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Bale, J. B., Park, R. U., Liu, Y., Gonen, S., Gonen, T., Cascio, D., King, N. P., Yeates, T. O., and Baker, D. (2015) Structure of a designed tetrahedral protein assembly variant engineered to have improved soluble expression. Protein Sci. 24, 1695-701
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
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
Lee, K., Gu, S., Jin, L., Le, T. Tuc Nghi, Cheng, L. W., Strotmeier, J., Kruel, A. Magdalena, Yao, G., Perry, K., Rummel, A., and Jin, R. (2013) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog. 9, e1003690
Lee, K., Gu, S., Jin, L., Le, T. Tuc Nghi, Cheng, L. W., Strotmeier, J., Kruel, A. Magdalena, Yao, G., Perry, K., Rummel, A., and Jin, R. (2013) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog. 9, e1003690
Bae, B., Feklistov, A., Lass-Napiorkowska, A., Landick, R., and Darst, S. A. (2015) Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 10.7554/eLife.08504
Bae, B., Feklistov, A., Lass-Napiorkowska, A., Landick, R., and Darst, S. A. (2015) Structure of a bacterial RNA polymerase holoenzyme open promoter complex. Elife. 10.7554/eLife.08504
Li, W., Schulman, S., Dutton, R. J., Boyd, D., Beckwith, J., and Rapoport, T. A. (2010) Structure of a bacterial homologue of vitamin K epoxide reductase. Nature. 463, 507-12
Lai, Y. - T., Cascio, D., and Yeates, T. O. (2012) Structure of a 16-nm cage designed by using protein oligomers. Science. 336, 1129
York, N. J., Lockart, M. M., Sardar, S., Khadka, N., Shi, W., Stenkamp, R. E., Zhang, J., Kiser, P. D., and Pierce, B. S. (2021) Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center. J Biol Chem. 10.1016/j.jbc.2021.100492
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Tu, D., Zhu, Z., Zhou, A. Y., Yun, C. -hong, Lee, K. - E., Toms, A. V., Li, Y., Dunn, G. P., Chan, E., Thai, T., Yang, S., Ficarro, S. B., Marto, J. A., Jeon, H., Hahn, W. C., Barbie, D. A., and Eck, M. J. (2013) Structure and ubiquitination-dependent activation of TANK-binding kinase 1. Cell Rep. 3, 747-58
Tu, D., Zhu, Z., Zhou, A. Y., Yun, C. -hong, Lee, K. - E., Toms, A. V., Li, Y., Dunn, G. P., Chan, E., Thai, T., Yang, S., Ficarro, S. B., Marto, J. A., Jeon, H., Hahn, W. C., Barbie, D. A., and Eck, M. J. (2013) Structure and ubiquitination-dependent activation of TANK-binding kinase 1. Cell Rep. 3, 747-58
Vigdorovich, V., Ramagopal, U. A., Lázár-Molnár, E., Sylvestre, E., Lee, J. Sik, Hofmeyer, K. A., Zang, X., Nathenson, S. G., and Almo, S. C. (2013) Structure and T cell inhibition properties of B7 family member, B7-H3. Structure. 21, 707-17
Vigdorovich, V., Ramagopal, U. A., Lázár-Molnár, E., Sylvestre, E., Lee, J. Sik, Hofmeyer, K. A., Zang, X., Nathenson, S. G., and Almo, S. C. (2013) Structure and T cell inhibition properties of B7 family member, B7-H3. Structure. 21, 707-17
Nicoludis, J. M., Lau, S. - Y., Schärfe, C. P. I., Marks, D. S., Weihofen, W. A., and Gaudet, R. (2015) Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity. Structure. 23, 2087-98
Yang, T., Liu, Q., Kloss, B., Bruni, R., Kalathur, R. C., Guo, Y., Kloppmann, E., Rost, B., Colecraft, H. M., and Hendrickson, W. A. (2014) Structure and selectivity in bestrophin ion channels. Science. 346, 355-9
Wasmuth, E. V., Zinder, J. C., Zattas, D., Das, M., and Lima, C. D. (2017) Structure and reconstitution of yeast Mpp6-nuclear exosome complexes reveals that Mpp6 stimulates RNA decay and recruits the Mtr4 helicase. Elife. 10.7554/eLife.29062
Levin, E. J., Cao, Y., Enkavi, G., Quick, M., Pan, Y., Tajkhorshid, E., and Zhou, M. (2012) Structure and permeation mechanism of a mammalian urea transporter. Proc Natl Acad Sci U S A. 109, 11194-9
Horton, J. R., Nugent, R. L., Li, A., Mabuchi, M. Yamada, Fomenkov, A., Cohen-Karni, D., Griggs, R. M., Zhang, X., Wilson, G. G., Zheng, Y., Xu, S. - Y., and Cheng, X. (2014) Structure and mutagenesis of the DNA modification-dependent restriction endonuclease AspBHI. Sci Rep. 4, 4246
Li, H., Hwang, Y., Perry, K., Bushman, F., and Van Duyne, G. D. (2016) Structure and Metal Binding Properties of a Poxvirus Resolvase. J Biol Chem. 291, 11094-104
Dieck, C. L., Tzoneva, G., Forouhar, F., Carpenter, Z., Ambesi-Impiombato, A., Sanchez-Martin, M., Kirschner-Schwabe, R., Lew, S., Seetharaman, J., Tong, L., and Ferrando, A. A. (2018) Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. Cancer Cell. 34, 136-147.e6
Park, E., Kim, N., Ficarro, S. B., Zhang, Y., Lee, B. Il, Cho, A., Kim, K., Park, A. K. J., Park, W. - Y., Murray, B., Meyerson, M., Beroukhim, R., Marto, J. A., Cho, J., and Eck, M. J. (2015) Structure and mechanism of activity-based inhibition of the EGF receptor by Mig6. Nat Struct Mol Biol. 22, 703-711
Sanches, M., Duffy, N. M., Talukdar, M., Thevakumaran, N., Chiovitti, D., Canny, M. D., Lee, K., Kurinov, I., Uehling, D., Al-awar, R., Poda, G., Prakesch, M., Wilson, B., Tam, V., Schweitzer, C., Toro, A., Lucas, J. L., Vuga, D., Lehmann, L., Durocher, D., Zeng, Q., Patterson, J. B., and Sicheri, F. (2014) Structure and mechanism of action of the hydroxy-aryl-aldehyde class of IRE1 endoribonuclease inhibitors. Nat Commun. 5, 4202

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