Major differences in antigen-processing correlate with a single Arg71↔Lys substitution in HLA-DR molecules predisposing to rheumatoid arthritis and with their selective interactions with 70-kDA heat shock protein chaperones

Journal of Immunology

Volumn 169, Issue 6, 2002, Pages 3015-3020

  Roth, Sabine ^a   Willcox, Nicholas ^a   Rzepka, Rita ^a   Mayer, Matthias P ^a   Melchers, Inga ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHOLINERGIC RECEPTOR; EPITOPE; HEAT SHOCK PROTEIN; HLA DR ANTIGEN; RECEPTOR SUBUNIT; T LYMPHOCYTE RECEPTOR;

ALLELE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGEN BINDING; ANTIGEN PRESENTATION; ARTICLE; CONTROLLED STUDY; CORRELATION ANALYSIS; DISEASE ASSOCIATION; DISEASE PREDISPOSITION; DNA POLYMORPHISM; GENE SEQUENCE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; IMMUNE RESPONSE; LYMPHOCYTE CLONE; MOLECULAR INTERACTION; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; RHEUMATOID ARTHRITIS; SEQUENCE ANALYSIS;

ESCHERICHIA COLI;

EID: 0037105396     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.169.6.3015     Document Type: Article

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