Engineering Aglycosylated IgG Variants with Wild-Type or Improved Binding Affinity to Human Fc Gamma RIIA and Fc Gamma RIIIAs

Keyphrases

• Phagocytosis 100%
• Binding Affinity 100%
• Human IgG1 66%
• Lung Metastasis 66%
• Fcγ Receptor 66%
• Tumor Cells 33%
• Therapeutic Antibody 33%
• Low Affinity 33%
• Highly Sensitive 33%
• IgG1 Fc 33%
• Effector Function 33%
• Mathematical Model 33%
• Tumor Control 33%
• O-glycosylation 33%
• Glycosylation Site 33%
• Asparagine 33%
• Biophysical Properties 33%
• Expression System 33%
• N-linked Glycosylation 33%
• Main Drivers 33%
• Serum Half-life 33%
• B16F10 33%
• CH2 Domain 33%
• Fc Variants 33%
• Deuterium Incorporation 33%
• FG Loop 33%
• Deuterium Uptake 33%

Immunology and Microbiology

• Wild Type 100%
• Binding Affinity 100%
• Fc Receptor 66%
• Phagocytosis 66%
• Glycosylation 66%
• Immunoglobulin G1 66%
• Tumor Cell 33%
• Therapeutic Antibodies 33%
• Gene Expression System 33%
• Deglycosylation 33%
• Cell Phagocytosis 33%
• Plasma Half Life 33%

Biochemistry, Genetics and Molecular Biology

• Wild Type 100%
• Binding Affinity 100%
• Phagocytosis 66%
• Fc Receptor 66%
• N-Linked Glycosylation 66%
• Gene Expression System 33%
• Asparagine 33%
• Deglycosylation 33%
• Cell Phagocytosis 33%
• Plasma Half Life 33%
• Therapeutic Antibodies 33%