Comparative Study of the N-Glycans of Human Monoclonal Immunoglobulins M Produced by Hybridoma and Parental Cells
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing FcγRI and/or FcγRII receptors
2. Biological significance of carbohydrate chains on monoclonal antibodies.
Cited by 8 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Quantitative isomer-specific N-glycan fingerprinting using isotope coded labeling and high performance liquid chromatography–electrospray ionization-mass spectrometry with graphitic carbon stationary phase;Journal of Chromatography A;2015-02
2. Roles for major histocompatibility complex glycosylation in immune function;Seminars in Immunopathology;2012-03-30
3. Human Follicular Lymphoma Cells Contain Oligomannose Glycans in the Antigen-binding Site of the B-cell Receptor;Journal of Biological Chemistry;2007-03
4. Human Serum IgM Glycosylation;Journal of Biological Chemistry;2005-08
5. Site-specific characterization of the N-linked oligosaccharides of a murine immunoglobulin M by high-performance liquid chromatography/electrospray mass spectrometry;Analytical Biochemistry;2003-03
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