The presence of citrullinated proteins is not specific for rheumatoid synovial tissue. - Wikidata - awgldk - TriplyDB

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

http://www.wikidata.org/entity/Q45141270

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Antibodies to citrullinated proteins and differences in clinical progression of rheumatoid arthritis Citrullinated proteins have increased immunogenicity and arthritogenicity and their presence in arthritic joints correlates with disease severity Psoriatic arthritis synovial histopathology: commentary on the article by Kruithof and colleagues The role of citrullinated protein antibodies in predicting erosive disease in rheumatoid arthritis: a systematic literature review and meta-analysis Citrullination-dependent differential presentation of a self-peptide by HLA-B27 subtypes Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis Identification of novel citrullinated autoantigens of synovium in rheumatoid arthritis using a proteomic approach Multinational evidence-based recommendations on how to investigate and follow-up undifferentiated peripheral inflammatory arthritis: integrating systematic literature research and expert opinion of a broad international panel of rheumatologists in t Features of the synovium of individuals at risk of developing rheumatoid arthritis: implications for understanding preclinical rheumatoid arthritis The prevalence and diagnostic performance of anti-cyclic citrullinated peptide antibody in rheumatoid arthritis: the predictive and discriminative ability of serum antibody level in recognizing rheumatoid arthritis.Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and α-enolase: implications for autoimmunity in rheumatoid arthritis Role of anti-citrullinated protein antibodies in diagnosis and prognosis of rheumatoid arthritis.Anti-citrullinated protein antibodies and their clinical utility in rheumatoid arthritis.Relationship between anti-CCP antibodies and oxidant and anti-oxidant activity in patients with rheumatoid arthritis Functional haplotypes of PADI4: relevance for rheumatoid arthritis specific synovial intracellular citrullinated proteins and anticitrullinated protein antibodies Cytokines pre-determined by genetic factors are involved in pathogenesis of Rheumatoid arthritis.Local administration of glucocorticoids decreases synovial citrullination in rheumatoid arthritis.Myocardial citrullination in rheumatoid arthritis: a correlative histopathologic study.Autoimmunity against fibrinogen mediates inflammatory arthritis in mice.Changes in proliferation kinetics of T cells: a new predictive cellular biomarkers for early rheumatoid arthritis?Development of synthetic anti-cyclic citrullinated peptide antibody and its arthritogenic role.Citrullinated calreticulin potentiates rheumatoid arthritis shared epitope signaling.Posttranslational Protein Modification in the Salivary Glands of Sjögren's Syndrome Patients.Identification of a novel chemokine-dependent molecular mechanism underlying rheumatoid arthritis-associated autoantibody-mediated bone loss.Release of Active Peptidyl Arginine Deiminases by Neutrophils Can Explain Production of Extracellular Citrullinated Autoantigens in Rheumatoid Arthritis Synovial Fluid Citrullination by peptidylarginine deiminase in rheumatoid arthritis.Anti-CCP2 antibodies: an overview and perspective of the diagnostic abilities of this serological marker for early rheumatoid arthritis.The Clinical Application of Anti-CCP in Rheumatoid Arthritis and Other Rheumatic Diseases.Rheumatoid arthritis and smoking: putting the pieces together PADI4 haplotypes in association with RA Mexican patients, a new prospect for antigen modulation.Heightened immune response to autocitrullinated Porphyromonas gingivalis peptidylarginine deiminase: a potential mechanism for breaching immunologic tolerance in rheumatoid arthritis.Musculoskeletal manifestations of inflammatory bowel disease.Utility of synovial biopsy.The relevance of citrullinated vimentin in the production of antibodies against citrullinated proteins and the pathogenesis of rheumatoid arthritis.Citrullination of autoantigens: upstream of TNFα in the pathogenesis of rheumatoid arthritis.Anti-citrullinated protein antibodies (ACPA) in early rheumatoid arthritis.Should rheumatoid factor in rheumatoid arthritis be sent to Davy Jones's Locker?Pre-rheumatoid arthritis: predisposition and transition to clinical synovitis.Inflammation and rheumatoid arthritis.

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P2860

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

http://www.wikidata.org/entity/Q45141270

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

name

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@en

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@nl

type

label

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@en

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@nl

prefLabel

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@en

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@nl

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P1433

Arthritis & Rheumatology

P1476

The presence of citrullinated proteins is not specific for rheumatoid synovial tissue.

@en

P2093

Erik R Vossenaar

http://www.w3.org/2001/XMLSchema#string

Jos M Raats

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Maarten C Kraan

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Paul P Tak

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Tom J M Smeets

http://www.w3.org/2001/XMLSchema#string

Walther J van Venrooij

http://www.w3.org/2001/XMLSchema#string

P2860

The major synovial targets of the rheumatoid arthritis-specific antifilaggrin autoantibodies are deiminated forms of the alpha- and beta-chains of fibrin.

Cutting edge: the conversion of arginine to citrulline allows for a high-affinity peptide interaction with the rheumatoid arthritis-associated HLA-DRB1*0401 MHC class II molecule.

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3485-3494

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scholarly article

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10.1002/ART.20584

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11

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50

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2004-11-01T00:00:00Z

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8192095

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15529392

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