ReviewFrontiers in immunology2013
HLA-DM Focuses on Conformational Flexibility Around P1 Pocket to Catalyze Peptide Exchange.
Review in Frontiers in immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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
10 citing papers in PubMed.
- Molecular origin, discovery, validation and application of neoantigens.Asian journal of pharmaceutical sciences · 2026Review
- Implications of MHC-restricted immunopeptidome in transplantation.Frontiers in immunology · 2024Review
- Human Hepatitis B Viral Infection Outcomes Are Linked to Naturally Occurring Variants ofJournal of immunology (Baltimore, Md. : 1950) · 2020Article
- MHC-II alleles shape the CDR3 repertoires of conventional and regulatory naïve CD4Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Predicting Antigen Presentation-What Could We Learn From a Million Peptides?Frontiers in immunology · 2018Review
- Specific β-Turns Precede PPIIFrontiers in chemistry · 2018Article
- Antigen Processing and Presentation Mechanisms in Myeloid Cells.Microbiology spectrum · 2016Review
- Evaluating the Role of HLA-DM in MHC Class II-Peptide Association Reactions.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- Susceptibility to HLA-DM protein is determined by a dynamic conformation of major histocompatibility complex class II molecule bound with peptide.The Journal of biological chemistry · 2014Article
- A novel method to measure HLA-DM-susceptibility of peptides bound to MHC class II molecules based on peptide binding competition assay and differential IC(50) determination.Journal of immunological methods · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Peptides presented by major histocompatibility complex class II (MHCII) molecules to CD4+ T cells play a central role in the initiation of adaptive immunity. This antigen presentation process is characterized by the proteolytic cleavage of foreign and self proteins, and loading of the resultant peptides onto MHCII molecules. Loading and exchange of antigenic peptides is catalyzed by a non-classical MHCII molecule, HLA-DM. The impact of HLA-DM on epitope selection has been appreciated for a long time. However, the molecular mechanism by which HLA-DM mediates peptide exchange remains elusive. Here, we review recent efforts in elucidating how HLA-DM works, highlighted by two recently solved co-structures of HLA-DM bound to HLA-DO (a natural inhibitor of HLA-DM), or to HLA-DR1 (a common MHCII). In light of these efforts, a model for HLA-DM action in which HLA-DM utilizes conformational flexibility around the P1 pocket of the MHCII-peptide complex to catalyze peptide exchange is proposed.
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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.