N-glycosylation of recombinant human interferon-gamma produced in different animal expression systems. - Wikidata - wikimedia - TriplyDB

N-glycosylation of recombinant human interferon-gamma produced in different animal expression systems.

N-glycosylation of recombinant human interferon-gamma produced in different animal expression systems.

http://www.wikidata.org/entity/Q30430759

about

Glycan engineering of proteins with whole living yeast cells expressing rat liver alpha2,3-sialytransferase in the porous cell wall.Baculovirus superinfection: a probable restriction factor on the surface display of proteins for library screening.In vivo protein crystallization in combination with highly brilliant radiation sources offers novel opportunities for the structural analysis of post-translationally modified eukaryotic proteins.Oligoadenylate synthetase/protein kinase R pathways and alphabeta TCR+ T cells are required for adenovirus vector: IFN-gamma inhibition of herpes simplex virus-1 in cornea.Analysis of the N-glycans of recombinant human Factor IX purified from transgenic pig milk Posttranslational processing of recombinant human interferon-gamma in animal expression systems.Monitoring proteolysis of recombinant human interferon-gamma during batch culture of Chinese hamster ovary cells.N-linked glycosylation of the liver cancer biomarker GP73 Expression of recombinant human interferon-γ with antiviral activity in the bi-cistronic baculovirus-insect/larval system.Na-butyrate increases the production and alpha2,6-sialylation of recombinant interferon-gamma expressed by alpha2,6- sialyltransferase engineered CHO cells.Overview of the baculovirus expression system.Expression of canine interferon-beta by a recombinant vaccinia virus.Release and preparation of intact and unreduced N-linked oligosaccharides from Sf-9 insect cells.Tetramerization domain of human butyrylcholinesterase is at the C-terminus.Peculiar monomeric interferon gammas, IFNγrel 1 and IFNγrel 2, in ginbuna crucian carp.Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle.Choice of cellular protein expression system.Genomic analysis of a hybridoma batch cell culture metabolic status in a standard laboratory 5 L bioreactor.Glycation and post-translational processing of human interferon-gamma expressed in Escherichia coli.Baculovirus Surface Display of Immunogenic Proteins for Vaccine Development

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P2860

N-glycosylation of recombinant human interferon-gamma produced in different animal expression systems.

http://www.wikidata.org/entity/Q30430759

description

1995 nî lūn-bûn

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1995 թուականի Յունիսին հրատարակուած գիտական յօդուած

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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N-glycosylation of recombinant ...... ent animal expression systems.

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Dobrovolsky VN

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Freedman RB

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Hoare M

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P2860

Assembly of asparagine-linked oligosaccharides

Clearing up glycoprotein hormones.

Site-specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorption mass spectrometry.

Structural analysis and localization of the carbohydrate moieties of a soluble human interferon gamma receptor produced in baculovirus-infected insect cells.

Recognition of complex oligosaccharides by the multi-subunit asialoglycoprotein receptor.

Glycosylation of recombinant proteins: problems and prospects.

Control of IgG/Fc glycosylation: a comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs.

Recombinant human interferon-gamma. Differences in glycosylation and proteolytic processing lead to heterogeneity in batch culture.

Identification, quantification, and characterization of glycopeptides in reversed-phase HPLC separations of glycoprotein proteolytic digests.

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592-596

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scholarly article

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10.1038/NBT0695-592

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6

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13

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1045381734

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