The Peptide Repertoires of HLA-B27 Subtypes Differentially Associated to Spondyloarthropathy (B*2704 and B*2706) Differ by Specific Changes at Three Anchor Positions

This publication has 37 references indexed in Scilit:

• A single amino acid change makes the peptide specificity of B*3910 unrelated to B*3901 and closer to a group of HLA‐B proteins including the malaria‐protecting allotype HLA‐B53
  Tissue Antigens, 1998
• Spontaneous inflammatory arthritis in HLA-B27 transgenic mice lacking beta 2-microglobulin: a model of human spondyloarthropathies.
  The Journal of Experimental Medicine, 1995
• The peptide-binding specificity of HLA-B27 subtype (B∗2705) analyzed by the use of polyalanine model peptides
  Human Immunology, 1994
• The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
  Cell, 1992
• Identification of self peptides bound to purified HLA-B27
  Nature, 1991
• Guilt by association: HLA-B27 and ankylosing spondylitis
  Immunology Today, 1990
• Association of class I major histocompatibility heavy and light chains induced by viral peptides
  Nature, 1989
• Host resistance directed selectively against H-2-deficient lymphoma variants. Analysis of the mechanism.
  The Journal of Experimental Medicine, 1985
• Recognition of HLA-B27 and related antigen by a monoclonal antibody
  Human Immunology, 1982
• Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis
  Cell, 1978