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anti-citrullinated protein antibodies
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Antigen-specific Fab profiling achieves molecular-resolution analysis of human autoantibody repertoires in rheumatoid arthritis
N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line
A photoaffinity glycan-labeling approach to investigate immunoglobulin glycan-binding partners
Effect of antigen valency on autoreactive B-cell targeting
IgG Fab glycans hinder FcRn-mediated placental transport
Bitter Sweet Symphony
Glycobiology of rheumatic diseases
At Critically Low Antigen Densities, IgM Hexamers Outcompete Both IgM Pentamers and IgG1 for Human Complement Deposition and Complement-Dependent Cytotoxicity
IgG anti-citrullinated protein antibody variable domain glycosylation increases before the onset of rheumatoid arthritis and stabilizes thereafter
Surface Ig variable domain glycosylation affects autoantigen binding and acts as threshold for human autoreactive B cell activation
Surface Ig variable domain glycosylation affects autoantigen binding and acts as threshold for human autoreactive B cell activation
Cross-reactivity of IgM anti-modified protein antibodies in rheumatoid arthritis despite limited mutational load
Genetic predisposition (HLA-SE) is associated with ACPA-IgG variable domain glycosylation in the predisease phase of RA
Onset of rheumatoid arthritis after COVID-19: coincidence or connected?
Checkpoints controlling the induction of B cell mediated autoimmunity in human autoimmune diseases
Antibodies and B cells recognising citrullinated proteins display a broad cross-reactivity towards other post-translational modifications
On the presence of HLA-SE alleles and ACPA-IgG variable domain glycosylation in the phase preceding the development of rheumatoid arthritis
On the presence of HLA-SE alleles and ACPA-IgG variable domain glycosylation in the phase preceding the development of rheumatoid arthritis
Different classes of anti-modified protein antibodies are induced on exposure to antigens expressing only one type of modification