Role of glycosylation on the secretion and biological activity of erythropoietin.
about
Development and characterization of novel erythropoiesis stimulating protein (NESP)Glycoengineering of interferon-β 1a improves its biophysical and pharmacokinetic propertiesAsn to Lys mutations at three sites which are N-glycosylated in the mammalian protein decrease the aggregation of Escherichia coli-derived erythropoietin.Effect of active oxygen radicals on protein and carbohydrate moieties of recombinant human erythropoietin.Erythropoietin and cancer: the unintended consequences of anemia correctionQuality of original and biosimilar epoetin productsProbing polypeptide GalNAc-transferase isoform substrate specificities by in vitro analysis2D-LC analysis of BRP 3 erythropoietin N-glycosylation using anion exchange fractionation and hydrophilic interaction UPLC reveals long poly-N-acetyl lactosamine extensions.The influence of artificially introduced N-glycosylation sites on the in vitro activity of Xenopus laevis erythropoietin.Analytical detection and characterization of biopharmaceutical glycosylation by MS.Automated synthesis of oligosaccharides as a basis for drug discovery.Post-translational modifications in the context of therapeutic proteins.Mammalian α-1,6-Fucosyltransferase (FUT8) Is the Sole Enzyme Responsible for the N-Acetylglucosaminyltransferase I-independent Core Fucosylation of High-mannose N-GlycansThe Golgi CMP-sialic acid transporter: A new CHO mutant provides functional insightsMicrobial glucoamylases: characteristics and applications.Current state and perspectives on erythropoietin production.Prospects in the total synthesis of protein therapeutics.Structural identification of modified amino acids on the interface between EPO and its receptor from EPO BRP, human recombinant erythropoietin by LC/MS analysis.Glycan Remodeling of Human Erythropoietin (EPO) Through Combined Mammalian Cell Engineering and Chemoenzymatic Transglycosylation.Roles of silkworm endoplasmic reticulum chaperones in the secretion of recombinant proteins expressed by baculovirus system.RNAi suppression of β-N-acetylglucosaminidase (BmFDL) for complex-type N-linked glycan synthesis in cultured silkworm cells.Plant-produced human recombinant erythropoietic growth factors support erythroid differentiation in vitro.Cellular trafficking and degradation of erythropoietin and novel erythropoiesis stimulating protein (NESP).Engineering of sialylated mucin-type O-glycosylation in plants.Neuroprotection of photoreceptors by direct delivery of erythropoietin to the retina of the retinal degeneration slow mouse.Enhanced erythropoietin heterogeneity in a CHO culture is caused by proteolytic degradation and can be eliminated by a high glutamine levelStructural Identification of a Non-Glycosylated Variant at Ser126 for O-Glycosylation Site from EPO BRP, Human Recombinant Erythropoietin by LC/MS Analysis.Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stabilitySubstitution of asparagine residues in Aspergillus awamori glucoamylase by site-directed mutagenesis to eliminate N-glycosylation and inactivation by deamidation.Structural requirements for additional N-linked carbohydrate on recombinant human erythropoietin.Choice of cellular protein expression system.Effect of hydrocortisone on the production and glycosylation of an Fc-fusion protein in CHO cell cultures.The zebrafish erythropoietin: functional identification and biochemical characterization.Chemoenzymatic Glycan Remodeling of Natural and Recombinant Glycoproteins.Platforms for Recombinant Therapeutic Glycoprotein Production.Sensitive and comprehensive analysis of O-glycosylation in biotherapeutics: a case study of novel erythropoiesis stimulating protein.High-level expression of secreted complex glycosylated recombinant human erythropoietin in the Physcomitrella Delta-fuc-t Delta-xyl-t mutant.Genetic disruption of multiple α1,2-mannosidases generates mammalian cells producing recombinant proteins with high-mannose-type N-glycans.
P2860
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P2860
Role of glycosylation on the secretion and biological activity of erythropoietin.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Role of glycosylation on the secretion and biological activity of erythropoietin.
@en
type
label
Role of glycosylation on the secretion and biological activity of erythropoietin.
@en
prefLabel
Role of glycosylation on the secretion and biological activity of erythropoietin.
@en
P2093
P356
P1433
P1476
Role of glycosylation on the secretion and biological activity of erythropoietin.
@en
P2093
Jacobsen F
Lorenzini T
P304
P356
10.1021/BI00156A003
P407
P577
1992-10-01T00:00:00Z