The peptide-binding specificity of HLA-B27 subtype (B∗2705) analyzed by the use of polyalanine model peptides

This publication has 17 references indexed in Scilit:

• Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
  Cell, 1993
• Unfolded HLA class I α chains and their use in an assay of HLA class-I-peptide binding
  Human Immunology, 1993
• Deconstructing the MHC
  Nature, 1992
• The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
  Cell, 1992
• Characterization of Peptides Bound to the Class I MHC Molecule HLA-A2.1 by Mass Spectrometry
  Science, 1992
• Identification of self peptides bound to purified HLA-B27
  Nature, 1991
• The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
  Nature, 1991
• Peptide-induced conformational change of the class I heavy chain
  Nature, 1991
• Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
  Nature, 1991
• Isolation and analysis of naturally processed viral peptides as recognized by cytotoxic T cells
  Nature, 1990