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A single glycan on IgE is indispensable for initiation of anaphylaxis.
A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs.
Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc.
Engineered Sialylation of Pathogenic Antibodies In Vivo Attenuates Autoimmune Disease.
Cis interaction between sialylated Fc?RIIA and the aI-domain of Mac-1 limits antibody-mediated neutrophil recruitment.
SIGN receptors and the antiinflammatory activity of sialylated IgG Fcs
Glycoengineering In Vivo
The role of differential IgG glycosylation in the interaction of antibodies with Fc?Rs in vivo.
Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity.
Novel Roles of IgE Glycosylation in Anaphylaxis
IgE Glycosylation in Health and Disease.
Sialylation of immunoglobulin E is a determinant of allergic pathogenicity.
Glycoengineering IgA1 in IgA nephropathy
Examining IgG4 sialylation as a gain of function post-translation modification in IgG4-related diseases
Harnessing the anti-inflammatory activity of extracellular sialylation of IgG.