Fc Gamma Receptor Glycosylation Modulates the Binding of IgG Glycoforms: A Requirement for Stable Antibody Interactions-Reference-Cited by-同舟云学术

Fc Gamma Receptor Glycosylation Modulates the Binding of IgG Glycoforms: A Requirement for Stable Antibody Interactions

Published:2014-11-11 Issue:12 Volume:13 Page:5471-5485
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Hayes Jerrard M.¹²,Frostell Asa³,Cosgrave Eoin F. J.⁴,Struwe Weston B.⁵,Potter Oscar⁶,Davey Gavin P.¹,Karlsson Robert³,Anneren Cecilia³,Rudd Pauline M.²

Affiliation:

1. School of Biochemistry & Immunology, Trinity Biomedical Sciences Institute, Trinity College, Pearse St. Dublin 2, Dublin, Ireland

2. NIBRT-Glycoscience Group, NIBRT-The National Institute for Bioprocessing, Research, and Training, Foster Avenue, Blackrock, County Dublin, Ireland

3. GE Healthcare, Rapsgatan 23, SE-75184 Uppsala, Sweden

4. Pharmaceutical Life Sciences Group, Waters Corporation, 34 Maple Street, Milford, Massachusetts 01757, United States

5. Chemistry Research Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom

6. Agilent Technologies, Inc., 5301 Stevens Creek Boulevard, Santa Clara, California 95051, United States

Funder

GE Healthcare

National Institute for Bioprocessing, Research and Training

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/pr500414q

Reference43 articles.

1. Phagocytosis mediated by three distinct Fc gamma receptor classes on human leukocytes.

2. The increase in intracellular free calcium associated with IgG gamma 2b/gamma 1 Fc receptor-ligand interactions: role in phagocytosis.

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