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Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

http://www.wikidata.org/entity/Q37068434

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Engineered IgG1-Fc--one fragment to bind them all Fc glycans of therapeutic antibodies as critical quality attributes Translating basic mechanisms of IgG effector activity into next generation cancer therapies Selective Deactivation of Serum IgG: A General Strategy for the Enhancement of Monoclonal Antibody Receptor Interactions Engineering Hydrophobic Protein–Carbohydrate Interactions to Fine-Tune Monoclonal Antibodies Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies Advances in Therapeutic Fc Engineering - Modulation of IgG-Associated Effector Functions and Serum Half-life Advances in Antibody Design Enhanced potency of a fucose-free monoclonal antibody being developed as an Ebola virus immunoprotectant.Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells.Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system.Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements.Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: a FACS-based, high-throughput selection and analytical tool.Therapeutic antibody engineering by high efficiency cell screening.Chimeric antigen receptors with mutated IgG4 Fc spacer avoid fc receptor binding and improve T cell persistence and antitumor efficacy Automated pipeline for rapid production and screening of HIV-specific monoclonal antibodies using pichia pastoris A switchable yeast display/secretion system Lepidopteran cells, an alternative for the production of recombinant antibodies?The Structural Role of Antibody N-Glycosylation in Receptor Interactions Efficient expression of full-length antibodies in the cytoplasm of engineered bacteria.Chemoenzymatic glycoengineering of intact IgG antibodies for gain of functions.Structural insights into the interaction of human IgG1 with FcγRI: no direct role of glycans in binding.Revisiting the role of glycosylation in the structure of human IgG Fc.Structural characterization of GASDALIE Fc bound to the activating Fc receptor FcγRIIIa.Structure and function of immunoglobulins Recombinant antibodies: engineering and production in yeast and bacterial hosts.Novel roles for the IgG Fc glycan.Fc receptor-targeted therapies for the treatment of inflammation, cancer and beyond.Quality attributes of recombinant therapeutic proteins: an assessment of impact on safety and efficacy as part of a quality by design development approach.Molecular engineering of antibodies for therapeutic and diagnostic purposes.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease.Unnatural amino acids in novel antibody conjugates.Inhibitory Fcγ receptor engagement drives adjuvant and anti-tumor activities of agonistic CD40 antibodies.Structural analysis of Fc/FcγR complexes: a blueprint for antibody design.Engineering Aglycosylated IgG Variants with Wild-Type or Improved Binding Affinity to Human Fc Gamma RIIA and Fc Gamma RIIIAs.Engineering broadly neutralizing antibodies for HIV prevention and therapy.A monoclonal antibody against hinge-cleaved IgG restores effector function to proteolytically-inactivated IgGs in vitro and in vivo.Immunoglobulin Glycosylation Effects in Allergy and Immunity.

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P2860

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

http://www.wikidata.org/entity/Q37068434

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 12 December 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

@en

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors.

@nl

type

label

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

@en

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors.

@nl

prefLabel

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

@en

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors.

@nl

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PNAS.0809257105

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

P1476

Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors

@en

P2093

Jeffrey V Ravetch

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

K Dane Wittrup

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

Nathaniel W Silver

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

René G Ott

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

Stephen L Sazinsky

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

P2860

Immunotherapy: past, present and future

Role of oligosaccharide residues of IgG1-Fc in Fc gamma RIIb binding

Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa

Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha

The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex

The structure of a human type III Fcgamma receptor in complex with Fc

Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity

Structural characterization of a mutated, ADCC-enhanced human Fc fragment

Fcgamma receptors as regulators of immune responses

The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms.

P304

20167-20172

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scholarly article

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10.1073/PNAS.0809257105

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51

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105

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2008-12-12T00:00:00Z

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23655172

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19074274

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2629253

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