ReviewCritical reviews in biochemistry and molecular biology2019
Structural aspects of chaperone-mediated peptide loading in the MHC-I antigen presentation pathway.
Review in Critical reviews in biochemistry and molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Pan-cancer analysis identifies immunoproteasome as the predominant survival-associated component of antigen processing machinery.Translational oncology · 2026Article
- Review
- Chaperones and Catalysts: How Antigen Presentation Pathways Cope With Biological Necessity.Frontiers in immunology · 2022Review
- HLA polymorphism and tapasin independence influence outcomes of HIV and dengue virus infection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational Plasticity of HLA-B27 Molecules Correlates Inversely With Efficiency of Negative T Cell Selection.Frontiers in immunology · 2020Article
- Sequence-structure-function relationships in class I MHC: A local frustration perspective.PloS one · 2020Article
- Metal-triggered conformational reorientation of a self-peptide bound to a disease-associated HLA-B*27 subtype.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Recognition of foreign and dysregulated antigens by the cellular innate and adaptive immune systems is in large part dependent on the cell surface display of peptide/MHC (pMHC) complexes. The formation of such complexes requires the generation of antigenic peptides, proper folding of MHC molecules, loading of peptides onto MHC molecules, glycosylation, and transport to the plasma membrane. This complex series of biosynthetic, biochemical, and cell biological reactions is known as "antigen processing and presentation". Here, we summarize recent work, focused on the structural and functional characterization of the key MHC-I-dedicated chaperones, tapasin, and TAPBPR. The mechanisms reflect the ability of conformationally flexible molecules to adapt to their ligands, and are comparable to similar processes that are exploited in peptide antigen loading in the MHC-II pathway.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.