Publications

Found 41 results
Filters: Author is Yeates, Todd O  [Clear All Filters]
2014
King, N. P., Bale, J. B., Sheffler, W., McNamara, D. E., Gonen, S., Gonen, T., Yeates, T. O., and Baker, D. (2014) Accurate design of co-assembling multi-component protein nanomaterials. Nature. 510, 103-8
Sinha, S., Cheng, S., Sung, Y. Won, McNamara, D. E., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2014) Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment. J Mol Biol. 426, 2328-45
Thompson, M. C., Wheatley, N. M., Jorda, J., Sawaya, M. R., Gidaniyan, S. D., Ahmed, H., Yang, Z., McCarty, K. N., Whitelegge, J. P., and Yeates, T. O. (2014) Identification of a unique Fe-S cluster binding site in a glycyl-radical type microcompartment shell protein. J Mol Biol. 426, 3287-304
Okamoto, R., Mandal, K., Sawaya, M. R., Kajihara, Y., Yeates, T. O., and Kent, S. B. H. (2014) (Quasi-)racemic X-ray structures of glycosylated and non-glycosylated forms of the chemokine Ser-CCL1 prepared by total chemical synthesis. Angew Chem Int Ed Engl. 53, 5194-8
Jiménez-Osés, G., Osuna, S., Gao, X., Sawaya, M. R., Gilson, L., Collier, S. J., Huisman, G. W., Yeates, T. O., Tang, Y., and Houk, K. N. (2014) The role of distant mutations and allosteric regulation on LovD active site dynamics. Nat Chem Biol. 10, 431-6
Wheatley, N. M., Sundberg, C. D., Gidaniyan, S. D., Cascio, D., and Yeates, T. O. (2014) Structure and identification of a pterin dehydratase-like protein as a ribulose-bisphosphate carboxylase/oxygenase (RuBisCO) assembly factor in the α-carboxysome.. J Biol Chem. 289, 7973-81
Thompson, M. C., Crowley, C. S., Kopstein, J., Bobik, T. A., and Yeates, T. O. (2014) Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 70, 1584-90
Lai, Y. - T., Reading, E., Hura, G. L., Tsai, K. - L., Laganowsky, A., Asturias, F. J., Tainer, J. A., Robinson, C. V., and Yeates, T. O. (2014) Structure of a designed protein cage that self-assembles into a highly porous cube. Nat Chem. 6, 1065-71

Pages