Modulating IgG effector function by Fc glycan engineering. - Wikidata - awgldk - TriplyDB

Modulating IgG effector function by Fc glycan engineering.

Modulating IgG effector function by Fc glycan engineering.

http://www.wikidata.org/entity/Q41677985

about

Fc-Galactosylation of Human Immunoglobulin Gamma Isotypes Improves C1q Binding and Enhances Complement-Dependent Cytotoxicity Improving Antibody-Based Cancer Therapeutics Through Glycan Engineering.Glycosylation of IgG-Fc: a molecular perspective.Modulating Cytotoxic Effector Functions by Fc Engineering to Improve Cancer Therapy Engineered Sialylation of Pathogenic Antibodies In Vivo Attenuates Autoimmune Disease.Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics.Preparation and biological activities of anti-HER2 monoclonal antibodies with fully core-fucosylated homogeneous bi-antennary complex-type glycans.Chemoenzymatic Glycan Remodeling of Natural and Recombinant Glycoproteins.Differential antibody glycosylation in autoimmunity: sweet biomarker or modulator of disease activity?Implementation of Glycan Remodeling to Plant-Made Therapeutic Antibodies.Designer α1,6-Fucosidase Mutants Enable Direct Core Fucosylation of Intact N-Glycopeptides and N-Glycoproteins.Modulation of IgG1 immunoeffector function by glycoengineering of the GDP-fucose biosynthesis pathway.One-pot enzymatic glycan remodeling of a therapeutic monoclonal antibody by endoglycosidase S (Endo-S) from Streptococcus pyogenes.Novel Concepts of Altered Immunoglobulin G Galactosylation in Autoimmune Diseases.Assessing the Heterogeneity of the Fc-Glycan of a Therapeutic Antibody Using an engineered FcγReceptor IIIa-Immobilized Column.Site-specific immobilization of endoglycosidases for streamlined chemoenzymatic glycan remodeling of antibodies.Antibody Engineering for Optimized Immunotherapy in Alzheimer's Disease.Acceptor range of endo-β-N-acetylglucosaminidase mutant endo-CC N180H: from monosaccharide to antibody.The Role of Fc Gamma Receptors in Broad Protection against Influenza Viruses Hapten-mediated recruitment of polyclonal antibodies to tumors engenders antitumor immunity MIgGGly (mouse IgG glycosylation analysis) - a high-throughput method for studying Fc-linked IgG N-glycosylation in mice with nanoUPLC-ESI-MS Improving Immunotherapy Through Glycodesign

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Modulating IgG effector function by Fc glycan engineering.

http://www.wikidata.org/entity/Q41677985

description

2017 nî lūn-bûn

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2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Modulating IgG effector function by Fc glycan engineering.

@en

type

label

Modulating IgG effector function by Fc glycan engineering.

@en

prefLabel

Modulating IgG effector function by Fc glycan engineering.

@en

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PNAS.1702173114

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Modulating IgG effector function by Fc glycan engineering

@en

P2093

David J DiLillo

http://www.w3.org/2001/XMLSchema#string

Jeffrey V Ravetch

http://www.w3.org/2001/XMLSchema#string

Lai-Xi Wang

http://www.w3.org/2001/XMLSchema#string

Stylianos Bournazos

http://www.w3.org/2001/XMLSchema#string

Tiezheng Li

http://www.w3.org/2001/XMLSchema#string

P2860

Broadly neutralizing hemagglutinin stalk-specific antibodies require FcγR interactions for protection against influenza virus in vivo

Unique carbohydrate-carbohydrate interactions are required for high affinity binding between Fc RIII and antibodies lacking core fucose

Engineering Hydrophobic Protein–Carbohydrate Interactions to Fine-Tune Monoclonal Antibodies

In vitro glycoengineering of IgG1 and its effect on Fc receptor binding and ADCC activity

FcgammaRIV: a novel FcR with distinct IgG subclass specificity

Fcgamma receptors as regulators of immune responses

Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity.

Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity.

Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc.

High-throughput IgG Fc N-glycosylation profiling by mass spectrometry of glycopeptides.

P304

3485-3490

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scholarly article

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10.1073/PNAS.1702173114

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13

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114

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28289219

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5380036

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