ArticleCell2014
Deconstructing the peptide-MHC specificity of T cell recognition.
Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 352 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
352 citing papers in PubMed, 563 citations in OpenAlex.
- Preexisting memory CD4+ T cells contribute to the primary response in an HIV-1 vaccine trial.The Journal of clinical investigation · 2021Trial
- Discovery and engineering of bispecific TCR-mimic antibodies targeting peptide-HLA complex.mAbs · 2026Article
- Calibrating T cell responsiveness through interactions with self.Nature reviews. Immunology · 2026Review
- Discovery of Post-Translationally Modified Epitopes in Autoimmunity: Someone Has to Fish so Everyone Can Eat.Immunological reviews · 2026Review
- Entering the Age of Specificity in T Cell Immunity.Immunological reviews · 2026Review
- Structural T-Cell Receptor Analysis in the Age of Machine Learning.Immunological reviews · 2026Review
- Central T cell tolerance from sparse peptide sampling.Science advances · 2026Article
- What Does the Shape Space of T Cell Epitopes Look Like?Immunological reviews · 2026Review
- The Role of the T Cell Receptor Sequence in Shaping T Cell Functional Fate.Immunological reviews · 2026Review
- Unbiased avidity-based isolation of antigen-specific T cells.Journal for immunotherapy of cancer · 2026Article
- Generation and MHC class II loading of an endogenous influenza epitope revealed by a T cell receptor-like antibody.bioRxiv : the preprint server for biology · 2026Article
- MHC Attention: Identifying HLA-E presented cancer antigens through deep learning and high-throughput screening.bioRxiv : the preprint server for biology · 2026Article
- General prediction of T cell receptor antigen specificity from sequence using AlphaFold 3.bioRxiv : the preprint server for biology · 2026Article
- The evolution of display technologies for antibody drug discovery.Trends in biotechnology · 2026Review
- Ambient temperature regulates CD4iScience · 2026Article
- Deep peptide recognition profiling decodes TCR specificity and enables disease-associated antigen discovery.Nature biotechnology · 2026Article
- Advances in predicting T cell epitope recognition for cancer immunotherapy.Nature cancer · 2026Review
- Antigen specificity of clonally enriched CD8Nature immunology · 2026Article
- Decoding TCR recognition via geometric deep learning of immunological fingerprints.Briefings in bioinformatics · 2026Article
- De novo identification of the specificities of recurrently identified human T cell receptors.Science advances · 2026Article
292 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
In order to survey a universe of major histocompatibility complex (MHC)-presented peptide antigens whose numbers greatly exceed the diversity of the T cell repertoire, T cell receptors (TCRs) are thought to be cross-reactive. However, the nature and extent of TCR cross-reactivity has not been conclusively measured experimentally. We developed a system to identify MHC-presented peptide ligands by combining TCR selection of highly diverse yeast-displayed peptide-MHC libraries with deep sequencing. Although we identified hundreds of peptides reactive with each of five different mouse and human TCRs, the selected peptides possessed TCR recognition motifs that bore a close resemblance to their known antigens. This structural conservation of the TCR interaction surface allowed us to exploit deep-sequencing information to computationally identify activating microbial and self-ligands for human autoimmune TCRs. The mechanistic basis of TCR cross-reactivity described here enables effective surveillance of diverse self and foreign antigens without necessitating degenerate recognition of nonhomologous peptides.
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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.