ATP binding without hydrolysis switches sulfonylurea receptor 1 (SUR1) to outward-facing conformations that activate K ATP channels.

MLA

Sikimic, Jelena, et al. “ATP Binding without Hydrolysis Switches Sulfonylurea Receptor 1 (SUR1) to Outward-Facing Conformations That Activate K ATP Channels.” The Journal of Biological Chemistry, vol. 294, no. 10, Mar. 2019, pp. 3707–19. EBSCOhost, https://doi.org/10.1074/jbc.RA118.005236.

APA

Sikimic, J., McMillen, T. S., Bleile, C., Dastvan, F., Quast, U., Krippeit-Drews, P., Drews, G., & Bryan, J. (2019). ATP binding without hydrolysis switches sulfonylurea receptor 1 (SUR1) to outward-facing conformations that activate K ATP channels. The Journal of Biological Chemistry, 294(10), 3707–3719. https://doi.org/10.1074/jbc.RA118.005236

Chicago

Sikimic, Jelena, Timothy S McMillen, Cita Bleile, Frank Dastvan, Ulrich Quast, Peter Krippeit-Drews, Gisela Drews, and Joseph Bryan. 2019. “ATP Binding without Hydrolysis Switches Sulfonylurea Receptor 1 (SUR1) to Outward-Facing Conformations That Activate K ATP Channels.” The Journal of Biological Chemistry 294 (10): 3707–19. doi:10.1074/jbc.RA118.005236.