PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
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
32776095-5	2021	MMP10, the principal gene upregulated when cells carrying sialylated core 1 glycans were stimulated with EGF, is also upregulated in ER positive breast carcinoma reported to express high levels of ST3Gal1 and hence mainly core 1 sialylated O-glycans.	o-glycans	240-249	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	197-204
30375371-0	2018	Sialyltransferase ST3GAL1 promotes cell migration, invasion, and TGF-beta1-induced EMT and confers paclitaxel resistance in ovarian cancer.	Paclitaxel	99-109	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-25
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
33177111-2	2021	ST3GAL1 is a sialyltransferase that adds sialic acid to core 1 glycans, thereby terminating glycan chain extension.	Polysaccharides	63-70	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7
33177111-2	2021	ST3GAL1 is a sialyltransferase that adds sialic acid to core 1 glycans, thereby terminating glycan chain extension.	Polysaccharides	63-69	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7
31784620-0	2019	Structural and functional role of disulphide bonds and substrate binding residues of the human beta-galactoside alpha-2,3-sialyltransferase 1 (hST3Gal1).	disulphide	34-44	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	95-141
31784620-0	2019	Structural and functional role of disulphide bonds and substrate binding residues of the human beta-galactoside alpha-2,3-sialyltransferase 1 (hST3Gal1).	disulphide	34-44	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	143-151
31784620-6	2019	To gain further understanding of the correlation among structure, activity and stability, the in vitro role of hST3Gal1 disulphide bonds was analysed.	disulphide	120-130	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	111-119
32583304-5	2020	The expression of Neu5Acalpha2-3Galbeta1-3GalNAc- (sialyl-3T antigen) which is the product of alpha2,3-sialyltransferase-I (ST3Gal-I) was substantially increased.	neu5acalpha2-3galbeta1-3galnac	18-48	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	124-132
30959459-6	2019	Structure comparisons revealed similar disulfide bonds also in ST3Gal-I, suggesting that this O-glycan and glycolipid modifying sialyltransferase is also sensitive to hypoxia and thereby contribute to attenuated sialylation of O-linked glycans in hypoxic cells.	Disulfides	39-48	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	63-71
30959459-6	2019	Structure comparisons revealed similar disulfide bonds also in ST3Gal-I, suggesting that this O-glycan and glycolipid modifying sialyltransferase is also sensitive to hypoxia and thereby contribute to attenuated sialylation of O-linked glycans in hypoxic cells.	o-glycan	94-102	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	63-71
30959459-6	2019	Structure comparisons revealed similar disulfide bonds also in ST3Gal-I, suggesting that this O-glycan and glycolipid modifying sialyltransferase is also sensitive to hypoxia and thereby contribute to attenuated sialylation of O-linked glycans in hypoxic cells.	o-linked glycans	227-243	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	63-71
30252131-1	2019	ST3Gal1 is a key sialyltransferase which adds alpha2,3-linked sialic acid to substrates and generates core 1 O-glycan structure.	alpha2,3-linked sialic acid	46-73	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7
30252131-1	2019	ST3Gal1 is a key sialyltransferase which adds alpha2,3-linked sialic acid to substrates and generates core 1 O-glycan structure.	o-glycan	109-117	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7
30619255-8	2018	Consistent with similar reports in T cells, ST3Gal1 overexpression in B cells in vitro induced drastic shortening in O-glycans, which we confirmed by both antibody staining and mass spectrometric O-glycomic analysis.	o-glycans	117-126	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	44-51
30619255-9	2018	Unexpectedly, ST3Gal1-induced changes in O-glycan length also correlated with altered binding of two glycosylation-sensitive CD45 antibodies, RA3-6B2 (more commonly called B220) and MEM55, which (in humans) have previously been reported to favor binding to naive/GC subsets and memory/plasmablast subsets, respectively.	o-glycan	41-49	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	14-21
30619255-12	2018	Thus, our data suggest that O-glycan remodeling is a feature of B cell differentiation, dually regulated by ST3Gal1 and GCNT1, that ultimately results in expression of distinct O-glycosylation states/CD45 glycoforms at each stage of B cell differentiation.	o-glycan	28-36	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	108-115
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.	Cytidine Monophosphate	79-101	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
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.	Galactose	117-126	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7
30375371-8	2018	Furthermore, overexpression of ST3GAL1 increases resistance to paclitaxel while downregulation of ST3GAL1 decreases resistance to paclitaxel in vitro, and overexpression of ST3GAL1 increases tumorigenicity and resistance to paclitaxel in vivo.	Paclitaxel	63-73	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	31-38
30375371-8	2018	Furthermore, overexpression of ST3GAL1 increases resistance to paclitaxel while downregulation of ST3GAL1 decreases resistance to paclitaxel in vitro, and overexpression of ST3GAL1 increases tumorigenicity and resistance to paclitaxel in vivo.	Paclitaxel	130-140	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	98-105
30375371-8	2018	Furthermore, overexpression of ST3GAL1 increases resistance to paclitaxel while downregulation of ST3GAL1 decreases resistance to paclitaxel in vitro, and overexpression of ST3GAL1 increases tumorigenicity and resistance to paclitaxel in vivo.	Paclitaxel	130-140	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	98-105
30375371-8	2018	Furthermore, overexpression of ST3GAL1 increases resistance to paclitaxel while downregulation of ST3GAL1 decreases resistance to paclitaxel in vitro, and overexpression of ST3GAL1 increases tumorigenicity and resistance to paclitaxel in vivo.	Paclitaxel	130-140	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	98-105
30375371-8	2018	Furthermore, overexpression of ST3GAL1 increases resistance to paclitaxel while downregulation of ST3GAL1 decreases resistance to paclitaxel in vitro, and overexpression of ST3GAL1 increases tumorigenicity and resistance to paclitaxel in vivo.	Paclitaxel	130-140	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	98-105
30375371-12	2018	ST3GAL1 may be a promising target for overcoming paclitaxel resistance in ovarian carcinoma.	Paclitaxel	49-59	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	0-7
26733198-3	2016	Here we compare the labeling of sialoglycoproteins in undifferentiated and differentiated human erythroleukemia cells (HEL) using SEEL using the sialyltransferases ST6Gal1 and ST3Gal1, which label N- and O-glycans, respectively.	n- and o-glycans	197-213	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	176-183
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.	Cytidine Monophosphate	168-171	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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.	Sialic Acids	172-184	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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.	Cytidine Monophosphate	168-172	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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.	neu5n	206-211	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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.	(4pentynoyl)neuraminic acid	212-239	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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.	cmp-sianal	241-251	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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.	Cytidine Monophosphate	186-189	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	146-154
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
27166796-5	2016	We report the successful expression of active human sialyltransferases ST3Gal1 and ST6Gal1 in commercial Escherichia coli strains designed for production of disulfide-containing proteins.	Disulfides	157-166	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	71-78
29569918-2	2018	Here, we report on the development of chemoenzymatic histology of membrane polysaccharide (CHoMP)-based methods for the detection of O- and N-linked glycans on tissue sections via the use of sialyltransferases ST3Gal1 and ST6Gal1, respectively.	Polysaccharides	75-89	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	210-217
29569918-2	2018	Here, we report on the development of chemoenzymatic histology of membrane polysaccharide (CHoMP)-based methods for the detection of O- and N-linked glycans on tissue sections via the use of sialyltransferases ST3Gal1 and ST6Gal1, respectively.	chomp	91-96	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	210-217
29569918-2	2018	Here, we report on the development of chemoenzymatic histology of membrane polysaccharide (CHoMP)-based methods for the detection of O- and N-linked glycans on tissue sections via the use of sialyltransferases ST3Gal1 and ST6Gal1, respectively.	o- and n-linked glycans	133-156	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	210-217
27088512-4	2016	The altered expression level of ST3GAL1 was found corresponding to the drug-resistant phenotype (with and without adriamycin resistance) of CML cell lines both in vitro and in vivo.	Doxorubicin	114-124	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	32-39
23275522-4	2012	Using the breast cancer cell line T47D, we have shown that PGE2, one of the final products of the cyclooxygenase-2 (COX-2) pathway, can induce the mRNA expression of the sialyltransferase alpha-2,3-sialyltransferase-3 (ST3Gal-I), resulting in increased sialyltransferase activity, demonstrated by a reduction in PNA lectin staining.	Dinoprostone	59-63	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	219-227
26452603-5	2015	We report the successful modification with Leg5Ac7Ac of a glycolipid, GM1a, and two glycoproteins, interferon-alpha2b and alpha1-antitrypsin, by means of two mammalian sialyltransferases, namely porcine ST3Gal1 and human ST6Gal1.	N,N-diacetyllegionaminate	43-52	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	203-210
26452603-5	2015	We report the successful modification with Leg5Ac7Ac of a glycolipid, GM1a, and two glycoproteins, interferon-alpha2b and alpha1-antitrypsin, by means of two mammalian sialyltransferases, namely porcine ST3Gal1 and human ST6Gal1.	Glycolipids	58-68	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	203-210
26391208-1	2015	UNLABELLED: The sialyl-T antigen sialylalpha2-3Galbeta1-3GalNAc is a common O-glycan structure in human glycoproteins and is synthesized by sialyltransferase ST3Gal1.	o-glycan	76-84	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	158-165
23300007-3	2013	Kinetic analyses of mutants of ST3Gal-I, in conjunction with structural studies, have confirmed the mechanistic roles of His302 and His319 as general acid and base catalysts, respectively, and have quantitated other interactions with the cytosine monophosphate-N-acetyl beta-neuraminic acid donor substrate.	cytosine monophosphate-n-acetyl beta-neuraminic acid	238-290	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	31-39
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
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
26258617-7	2015	Expression levels of sialyltransferases ST3GAL1 and ST3GAL4 were upregulated in the HRMECs after high-glucose stimulation.	Glucose	102-109	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	40-47
26258617-8	2015	Consistent with the real-time PCR data, high-glucose stimulation elevated the protein levels of ST3GAL1 (117.4 +- 14.9 pg/mg, P < 0.01) and ST3GAL4 (6.1 +- 0.9 pg/mg, P < 0.05) in the HRMECs compared with the cells cultured with low-glucose culture media (ST3GAL1, 64.4 +- 5.8 pg/mg; ST3GAL4, 3.8 +- 0.3 pg/mg).	Glucose	45-52	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	96-103
26258617-8	2015	Consistent with the real-time PCR data, high-glucose stimulation elevated the protein levels of ST3GAL1 (117.4 +- 14.9 pg/mg, P < 0.01) and ST3GAL4 (6.1 +- 0.9 pg/mg, P < 0.05) in the HRMECs compared with the cells cultured with low-glucose culture media (ST3GAL1, 64.4 +- 5.8 pg/mg; ST3GAL4, 3.8 +- 0.3 pg/mg).	Glucose	45-52	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	262-269
26258617-8	2015	Consistent with the real-time PCR data, high-glucose stimulation elevated the protein levels of ST3GAL1 (117.4 +- 14.9 pg/mg, P < 0.01) and ST3GAL4 (6.1 +- 0.9 pg/mg, P < 0.05) in the HRMECs compared with the cells cultured with low-glucose culture media (ST3GAL1, 64.4 +- 5.8 pg/mg; ST3GAL4, 3.8 +- 0.3 pg/mg).	Glucose	239-246	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	96-103
22534569-6	2012	Therefore, we found that changes in the structure of O-linked oligosaccharides, resulting in the occurrence of T antigen, are at least partially associated with MUC1 overexpression which down-regulates the expression of C2GnT1 and ST3Gal I.	o-linked oligosaccharides	53-78	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	231-239
21165949-4	2011	GD1a is synthesized from GM1 by alpha2,3 sialyltransferase (ST3Gal) I and mainly by ST3Gal II.	G(M1) Ganglioside	25-28	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	32-69
22969905-6	2012	The differentially expressed genes, such as ST3GalI, FUT8, beta3GalT5, MGAT3 and MGAT5, were mainly involved in the synthesis of N-glycan and glycolipids, particularly the sialyl Lewis antigen.	n-glycan	129-137	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	44-51
22969905-6	2012	The differentially expressed genes, such as ST3GalI, FUT8, beta3GalT5, MGAT3 and MGAT5, were mainly involved in the synthesis of N-glycan and glycolipids, particularly the sialyl Lewis antigen.	Glycolipids	142-153	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	44-51
21165949-7	2011	The expression of ST3Gal I and II was mildly induced by phorbol-12-myristate-13-acetate (PMA), and PMA-induced expression of ST3Gal I and ST3Gal II was inhibited by NF-kappaB decoy oligodeoxynucleotides (ODN) but not by AP-1 decoy ODN.	Tetradecanoylphorbol Acetate	56-87	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-33
21165949-7	2011	The expression of ST3Gal I and II was mildly induced by phorbol-12-myristate-13-acetate (PMA), and PMA-induced expression of ST3Gal I and ST3Gal II was inhibited by NF-kappaB decoy oligodeoxynucleotides (ODN) but not by AP-1 decoy ODN.	Tetradecanoylphorbol Acetate	56-87	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-26
21165949-7	2011	The expression of ST3Gal I and II was mildly induced by phorbol-12-myristate-13-acetate (PMA), and PMA-induced expression of ST3Gal I and ST3Gal II was inhibited by NF-kappaB decoy oligodeoxynucleotides (ODN) but not by AP-1 decoy ODN.	Tetradecanoylphorbol Acetate	89-92	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-33
21165949-7	2011	The expression of ST3Gal I and II was mildly induced by phorbol-12-myristate-13-acetate (PMA), and PMA-induced expression of ST3Gal I and ST3Gal II was inhibited by NF-kappaB decoy oligodeoxynucleotides (ODN) but not by AP-1 decoy ODN.	Tetradecanoylphorbol Acetate	89-92	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-26
21165949-7	2011	The expression of ST3Gal I and II was mildly induced by phorbol-12-myristate-13-acetate (PMA), and PMA-induced expression of ST3Gal I and ST3Gal II was inhibited by NF-kappaB decoy oligodeoxynucleotides (ODN) but not by AP-1 decoy ODN.	Tetradecanoylphorbol Acetate	99-102	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-33
21165949-7	2011	The expression of ST3Gal I and II was mildly induced by phorbol-12-myristate-13-acetate (PMA), and PMA-induced expression of ST3Gal I and ST3Gal II was inhibited by NF-kappaB decoy oligodeoxynucleotides (ODN) but not by AP-1 decoy ODN.	Tetradecanoylphorbol Acetate	99-102	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	18-26
11719190-3	2001	We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase.	mhci	67-71	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	255-263
19508952-9	2009	A ST3Gal-I mutant protein which was converted (335)Arg residue in the C-terminal region to Glu, was rather insensitive to the PM, suggesting that specific C-terminal basic amino acid of ST3Gal-I is involved in the binding to PMs.	Arginine	51-54	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	2-10
19508952-9	2009	A ST3Gal-I mutant protein which was converted (335)Arg residue in the C-terminal region to Glu, was rather insensitive to the PM, suggesting that specific C-terminal basic amino acid of ST3Gal-I is involved in the binding to PMs.	Arginine	51-54	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	186-194
19508952-9	2009	A ST3Gal-I mutant protein which was converted (335)Arg residue in the C-terminal region to Glu, was rather insensitive to the PM, suggesting that specific C-terminal basic amino acid of ST3Gal-I is involved in the binding to PMs.	Glutamic Acid	91-94	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	2-10
19508952-9	2009	A ST3Gal-I mutant protein which was converted (335)Arg residue in the C-terminal region to Glu, was rather insensitive to the PM, suggesting that specific C-terminal basic amino acid of ST3Gal-I is involved in the binding to PMs.	Glutamic Acid	91-94	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	186-194
19508952-9	2009	A ST3Gal-I mutant protein which was converted (335)Arg residue in the C-terminal region to Glu, was rather insensitive to the PM, suggesting that specific C-terminal basic amino acid of ST3Gal-I is involved in the binding to PMs.	Tolonium Chloride	166-171	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	2-10
19508952-9	2009	A ST3Gal-I mutant protein which was converted (335)Arg residue in the C-terminal region to Glu, was rather insensitive to the PM, suggesting that specific C-terminal basic amino acid of ST3Gal-I is involved in the binding to PMs.	Tolonium Chloride	166-171	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	186-194
18080182-8	2008	Three main ST genes are committed with this rearrangement: ST6Gal1 is specifically involved in the augmented alpha 2-6-sialylated N-glycans; ST3Gal1 contributes for the alpha2-3-sialylation of O-glycans, particularly T antigens; and ST3Gal4 may contribute for the increased alpha2-3-sialylated N-glycans.	o-glycans	193-202	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	141-148
18080182-8	2008	Three main ST genes are committed with this rearrangement: ST6Gal1 is specifically involved in the augmented alpha 2-6-sialylated N-glycans; ST3Gal1 contributes for the alpha2-3-sialylation of O-glycans, particularly T antigens; and ST3Gal4 may contribute for the increased alpha2-3-sialylated N-glycans.	n-glycans	294-303	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	141-148
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
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.	1 o-glycans	111-122	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	4-12
17101770-5	2007	We further show that ST3Gal-I function is regulated by a posttranscriptional mechanism operating distal to Golgi core 2 O glycosylation and is invariably linked to CD8+ T-cell contraction following viral (lymphocytic choriomeningitis virus) infection and bacterial (staphylococcal enterotoxin B) antigen immunization.	hippuric acid	118-121	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	21-29
15141079-5	2004	The transcription of genes for fucosyltransferase VII (FUT7), sialyltransferase ST3Gal-I (ST3O), and UDP-galactose transporter-1 (UGT1), which are all known to be involved in the synthesis of the carbohydrate ligands for E-selectin, was significantly induced in cancer cells by hypoxic culture.	Carbohydrates	196-208	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	90-94
19508952-5	2009	Several tungstate-type PMs inhibited Gal: alpha2,3-sialyltransferase-I (ST3Gal-I) activity at sub-nanomolar levels.	tungstate-type pms	8-26	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	72-80
19508952-5	2009	Several tungstate-type PMs inhibited Gal: alpha2,3-sialyltransferase-I (ST3Gal-I) activity at sub-nanomolar levels.	cyclohexenoesculetin-beta-galactoside	37-40	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	72-80
19508952-7	2009	By certain vanadate-type PMs, ST3Gal-I and Gal 3-O-sulfotransferase-2 (Gal3ST-2) were specifically inhibited at nanomolar levels.	Vanadates	11-19	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	30-38
14722111-0	2004	Structure-function analysis of the human sialyltransferase ST3Gal I: role of n-glycosylation and a novel conserved sialylmotif.	Nitrogen	12-13	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	59-67
14722111-11	2004	Although the human ST3Gal I has four N-glycan attachment sites in its catalytic domain that are potentially glycosylated, none of them was shown to be necessary for enzyme activity.	n-glycan	37-45	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	19-27
12379642-1	2002	The mammalian Galbeta1,3GalNAc-specific alpha2,3-sialyltransferase (ST3Gal I) was expressed as a secreted glycoprotein in High Five (Trichoplusia ni) cells.	3galnac	23-30	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	68-76
12379642-3	2002	We found that the hexapeptide, NH(2)-GNWWWW, exhibited the most strong inhibition of ST3Gal I among five different hexapeptides that were finally selected.	nh(2)-gnwwww	31-43	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	85-93
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.	Cytidine Monophosphate	139-142	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	24-32
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
11719190-3	2001	We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase.	o-glycan	215-223	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	255-263
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
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.	galbeta1-3galnac disaccharide	185-214	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.	galbeta1-3galnac disaccharide	185-214	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	60-68
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.	o-glycans	235-244	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.	o-glycans	235-244	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	60-68
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.	Glycolipids	249-260	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.	Glycolipids	249-260	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	60-68
11118434-0	2001	The relative activities of the C2GnT1 and ST3Gal-I glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1.	o-glycan	82-90	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	42-50
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
11118434-8	2001	Transfection of a C2GnT1 expressing line with ST3Gal-I restored SM3 binding and reduced GlcNAc incorporation into MUC1 O-glycans.	SM3	64-67	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	46-54
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.	Galactose	106-115	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	65-73
10755614-0	2000	The ST3Gal-I sialyltransferase controls CD8+ T lymphocyte homeostasis by modulating O-glycan biosynthesis.	o-glycan	84-92	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	4-12
11118434-8	2001	Transfection of a C2GnT1 expressing line with ST3Gal-I restored SM3 binding and reduced GlcNAc incorporation into MUC1 O-glycans.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	88-94	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	46-54
11118434-8	2001	Transfection of a C2GnT1 expressing line with ST3Gal-I restored SM3 binding and reduced GlcNAc incorporation into MUC1 O-glycans.	o-glycans	119-128	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	46-54
10755614-3	2000	We find that the ST3Gal-I sialyltransferase is required for core 1 O-glycan sialylation and its deficiency induces core 2 O-glycan biosynthesis.	o-glycan	67-75	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	17-25
10755614-3	2000	We find that the ST3Gal-I sialyltransferase is required for core 1 O-glycan sialylation and its deficiency induces core 2 O-glycan biosynthesis.	o-glycan	122-130	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	17-25
10755614-6	2000	Control of core 1 O-glycan sialylation in T lymphocytes by ST3Gal-I comprises a homeostatic mechanism that eliminates CD8+ T cells by apoptosis while facilitating the production of viable CD8+ memory T cells.	o-glycan	18-26	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	59-67
10453033-3	1999	Northern blot analyses showed that Gal beta 1-4GlcNAc alpha 2, 6-sialyltransferase (ST6N) mRNA was up-regulated in cultured HUVEC by IL-1 or IL-4 alone, but that the expression was enhanced by costimulation, whereas the level of Gal beta 1-4GlcNAc/Gal beta 1-3GalNAc alpha2,3-sialyltransferase (ST3ON) mRNA was unchanged.	4glcnac	46-53	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	248-293
10683317-2	2000	Estradiol induced a statistically significant increase in ST3Gal III and a decrease in ST6Gal I, whereas the two other enzymes, ST3Gal IV and ST3Gal I, are not modified and expression of the fifth enzyme, ST3Gal II, was very low or not detectable.	Estradiol	0-9	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	58-66
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
10453033-3	1999	Northern blot analyses showed that Gal beta 1-4GlcNAc alpha 2, 6-sialyltransferase (ST6N) mRNA was up-regulated in cultured HUVEC by IL-1 or IL-4 alone, but that the expression was enhanced by costimulation, whereas the level of Gal beta 1-4GlcNAc/Gal beta 1-3GalNAc alpha2,3-sialyltransferase (ST3ON) mRNA was unchanged.	1-4glcnac	44-53	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	248-293
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.	Sugars	56-61	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	118-161
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-Acetylneuraminic Acid	148-159	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	218-225
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
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
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.	o-glycan	90-98	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	53-61
1827755-9	1991	Among them, Gal beta 1----3GalNAc alpha 2----3sialyltransferase and Gal beta 1----4(3)GlcNAc alpha 2----3sialyltransferase were much lower in the RA- or 6-TG-resistant HL-60 subline than in wild-type HL-60 cells.	Thioguanine	153-157	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	12-63
2379165-0	1990	Human leukemic myeloblasts and myeloblastoid cells contain the enzyme cytidine 5"-monophosphate-N-acetylneuraminic acid:Gal beta 1-3GalNAc alpha (2-3)-sialyltransferase.	(2S,4S,5R)-5-acetamido-2,4-dihydroxy-6-[(1R,2R)-1,2,3-trihydroxypropyl]oxane-2-carboxylic acid;[(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl dihydrogen phosphate	70-119	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	120-168
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
34206740-6	2021	These stimuli alter mRNA levels of sialyltransferases such as ST3Gal1, ST6Gal1, or ST3Gal4, suggesting that sialylation of N-glycans is regulated by transcriptional control of sialyltransferases.	n-glycans	123-132	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	62-69
34324649-4	2021	The O-glycan sialyltransferase St3gal1 add sialic acid specifically on the TF-antigen.	o-glycan	4-12	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	31-38
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
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.	Galactose	93-102	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.	Galactose	93-102	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	259-266
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.	Disaccharides	123-136	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.	Disaccharides	123-136	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	259-266