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July 3, 1995Proceedings of the National Academy of SciencesOpen Access

Naturally processed peptides from two disease-resistance-associated HLA-DR13 alleles show related sequence motifs and the effects of the dimorphism at position 86 of the HLA-DR beta chain.

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Authors

MDMiles P. DavenportUNSW SydneyCQCheryl L. QuinnItasca Consultants (United States)RCRoman M. ChiczSanofi (France)

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Cite This Study

Davenport et al. (1995) studied this question.

synapsesocial.com/papers/6a7327e7feeedbd807c23134https://doi.org/10.1073/pnas.92.14.6567
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Identification of a motif for HLA-DR1 binding peptides using M13 display libraries.1992 · 222 citations
  2. 2Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands.1994 · 81 citations
  3. 3Allelic variation in the DR subregion of the human major histocompatibility complex.1987 · 220 citations
  4. 4Differential effect of polymorphism at HLA-DR1 beta-chain positions 85 and 86 on binding and recognition of DR1-restricted antigenic peptides1993 · 66 citations