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- Lai-Xi Wang
- Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA;, , , ,
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- Xin Tong
- Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA;, , , ,
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- Chao Li
- Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA;, , , ,
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- John P. Giddens
- Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA;, , , ,
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- Tiezheng Li
- Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA;, , , ,
説明
<jats:p>Antibodies are immunoglobulins that play essential roles in immune systems. All antibodies are glycoproteins that carry at least one or more conserved N-linked oligosaccharides ( N-glycans) at the Fc domain. Many studies have demonstrated that both the presence and fine structures of the attached glycans can exert a profound impact on the biological functions and therapeutic efficacy of antibodies. However, antibodies usually exist as mixtures of heterogeneous glycoforms that are difficult to separate in pure glycoforms. Recent progress in glycoengineering has provided useful methods that enable production of glycan-defined and site-selectively modified antibodies for functional studies and for improved therapeutic efficacy. This review highlights major approaches in glycoengineering of antibodies with a focus on recent advances in three areas: glycoengineering through glycan biosynthetic pathway manipulation, glycoengineering through in vitro chemoenzymatic glycan remodeling, and glycoengineering of antibodies for site-specific antibody–drug conjugation.</jats:p>
収録刊行物
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- Annual Review of Biochemistry
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Annual Review of Biochemistry 88 (1), 433-459, 2019-06-20
Annual Reviews
