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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
Sui, X., Weitz, A. C., Farquhar, E. R., Badiee, M., Banerjee, S., von Lintig, J., Tochtrop, G. P., Palczewski, K., Hendrich, M. P., and Kiser, P. D. (2017) Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Biochemistry. 56, 2836-2852
Miallau, L., Faller, M., Chiang, J., Arbing, M., Guo, F., Cascio, D., and Eisenberg, D. (2009) Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J Biol Chem. 284, 276-83
Fath, S., Mancias, J. D., Bi, X., and Goldberg, J. (2007) Structure and organization of coat proteins in the COPII cage. Cell. 129, 1325-36
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
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
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
Guo, X., Schmiege, P., Assafa, T. E., Wang, R., Xu, Y., Donnelly, L., Fine, M., Ni, X., Jiang, J., Millhauser, G., Feng, L., and Li, X. (2022) Structure and mechanism of human cystine exporter cystinosin. Cell. 185, 3739-3752.e18
Guo, X., Schmiege, P., Assafa, T. E., Wang, R., Xu, Y., Donnelly, L., Fine, M., Ni, X., Jiang, J., Millhauser, G., Feng, L., and Li, X. (2022) Structure and mechanism of human cystine exporter cystinosin. Cell. 185, 3739-3752.e18
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
Singh, M., Wang, Z., Cascio, D., and Feigon, J. (2015) Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1. J Mol Biol. 427, 807-23
Singh, M., Gonzales, F. A., Cascio, D., Heckmann, N., Chanfreau, G., and Feigon, J. (2009) Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem. 284, 1906-16
Trachman, R. J., Autour, A., C Y Jeng, S., Abdolahzadeh, A., Andreoni, A., Cojocaru, R., Garipov, R., Dolgosheina, E. V., Knutson, J. R., Ryckelynck, M., Unrau, P. J., and Ferré-D'Amaré, A. R. (2019) Structure and functional reselection of the Mango-III fluorogenic RNA aptamer. Nat Chem Biol. 15, 472-479
Geng, Y., Xiong, D., Mosyak, L., Malito, D. L., Kniazeff, J., Chen, Y., Burmakina, S., Quick, M., Bush, M., Javitch, J. A., Pin, J. - P., and Fan, Q. R. (2012) Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2. Nat Neurosci. 15, 970-8
Hubin, E. A., Fay, A., Xu, C., Bean, J. M., Saecker, R. M., Glickman, M. S., Darst, S. A., and Campbell, E. A. (2017) Structure and function of the mycobacterial transcription initiation complex with the essential regulator RbpA. Elife. 10.7554/eLife.22520
Feld, G. K., El-Etr, S., Corzett, M. H., Hunter, M. S., Belhocine, K., Monack, D. M., Frank, M., Segelke, B. W., and Rasley, A. (2014) Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host cell invasion. J Biol Chem. 289, 30668-30679
Feld, G. K., El-Etr, S., Corzett, M. H., Hunter, M. S., Belhocine, K., Monack, D. M., Frank, M., Segelke, B. W., and Rasley, A. (2014) Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host cell invasion. J Biol Chem. 289, 30668-30679
Patteson, J. B., Fortinez, C. Marie, Putz, A. T., Rodriguez-Rivas, J., L Bryant, H., Adhikari, K., Weigt, M., T Schmeing, M., and Li, B. (2022) Structure and Function of a Dehydrating Condensation Domain in Nonribosomal Peptide Biosynthesis. J Am Chem Soc. 144, 14057-14070
Dürr, K. L., Chen, L., Stein, R. A., De Zorzi, R., I Folea, M., Walz, T., Mchaourab, H. S., and Gouaux, E. (2014) Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states. Cell. 158, 778-792
Fan, J., and Pavletich, N. P. (2012) Structure and conformational change of a replication protein A heterotrimer bound to ssDNA. Genes Dev. 26, 2337-47
Barton, W. A., Liu, B. P., Tzvetkova, D., Jeffrey, P. D., Fournier, A. E., Sah, D., Cate, R., Strittmatter, S. M., and Nikolov, D. B. (2003) Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins. EMBO J. 22, 3291-302
Fraser, B. J., Beldar, S., Seitova, A., Hutchinson, A., Mannar, D., Li, Y., Kwon, D., Tan, R., Wilson, R. P., Leopold, K., Subramaniam, S., Halabelian, L., Arrowsmith, C. H., and Bénard, F. (2022) Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation. Nat Chem Biol. 10.1038/s41589-022-01059-7
Baytshtok, V., Fei, X., Grant, R. A., Baker, T. A., and Sauer, R. T. (2016) A Structurally Dynamic Region of the HslU Intermediate Domain Controls Protein Degradation and ATP Hydrolysis. Structure. 24, 1766-1777
Tuukkanen, A. T., Freire, D., Chan, S., Arbing, M. A., Reed, R. W., Evans, T. J., Zenkeviciutė, G., Kim, J., Kahng, S., Sawaya, M. R., Chaton, C. T., Wilmanns, M., Eisenberg, D., Parret, A. H. A., and Korotkov, K. V. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 10.1016/j.jmb.2018.11.003

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