HLA-DR1001 presents “altered-self” peptides derived from joint-associated proteins by accepting citrulline in three of its binding pockets-Reference-Cited by-同舟云学术

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HLA-DR1001 presents “altered-self” peptides derived from joint-associated proteins by accepting citrulline in three of its binding pockets

Published:2010-06-07 Issue:10 Volume:62 Page:2909-2918
ISSN:0004-3591
Container-title:Arthritis & Rheumatism
language:en
Short-container-title:Arthritis & Rheumatism

Author:

James Eddie A.,Moustakas Antonis K.,Bui John,Papadopoulos George K.,Bondinas George,Buckner Jane H.,Kwok William W.

Publisher

Wiley

Subject

Pharmacology (medical),Immunology,Rheumatology,Immunology and Allergy

Reference44 articles.

1. Auto-antibodies and autoreactive T-cells in rheumatoid arthritis: pathogenetic players and diagnostic tools;Steiner;Clin Rev Allergy Immunol,2007

2. Rheumatoid factor and anticitrullinated protein antibodies in rheumatoid arthritis: diagnostic value, associations with radiological progression rate, and extra-articular manifestations;De Rycke;Ann Rheum Dis,2004

3. Reshaping the shared epitope hypothesis: HLA-associated risk for rheumatoid arthritis is encoded by amino acid substitutions at positions 67-74 of the HLA-DRB1 molecule;De Vries;Arthritis Rheum,2002

4. A structural model for TCR recognition of the HLA class II shared epitope sequence implicated in susceptibility to rheumatoid arthritis;Penzotti;J Autoimmun,1996

5. The rheumatoid arthritis shared epitope increases cellular susceptibility to oxidative stress by antagonizing an adenosine-mediated anti-oxidative pathway;Ling;Arthritis Res Ther,2007

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