Journal article
Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis
- Abstract:
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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...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 4.1MB)
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- Publisher copy:
- 10.1021/ja306068g
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Authors
Funding
+ Sir Henry Wellcome Postdoctoral Fellow
More from this funder
Funding agency for:
Bowden, T
Grant:
089026/Z/09/Z
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Bibliographic Details
- 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:
- 2012-10-01
- DOI:
- EISSN:
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1520-5126
- ISSN:
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0002-7863
- Source identifiers:
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353920
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:353920
- UUID:
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uuid:4f06077c-53dd-4e36-b0bf-9be13bba144c
- Local pid:
- pubs:353920
- Deposit date:
- 2013-11-16
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2012
- Notes:
- Copyright © 2012 American Chemical Society
- Licence:
- Other
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