PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
28295160-3	2017	By introducing the 1,3,4-O-Bu3 ManNAc analog at 200-300 microM into cell culture media, the intracellular sialic acid content of EPO-expressing cells increased ~8-fold over untreated controls while the level of cellular sialylated glycoconjugates increased significantly as well.	1,3,4-o-bu3 mannac	19-37	erythropoietin	Cricetulus griseus	129-132
30221828-2	2019	In this study, butyrate supplied by the precursor molecule 1,3,4-O-Bu3 ManNAc is applied to overcome the negative effects of NaBu on glycan quality while simultaneously increasing the productivity of the model recombinant erythropoietin (EPO).	1,3,4-o-bu3 mannac	59-77	erythropoietin	Cricetulus griseus	222-236
30221828-2	2019	In this study, butyrate supplied by the precursor molecule 1,3,4-O-Bu3 ManNAc is applied to overcome the negative effects of NaBu on glycan quality while simultaneously increasing the productivity of the model recombinant erythropoietin (EPO).	1,3,4-o-bu3 mannac	59-77	erythropoietin	Cricetulus griseus	238-241
30221828-3	2019	The beneficial impact of 1,3,4-O-Bu3 ManNAc on EPO glycan quality, while evident in wild-type CHO cells, is particularly pronounced in glycoengineered CHO cells with stable overexpression of beta-1,4- and beta-1,6-N-acetylglucosaminyltransferases (GnTIV and GnTV) and alpha-2,6-sialyltransferase (ST6) enzymes responsible for N-glycan antennarity and sialylation.	1,3,4-o-bu3 mannac	25-43	erythropoietin	Cricetulus griseus	47-50
30221828-3	2019	The beneficial impact of 1,3,4-O-Bu3 ManNAc on EPO glycan quality, while evident in wild-type CHO cells, is particularly pronounced in glycoengineered CHO cells with stable overexpression of beta-1,4- and beta-1,6-N-acetylglucosaminyltransferases (GnTIV and GnTV) and alpha-2,6-sialyltransferase (ST6) enzymes responsible for N-glycan antennarity and sialylation.	1,3,4-o-bu3 mannac	25-43	beta-galactoside alpha-2,6-sialyltransferase 1	Cricetulus griseus	268-295
30221828-4	2019	Supplementation of 1,3,4-O-Bu3 ManNAc achieves approximately 30% sialylation enhancement on EPO protein in wild-type CHO cells.	1,3,4-o-bu3 mannac	19-37	erythropoietin	Cricetulus griseus	92-95
30221828-7	2019	Moreover, a detailed mass spectrometric ESI-LC-MS/MS characterization of glycans at each of the three N-glycosylation sites of EPO showed that the 1st N-site is highly sialylated and either the negative impact of NaBu or the beneficial effect 1,3,4-O-Bu3 ManNAc treatments mainly affects the 2nd and 3rd N-glycan sites of EPO protein.	1,3,4-o-bu3 mannac	243-261	erythropoietin	Cricetulus griseus	127-130
29427449-3	2018	Supplementation with 1,3,4-O-Bu3 ManNAc for two stable CHO cell lines, expressing human erythropoietin or IgG, enhanced protein expression for both products with negligible impact on cell growth, viability, glucose utilization, and lactate accumulation.	1,3,4-o-bu3 mannac	21-39	erythropoietin	Homo sapiens	88-102
30221828-8	2019	In summary, these results demonstrate 1,3,4-O-Bu3 ManNAc can compensate for the negative effect of NaBu on EPO glycan quality while simultaneously enhancing recombinant protein yields.	1,3,4-o-bu3 mannac	38-56	erythropoietin	Cricetulus griseus	107-110
28295160-4	2017	For example, addition of 200-300 microM 1,3,4-O-Bu3 ManNAc resulted in >40% increase in final sialic acid content of recombinant EPO, while natural ManNAc at ~100 times higher concentration of 20 mM produced a less profound change in EPO sialylation.	1,3,4-o-bu3 mannac	40-58	erythropoietin	Cricetulus griseus	132-135
28295160-4	2017	For example, addition of 200-300 microM 1,3,4-O-Bu3 ManNAc resulted in >40% increase in final sialic acid content of recombinant EPO, while natural ManNAc at ~100 times higher concentration of 20 mM produced a less profound change in EPO sialylation.	1,3,4-o-bu3 mannac	40-58	erythropoietin	Cricetulus griseus	237-240