ArticleFrontiers in immunology2025
How conformational changes near the F pocket of MHC class I proteins mediate chaperone assisted peptide loading.
Article in Frontiers in immunology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Mouse TAPBPR shows functional similarity to human TAPBPR in shaping the MHC-I immunopeptidome.Frontiers in immunology · 2026Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Efficient recognition of antigenic peptides bound to major histocompatibility complex (MHC) class I molecules on the surface of cells by immune cells requires sufficiently stable peptide-MHC I complexes. Antigenic peptides of 8-10 amino acids are typically bound in a narrow cleft between two flanking α Methods: The role of this α Results: The α Conclusions: The simulations indicate that the conformational shifts of the α
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Registered trials
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