PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33177111-2	2021	ST3GAL1 is a sialyltransferase that adds sialic acid to core 1 glycans, thereby terminating glycan chain extension.	N-Acetylneuraminic Acid	41-52	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7	
2510824-1	1989	This paper presents kinetic properties of the transfer of several synthetic 9-substituted sialic acid analogues onto N- or O-linked glycoprotein glycans by four purified mammalian sialyltransferases: Gal beta 1,4GlcNac alpha 2,6sialyltransferase, Gal beta-1,4(3)GlcNAc alpha 2,3-sialyltransferase, Gal beta 1,3GalNAc alpha 2,3sialyltransferase, and GalNAc alpha 2,6sialyltransferase.	N-Acetylneuraminic Acid	90-101	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	298-343	
30375371-3	2018	ST3GAL1 is a sialyltransferase that catalyzes the transfer of sialic acid from cytidine monophosphate-sialic acid to galactose-containing substrates and is associated with cancer progression and chemoresistance.	N-Acetylneuraminic Acid	62-73	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7	
30375371-3	2018	ST3GAL1 is a sialyltransferase that catalyzes the transfer of sialic acid from cytidine monophosphate-sialic acid to galactose-containing substrates and is associated with cancer progression and chemoresistance.	N-Acetylneuraminic Acid	102-113	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7	
10561455-4	1999	in situ hybridization of primary breast tissue showed that a sialyltransferase (ST3Gal I), responsible for adding sialic acid to core 1 thereby terminating chain extension, is elevated in primary breast carcinomas when compared to normal or benign tissue.	N-Acetylneuraminic Acid	114-125	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	61-88	
28395125-0	2017	Probing the CMP-Sialic Acid Donor Specificity of Two Human beta-d-Galactoside Sialyltransferases (ST3Gal I and ST6Gal I) Selectively Acting on O- and N-Glycosylproteins.	N-Acetylneuraminic Acid	16-27	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	98-106	
28395125-4	2017	In this study, we devised several approaches to investigate the donor specificity of the human beta-d-galactoside sialyltransferases ST6Gal I and ST3Gal I by using two CMP-sialic acids: CMP-Neu5Ac, and CMP-Neu5N-(4pentynoyl)neuraminic acid (CMP-SiaNAl), an unnatural CMP-sialic acid donor with an extended and functionalized N-acyl moiety.	N-Acetylneuraminic Acid	172-183	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154	
12379642-4	2002	The kinetic analysis of ST3Gal I inhibition demonstrated that this hexapeptide could act as a competitive inhibitor (K(i) = 1.1 microm) on CMP-NeuAc binding to the enzyme.	N-Acetylneuraminic Acid	143-148	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	24-32	
11690653-1	2001	The CMP-Neu5Ac:Galbeta1-3GalNAc alpha2,3-sialyltransferase (ST3Gal I, EC 2.4.99.4) is a Golgi membrane-bound type II glycoprotein that catalyses the transfer of sialic acid residues to Galbeta1-3GalNAc disaccharide structures found on O-glycans and glycolipids.	N-Acetylneuraminic Acid	161-172	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	4-58	
11690653-1	2001	The CMP-Neu5Ac:Galbeta1-3GalNAc alpha2,3-sialyltransferase (ST3Gal I, EC 2.4.99.4) is a Golgi membrane-bound type II glycoprotein that catalyses the transfer of sialic acid residues to Galbeta1-3GalNAc disaccharide structures found on O-glycans and glycolipids.	N-Acetylneuraminic Acid	161-172	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	60-68	
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-Acetylneuraminic Acid	41-52	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-26	
17101770-2	2007	The ST3Gal-I sialyltransferase is a candidate mechanistic component and catalyzes sialic acid addition to core 1 O-glycans during protein O glycosylation.	N-Acetylneuraminic Acid	82-93	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	4-12	
11394903-4	2001	Kinetic analysis shows that it is a CMP-Neu5Ac competitive inhibitor with for ST3Gal I with an inhibition constant (K(i)) of 2.1 microM.	N-Acetylneuraminic Acid	40-46	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	78-86	
11118434-2	2001	We have analyzed whether competition by the glycosyltransferase, ST3Gal-I, which transfers sialic acid to galactose in the core 1 substrate, is key to this switch in MUC1 glycosylation that results in the expression of the cancer-associated SM3 epitope.	N-Acetylneuraminic Acid	91-102	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	65-73	
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-Acetylneuraminic Acid	148-159	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	218-225	
34813786-7	2022	These results could imply that an ancestral tunicate ST3Gal-I in C. savignyi would prefer O-glycan onto glycoproteins as its sialic acid acceptor than vertebrate enzymes.	N-Acetylneuraminic Acid	125-136	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	53-61	
34324649-4	2021	The O-glycan sialyltransferase St3gal1 add sialic acid specifically on the TF-antigen.	N-Acetylneuraminic Acid	43-54	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	31-38	
35507766-1	2022	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	74-85	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	32-39	
35507766-1	2022	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	74-85	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	259-266