The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding.

MLA

Leth-Espensen, Katrine Z., et al. “The Intrinsic Instability of the Hydrolase Domain of Lipoprotein Lipase Facilitates Its Inactivation by ANGPTL4-Catalyzed Unfolding.” Proceedings of the National Academy of Sciences of the United States of America, vol. 118, no. 12, Mar. 2021, pp. 1–12. EBSCOhost, https://doi.org/10.1073/pnas.2026650118.

APA

Leth-Espensen, K. Z., Kristensen, K. K., Kumari, A., Winther, A.-M. L., Young, S. G., Jörgensen, T. J. D., & Ploug, M. (2021). The intrinsic instability of the hydrolase domain of lipoprotein lipase facilitates its inactivation by ANGPTL4-catalyzed unfolding. Proceedings of the National Academy of Sciences of the United States of America, 118(12), 1–12. https://doi.org/10.1073/pnas.2026650118

Chicago

Leth-Espensen, Katrine Z., Kristian K. Kristensen, Anni Kumari, Anne-Marie L. Winther, Stephen G. Young, Thomas J. D. Jörgensen, and Michael Ploug. 2021. “The Intrinsic Instability of the Hydrolase Domain of Lipoprotein Lipase Facilitates Its Inactivation by ANGPTL4-Catalyzed Unfolding.” Proceedings of the National Academy of Sciences of the United States of America 118 (12): 1–12. doi:10.1073/pnas.2026650118.