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Published in 2022 at "Biotechnology and Bioengineering"
DOI: 10.1002/bit.28066
Abstract: Glycosylation can be a critical quality attribute in biologic manufacturing. In particular, it has implications on the half‐life, immunogenicity, and pharmacokinetics of therapeutic monoclonal antibodies (mAbs), and must be closely monitored throughout drug development and…
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Keywords:
therapeutic antibody;
antibody glycosylation;
glycosylation;
downstream ... See more keywords
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2
Published in 2023 at "Chemical communications"
DOI: 10.1039/d3cc00672g
Abstract: A comprehensive structure-activity relationship study on antibody Fc-glycosylation has been performed using the chimeric anti-SSEA4 antibody chMC813-70 as a model. The α-2,6 sialylated biantennary complex type glycan was identified as the optimal Fc-glycan with significant…
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Keywords:
glycosylation optimal;
study antibody;
effector functions;
antibody glycosylation ... See more keywords
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Published in 2019 at "Glycobiology"
DOI: 10.1093/glycob/cwz048
Abstract: Abstract Protein N- and O-glycosylation are well known co- and post-translational modifications of immunoglobulins. Antibody glycosylation on the Fab and Fc portion is known to influence antigen binding and effector functions, respectively. To study associations…
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Keywords:
antibody glycosylation;
analysis;
monitoring immunoglobulin;
glycosylation ... See more keywords
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1
Published in 2022 at "Immunology"
DOI: 10.1111/imm.13481
Abstract: In this study we show that glycosylation is relevant for immune recognition of therapeutic antibodies, and that defined glycan structures can modulate immunogenicity. Concerns regarding immunogenicity arise from the high heterogeneity in glycosylation that is…
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Keywords:
recognition;
antigen recognition;
immunogenicity;
antibody glycosylation ... See more keywords