Antigen Presentation: One size fits all

[1]  J. Rothbard,et al.  Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands. , 1994, Journal of immunology.

[2]  Don C. Wiley,et al.  Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide , 1994, Nature.

[3]  J. Rothbard,et al.  Exploration of requirements for peptide binding to HLA DRB1*0101 and DRB1*0401. , 1994, Journal of immunology.

[4]  D. Wiley,et al.  Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1 , 1993, Nature.

[5]  P. A. Peterson,et al.  Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. , 1994, Science.

[6]  William S. Lane,et al.  Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle , 1992, Nature.

[7]  P. A. Peterson,et al.  Emerging principles for the recognition of peptide antigens by MHC class I molecules. , 1992, Science.

[8]  D. Wiley,et al.  Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. , 1991, Journal of molecular biology.

[9]  D. Wiley,et al.  Peptide binding to HLA‐DR1: a peptide with most residues substituted to alanine retains MHC binding. , 1990, The EMBO journal.

[10]  M. A. Saper,et al.  The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens , 1987, Nature.

[11]  M. A. Saper,et al.  Structure of the human class I histocompatibility antigen, HLA-A2 , 1987, Nature.