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Tararina, M. A., Yee, D. A., Tang, Y., and Christianson, D. W. (2022) Structure of the Repurposed Fungal Terpene Cyclase FlvF Implicated in the C-N Bond-Forming Reaction of Flavunoidine Biosynthesis. Biochemistry. 10.1021/acs.biochem.2c00335
Tao, Y., Cheung, L. S., Li, S., Eom, J. - S., Chen, L. - Q., Xu, Y., Perry, K., Frommer, W. B., and Feng, L. (2015) Structure of a eukaryotic SWEET transporter in a homotrimeric complex. Nature. 527, 259-263
Tang, H., Demir, Ö., Kurniawan, F., Brown, W. L., Shi, K., Moeller, N. H., Carpenter, M. A., Belica, C., Orellana, K., Du, G., LeBeau, A. M., Amaro, R. E., Harris, R. S., and Aihara, H. (2021) Structural Characterization of a Minimal Antibody against Human APOBEC3B. Viruses. 10.3390/v13040663
Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., and Tyers, M. (2007) Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Cell. 129, 1165-76
Tanaka, S., Sawaya, M. R., and Yeates, T. O. (2010) Structure and mechanisms of a protein-based organelle in Escherichia coli. Science. 327, 81-4
Tabackman, A. A., Frankson, R., Marsan, E. S., Perry, K., and Cole, K. E. (2016) Structure of 'linkerless' hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket. J Struct Biol. 195, 373-378
Taabazuing, C. Y., Fermann, J., Garman, S., and Knapp, M. J. (2016) Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.. Biochemistry. 55, 277-86
T, R., Sharma, D., Lin, F., Choong, Y. Khai, Lim, C., Jobichen, C., and Zhang, C. (2023) Structural Understanding of Fungal Terpene Synthases for the Formation of Linear or Cyclic Terpene Products. ACS Catal. 13, 4949-4959
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Sysoeva, T. A., Bane, L. B., Xiao, D. Y., Bose, B., Chilton, S. S., Gaudet, R., and Burton, B. M. (2015) Structural characterization of the late competence protein ComFB from Bacillus subtilis. Biosci Rep. 10.1042/BSR20140174
Syroegin, E. A., Aleksandrova, E. V., and Polikanov, Y. S. (2022) Structural basis for the inability of chloramphenicol to inhibit peptide bond formation in the presence of A-site glycine. Nucleic Acids Res. 50, 7669-7679
Syroegin, E. A., Flemmich, L., Klepacki, D., Vázquez-Laslop, N., Micura, R., and Polikanov, Y. S. (2022) Structural basis for the context-specific action of the classic peptidyl transferase inhibitor chloramphenicol. Nat Struct Mol Biol. 29, 152-161
Swofford, C. A., Nordeen, S. A., Chen, L., Desai, M. M., Chen, J., Springs, S. L., Schwartz, T. U., and Sinskey, A. J. (2022) Structure and Specificity of an Anti-Chloramphenicol Single Domain Antibody for Detection of Amphenicol Residues. Protein Sci. 10.1002/pro.4457
Svetlov, M. S., Syroegin, E. A., Aleksandrova, E. V., Atkinson, G. C., Gregory, S. T., Mankin, A. S., and Polikanov, Y. S. (2021) Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance. Nat Chem Biol. 10.1038/s41589-020-00715-0
Sung, R. - J., Zhang, M., Qi, Y., and Verdine, G. L. (2012) Sequence-dependent structural variation in DNA undergoing intrahelical inspection by the DNA glycosylase MutM. J Biol Chem. 287, 18044-54
Sung, R. - J., Zhang, M., Qi, Y., and Verdine, G. L. (2013) Structural and biochemical analysis of DNA helix invasion by the bacterial 8-oxoguanine DNA glycosylase MutM. J Biol Chem. 288, 10012-23
Sun, X. - J., Wang, Z., Wang, L., Jiang, Y., Kost, N., T Soong, D., Chen, W. - Y., Tang, Z., Nakadai, T., Elemento, O., Fischle, W., Melnick, A., Patel, D. J., Nimer, S. D., and Roeder, R. G. (2013) A stable transcription factor complex nucleated by oligomeric AML1-ETO controls leukaemogenesis. Nature. 500, 93-7
Sun, J., Paduch, M., Kim, S. - A., Kramer, R. M., Barrios, A. F., Lu, V., Luke, J., Usatyuk, S., Kossiakoff, A. A., and Tan, S. (2018) Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2. Proc Natl Acad Sci U S A. 10.1073/pnas.1805343115
Sukumar, N., Dewanti, A., Merli, A., Rossi, G. Luigi, Mitra, B., and F Mathews, S. (2009) Structures of the G81A mutant form of the active chimera of (S)-mandelate dehydrogenase and its complex with two of its substrates. Acta Crystallogr D Biol Crystallogr. 65, 543-52
Sukumar, N., Liu, S., Li, W., Mathews, F. S., Mitra, B., and Kandavelu, P. (2018) Structure of the monotopic membrane protein (S)-mandelate dehydrogenase at 2.2Å resolution.. Biochimie. 10.1016/j.biochi.2018.07.017
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
Sudhamsu, J., Lee, G. In, Klessig, D. F., and Crane, B. R. (2008) The structure of YqeH. An AtNOS1/AtNOA1 ortholog that couples GTP hydrolysis to molecular recognition. J Biol Chem. 283, 32968-76
Su, C. - C., Bolla, J. Reddy, Kumar, N., Radhakrishnan, A., Long, F., Delmar, J. A., Chou, T. - H., Rajashankar, K. R., Shafer, W. M., and Yu, E. W. (2015) Structure and function of Neisseria gonorrhoeae MtrF illuminates a class of antimetabolite efflux pumps. Cell Rep. 11, 61-70
Su, C. - C., Klenotic, P. A., Cui, M., Lyu, M., Morgan, C. E., and Yu, E. W. (2021) Structures of the mycobacterial membrane protein MmpL3 reveal its mechanism of lipid transport. PLoS Biol. 19, e3001370
Su, M., Gao, F., Yuan, Q., Mao, Y., Li, D. - L., Guo, Y., Yang, C., Wang, X. - H., Bruni, R., Kloss, B., Zhao, H., Zeng, Y., Ben Zhang, F. -, Marks, A. R., Hendrickson, W. A., and Chen, Y. - H. (2017) Structural basis for conductance through TRIC cation channels. Nat Commun. 8, 15103
Su, C. - C., Yin, L., Kumar, N., Dai, L., Radhakrishnan, A., Bolla, J. Reddy, Lei, H. - T., Chou, T. - H., Delmar, J. A., Rajashankar, K. R., Zhang, Q., Shin, Y. - K., and Yu, E. W. (2017) Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump. Nat Commun. 8, 171

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