Analytical FcRn affinity chromatography for functional characterization of monoclonal antibodies.
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The neonatal Fc receptor, FcRn, as a target for drug delivery and therapyIn vitro glycoengineering of IgG1 and its effect on Fc receptor binding and ADCC activityOxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodiesImpact of SPR biosensor assay configuration on antibody: Neonatal Fc receptor binding data.Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometryCharge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics.Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants.Targeting key angiogenic pathways with a bispecific CrossMAb optimized for neovascular eye diseases.A novel approach to investigate the effect of methionine oxidation on pharmacokinetic properties of therapeutic antibodies.Functional assessment of antibody oxidation by native mass spectrometry.Assessment of chemical modifications of sites in the CDRs of recombinant antibodies: Susceptibility vs. functionality of critical quality attributes.Novel human IgG1 and IgG4 Fc-engineered antibodies with completely abolished immune effector functions.Toward in vitro-to-in vivo translation of monoclonal antibody pharmacokinetics: Application of a neonatal Fc receptor-mediated transcytosis assay to understand the interplaying clearance mechanisms.Pharmacokinetic de-risking tools for selection of monoclonal antibody lead candidates.Target-independent variable region mediated effects on antibody clearance can be FcRn independent.Conformational Destabilization of Immunoglobulin G Increases the Low pH Binding Affinity with the Neonatal Fc Receptor.Enrichment of high affinity subclasses and glycoforms from serum-derived IgG using FcγRs as affinity ligands.A Two-pronged Binding Mechanism of IgG to the Neonatal Fc Receptor Controls Complex Stability and IgG Serum Half-life.Evaluation of an FcRn affinity chromatographic method for IgG1-type antibodies and evaluation of IgG variants.A human endothelial cell-based recycling assay for screening of FcRn targeted molecules.Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics.Assessment of susceptible chemical modification sites of trastuzumab and endogenous human immunoglobulins at physiological conditions
P2860
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P2860
Analytical FcRn affinity chromatography for functional characterization of monoclonal antibodies.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 29 May 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@en
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@nl
type
label
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@en
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@nl
prefLabel
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@en
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@nl
P2093
P2860
P356
P1476
Analytical FcRn affinity chrom ...... tion of monoclonal antibodies.
@en
P2093
Apollon Papadimitriou
Felix Fingas
Georg Drabner
Hubert Hertenberger
Jan Olaf Stracke
Johannes Auer
Lothar Kling
Petra Rueger
Stefan Koch
Stefan Seeber
P2860
P304
P356
10.4161/MABS.24981
P577
2013-05-29T00:00:00Z