PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8909998-5	1996	The decrease in mucin sialylation was achieved through the in situ beta-galactosylation of GalNAc alpha-O-benzyl into Gal beta 1-3GalNAc alpha-O-benzyl, which acts as a competitive substrate of Gal beta 1-3GalNAc alpha 2,3-sialyltransferase, as shown by the intracellular accumulation of NeuAc alpha 2-3Gal beta 1-3GalNAc alpha-O-benzyl in treated cells.	N-acetylgalactosaminuronic acid	91-97	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	194-240	
9628888-1	1998	Exposure for 24 h of mucus-secreting HT-29 cells to the sugar analogue GalNAc-alpha-O-benzyl results in inhibition of Galbeta1-3GalNAc:alpha2,3-sialyltransferase, reduced mucin sialylation, and inhibition of their secretion (Huet, G., I. Kim, C. de Bolos, J.M.	N-acetylgalactosaminuronic acid	71-77	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	118-161	
7655169-10	1995	The catalytic domain of the cloned sequence was expressed in transfected cells and was shown to be competent in mediating the specific synthesis of sialic acid alpha 2,3 to Gal(beta 1,3)GalNAc-R. Genomic sequences for SiaT-4a were also isolated and examined.	N-acetylgalactosaminuronic acid	186-192	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	218-225	
26552809-2	2015	Sialyltransferase ST3GAL-1, which adds a sialic acid in an alpha-2,3 linkage to Gal beta1,3 GalNAc, preforms an important role in modulating cellular behaviors.	N-acetylgalactosaminuronic acid	92-98	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-26