ArticleProceedings of the National Academy of Sciences of the United States of America2009
Phosphorylated self-peptides alter human leukocyte antigen class I-restricted antigen presentation and generate tumor-specific epitopes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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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
47 citing papers in PubMed, 83 citations in OpenAlex.
- Beyond Sequence: Posttranslational Remodeling of Antigens in Autoimmunity.Immunological reviews · 2026Review
- Review
- Phosphorylation shapes antigen presentation and immune recognition: mechanistic insights and translational perspectives.Frontiers in immunology · 2026Review
- Antigen presentation of post-translationally modified peptides in major histocompatibility complexes.Immunology and cell biology · 2025Review
- Relevance of mutation-derived neoantigens and non-classical antigens for anticancer therapies.Human vaccines & immunotherapeutics · 2024Review
- Tumor Antigens beyond the Human Exome.International journal of molecular sciences · 2024Review
- Phosphopeptide Neoantigens as Emerging Targets in Cancer Immunotherapy.Journal of cancer immunology · 2024Article
- Circular RNA vaccine in disease prevention and treatment.Signal transduction and targeted therapy · 2023Review
- The landscape of MHC-presented phosphopeptides yields actionable shared tumor antigens for cancer immunotherapy across multiple HLA alleles.Journal for immunotherapy of cancer · 2023Article
- Molecular mechanism of phosphopeptide neoantigen immunogenicity.Nature communications · 2023Article
- Post-Translational Modifications in Tumor-Associated Antigens as a Platform for Novel Immuno-Oncology Therapies.Cancers · 2022Review
- Boosting Antitumor Immunity with an Expanded Neoepitope Landscape.Cancer research · 2022Review
- Deciphering the landscape of phosphorylated HLA-II ligands.iScience · 2022Article
- Phosphosite-dependent presentation of dual phosphorylated peptides by MHC class I molecules.iScience · 2022Article
- A TCR mimic monoclonal antibody reactive with the "public" phospho-neoantigen pIRS2/HLA-A*02:01 complex.JCI insight · 2022Article
- Mitochondrial Proteins as Source of Cancer Neoantigens.International journal of molecular sciences · 2022Review
- Structural aspects of chemical modifications in the MHC-restricted immunopeptidome; Implications for immune recognition.Frontiers in chemistry · 2022Review
- What's next in cancer immunotherapy? - The promise and challenges of neoantigen vaccination.Oncoimmunology · 2022Review
- Characteristics of Immune Memory and Effector Activity to Cancer-Expressed MHC Class I Phosphopeptides Differ in Healthy Donors and Ovarian Cancer Patients.Cancer immunology research · 2021Article
- caAtlas: An immunopeptidome atlas of human cancer.iScience · 2021Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Human leukocyte antigen (HLA) class I molecules present a variety of posttranslationally modified epitopes at the cell surface, although the consequences of such presentation remain largely unclear. Phosphorylation plays a critical cellular role, and deregulation in phosphate metabolism is associated with disease, including autoimmunity and tumor immunity. We have solved the high-resolution structures of 3 HLA A2-restricted phosphopeptides associated with tumor immunity and compared them with the structures of their nonphosphorylated counterparts. Phosphorylation of the epitope was observed to affect the structure and mobility of the bound epitope. In addition, the phosphoamino acid stabilized the HLA peptide complex in an epitope-specific manner and was observed to exhibit discrete flexibility within the antigen-binding cleft. Collectively, our data suggest that phosphorylation generates neoepitopes that represent demanding targets for T-cell receptor ligation. These findings provide insights into the mode of phosphopeptide presentation by HLA as well as providing a platform for the rational design of a generation of posttranslationally modified tumor vaccines.
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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.