Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG
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Engineering a Monomeric Fc Domain Modality by N-Glycosylation for the Half-life Extension of BiotherapeuticsOpening the door to innovationResolving the micro-heterogeneity and structural integrity of monoclonal antibodies by hybrid mass spectrometric approachesQUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Generation and Characterization of an IgG4 Monomeric Fc Platform.Production of α2,6-sialylated IgG1 in CHO cellsEndo-F3 Glycosynthase Mutants Enable Chemoenzymatic Synthesis of Core-fucosylated Triantennary Complex Type Glycopeptides and Glycoproteins.Production of stable bispecific IgG1 by controlled Fab-arm exchange: scalability from bench to large-scale manufacturing by application of standard approaches.Consequences of glycan truncation on Fc structural integrity.The role of structural proteomics in vaccine development: recent advances and future prospects.Fc Engineering of Human IgG1 for Altered Binding to the Neonatal Fc Receptor Affects Fc Effector Functions.Aspergillus niger Prolyl Endoprotease for Hydrogen-Deuterium Exchange Mass Spectrometry and Protein Structural Studies.Lysine conjugation properties in human IgGs studied by integrating high-resolution native mass spectrometry and bottom-up proteomics.In-depth qualitative and quantitative analysis of composite glycosylation profiles and other micro-heterogeneity on intact monoclonal antibodies by high-resolution native mass spectrometry using a modified OrbitrapCorrelations between changes in conformational dynamics and physical stability in a mutant IgG1 mAb engineered for extended serum half-life.Epitope characterization of anti-JAM-A antibodies using orthogonal mass spectrometry and surface plasmon resonance approaches.Impact of Glycosylation on the Local Backbone Flexibility of Well-Defined IgG1-Fc Glycoforms Using Hydrogen Exchange-Mass Spectrometry
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P2860
Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 13 February 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
Mutation of Y407 in the CH3 do ...... ion and structure of human IgG
@en
Mutation of Y407 in the CH3 do ...... on and structure of human IgG.
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type
label
Mutation of Y407 in the CH3 do ...... ion and structure of human IgG
@en
Mutation of Y407 in the CH3 do ...... on and structure of human IgG.
@nl
prefLabel
Mutation of Y407 in the CH3 do ...... ion and structure of human IgG
@en
Mutation of Y407 in the CH3 do ...... on and structure of human IgG.
@nl
P2093
P2860
P356
P1476
Mutation of Y407 in the CH3 do ...... ion and structure of human IgG
@en
P2093
Albert J R Heck
Ewald T J van den Bremer
Janine Schuurman
Patrick H C van Berkel
Paul W H I Parren
Rebecca J Rose
P2860
P304
P356
10.4161/MABS.23532
P577
2013-02-13T00:00:00Z