New insights into the T cell synapse from single molecule techniques
Author:
Publisher
Springer Science and Business Media LLC
Subject
Energy Engineering and Power Technology,Fuel Technology
Link
http://www.nature.com/articles/nri3066.pdf
Reference119 articles.
1. Irvine, D. J., Purbhoo, M. A., Krogsgaard, M. & Davis, M. M. Direct observation of ligand recognition by T cells. Nature 419, 845–849 (2002).
2. Huang, J. et al. The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness. Nature 464, 932–936 (2010). This paper used micromanipulation of T cells and peptide–MHC-coated erythrocyte probes to determine 2D kinetic rates for the formation of initial TCR–peptide–MHC interactions.
3. Huppa, J. B. et al. TCR–peptide–MHC interactions in situ show accelerated kinetics and increased affinity. Nature 463, 963–967 (2010). This paper used single molecule FRET to determine that an active mechanism increases the off-rate for the TCR–peptide–MHC interaction in an immunological synapse.
4. Lillemeier, B. F. et al. TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nature Immunol. 11, 90–96 (2010). This paper used electron microscopy, PALM and FCS measurements to support a model of TCR+ and LAT+ protein islands.
5. Purbhoo, M. A. et al. Dynamics of subsynaptic vesicles and surface microclusters at the immunological synapse. Sci. Signal. 3, ra36 (2010). This study used confocal microscopy to support a model in which LAT-containing vesicles dock with TCR complexes to form signalling complexes required for early TCR signalling.
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