Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose

By C. Ferrara, Sandra Grau, Christian Jäger, P. Sondermann, P. Brünker, I. Waldhauer, M. Hennig, A. Ruf, A. Rufer, M. Stihle and 2 more. Proceedings of the National Academy of Sciences of the United States of America, 2011

777 citations recorded by the source corpus.

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

View Paper: https://www.semanticscholar.org/paper/8e77c2ff456cc4eb231b1ed2d9d0867ef9fa8ef1

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Citations in the corpus

• IgG Subclasses and Allotypes: From Structure to Effector Functions (2014, background): “has pinpointed this interaction to be due to carbohydrate–carbohydrate interactions between the glycan on N297 of the heavy chain and glycosylation of FcγRIIIa at position 162 – a position unique to both FcγRIIIa and FcγRIIIb (46).”