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- W2040650010 abstract "T-cell epitopes form the basis of many vaccines, diagnostics, and reagents. Current methods for the in silico identification of T-cell epitopes rely, in the main, on the accurate quantitative prediction of peptide-Major Histocompatibility Complex (pMHC) affinity using data-driven computational approaches. Here, we describe a dataset of experimentally determined pMHC binding affinities for the problematic human class I allele HLA-B*2705. Using an in-house, FACS-based, MHC stabilization assay, we measured binding of 223 peptides. This dataset includes both nonbinding and binding peptides, with measured affinities (expressed as <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M1><mml:mrow><mml:msub><mml:mrow><mml:mo>−</mml:mo><mml:mtext>log</mml:mtext></mml:mrow><mml:mrow><mml:mn>10</mml:mn></mml:mrow></mml:msub></mml:mrow></mml:math> of the half-maximal binding level) ranging from 1.2 to 7.4. This dataset should provide a useful independent benchmark for new and existing methods for predicting peptide binding to HLA-B*2705." @default.
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- W2040650010 date "2014-04-27" @default.
- W2040650010 modified "2023-09-23" @default.
- W2040650010 title "A Dataset of Experimental HLA-B*2705 Peptide Binding Affinities" @default.
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- W2040650010 doi "https://doi.org/10.1155/2014/914684" @default.
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