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N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line
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
Anti Citrullinated Protein Antibodies-IgG variable domain glycosylation in rheumatoid arthritis
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
N-Linked Glycans in the Variable Domain of IgG Anti-Citrullinated Protein Antibodies Predict the Development of Rheumatoid Arthritis
Different classes of anti-modified protein antibodies are induced on exposure to antigens expressing only one type of modification
Response to: 'Acquiring new N-glycosylation sites in variable regions of immunoglobulin genes by somatic hypermutation is a common feature of autoimmune diseases' by Visser et al
ACPA IgG galactosylation associates with disease activity in pregnant patients with rheumatoid arthritis
The extensive glycosylation of the ACPA variable domain observed for ACPA-IgG is absent from ACPA-IgM
HappyTools: A software for high-throughput HPLC data processing and quantitation
The extensive glycosylation of the ACPA variable domain observed for ACPA-IgG is absent from ACPA-IgM
B-cell receptor sequencing of anti-citrullinated protein antibody (ACPA) IgG-expressing B cells indicates a selective advantage for the introduction of N-glycosylation sites during somatic hypermutation
Adaptive antibody diversification through N-linked glycosylation of the immunoglobulin variable region
Variable domain glycosylation of ACPA-IgG: A missing link in the maturation of the ACPA response?
B Cell Receptor Sequencing of Anti-Citrullinated Protein Antibody Expressing B Cells Indicates a Selective Advantage for the Introduction of N-Glycosylation Sites during Somatic Hypermutation
REDUCED INCREASE OF ACPA IGG-FC GALACTOSYLATION DURING PREGNANCY IN COMPARISON TO TOTAL IGG: AN EXPLANATION WHY AUTOANTIBODY POSITIVE RA-PATIENTS IMPROVE LESS DURING PREGNANCY?
N-GLYCOSYLATION SITES IN THE VARIABLE DOMAIN OF B CELL RECEPTORS SPECIFIC FOR CITRULLINATED ANTIGENS

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