactose to complex N-glycans.	Galactose	244-253	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	147-155	
21173156-4	2011	ST6Gal-I adds an alpha2,6-linked sialic acid to the terminal galactose of N-linked glycans, and this modification blocks galectin binding to beta-galactosides.	Galactose	61-70	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	0-8	
23999306-1	2013	Human beta-galactoside alpha-2,6-sialyltransferase I (ST6Gal-I) establishes the final glycosylation pattern of many glycoproteins by transferring a sialyl moiety to a terminal galactose.	Galactose	176-185	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	54-62	
23999306-2	2013	Complete sialylation of therapeutic immunoglobulins is essential for their anti-inflammatory activity and protein stability, but is difficult to achieve in vitro owing to the limited activity of ST6Gal-I towards some galactose acceptors.	Galactose	217-226	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	195-203	
21692563-4	2011	In this study, we stably transfected Vero cells with cDNA of human alpha-2,6-sialyltransferase (SIAT1), an enzyme catalyzing alpha-2,6-sialylation of galactose on glycoproteins.	Galactose	150-159	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	96-101	
25465919-2	2014	Accumulating evidence shows that ST6GAL1, an enzyme that catalyzes the transfer of sialic acid onto galactose-containing substrates, is aberrantly expressed in various cancers and may affect cell motility and invasion.	Galactose	100-109	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	33-40	
12097641-3	2002	Although both ST3Gal-IV and ST6Gal-I sialyltransferases mask galactose linkages implicated as asialoglycoprotein receptor ligands, only ST3Gal-IV deficiency promotes asialoglycoprotein clearance mechanisms with a reduction in plasma levels of VWF and platelets.	Galactose	61-70	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	28-36	
16897185-5	2006	In support of this observation, the cDNA microarray assay and reverse transcription-polymerase chain reaction (RT-PCR) analysis showed that the gene expression of the alpha-2,6-sialyltransferase I (ST6Gal I), which transfers sialic acid to galactose residues of N-glycans, decreases in the aged cells.	Galactose	240-249	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	198-206	
35371997-3	2022	The sialyltransferase ST6Gal1, with high expression in specific hematopoietic cell types, is the only enzyme thought to catalyze the terminal addition of sialic acids in an alpha2-6-linkage to galactose on N-glycans in such cells.	Galactose	193-202	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	22-29	
9838208-2	1998	Terminal sialylation of native human proteins is characteristically in both alpha-2,3 and alpha-2,6 linkage to galactose at the termini of N-linked oligosaccharides but only in alpha-2,3 linkage in recombinant proteins expressed in hamster cells which do not express alpha-2, 6-sialyltransferase (ST6GalI) (EC 2.4.99.1).	Galactose	111-120	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	297-304	
11425186-4	2000	The addition of sialic acid in alpha2,6-linkage to the galactose residue of lactosamine (type 2 chains) is catalyzed by beta-galactoside alpha2,6-sialyltransferase (ST6Gal.I).	Galactose	55-64	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	165-173