Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity.

MLA

Dunn, Steven M., et al. “Directed Evolution of Human T Cell Receptor CDR2 Residues by Phage Display Dramatically Enhances Affinity for Cognate Peptide-MHC without Increasing Apparent Cross-Reactivity.” Protein Science: A Publication of the Protein Society, vol. 15, no. 4, Apr. 2006, pp. 710–21. EBSCOhost, https://doi.org/10.1110/ps.051936406.

APA

Dunn, S. M., Rizkallah, P. J., Baston, E., Mahon, T., Cameron, B., Moysey, R., Gao, F., Sami, M., Boulter, J., Li, Y., & Jakobsen, B. K. (2006). Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity. Protein Science: A Publication of the Protein Society, 15(4), 710–721. https://doi.org/10.1110/ps.051936406

Chicago

Dunn, Steven M., Pierre J. Rizkallah, Emma Baston, Tara Mahon, Brian Cameron, Ruth Moysey, Feng Gao, et al. 2006. “Directed Evolution of Human T Cell Receptor CDR2 Residues by Phage Display Dramatically Enhances Affinity for Cognate Peptide-MHC without Increasing Apparent Cross-Reactivity.” Protein Science: A Publication of the Protein Society 15 (4): 710–21. doi:10.1110/ps.051936406.