about
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.Alternative molecular formats and therapeutic applications for bispecific antibodiesOptimizing antibody expression by using the naturally occurring framework diversity in a live bacterial antibody display systemIdentification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperoninsSustained Brown Fat Stimulation and Insulin Sensitization by a Humanized Bispecific Antibody Agonist for Fibroblast Growth Factor Receptor 1/βKlotho Complex.Efficient production of bispecific IgG of different isotypes and species of origin in single mammalian cells.Antitumor efficacy of a bispecific antibody that targets HER2 and activates T cells.Design and Pharmacokinetic Characterization of Novel Antibody Formats for Ocular Therapeutics.Precise quantification of mixtures of bispecific IgG produced in single host cells by liquid chromatography-Orbitrap high-resolution mass spectrometry.Evading pre-existing anti-hinge antibody binding by hinge engineering.Effector-attenuating Substitutions That Maintain Antibody Stability and Reduce Toxicity in Mice.Characterization of Chain Pairing Variants of Bispecific IgG Expressed in a Single Host Cell by High-Resolution Native and Denaturing Mass Spectrometry.A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.Tethered-variable CL bispecific IgG: an antibody platform for rapid bispecific antibody screening.High-resolution glycosylation site-engineering method identifies MICA epitope critical for shedding inhibition activity of anti-MICA antibodiesDeterminants of Translocation and Folding of TreF, a Trehalase ofEscherichia coliAvidity-based binding to HER2 results in selective killing of HER2-overexpressing cells by anti-HER2/CD3Single cell-produced and in vitro-assembled anti-FcRH5/CD3 T-cell dependent bispecific antibodies have similar in vitro and in vivo propertiesSusceptibility of Antibody CDR Residues to Chemical Modifications Can Be Revealed Prior to Antibody Humanization and Aid in the Lead Selection ProcessPrediction of methionine oxidation risk in monoclonal antibodies using a machine learning methodProduction, characterization, and in vivo half-life extension of polymeric IgA molecules in miceHigh-throughput antibody screening from complex matrices using intact protein electrospray mass spectrometry
P50
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P50
description
researcher, ORCID id # 0000-0002-0570-9700
@en
wetenschapper
@nl
name
Christoph Spiess
@ast
Christoph Spiess
@en
Christoph Spiess
@es
Christoph Spiess
@nl
type
label
Christoph Spiess
@ast
Christoph Spiess
@en
Christoph Spiess
@es
Christoph Spiess
@nl
prefLabel
Christoph Spiess
@ast
Christoph Spiess
@en
Christoph Spiess
@es
Christoph Spiess
@nl
P106
P31
P496
0000-0002-0570-9700