Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor Fc∊RI.

MLA

Dhaliwal, Balvinder, et al. “Crystal Structure of IgE Bound to Its B-Cell Receptor CD23 Reveals a Mechanism of Reciprocal Allosteric Inhibition with High Affinity Receptor Fc∊RI.” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 31, July 2012, pp. 12686–91. EBSCOhost, https://doi.org/10.1073/pnas.1207278109.

APA

Dhaliwal, B., Daopeng Yuan, Pang, M. O. Y., Henry, A. J., Cain, K., Oxbrow, A., Fabiane, S. M., Beavil, A. J., McDonnell, J. M., Gould, H. J., & Sutton, B. J. (2012). Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor Fc∊RI. Proceedings of the National Academy of Sciences of the United States of America, 109(31), 12686–12691. https://doi.org/10.1073/pnas.1207278109

Chicago

Dhaliwal, Balvinder, Daopeng Yuan, Marie O. Y. Pang, Alistair J. Henry, Katharine Cain, Amanda Oxbrow, Stella M. Fabiane, et al. 2012. “Crystal Structure of IgE Bound to Its B-Cell Receptor CD23 Reveals a Mechanism of Reciprocal Allosteric Inhibition with High Affinity Receptor Fc∊RI.” Proceedings of the National Academy of Sciences of the United States of America 109 (31): 12686–91. doi:10.1073/pnas.1207278109.