Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.
about
Editing peptide presentation to T cells.Empty conformers of HLA-B preferentially bind CD8 and regulate CD8+ T cell function.Variations in HLA-B cell surface expression, half-life and extracellular antigen receptivity.Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide bindingThe Role of Molecular Flexibility in Antigen Presentation and T Cell Receptor-Mediated Signaling
P2860
Structure of the TAPBPR-MHC I complex defines the mechanism of peptide loading and editing.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
@wuu
2017年学术文章
@zh-cn
2017年学术文章
@zh-hans
2017年学术文章
@zh-my
2017年学术文章
@zh-sg
2017年學術文章
@yue
2017年學術文章
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2017年學術文章
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name
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@en
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@nl
type
label
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@en
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@nl
prefLabel
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@en
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@nl
P2860
P356
P1433
P1476
Structure of the TAPBPR-MHC I ...... f peptide loading and editing.
@en
P2860
P304
P356
10.1126/SCIENCE.AAO6001
P407
P577
2017-10-12T00:00:00Z