CeLLaTe Raw Data
Collection
This collection contains raw dataset zips, consisting of LabelStudio-formatted .json files, named by their corresponding Europe PMC identifiers. • 5 items • Updated
PMCID stringclasses 8
values | sentence stringlengths 5 960 | entities listlengths 0 13 | __index_level_0__ int64 0 751 |
|---|---|---|---|
PMC12503014 | While Chinese hamster ovary (CHO) cells continue to be the workhorse of recombinant therapeutic protein production, decades of genetic divergence in the industrially relevant CHO‐K1 and CHO‐S cell lines, are likely to have resulted in differing glycosylation capabilities. | [
{
"end": 181,
"label": "CellLine",
"start": 175,
"text": "CHO‐K1"
},
{
"end": 191,
"label": "CellLine",
"start": 186,
"text": "CHO‐S"
},
{
"end": 39,
"label": "CellLine",
"start": 6,
"text": "Chinese hamster ovary (CHO) cells"
}
] | 0 |
PMC12503014 | Glycosylation can influence the efficacy, serum half‐life, and safety of biologics, and as a critical quality attribute of glycoprotein biopharmaceuticals, it is essential to better understand how major CHO cell manufacturing platforms diverge. | [] | 1 |
PMC12503014 | We used matrix‐assisted laser desorption ionization‐time of flight mass spectrometry to perform N‐glycomic analyses comparing CHO‐K1 cells, CHO‐S cells and antibody‐producing daughter cell lines. | [
{
"end": 145,
"label": "CellLine",
"start": 140,
"text": "CHO‐S"
},
{
"end": 132,
"label": "CellLine",
"start": 126,
"text": "CHO‐K1"
}
] | 2 |
PMC12503014 | The results reveal that genetic divergence in these industrially relevant cell lines, as well as the burden of antibody production, lead to significant differences in antennal branching and terminal elaboration in the cellular N‐glycome. | [] | 3 |
PMC12503014 | More specifically, CHO‐K1 cells produce larger and more complex N‐glycans with higher levels of sialylation than CHO‐S cells, and antibody production was associated with increased antennal branching. | [
{
"end": 25,
"label": "CellLine",
"start": 19,
"text": "CHO‐K1"
},
{
"end": 118,
"label": "CellLine",
"start": 113,
"text": "CHO‐S"
}
] | 4 |
PMC12503014 | Additionally, these findings were also reflected in the N‐glycomic profiles of IgG1‐Fc constructs produced in either CHO‐K1 and CHO‐S cells. | [
{
"end": 123,
"label": "CellLine",
"start": 117,
"text": "CHO‐K1"
},
{
"end": 133,
"label": "CellLine",
"start": 128,
"text": "CHO‐S"
}
] | 5 |
PMC12503014 | Chinese hamster ovary (CHO) cells are currently the most important manufacturing platform for the multibillion USD biopharmaceutical industry. | [
{
"end": 33,
"label": "CellLine",
"start": 0,
"text": "Chinese hamster ovary (CHO) cells"
}
] | 6 |
PMC12503014 | From 2018 to 2022, nearly 70% of approved biopharmaceuticals, and 85% of novel macromolecules (i.e., excluding biosimilars), were produced in CHO cells (G. Walsh and E. Walsh 2022). | [
{
"end": 145,
"label": "CellLine",
"start": 142,
"text": "CHO"
}
] | 7 |
PMC12503014 | An even larger proportion of monoclonal antibodies (mAbs), 89%, were produced in these hosts (G. Walsh and E. Walsh 2022). | [] | 8 |
PMC12503014 | In the decades since the first biopharmaceuticals were clinically approved, CHO cells came to dominate the manufacturing landscape partly because of human‐compatible glycosylation profiles and high production titers (10–15 g∙L) (Puetz and Wurm 2019). | [
{
"end": 79,
"label": "CellLine",
"start": 76,
"text": "CHO"
}
] | 9 |
PMC12503014 | Despite the advantages of such a platform, glycosylation is not a template‐driven process and remains a heterogenous affair even in CHO cells. | [
{
"end": 135,
"label": "CellLine",
"start": 132,
"text": "CHO"
}
] | 10 |
PMC12503014 | Enzyme competition for substrates in the cellular glycosylation reaction networks generates a mixture of glycan structures on glycoprotein therapeutics. | [] | 11 |
PMC12503014 | N‐ and O‐glycosylation both directly and indirectly modulate biopharmaceutical efficacy, serum half‐life, and immunogenic responses, which is why increased control over CHO cell glycosylation and in vivo glycoengineering are useful strategies that require a deep understanding of CHO cell glycosylation capabilities. | [] | 12 |
PMC12503014 | While glycosylation is not present in all recombinant therapeutic proteins and can be engineered out when functionally redundant, it remains a critical quality attribute of glycoprotein therapeutics under the FDA's “Quality by Design” paradigm. | [] | 13 |
PMC12503014 | In fact, reproducible glycosylation profiles are essential for the development of biosimilars that accurately mimic originator products. | [] | 14 |
PMC12503014 | Furthermore, glycoengineering can serve as a foundation for diverse strategies aimed at enhancing the quality of biopharmaceuticals in the development of biobetters. | [] | 15 |
PMC12503014 | A previous mass spectrometry (MS) glycomic analysis of N‐ and O‐glycans from CHO‐Pro5 cells and a panel of glycosylation mutants forms the basis of our current understanding of the CHO cell glycosylation machinery (North et al. 2010). | [
{
"end": 85,
"label": "CellLine",
"start": 77,
"text": "CHO‐Pro5"
},
{
"end": 184,
"label": "CellLine",
"start": 181,
"text": "CHO"
}
] | 16 |
PMC12503014 | The data reported only simple mono‐ or disialylated core‐1 O‐glycan structures (+/−NeuAca2,3Galβ1,3‐(+/−NeuAca2,6)GalNAcα‐Ser/Thr) were produced by CHO cells, however, the N‐glycomic profiles revealed spectra with high mannose (Man) N‐glycans together with a wide range of complex N‐glycans. | [] | 17 |
PMC12503014 | In CHO cells, the complex N‐glycome includes a mixture of bi‐, tri‐, and tetra‐antennary N‐glycans that can form large structures with highly extended antennae including up to 26 lactosamine (LacNAc; Gal‐GlcNAc) units. | [
{
"end": 6,
"label": "CellLine",
"start": 3,
"text": "CHO"
}
] | 18 |
PMC12503014 | The antennae can also be capped by N‐acetylneuraminic acid (NeuAc sialic acid) and fucose (Fuc) was found to be present only in the chitobiose core. | [] | 19 |
PMC12503014 | While these experiments generated a wealth of glycomic data for CHO cells, the Pro5 cells in this study are not the dominant cell line used in industry for the manufacturing of biopharmaceutical products. | [
{
"end": 67,
"label": "CellLine",
"start": 64,
"text": "CHO"
},
{
"end": 83,
"label": "CellLine",
"start": 79,
"text": "Pro5"
}
] | 20 |
PMC12503014 | In fact, CHO‐K1 and CHO‐S cells are some of the most commonly used cell lines for industrial bioprocesses in the pharmaceutical industry (F. Wurm and M. Wurm 2017). | [
{
"end": 15,
"label": "CellLine",
"start": 9,
"text": "CHO‐K1"
},
{
"end": 25,
"label": "CellLine",
"start": 20,
"text": "CHO‐S"
}
] | 21 |
PMC12503014 | It is not possible to exactly determine the precise pedigree of CHO cell lines in use today, however, a review by Wurm and Wurm traces the origins of the CHO‐K1 cell line to the late 1960s, whereas the CHO‐S cell line emerged in the 1970s (F. Wurm and M. Wurm 2017). | [
{
"end": 160,
"label": "CellLine",
"start": 154,
"text": "CHO‐K1"
},
{
"end": 207,
"label": "CellLine",
"start": 202,
"text": "CHO‐S"
},
{
"end": 78,
"label": "CellLine",
"start": 64,
"text": "CHO cell lines"
}
] | 22 |
PMC12503014 | The initially immortalized CHO cells, and all the CHO cell lines that have since emerged, were released from the constraints imposed by diploidy control, and subsequently evolved with higher rates of DNA mutations and changes in gene expression profiles (F. Wurm and M. Wurm 2017). | [
{
"end": 30,
"label": "CellLine",
"start": 27,
"text": "CHO"
},
{
"end": 64,
"label": "CellLine",
"start": 50,
"text": "CHO cell lines"
}
] | 23 |
PMC12503014 | Inherent genetic instability in CHO cells and a lack of “true” clonality is not necessarily an issue for the reliable production of high‐quality biopharmaceuticals. | [
{
"end": 35,
"label": "CellLine",
"start": 32,
"text": "CHO"
}
] | 24 |
PMC12503014 | However, it is likely that over decades of culturing—often in a variety of conditions that alter selective pressures—and many cell division events, the genetic divergence between, and indeed, within CHO “cell lines” could be of significance. | [
{
"end": 215,
"label": "CellLine",
"start": 199,
"text": "CHO “cell lines”"
}
] | 25 |
PMC12503014 | While clonal selection is a standard process in industry that includes glycosylation as a selection criterion, genetic divergence may increase with each cell division event, potentially leading to heterogenous glycosylation capabilities and loss of “clonality.” | [] | 26 |
PMC12503014 | We posited that such genetic divergence might be reflected in the expression levels of glycosylation genes and consequently affect the N‐glycosylation profiles of different CHO cell lines and the recombinant glycoprotein therapeutics produced in these cells. | [
{
"end": 187,
"label": "CellLine",
"start": 173,
"text": "CHO cell lines"
}
] | 27 |
PMC12503014 | A genomic comparison of the CHO‐K1, CHO‐S, and CHO‐DG44 cell lineages previously highlighted such genetic differences and suggested that further biochemical characterization of glycomic phenotypes was necessary (Lewis et al. 2013). | [
{
"end": 34,
"label": "CellLine",
"start": 28,
"text": "CHO‐K1"
},
{
"end": 41,
"label": "CellLine",
"start": 36,
"text": "CHO‐S"
},
{
"end": 55,
"label": "CellLine",
"start": 47,
"text": "CHO‐DG44"
}
] | 28 |
PMC12503014 | Herein, we present mass spectrometric N‐glycomic data that highlight differences in cellular N‐glycosylation in two industrially important CHO cell lineages: CHO‐K1 and CHO‐S. Our focus on N‐glycan profiles stems from the fact that most glycosylation in recombinant biopharmaceuticals, such as IgG mAbs, is N‐linked. | [
{
"end": 164,
"label": "CellLine",
"start": 158,
"text": "CHO‐K1"
},
{
"end": 174,
"label": "CellLine",
"start": 169,
"text": "CHO‐S"
},
{
"end": 156,
"label": "CellLine",
"start": 139,
"text": "CHO cell lineages"
}
] | 29 |
PMC12503014 | Additionally, CHO cell O‐glycosylation is limited to simple core‐1 structures with or without sialic acid capping and is less informative about the overall glycosylation machinery of CHO cells than N‐glycans. | [
{
"end": 186,
"label": "CellLine",
"start": 183,
"text": "CHO"
}
] | 30 |
PMC12503014 | Furthermore, we analyzed the N‐glycome of IgG mAb‐producing cells derived from CHO‐K1 and CHO‐S cells to determine whether the production and secretion of mAbs can itself influence the glycosylation machinery of CHO cells. | [
{
"end": 85,
"label": "CellLine",
"start": 79,
"text": "CHO‐K1"
},
{
"end": 95,
"label": "CellLine",
"start": 90,
"text": "CHO‐S"
},
{
"end": 215,
"label": "CellLine",
"start": 212,
"text": "CHO"
}
] | 31 |
PMC12503014 | The impact of increased metabolic pressure from the expression and secretion of recombinant mAbs on CHO cell N‐glycosylation is not sufficiently understood. | [
{
"end": 103,
"label": "CellLine",
"start": 100,
"text": "CHO"
}
] | 32 |
PMC12503014 | In fact, as the cell redirects limited resources toward antibody production away from biomass production, and the flux in the secretory pathway increases, the expression of glycosyltransferases and glycosidases, and the Golgi residence time of recombinant glycoproteins may be affected (Fan et al. 2015; Jimenez del Val ... | [] | 33 |
PMC12503014 | Finally, we analyzed the N‐glycomic profiles of a panel of antibody‐Fc constructs with novel glycosylation sites, produced in CHO‐S cells, and compared these to previously published data for the same constructs produced in CHO‐K1 cells. | [
{
"end": 131,
"label": "CellLine",
"start": 126,
"text": "CHO‐S"
},
{
"end": 229,
"label": "CellLine",
"start": 223,
"text": "CHO‐K1"
}
] | 34 |
PMC12503014 | To our knowledge, this is the first study investigating the cellular glycome of industrially relevant CHO cells and the impact of recombinant product expression and secretion on the glycosylation machinery of CHO cells. | [
{
"end": 105,
"label": "CellLine",
"start": 102,
"text": "CHO"
},
{
"end": 212,
"label": "CellLine",
"start": 209,
"text": "CHO"
}
] | 35 |
PMC12503014 | All cells were grown in CD‐CHO medium (Gibco, ThermoFisher Scientific, USA) with the relevant supplements added as shown in Table 1. | [] | 36 |
PMC12503014 | Solutions were prewarmed to 37°C and cells were incubated at 37°C with 5% CO2 and orbital shaking (16 mm orbit; SSL1 orbital shaker, Stuart) (see Table 1). | [] | 37 |
PMC12503014 | All centrifugations of CHO cells were performed at 800 rpm (120g; TX‐400 rotor, ThermoFisher Scientific, USA) for 5 min. | [
{
"end": 26,
"label": "CellLine",
"start": 23,
"text": "CHO"
}
] | 38 |
PMC12503014 | During cell revival, a 1 mL cell vial stored in liquid nitrogen (LN2) was thawed and resuspended in 9 mL prewarmed medium. | [] | 39 |
PMC12503014 | Cell density and culture viability were measured using a haemocytometer and trypan blue exclusion, and an NC‐3000 NucleoCounter with solution 18 and A8 NC‐slides according to manufacturer's instructions (Chemometec, Denmark). | [] | 40 |
PMC12503014 | Cells were then seeded at the appropriate density (see Table 1) in sterile vented flasks with 50 mL of total culture volume and split every 3 or 4 days. | [] | 41 |
PMC12503014 | Each cell line was cultured in biological triplicates and cells were harvested after three passages post‐revival. | [] | 42 |
PMC12503014 | Cell line‐specific incubator growth conditions. | [] | 43 |
PMC12503014 | l‐Glutamine (8 mM, #25030081 Gibco) HT supplement (10 mL·L, 100× dilution, #11067030, Gibco) l‐Glutamine (8 mM, #25030081, Gibco) Hygromycin B (500 μg·L, #10687010, Gibco) The construction, expression, and purification of the CHO‐K1 panel of Fc‐fragments have been described in detail (Blundell et al. 2019, 2020), while... | [
{
"end": 232,
"label": "CellLine",
"start": 226,
"text": "CHO‐K1"
},
{
"end": 381,
"label": "CellLine",
"start": 376,
"text": "CHO‐S"
}
] | 44 |
PMC12503014 | The N‐glycomic analysis is based on a previous protocol (North et al. 2010). | [] | 45 |
PMC12503014 | On Day 4 of the third subculture, 1 × 10 cells were harvested by centrifugation at 800 rpm (120g; TX‐400 rotor, Thermo) for 5 min. | [] | 46 |
PMC12503014 | Cell pellets were washed in phosphate‐buffered saline and pelleted again prior to storage at −80°C. | [] | 47 |
PMC12503014 | The cells were then sonicated in lysis buffer (25 mM Tris, 150 mM NaCl, 5 mM EDTA, and 1% CHAPS, pH 7.4) on ice—4 × 10 s in continuous mode at 40 amps (CV188 sonicator, Vibra‐Cell‐Sonics) with 1 min on ice in between each sonication step. | [] | 48 |
PMC12503014 | The samples were then dialyzed against 5 × 4.5 L of 50 mM ammonium bicarbonate (pH 8.5) at 4°C for 48 h and then lyophilized. | [] | 49 |
PMC12503014 | Extracted glycoproteins were then reduced with 1 mL of 2 mg/mL dithiothreitol in 0.6 M Tris buffer (pH 8.5) at 50°C for 60 min. | [] | 50 |
PMC12503014 | Carboxymethylation was then carried out via the addition of 1 mL of 12 mg/mL iodoacetic acid in 0.6 M Tris buffer (pH 8.5), where samples were incubated at room temperature, in the dark, for 90 min. | [] | 51 |
PMC12503014 | Samples were then dialyzed once more as described above, and lyophilized after 48 h. The reduced and carboxymethylated glycoproteins were resuspended in 700 µL of 50 mM ammonium bicarbonate and tryptically digested with the addition of 50 µL of 10 mg/mL porcine pancreas trypsin (EC 3.4.21.4; Sigma‐Aldrich) in 50 mM amm... | [] | 52 |
PMC12503014 | Glycopeptides were resuspended in 200 µL of 50 mM ammonium bicarbonate (pH 8.4) and 5 µL of recombinant PNGase F (EC 3.5.1.52, Roche, Switzerland) in glycerol was added to each sample. | [] | 53 |
PMC12503014 | The reaction was carried out at 37°C for 24 h—with the addition of a supplementary 5 µL aliquot of PNGase F after the first 8 h—and then lyophilized. | [] | 54 |
PMC12503014 | N‐glycans were then resuspended in 200 µL of 5% acetic acid (v/v) and separated from peptides and O‐glycopeptides by reverse phase chromatography using Sep‐Pak Classic C18 cartridges (Waters, USA) as described previously (North et al. 2010). | [] | 55 |
PMC12503014 | N‐glycans were eluted in 5 mL of 5% acetic acid (v/v). | [] | 56 |
PMC12503014 | At this stage, 1/3 of the purified N‐glycans were aliquoted for enzymatic digestion prior to derivatization, while the remaining 2/3 were derivatized directly following lyophilisation. | [] | 57 |
PMC12503014 | After the aliquots were taken from the 5 mL elution, volumes were reduced on a SpeedVac, and samples were then lyophilized. | [] | 58 |
PMC12503014 | The 1/3 aliquots of purified N‐glycans were resuspended in 400 µL of 50 mM sodium acetate (pH 5.5) and 8 µL of endo‐β‐galactosidase (EC 3.2.1.103, R&D Systems, Biotechne, USA) was added to each sample, which were then incubated at 37°C for 24 h, and then lyophilized. | [] | 59 |
PMC12503014 | Digested N‐glycans were resuspended in 200 µL of 5% acetic acid (v/v) and purified once more by reverse phase chromatography using Sep‐Pak Classic C18 cartridges (Waters, USA) with the same protocol as the post‐PNGase F chromatographic step. | [] | 60 |
PMC12503014 | The samples were then lyophilized and derivatized. | [] | 61 |
PMC12503014 | N‐glycans were permethylated with the sodium hydroxide procedure. | [] | 62 |
PMC12503014 | First, 5 pellets of sodium hydroxide (per sample) were ground in a dry glass mortar with 3 mL of anhydrous dimethylsulfoxide. | [] | 63 |
PMC12503014 | In total, 1 mL of the resulting slurry was then added to each sample tube together with 0.5 mL of methyl iodide and mixed vigorously with an automatic shaker for 15–45 min (until the slurry becomes a white paste that no longer mixes). | [] | 64 |
PMC12503014 | The reaction was quenched by the drop‐wise addition of water with constant agitation, after which 1 mL of chloroform was added to extract the permethylated N‐glycans. | [] | 65 |
PMC12503014 | The mixture was made up to ~5 mL with ultra‐pure water and vortexed vigorously for 30 s to wash out hydrophilic contaminants. | [] | 66 |
PMC12503014 | The hydrophobic and hydrophilic layers were separated rapidly by centrifugation, and the aqueous layer was then discarded. | [] | 67 |
PMC12503014 | A further four washes were performed by adding 5 mL of ultra‐pure water, vortexing for 30 s, and discarding the aqueous layer after centrifugation. | [] | 68 |
PMC12503014 | The chloroform layer was then dried under a gentle stream of nitrogen gas. | [] | 69 |
PMC12503014 | Permethylated N‐glycans were further purified from hydrophilic contaminants by reverse phase chromatography using Sep‐Pak Classic C18 cartridges (Waters, USA). | [] | 70 |
PMC12503014 | The cartridges were conditioned by eluting successively 5 mL methanol, 5 mL ultra‐pure water, 5 mL acetonitrile (MeCN), and reequilibrated with 3 × 5 mL ultra‐pure water. | [] | 71 |
PMC12503014 | The dry samples from the chloroform extraction were redissolved in 100 µL methanol, after which 100 µL of ultra‐pure water was added to each sample prior to loading onto the cartridge. | [] | 72 |
PMC12503014 | Once the sample was loaded, a 5 mL wash with ultra‐pure water was eluted and then 3 mL of each 15%, 35%, 50%, and 75% MeCN (v/v) were eluted and collected. | [] | 73 |
PMC12503014 | All fraction volumes were reduced on a SpeedVac and samples were then lyophilized. | [] | 74 |
PMC12503014 | The lyophilized permethylated N‐glycans were redissolved in 10 µL methanol and a 1 µL aliquot from each fraction was mixed with 1 µL of 3,4‐diamino‐benzophenone (DABP) matrix solution (10 mg/mL, in 75% MeCN, v/v). | [] | 75 |
PMC12503014 | 2 × 0.5 µL of the sample/matrix mixture were then spotted onto a clean matrix‐assisted laser desorption ionization (MALDI) plate and dried under vacuum. | [] | 76 |
PMC12503014 | The spotted plate was then loaded into a 4800 MALDI‐TOF/TOF mass spectrometer (Applied Biosystems, USA) for MS and MS/MS glycomic analyses. | [] | 77 |
PMC12503014 | MALDI‐MS data were collected in the positive ion mode, with a mass range of m/z 500–9000. | [] | 78 |
PMC12503014 | Four spectra (1000 shots each) were collected for each sample/spot with a laser intensity of 4000 and 20 kV accelerating voltage. | [] | 79 |
PMC12503014 | MS/MS analyses were performed on the same instrument, however, using the positive reflectron mode, with argon gas in the collision cell (at 10mbar pressure) to induce collisionally activated decomposition. | [] | 80 |
PMC12503014 | For these experiments, the potential difference between the source acceleration voltage and the collision cell was set to 1 kV. All structural assignments of N‐glycans were based on molecular ion composition, previous knowledge of biosynthetic pathways, and MS/MS fragmentation patterns. | [] | 81 |
PMC12503014 | Data Explorer (Applied Biosystems, USA) and GlycoWorkBench were used for the analysis of MALDI‐MS and MALDI‐MS/MS spectra (Ceroni et al. 2008). | [] | 82 |
PMC12503014 | Quantitative information of N‐glycans was derived from ion counts which do not consider ionization efficiencies and should therefore not be considered absolute values. | [] | 83 |
PMC12503014 | The relative abundances of galactose and NeuAc sialic acid in each sample were calculated by summing the relative intensities of galactose‐, or sialic acid‐containing N‐glycans and dividing by the sum of relative intensities for all assigned N‐glycans and finally expressed as a percentage (the number of Gal or NeuAc re... | [] | 84 |
PMC12503014 | The same method was used to analyze the relative abundance of core‐fucosylation, and oligomannose/complex N‐glycans. | [] | 85 |
PMC12503014 | This data omit monoisotopic peaks corresponding to putative very low abundance afucosylated structures that might be present in isotopic clusters (see Figures S5 and S6). | [] | 86 |
PMC12503014 | Samples for N‐glycomic analyses were prepared from CHO‐K1, CHO‐S, CHO‐K1mAb, and CHO‐SmAb cell cultures grown in suspension that were pelleted, washed, and sonicated. | [
{
"end": 57,
"label": "CellLine",
"start": 51,
"text": "CHO‐K1"
},
{
"end": 64,
"label": "CellLine",
"start": 59,
"text": "CHO‐S"
},
{
"end": 75,
"label": "CellLine",
"start": 66,
"text": "CHO‐K1mAb"
},
{
"end": 89,
"label": "CellLine",
"start"... | 87 |
PMC12503014 | Glycoproteins in the cell lysates were then reduced and carboxymethylated, and tryptically digested. | [] | 88 |
PMC12503014 | The N‐glycans were subsequently released from tryptic glycopeptides by PNGase F digestion, purified, and permethylated to increase the sensitivity of the MS analysis. | [] | 89 |
PMC12503014 | Endo‐β‐galactosidase enzymatic digests were also performed on purified N‐glycans prior to permethylation to enhance the structural characterization of cellular N‐glycans from CHO cells. | [
{
"end": 178,
"label": "CellLine",
"start": 175,
"text": "CHO"
}
] | 90 |
PMC12503014 | This enzyme cleaves the internal β1,4‐Gal linkage of antennal LacNAc's, and the resulting MS profiles offer additional insights into complex N‐glycan branching and terminal elaboration patterns. | [] | 91 |
PMC12503014 | Finally, the N‐glycans from purified IgG1‐Fc constructs produced in CHO‐S cells were also analyzed using MS and compared to previously published data for the same constructs produced in CHO‐K1 cells (Blundell et al. 2019, 2020). | [
{
"end": 73,
"label": "CellLine",
"start": 68,
"text": "CHO‐S"
},
{
"end": 192,
"label": "CellLine",
"start": 186,
"text": "CHO‐K1"
}
] | 92 |
PMC12503014 | We used MALDI‐MS to generate singly charged sodiated molecular ions ([M + Na]). | [] | 93 |
PMC12503014 | The MS spectra generated were then structurally annotated by mass fingerprinting and used to perform a semi‐quantitative analysis of relative intensities of different N‐glycan structures. | [] | 94 |
PMC12503014 | Our analysis was primarily focused on comparing the relative abundances of oligomannose N‐glycans and complex N‐glycans with variable levels of fucosylation, galactosylation, and sialylation and different branching patterns. | [] | 95 |
PMC12503014 | Furthermore, certain molecular ions detected in the MS spectra were analysed by MS/MS. | [] | 96 |
PMC12503014 | Through collisionally activated dissociation, MS/MS generates sequence‐informative fragment ions, which help to identify or confirm antennal structures, branching patterns, and linkage positions. | [] | 97 |
PMC12503014 | The low m/z range of the N‐glycan spectra of CHO‐K1, CHO‐S, CHO‐K1mAb, and CHO‐SmAb cells shows prominent signals corresponding oligomannose structures Man5GlcNAc2 to Man9GlcNAc2 (m/z 1579, 1783, 1988, 2192, and 2396), with a range of 70%–78% of summed monoisotopic peak intensities (see Figures 1 and 3, Table 2). | [
{
"end": 51,
"label": "CellLine",
"start": 45,
"text": "CHO‐K1"
},
{
"end": 58,
"label": "CellLine",
"start": 53,
"text": "CHO‐S"
},
{
"end": 69,
"label": "CellLine",
"start": 60,
"text": "CHO‐K1mAb"
},
{
"end": 83,
"label": "CellLine",
"start"... | 98 |
PMC12503014 | Additionally, the N‐glycomes of all the cell lines encompass a diverse array of complex N‐glycans, both with and without core fucose, featuring bi‐, tri‐, or tetra‐antennary branching (see Figures 2 and 3). | [] | 99 |
End of preview. Expand in Data Studio
README.md exists but content is empty.
- Downloads last month
- 38