ReviewNature reviews. Rheumatology2019
The structure, specificity and function of anti-citrullinated protein antibodies.
Review in Nature reviews. Rheumatology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.
- Diagnostic value of anti-citrullinated α-enolase peptide 1 antibody in patients with rheumatoid arthritis: A systematic review and meta-analysis.International journal of rheumatic diseases · 2021Pooled it
- Protective and Pathogenic Antibodies to Citrullinated Antigens.Immunological reviews · 2026Review
- Anti-Modified Protein Antibodies in Rheumatoid Arthritis: Pathogenic, Protective, or Passive Bystander?Immunological reviews · 2026Review
- Distinct HLA Associations for Antibody Multireactivity With Citrulline-Containing Type II Collagen Epitopes Versus More Limited Antibody Reactivity With Citrulline-Containing IgG Epitopes in Rheumatoid Arthritis.Arthritis & rheumatology (Hoboken, N.J.) · 2026Article
- The rheumatoid arthritis citrullinome is enriched in antigenic complement proteins.Arthritis research & therapy · 2026Article
- Rheumatoid factor and anti-citrullinated protein IgA antibodies in the diagnosis, prognosis and monitoring of patients with rheumatoid arthritis.Journal of translational autoimmunity · 2025Review
- Insights into the detection of AMPA cross-reactivity: comparing cyclic peptide- to protein-based assays.Arthritis research & therapy · 2025Article
- Virtual Probing on the Influence of CaCell biochemistry and biophysics · 2025Article
- Proteomic analysis of infiltrating neutrophils from rheumatoid arthritis synovial fluid and their contribution to protein carbamylation.Frontiers in immunology · 2025Article
- Helper T cells: A potential target for sex hormones to ameliorate rheumatoid arthritis? (Review).Molecular medicine reports · 2024Review
- B cells drive neuropathic pain-related behaviors in mice through IgG-Fc gamma receptor signaling.Science translational medicine · 2024Article
- The role of anti-citrullinated protein antibody in pathogenesis of RA.Clinical and experimental medicine · 2024Review
- The Lung in Rheumatoid Arthritis-Friend or Enemy?International journal of molecular sciences · 2024Review
- Review
- Seven-chain adaptive immune receptor repertoire analysis in rheumatoid arthritis reveals novel features associated with disease and clinically relevant phenotypes.Genome biology · 2024Article
- Exploring the Link between Hydrodynamic Size and Immunoglobulins of Circulating Immune Complexes in Rheumatoid Arthritis Patients.International journal of molecular sciences · 2024Article
- Immune tolerance of citrullinated peptides.Nature reviews. Rheumatology · 2024Article
- Review
- Breaking tolerance: autoantibodies can target protein posttranslational modifications.Current opinion in biotechnology · 2024Review
- The emerging role of neutrophil extracellular traps in the progression of rheumatoid arthritis.Frontiers in immunology · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this Perspectives article, we outline a proposed model for understanding the specificity and function of anti-citrullinated protein antibodies (ACPAs). We suggest that ACPAs vary in specificity between two extremes: some are 'promiscuous' in that they are highly specific for the citrulline side chain, but cross-react with a range of citrullinated peptides, whereas others are 'private' in that their recognition of citrulline as well as proximal amino acid side chains enables protein-specific interactions. Promiscuous ACPAs tend to dominate in the sera both before and after the onset of rheumatoid arthritis, but their functional role has not been clarified. No firm evidence exists that these ACPAs are pathogenic. By contrast, private ACPAs encompass antibodies that specifically recognize citrullinated epitopes on joint proteins or that cross-react with joint proteins, thereby opening up the possibility that these private ACPAs are arthritogenic. These joint-reactive antibodies are more likely to target joints by binding to joint tissues and to promote the formation of local immune complexes leading to bone erosions, pain and arthritis.
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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.