Publications

Found 5 results
Filters: Author is Lee, John K  [Clear All Filters]
2013
Chae, P. Seok, Rana, R. R., Gotfryd, K., Rasmussen, S. G. F., Kruse, A. C., Cho, K. Ho, Capaldi, S., Carlsson, E., Kobilka, B., Loland, C. J., Gether, U., Banerjee, S., Byrne, B., Lee, J. K., and Gellman, S. H. (2013) Glucose-neopentyl glycol (GNG) amphiphiles for membrane protein study. Chem Commun (Camb). 49, 2287-9
2015
Murphy, M. W., Lee, J. K., Rojo, S., Gearhart, M. D., Kurahashi, K., Banerjee, S., Loeuille, G. - A., Bashamboo, A., McElreavey, K., Zarkower, D., Aihara, H., and Bardwell, V. J. (2015) An ancient protein-DNA interaction underlying metazoan sex determination. Nat Struct Mol Biol. 22, 442-51
2018
Bohl, T. E., Shi, K., Lee, J. K., and Aihara, H. (2018) Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. Nat Commun. 9, 377
Lee, J. K., Bosnakovski, D., Toso, E. A., Dinh, T., Banerjee, S., Bohl, T. E., Shi, K., Orellana, K., Kyba, M., and Aihara, H. (2018) Crystal Structure of the Double Homeodomain of DUX4 in Complex with DNA. Cell Rep. 25, 2955-2962.e3
Bohl, T. E., Ieong, P., Lee, J. K., Lee, T., Kankanala, J., Shi, K., Demir, Ö., Kurahashi, K., Amaro, R. E., Wang, Z., and Aihara, H. (2018) The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release. J Biol Chem. 10.1074/jbc.RA118.002503