- Abstract:
-
Human IgG Fc glycosylation modulates immunological effector functions such as antibody-dependent cellular cytotoxicity and phagocytosis. Engineering of Fc glycans therefore enables fine-tuning of the therapeutic properties of monoclonal antibodies. The N-linked glycans of Fc are typically complex-type, forming a network of noncovalent interactions along the protein surface of the Cγ2 domain. Here, we manipulate the mammalian glycan-processing pathway to trap IgG1 Fc at sequential stages of ma...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 4.1MB)
-
- Publisher copy:
- 10.1021/ja306068g
-
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- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Journal of the American Chemical Society Journal website
- Volume:
- 134
- Issue:
- 42
- Pages:
- 17554-17563
- Publication date:
- 2012-10-05
- DOI:
- EISSN:
-
1520-5126
- ISSN:
-
0002-7863
- URN:
-
uuid:4f06077c-53dd-4e36-b0bf-9be13bba144c
- Source identifiers:
-
353920
- Local pid:
- pubs:353920
- Language:
- English
- Keywords:
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2012
- Notes:
- Copyright © 2012 American Chemical Society
Journal article
Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis
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