ArticleNature chemical biology2022
TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules.
Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Engineering high-fidelity tapasin variants to enhance MHC-I antigen presentation.The Journal of biological chemistry · 2026Article
- A miniaturized MR1 metabolite display system with native-like protein features.bioRxiv : the preprint server for biology · 2026Article
- Molecular Insights Into MR1-Mediated T Cell Immunity: Lessons Learned and Unanswered Questions.Immunological reviews · 2025Review
- Identification and biophysical characterization of Plasmodium peptide binding by common African HLAs.Scientific reports · 2025Article
- CryoEM structure of an MHC-I/TAPBPR peptide-bound intermediate reveals the mechanism of antigen proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- MR1 antigen presentation to MAIT cells and other MR1-restricted T cells.Nature reviews. Immunology · 2024Review
- Delivery of loaded MR1 monomer results in efficient ligand exchange to host MR1 and subsequent MR1T cell activation.Communications biology · 2024Article
- Conformational plasticity of RAS Q61 family of neoepitopes results in distinct features for targeted recognition.Nature communications · 2023Article
- Introducing Molecular Chaperones into the Causality and Prospective Management of Autoimmune Hepatitis.Digestive diseases and sciences · 2023Review
- Molecular insights into metabolite antigen recognition by mucosal-associated invariant T cells.Current opinion in immunology · 2023Review
- Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes.Science advances · 2023Article
- Chaperone function in antigen presentation by MHC class I molecules-tapasin in the PLC and TAPBPR beyond.Frontiers in immunology · 2023Review
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9 authors at 3 institutions in 1 country.
Funding
Abstract
Chaperones tapasin and transporter associated with antigen processing (TAP)-binding protein related (TAPBPR) associate with the major histocompatibility complex (MHC)-related protein 1 (MR1) to promote trafficking and cell surface expression. However, the binding mechanism and ligand dependency of MR1/chaperone interactions remain incompletely characterized. Here in vitro, biochemical and computational studies reveal that, unlike MHC-I, TAPBPR recognizes MR1 in a ligand-independent manner owing to the absence of major structural changes in the MR1 α
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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.