Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity.

By S. Krapp, Y. Mimura, R. Jefferis, R. Huber, P. Sondermann. Journal of Molecular Biology, 2003

665 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/0f10ef688bef2654eafffdf89e94d298f3fceba4

How researchers see this paper

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In Immunology

1. I. Waldhauer

In Molecular Biology

1. A. Teplyakov
2. Gary Gilliland
3. Dennis R. Goulet
4. M. Chiu

In Radiology, Nuclear Medicine and Imaging

1. A. Teplyakov
2. Gary Gilliland
3. Dennis R. Goulet
4. M. Chiu

Citations in the corpus

• Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose (2011, background): “By incrementally truncating the Fc-oligosaccharides, it was shown that the decreased interactions with FcγRs result from increased conformational changes in the individual CH2 domains and from a “closed” Fc conformation generated through a mutual approach of both CH2 domains (5).”
• Antibody Structure and Function: The Basis for Engineering Therapeutics (2019, background): “Several Fc crystal structures with different glycoform variants [65,71,72] and aglycosylated forms [73,74] have been reported.”