Significance of the six peptide-binding pockets of HLA-A2.1 in influenza a matrix peptide-specific cytotoxic T-lymphocyte reactivity
- 31 October 1994
- journal article
- Published by Elsevier BV in Human Immunology
- Vol. 41 (2), 160-166
- https://doi.org/10.1016/0198-8859(94)90010-8
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 moleculesCell, 1993
- The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHCCell, 1992
- HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptidesNature, 1992
- Identification of self peptides bound to purified HLA-B27Nature, 1991
- The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformationNature, 1991
- Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC moleculesNature, 1991
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991
- Antigen Recognition by Class I-Restricted T LymphocytesAnnual Review of Immunology, 1989
- Partial purification and some properties of BB7.2 a cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28Human Immunology, 1981
- A monoclonal antibody that recognizes an antigenic determinant shared by HLA A2 and B17Human Immunology, 1980