ReviewMolecular immunology2012
T cell antigen recognition at the cell membrane.
Review in Molecular immunology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- NCAPD2 Modulates MHC-I Antigen Presentation via the PI3K/AKT Axis to Drive Metastatic Progression in Gastric Cancer.Digestive diseases and sciences · 2026Article
- Receptor-Ligand Binding: Effect of Mechanical Factors.International journal of molecular sciences · 2023Review
- Optical sensing and control of T cell signaling pathways.Frontiers in physiology · 2023Review
- Two-dimensional measurements of receptor-ligand interactions.Frontiers in molecular biosciences · 2023Review
- Targeting cathepsin B by cycloastragenol enhances antitumor immunity of CD8 T cells via inhibiting MHC-I degradation.Journal for immunotherapy of cancer · 2022Article
- Role of Histone Deacetylases in T-Cell Development and Function.International journal of molecular sciences · 2022Review
- Fluctuations in T cell receptor and pMHC interactions regulate T cell activation.Journal of the Royal Society, Interface · 2022Article
- Insights into intercellular receptor-ligand binding kinetics in cell communication.Frontiers in bioengineering and biotechnology · 2022Review
- A structural-based machine learning method to classify binding affinities between TCR and peptide-MHC complexes.Molecular immunology · 2021Article
- Structure-based identification of inhibitors disrupting the CD2-CD58 interactions.Journal of computer-aided molecular design · 2021Article
- A computational study of co-inhibitory immune complex assembly at the interface between T cells and antigen presenting cells.PLoS computational biology · 2021Article
- Endothelial activation and dysfunction in COVID-19: from basic mechanisms to potential therapeutic approaches.Signal transduction and targeted therapy · 2020Review
- A Head Start: CAR-T Cell Therapy for Primary Malignant Brain Tumors.Current treatment options in oncology · 2020Review
- T-Cell Mechanobiology: Force Sensation, Potentiation, and Translation.Frontiers in physics · 2019Article
- Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell.Journal of visualized experiments : JoVE · 2015Article
- Identification of Owl Monkey CD4 Receptors Broadly Compatible with Early-Stage HIV-1 Isolates.Journal of virology · 2015Article
- Novel CD4-Based Bispecific Chimeric Antigen Receptor Designed for Enhanced Anti-HIV Potency and Absence of HIV Entry Receptor Activity.Journal of virology · 2015Article
- Experimental and theoretical bases for mechanisms of antigen discrimination by T cells.Biophysics (Nagoya-shi, Japan) · 2015Review
- Quantitative analysis of T cell receptor complex interaction sites using genetically encoded photo-cross-linkers.ACS chemical biology · 2014Article
- 2D TCR-pMHC-CD8 kinetics determines T-cell responses in a self-antigen-specific TCR system.European journal of immunology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
T cell antigen receptors (TCRs) on the surface of T cells bind specifically to particular peptide bound major histocompatibility complexes (pMHCs) presented on the surface of antigen presenting cells (APCs). This interaction is a key event in T cell antigen recognition and activation. Most studies have used surface plasmon resonance (SPR) to measure the in vitro binding kinetics of TCR-pMHC interactions in solution using purified proteins. However, these measurements are not physiologically precise, as both TCRs and pMHCs are membrane-associated molecules which are regulated by their cellular environments. Recently, single-molecule förster resonance energy transfer (FRET) and single-molecule mechanical assays were used to measure the in situ binding kinetics of TCR-pMHC interactions on the surface of live T cells. These studies have provided exciting insights into the biochemical basis of T cell antigen recognition and suggest that TCRs serially engage with a small number of antigens with very fast kinetics in order to maximize TCR signaling and sensitivity.
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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.