PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
10779678-7	2000	Interferon-gamma purified from the universal host carried 40.4% alpha2,6- and 59.6% alpha2,3-sialic acid residues and showed improved pharmacokinetics in clearance studies when compared to interferon-gamma produced by normal CHO cells.	alpha2,3-sialic acid	84-104	interferon gamma	Cricetulus griseus	0-16
18713811-5	2008	Biochemical analyses indicate that recombinant interferon-gamma (IFN-gamma) produced by the mutant cells lack sialic acid.	N-Acetylneuraminic Acid	110-121	interferon gamma	Cricetulus griseus	47-63
18713811-5	2008	Biochemical analyses indicate that recombinant interferon-gamma (IFN-gamma) produced by the mutant cells lack sialic acid.	N-Acetylneuraminic Acid	110-121	interferon gamma	Cricetulus griseus	65-74
18496872-0	2008	Influence of intracellular nucleotide and nucleotide sugar contents on recombinant interferon-gamma glycosylation during batch and fed-batch cultures of CHO cells.	nucleotide sugar	42-58	interferon gamma	Cricetulus griseus	83-99
15593097-2	2005	In this study, we describe a dynamic on-line fed-batch strategy based on low glutamine/glucose concentrations and its impact on cellular metabolism and, more importantly, the productivity and N-glycosylation quality of a model recombinant glycoprotein, interferon gamma (IFN-gamma).	Glutamine	77-86	interferon gamma	Cricetulus griseus	253-280
15593097-2	2005	In this study, we describe a dynamic on-line fed-batch strategy based on low glutamine/glucose concentrations and its impact on cellular metabolism and, more importantly, the productivity and N-glycosylation quality of a model recombinant glycoprotein, interferon gamma (IFN-gamma).	Glucose	87-94	interferon gamma	Cricetulus griseus	253-280
10779678-7	2000	Interferon-gamma purified from the universal host carried 40.4% alpha2,6- and 59.6% alpha2,3-sialic acid residues and showed improved pharmacokinetics in clearance studies when compared to interferon-gamma produced by normal CHO cells.	cho	225-228	interferon gamma	Cricetulus griseus	0-16
18600949-6	1992	However, the specific rate of IFN-gamma production was significantly lower at the higher glucose feed concentration.	Glucose	89-96	interferon gamma	Cricetulus griseus	30-39
19003337-0	1999	Na-butyrate increases the production and alpha2,6-sialylation of recombinant interferon-gamma expressed by alpha2,6- sialyltransferase engineered CHO cells.	na-butyrate	0-11	interferon gamma	Cricetulus griseus	77-93
9698230-6	1998	Based on the integrated peak area for each compound in the chromatograms, the percentage for each glycan was utilized to quantify the glycosylation pattern of the interferon-gamma.	Polysaccharides	98-104	interferon gamma	Cricetulus griseus	163-179
9698230-7	1998	Finally, sialylation and antennarity structure percentages at the two glycosylation sites were chosen as the quality indicators in process monitoring of interferon-gamma production from a serum-free suspension-batch CHO culture.	cho	216-219	interferon gamma	Cricetulus griseus	153-169
10099302-0	1998	Improvement of interferon-gamma sialylation in Chinese hamster ovary cell culture by feeding of N-acetylmannosamine.	N-acetylmannosamine	96-115	interferon gamma	Cricetulus griseus	15-31
10099302-2	1998	In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis.	N-acetylmannosamine	192-211	interferon gamma	Cricetulus griseus	59-75
10099302-2	1998	In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis.	N-acetylmannosamine	192-211	interferon gamma	Cricetulus griseus	77-86
10099302-2	1998	In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis.	N-acetylmannosamine	213-219	interferon gamma	Cricetulus griseus	59-75
10099302-2	1998	In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis.	N-acetylmannosamine	213-219	interferon gamma	Cricetulus griseus	77-86
10099302-2	1998	In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis.	N-Acetylneuraminic Acid	259-270	interferon gamma	Cricetulus griseus	59-75
10099302-2	1998	In this study, the incomplete intracellular sialylation of interferon-gamma (IFN-gamma), produced by Chinese hamster ovary cell culture, was minimized by supplementing the culture medium with N-acetylmannosamine (ManNAc), a direct intracellular precursor for sialic acid synthesis.	N-Acetylneuraminic Acid	259-270	interferon gamma	Cricetulus griseus	77-86
10099302-7	1998	When radiolabeled ManNAc was used to trace the incorporation of the precursor, it was found that supplemental ManNAc was exclusively incorporated into IFN-gamma as sialic acid and that, at 20 mM ManNAc feeding, nearly 100% of product sialylation originated from the supplemental precursor.	N-acetylmannosamine	110-116	interferon gamma	Cricetulus griseus	151-160
10099302-7	1998	When radiolabeled ManNAc was used to trace the incorporation of the precursor, it was found that supplemental ManNAc was exclusively incorporated into IFN-gamma as sialic acid and that, at 20 mM ManNAc feeding, nearly 100% of product sialylation originated from the supplemental precursor.	N-Acetylneuraminic Acid	164-175	interferon gamma	Cricetulus griseus	151-160
10099302-7	1998	When radiolabeled ManNAc was used to trace the incorporation of the precursor, it was found that supplemental ManNAc was exclusively incorporated into IFN-gamma as sialic acid and that, at 20 mM ManNAc feeding, nearly 100% of product sialylation originated from the supplemental precursor.	N-acetylmannosamine	110-116	interferon gamma	Cricetulus griseus	151-160
22358930-3	1996	The enzyme was expressed efficiently, and resulted in up to 60% of the total sialic acids on interferon-gamma being linked in the alpha2,6-conformation.	Sialic Acids	77-89	interferon gamma	Cricetulus griseus	93-109
18613236-0	1993	The effect of the dilution rate on CHO cell physiology and recombinant interferon-gamma production in glucose-limited chemostat culture.	Glucose	102-109	interferon gamma	Cricetulus griseus	71-87
18642238-3	1997	In batch cultures, decreased sialylation was observed at each of the glycosylation sites (i.e., Asn(25) and Asn(97)) of IFN-gamma with the use of elevated concentrations of the peptone.	Asparagine	96-99	interferon gamma	Cricetulus griseus	120-129
18642238-3	1997	In batch cultures, decreased sialylation was observed at each of the glycosylation sites (i.e., Asn(25) and Asn(97)) of IFN-gamma with the use of elevated concentrations of the peptone.	Asparagine	108-111	interferon gamma	Cricetulus griseus	120-129
7876143-5	1995	The IFN gamma R-IgG3 fusion protein was secreted into the culture medium as a 175-kDa glycoprotein and was purified over Protein G-Sepharose, DEAE-Sepharose, and size exclusion chromatography.	Sepharose	131-140	interferon gamma	Cricetulus griseus	4-13
7876143-5	1995	The IFN gamma R-IgG3 fusion protein was secreted into the culture medium as a 175-kDa glycoprotein and was purified over Protein G-Sepharose, DEAE-Sepharose, and size exclusion chromatography.	deae-sepharose	142-156	interferon gamma	Cricetulus griseus	4-13
7765933-4	1994	Partially substituting the bovine serum albumin content of the medium with a fatty-acid free preparation also improved interferon-gamma glycosylation, possibly indicating that oxidised lipids carried on Cohn fraction V albumin may damage the glycosylation process.	Fatty Acids	77-87	interferon gamma	Cricetulus griseus	119-135
18600949-7	1992	Under glucose limitation, the proportion of fully glycosylated IFN-gamma produced by these cells was less than that produced in the early stages of batch cultures.	Glucose	6-13	interferon gamma	Cricetulus griseus	63-72
18600949-8	1992	The proportion of fully glycosylated IFN-gamma increased during transient periods of glucose excess, suggesting that the culture environment influences the glycosylation of IFN-gamma.	Glucose	85-92	interferon gamma	Cricetulus griseus	37-46