Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometry
about
Targeting FcRn for the modulation of antibody dynamicsThe neonatal Fc receptor, FcRn, as a target for drug delivery and therapyNanobody Technology: A Versatile Toolkit for Microscopic Imaging, Protein-Protein Interaction Analysis, and Protein Function Exploration.Cutting-edge mass spectrometry methods for the multi-level structural characterization of antibody-drug conjugates.Global and Local Conformation of Human IgG Antibody Variants Rationalizes Loss of Thermodynamic Stability.Charge-mediated Fab-Fc interactions in an IgG1 antibody induce reversible self-association, cluster formation, and elevated viscosity.Conformational Destabilization of Immunoglobulin G Increases the Low pH Binding Affinity with the Neonatal Fc Receptor.Associations between an IgG3 polymorphism in the binding domain for FcRn, transplacental transfer of malaria-specific IgG3, and protection against Plasmodium falciparum malaria during infancy: A birth cohort study in BeninInstant Integrated Ultradeep Quantitative-structural Membrane Proteomics Discovered Post-translational Modification Signatures for Human Cys-loop Receptor Subunit Bias.The Role of Electron Transfer Dissociation in Modern Proteomics.Conformational characterization of nerve growth factor-β reveals that its regulatory pro-part domain stabilizes three loop regions in its mature part.Mapping the Interactions of Selective Biochemical Probes of Antibody Conformation by Hydrogen-Deuterium Exchange Mass Spectrometry.A Two-pronged Binding Mechanism of IgG to the Neonatal Fc Receptor Controls Complex Stability and IgG Serum Half-life.Ligand binding and conformational dynamics in a flavin-based electron-bifurcating enzyme complex revealed by Hydrogen-Deuterium Exchange Mass Spectrometry.A human endothelial cell-based recycling assay for screening of FcRn targeted molecules.Quantitative analysis of glycation and its impact on antigen binding.Changes in complementarity-determining regions significantly alter IgG binding to the neonatal Fc receptor (FcRn) and pharmacokinetics.Higher-order structural interrogation of antibodies using middle-down hydrogen/deuterium exchange mass spectrometry.Impact of Glycosylation on the Local Backbone Flexibility of Well-Defined IgG1-Fc Glycoforms Using Hydrogen Exchange-Mass Spectrometry
P2860
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P2860
Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometry
description
2014 nî lūn-bûn
@nan
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Investigating the interaction ...... ium exchange mass spectrometry
@ast
Investigating the interaction ...... ium exchange mass spectrometry
@en
Investigating the interaction ...... ium exchange mass spectrometry
@nl
type
label
Investigating the interaction ...... ium exchange mass spectrometry
@ast
Investigating the interaction ...... ium exchange mass spectrometry
@en
Investigating the interaction ...... ium exchange mass spectrometry
@nl
prefLabel
Investigating the interaction ...... ium exchange mass spectrometry
@ast
Investigating the interaction ...... ium exchange mass spectrometry
@en
Investigating the interaction ...... ium exchange mass spectrometry
@nl
P2093
P2860
P356
P1476
Investigating the interaction ...... ium exchange mass spectrometry
@en
P2093
Hubert Kettenberger
Maximiliane Hilger
Pernille Foged Jensen
Tilman Schlothauer
Vincent Larraillet
P2860
P304
P356
10.1074/MCP.M114.042044
P577
2014-11-06T00:00:00Z