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Rabinowitz, J. D., Beeson, C., Lyons, D. S., Davis, M. M., McConnell, H. M. (1996) Kinetic discrimination in T-cell activation. Proceedings of the National Academy of Sciences, 93 (4) 1401-1405 doi:10.1073/pnas.93.4.1401

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Reference TypeJournal (article/letter/editorial)
TitleKinetic discrimination in T-cell activation.
JournalProceedings of the National Academy of Sciences
AuthorsRabinowitz, J. D.Author
Beeson, C.Author
Lyons, D. S.Author
Davis, M. M.Author
McConnell, H. M.Author
Year1996 (February 20)Volume93
Issue4
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.93.4.1401Search in ResearchGate
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Mindat Ref. ID1584490Long-form Identifiermindat:1:5:1584490:7
GUID0
Full ReferenceRabinowitz, J. D., Beeson, C., Lyons, D. S., Davis, M. M., McConnell, H. M. (1996) Kinetic discrimination in T-cell activation. Proceedings of the National Academy of Sciences, 93 (4) 1401-1405 doi:10.1073/pnas.93.4.1401
Plain TextRabinowitz, J. D., Beeson, C., Lyons, D. S., Davis, M. M., McConnell, H. M. (1996) Kinetic discrimination in T-cell activation. Proceedings of the National Academy of Sciences, 93 (4) 1401-1405 doi:10.1073/pnas.93.4.1401
In(1996, February) Proceedings of the National Academy of Sciences Vol. 93 (4) Proceedings of the National Academy of Sciences

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Rabinowitz, J. D., Liang, M. N., Tate, K., Lee, C., Beeson, C., McConnell, H. M. (1997) Specific T cell recognition of kinetic isomers in the binding of peptide to class II major histocompatibility complex. Proceedings of the National Academy of Sciences, 94 (16) 8702-8707 doi:10.1073/pnas.94.16.8702
Beeson, C., McConnell, H. M. (1994) Kinetic intermediates in the reactions between peptides and proteins of major histocompatibility complex class II. Proceedings of the National Academy of Sciences, 91 (19) 8842-8845 doi:10.1073/pnas.91.19.8842
McConnell, H. M. (1996) Equilibration rates in lipid monolayers. Proceedings of the National Academy of Sciences, 93 (26) 15001-15003 doi:10.1073/pnas.93.26.15001
Hobson, A. H., Buckley, C. M., Aamand, J. L., Jorgensen, S. T., Diderichsen, B., McConnell, D. J. (1993) Activation of a bacterial lipase by its chaperone. Proceedings of the National Academy of Sciences, 90 (12) 5682-5686 doi:10.1073/pnas.90.12.5682
Boniface, J. J., Reich, Z., Lyons, D. S., Davis, M. M. (1999) Thermodynamics of T cell receptor binding to peptide-MHC: Evidence for a general mechanism of molecular scanning. Proceedings of the National Academy of Sciences, 96 (20) 11446-11451 doi:10.1073/pnas.96.20.11446
Bacher, M., Metz, C. N., Calandra, T., Mayer, K., Chesney, J., Lohoff, M., Gemsa, D., Donnelly, T., Bucala, R. (1996) An essential regulatory role for macrophage migration inhibitory factor in T-cell activation. Proceedings of the National Academy of Sciences, 93 (15) 7849-7854 doi:10.1073/pnas.93.15.7849
Six, A., Rast, J. P., McCormack, W. T., Dunon, D., Courtois, D., Li, Y., Chen, C.-l. H., Cooper, M. D. (1996) Characterization of avian T-cell receptor   genes. Proceedings of the National Academy of Sciences, 93 (26) 15329-15334 doi:10.1073/pnas.93.26.15329
Nakae, S., Suto, H., Kakurai, M., Sedgwick, J. D., Tsai, M., Galli, S. J. (2005) Mast cells enhance T cell activation: Importance of mast cell-derived TNF. Proceedings of the National Academy of Sciences, 102 (18) 6467-6472 doi:10.1073/pnas.0501912102
Wulfing, C., Sjaastad, M. D., Davis, M. M. (1998) Visualizing the dynamics of T cell activation: Intracellular adhesion molecule 1 migrates rapidly to the T cell/B cell interface and acts to sustain calcium levels. Proceedings of the National Academy of Sciences, 95 (11) 6302-6307 doi:10.1073/pnas.95.11.6302
Quan, L. T., Tewari, M., O'Rourke, K., Dixit, V., Snipas, S. J., Poirier, G. G., Ray, C., Pickup, D. J., Salvesen, G. S. (1996) Proteolytic activation of the cell death protease Yama/CPP32 by granzyme B. Proceedings of the National Academy of Sciences, 93 (5) 1972-1976 doi:10.1073/pnas.93.5.1972
Su, Z. D., Arooz, M. T., Chen, H. M., Gross, C. J., Tsong, T. Y. (1996) Least activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow circular dichroism. Proceedings of the National Academy of Sciences, 93 (6) 2539-2544 doi:10.1073/pnas.93.6.2539
 
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