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. Pt 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(Pt 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 (Pt 6): 386–96. doi:10.1107/S2059798324004066.