Results 71 to 80 of about 6,832 (204)

Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis [PDF]

open access: yes, 2009
Antibodies to citrulline-modifi ed proteins have a high diagnostic value in rheumatoid arthritis (RA). However, their biological role in disease development is still unclear.
Rikard Holmdahl   +46 more
core   +1 more source

A Secreted Bacterial Peptidylarginine Deiminase Can Neutralize Human Innate Immune Defenses

open access: yesmBio, 2018
The keystone oral pathogen Porphyromonas gingivalis is associated with severe periodontitis. Intriguingly, this bacterium is known to secrete large amounts of an enzyme that converts peptidylarginine into citrulline residues.
Tim Stobernack   +16 more
doaj   +1 more source

Host and bacterial factors linking periodontitis and rheumatoid arthritis

open access: yesFrontiers in Immunology, 2022
Observations from numerous clinical, epidemiological and serological studies link periodontitis with severity and progression of rheumatoid arthritis.
Anna Krutyhołowa   +7 more
doaj   +1 more source

Periodontitis and rheumatoid arthritis—Global efforts to untangle two complex diseases

open access: yesPeriodontology 2000, EarlyView.
Abstract Understanding the impact of oral health on rheumatoid arthritis (RA) will inform how best to manage patients with both periodontitis and RA. This review seeks to provide an update on interventional and mechanistic investigations, including a brief summary of European Research programs investigating the link between periodontitis and RA. Recent
Isabel Lopez‐Oliva   +2 more
wiley   +1 more source

Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis [PDF]

open access: yesBiochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2013
Peptidylarginine deiminases are a family of enzymes that mediate post-translational modifications of protein arginine residues by deimination or demethylimination to produce citrulline. In vitro, the activity of PADs is dependent on calcium and reductive reagents carrying a free sulfhydryl group.
Shu, Wang, Yanming, Wang
openaire   +2 more sources

Metabolic reprogramming of the immune response in periodontitis

open access: yesPeriodontology 2000, EarlyView.
Abstract Objective Periodontitis, a highly prevalent chronic inflammatory disease, is characterized by the progressive destruction of the tooth‐supporting tissues, ultimately causing tooth loss. In recent years, the emerging field of immunometabolism has revealed that immune cell function is tightly regulated by intracellular metabolic pathways that ...
Rafael Scaf de Molon   +3 more
wiley   +1 more source

ABAP: Antibody-based assay for peptidylarginine deiminase activity

open access: yesAnalytical Biochemistry, 2007
Members of the family of peptidylarginine deiminases (PADs, EC 3.5.3.15) catalyze the posttranslational modification of peptidylarginine into peptidylcitrulline. Citrulline-containing epitopes have been shown to be major and specific targets of autoantibodies produced by rheumatoid arthritis patients. Recently, the citrullination of histone proteins by
Zendman, A.J.W.   +9 more
openaire   +4 more sources

Comparison of changes in rheumatologic conditions between the patients with high and low anti-Porphyromonas gingivalis peptidylarginine deiminase (PPAD) immunoglobulin G (IgG) titers.

open access: yes, 2016
Comparison of changes in rheumatologic conditions between the patients with high and low anti-Porphyromonas gingivalis peptidylarginine deiminase (PPAD) immunoglobulin G (IgG) titers.
Tetsuo Kobayashi (807280)   +7 more
core   +1 more source

Regulation of p53 target gene expression by peptidylarginine deiminase 4 [PDF]

open access: yes, 2015
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.Histone Arg methylation has been correlated with transcriptional activation of p53 target genes.
Li, Pingxin   +7 more
core   +1 more source

Anti‐Carbamylated Protein Antibodies Stabilize Carbamylated Histone H3 to Promote Synovial Activation and Neutrophil Extracellular Trap‐Mediated Bone Loss in Rheumatoid Arthritis

open access: yesArthritis &Rheumatology, Volume 78, Issue 10, Page 2074-2081, October 2026.
Objective Carbamylation, a nonenzymatic post‐translational modification, contributes to rheumatoid arthritis (RA) pathogenesis. Anti‐carbamylated protein antibodies (anti‐CarP) occur in around 50% of patients with RA and associate with greater joint damage. Neutrophil extracellular traps (NETs) are a major source of carbamylated autoantigens. We sought
Shuichiro Nakabo   +9 more
wiley   +1 more source

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