ArticleScience advances2022
Surface Ig variable domain glycosylation affects autoantigen binding and acts as threshold for human autoreactive B cell activation.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
40 citing papers in PubMed, 69 citations in OpenAlex.
- Protective and Pathogenic Antibodies to Citrullinated Antigens.Immunological reviews · 2026Review
- Epigenetic regulation of B cell tolerance and dysfunction in autoimmune disease.Nature reviews. Immunology · 2026Review
- Anti-Modified Protein Antibodies in Rheumatoid Arthritis: Pathogenic, Protective, or Passive Bystander?Immunological reviews · 2026Review
- Site-specific profiling of structure and function of Igµ B cell receptor glycans.Nature communications · 2026Article
- IgG glycosylation dynamics in active lupus nephritis during the first year of immunosuppressive therapy.Frontiers in immunology · 2026Article
- Preclinical assessment of two FcγRI-specific antibodies that competitively inhibit immune complex-FcγRI binding to suppress autoimmune responses.Nature communications · 2025Article
- Recognition of Glycine Versus Nonglycine Citrulline Motifs Dictating the HLA Class II Association of Anticitrullinated Protein Antibodies: Insights From Autoantibody Profiling of 6,900 Scandinavian Patients With Rheumatoid Arthritis.Arthritis & rheumatology (Hoboken, N.J.) · 2025Article
- Modulation of immunoglobulin G oligomerization by variable domain glycans: A mechanism to regulate complement activation.PNAS nexus · 2025Article
- Altered IgGBiomedicines · 2025Article
- Elevated Fab glycosylation of autoantibodies maintained during B cell depletion therapy.Scientific reports · 2025Article
- Fc Proteoforms of ACPA IgG Discriminate Autoimmune Responses in Plasma and Synovial Fluid of Rheumatoid Arthritis Patients and Associate with Disease Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Anti-myeloperoxidase IgM B cells in anti-neutrophil cytoplasmic antibody-associated vasculitis.Nature communications · 2025Article
- Large-scale multicenter study reveals anticitrullinated SR-A peptide antibody as a biomarker and exacerbator for rheumatoid arthritis.Science advances · 2025Article
- Raider of the lostFrontiers in molecular biosciences · 2025Article
- GRB14: A prognostic biomarker driving tumor progression in gastric cancer through the PI3K/AKT signaling pathway by interacting with COBLL1.Open life sciences · 2025Article
- The evolutionary history of IGKC in mammals reveals ancient duplications and remarkable divergence in lagomorphs.Frontiers in immunology · 2025Article
- Deep sequencing of BCR heavy chain repertoires in myalgic encephalomyelitis/chronic fatigue syndrome.Frontiers in immunology · 2025Article
- Mitochondrial calcium shapes B cell signaling and mitochondrial function.Frontiers in immunology · 2025Article
- Distinct mucosal endotypes as initiators and drivers of rheumatoid arthritis.Nature reviews. Rheumatology · 2024Review
- The CH1 domain influences the expression and antigen sensing of the HIV-specific CH31 IgM-BCR and IgG-BCR.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
Corrections and comments
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Authors and funding
24 authors at 6 institutions in 5 countries.
Funding
Abstract
The hallmark autoantibodies in rheumatoid arthritis are characterized by variable domain glycans (VDGs). Their abundant occurrence results from the selective introduction of N-linked glycosylation sites during somatic hypermutation, and their presence is predictive for disease development. However, the functional consequences of VDGs on autoreactive B cells remain elusive. Combining crystallography, glycobiology, and functional B cell assays allowed us to dissect key characteristics of VDGs on human B cell biology. Crystal structures showed that VDGs are positioned in the vicinity of the antigen-binding pocket, and dynamic modeling combined with binding assays elucidated their impact on binding. We found that VDG-expressing B cell receptors stay longer on the B cell surface and that VDGs enhance B cell activation. These results provide a rationale on how the acquisition of VDGs might contribute to the breach of tolerance of autoreactive B cells in a major human autoimmune disease.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.