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- Publications
- Influence
In Vitro Glycoengineering of IgG1 and Its Effect on Fc Receptor Binding and ADCC Activity
- Marco Thomann, T. Schlothauer, +5 authors D. Reusch
- Medicine, Chemistry
- PloS one
- 12 August 2015
The importance and effect of Fc glycosylation of monoclonal antibodies with regard to biological activity is widely discussed and has been investigated in numerous studies. Fc glycosylation of… Expand
Novel human IgG1 and IgG4 Fc-engineered antibodies with completely abolished immune effector functions.
- T. Schlothauer, S. Herter, +7 authors Ekkehard Moessner
- Chemistry, Medicine
- Protein engineering, design & selection : PEDS
- 1 October 2016
Recombinant human IgG antibodies (hIgGs) completely devoid of binding to Fcγ receptors (FcγRs) and complement protein C1q, and thus with abolished immune effector functions, are of use for various… Expand
Cell type-specific and site directed N-glycosylation pattern of FcγRIIIa.
- Anne Zeck, G. Pohlentz, T. Schlothauer, J. Peter-Katalinić, Jörg Thomas Regula
- Chemistry, Medicine
- Journal of proteome research
- 11 May 2011
Human leukocyte receptor IIIa (hFcγRIIIa) plays a prominent role in the elimination of tumor cells by antibody-based cancer therapies. In previous studies, a major impact of the presence of… Expand
Multi-Angle Effector Function Analysis of Human Monoclonal IgG Glycovariants
- Tetyana Dashivets, Marco Thomann, Petra Rüger, Alexander Knaupp, J. Buchner, T. Schlothauer
- Biology, Medicine
- PloS one
- 11 December 2015
Therapeutic performance of recombinant antibodies relies on two independent mechanisms: antigen recognition and Fc-mediated antibody effector functions. Interaction of Fc-fragment with different FcR… Expand
Analytical FcRn affinity chromatography for functional characterization of monoclonal antibodies
- T. Schlothauer, P. Rueger, +9 authors A. Papadimitriou
- Chemistry, Medicine
- mAbs
- 29 May 2013
The neonatal Fc receptor (FcRn) is important for the metabolic fate of IgG antibodies in vivo. Analysis of the interaction between FcRn and IgG in vitro might provide insight into the structural and… Expand
Functional assessment of antibody oxidation by native mass spectrometry
- Markus Haberger, Anna-Katharina Heidenreich, +10 authors Patrick Bulau
- Chemistry, Medicine
- mAbs
- 22 May 2015
Oxidation of methionine (Met) residues is one of several chemical degradation pathways for recombinant IgG1 antibodies. Studies using several methodologies have indicated that Met oxidation in the… Expand
A Two-pronged Binding Mechanism of IgG to the Neonatal Fc Receptor Controls Complex Stability and IgG Serum Half-life*
- P. F. Jensen, Angela Schoch, +4 authors K. Rand
- Chemistry, Medicine
- Molecular & Cellular Proteomics
- 6 January 2017
The success of recombinant monoclonal immunoglobulins (IgG) is rooted in their ability to target distinct antigens with high affinity combined with an extraordinarily long serum half-life, typically… Expand
Assessment of susceptible chemical modification sites of trastuzumab and endogenous human immunoglobulins at physiological conditions
- I. Schmid, Lea Bonnington, +12 authors Patrick Bulau
- Chemistry, Medicine
- Communications Biology
- 5 April 2018
The quality control testing of chemical degradations in the bio-pharmaceutical industry is currently under controversial debate. Here we have systematically applied in vitro and in vivo stress… Expand
Determination of critical quality attributes for monoclonal antibodies using quality by design principles.
- Nadja Alt, T. Zhang, +6 authors R. Harris
- Computer Science, Medicine
- Biologicals : journal of the International…
- 1 September 2016
TLDR
Assessment of chemical modifications of sites in the CDRs of recombinant antibodies
- Markus Haberger, Katrin Bomans, +15 authors Patrick Bulau
- Chemistry, Medicine
- mAbs
- 17 January 2014
Modifications like asparagine deamidation, aspartate isomerization, methionine oxidation, and lysine glycation are typical degradations for recombinant antibodies. For the identification and… Expand