Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics.
about
Key factors influencing ADME properties of therapeutic proteins: A need for ADME characterization in drug discovery and developmentImpact of SPR biosensor assay configuration on antibody: Neonatal Fc receptor binding data.Evaluating the Use of Antibody Variable Region (Fv) Charge as a Risk Assessment Tool for Predicting Typical Cynomolgus Monkey PharmacokineticsPharmacokinetic properties of IgG and various Fc fusion proteins in mice.Aberrant bispecific antibody pharmacokinetics linked to liver sinusoidal endothelium clearance mechanism in cynomolgus monkeysBiophysical properties of the clinical-stage antibody landscape.Half-life extended biotherapeutics.Biological therapy targeting the IL-23/IL-17 axis in inflammatory bowel disease.Pharmacokinetics of monoclonal antibodies and Fc-fusion proteins.Assessment of disulfide and hinge modifications in monoclonal antibodiesPharmacokinetic de-risking tools for selection of monoclonal antibody lead candidates.Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo.Target-independent variable region mediated effects on antibody clearance can be FcRn independent.The interplay of non-specific binding, target-mediated clearance and FcRn interactions on the pharmacokinetics of humanized antibodies.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 role for macromolecular crowding in off-target binding of therapeutic antibodies.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.Modulation of protein A binding allows single-step purification of mouse bispecific antibodies that retain FcRn binding.Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics.
P2860
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P2860
Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Charge-mediated influence of t ...... Rn-dependent pharmacokinetics.
@ast
Charge-mediated influence of t ...... Rn-dependent pharmacokinetics.
@en
type
label
Charge-mediated influence of t ...... Rn-dependent pharmacokinetics.
@ast
Charge-mediated influence of t ...... Rn-dependent pharmacokinetics.
@en
prefLabel
Charge-mediated influence of t ...... Rn-dependent pharmacokinetics.
@ast
Charge-mediated influence of t ...... Rn-dependent pharmacokinetics.
@en
P2093
P2860
P356
P1476
Charge-mediated influence of t ...... cRn-dependent pharmacokinetics
@en
P2093
Angela Schoch
Gerhard Winter
Hubert Kettenberger
Julia Engert
Julia Heinrich
Olaf Mundigl
P2860
P304
P356
10.1073/PNAS.1408766112
P407
P577
2015-04-27T00:00:00Z