标题
Pharmacokinetic properties of IgG and various Fc fusion proteins in mice
作者
关键词
-
出版物
mAbs
Volume 8, Issue 1, Pages 120-128
出版商
Informa UK Limited
发表日期
2015-10-30
DOI
10.1080/19420862.2015.1113360
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- A novel in vitro assay to predict neonatal Fc receptor-mediated human IgG half-life
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- Fc fusion as a platform technology: potential for modulating immunogenicity
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- Engineered Fc based antibody domains and fragments as novel scaffolds
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- Engineered antibodies for molecular imaging of cancer
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- Monoclonal Antibodies with Identical Fc Sequences Can Bind to FcRn Differentially with Pharmacokinetic Consequences
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- Robust recombinant FcRn production in mammalian cells enabling oriented immobilization for IgG binding studies
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- Importance of Neonatal FcR in Regulating the Serum Half-Life of Therapeutic Proteins Containing the Fc Domain of Human IgG1: A Comparative Study of the Affinity of Monoclonal Antibodies and Fc-Fusion Proteins to Human Neonatal FcR
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- The effects of affinity and valency of an albumin-binding domain (ABD) on the half-life of a single-chain diabody-ABD fusion protein
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- Effects of glycosylation on the stability of protein pharmaceuticals
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