An alternative conformation of the N‐terminal loop of human dihydroorotate dehydrogenase drives binding to a potent antiproliferative agent.

MLA

Alberti, Marta, et al. “An Alternative Conformation of the N‐terminal Loop of Human Dihydroorotate Dehydrogenase Drives Binding to a Potent Antiproliferative Agent.” Acta Crystallographica: Section D, Structural Biology, vol. 80, no. 6, June 2024, pp. 386–96. EBSCOhost, https://doi.org/10.1107/S2059798324004066.

APA

Alberti, M., Poli, G., Broggini, L., Sainas, S., Rizzi, M., Boschi, D., Ferraris, D. M., Martino, E., Ricagno, S., Tuccinardi, T., Lolli, M. L., & Miggiano, R. (2024). An alternative conformation of the N‐terminal loop of human dihydroorotate dehydrogenase drives binding to a potent antiproliferative agent. Acta Crystallographica: Section D, Structural Biology, 80(6), 386–396. https://doi.org/10.1107/S2059798324004066

Chicago

Alberti, Marta, Giulio Poli, Luca Broggini, Stefano Sainas, Menico Rizzi, Donatella Boschi, Davide M. Ferraris, et al. 2024. “An Alternative Conformation of the N‐terminal Loop of Human Dihydroorotate Dehydrogenase Drives Binding to a Potent Antiproliferative Agent.” Acta Crystallographica: Section D, Structural Biology 80 (6): 386–96. doi:10.1107/S2059798324004066.