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Sharma, H., Yu, S., Kong, J., Wang, J., and Steitz, T. A. (2009) Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding. Proc Natl Acad Sci U S A. 106, 16604-9
Sharkey, M. A., Oliveira, T. F., Engel, P. C., and Khan, A. R. (2013) Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases. FEBS J. 280, 4681-92
Shao, Y., Huang, H., Qin, D., Li, N. - S., Koide, A., Staley, J. P., Koide, S., Kossiakoff, A. A., and Piccirilli, J. A. (2016) Specific Recognition of a Single-Stranded RNA Sequence by a Synthetic Antibody Fragment. J Mol Biol. 428, 4100-4114
Shankar, S., Chew, T. Weng, Chichili, V. Priyanka R., Low, B. Chuan, and Sivaraman, J. (2024) Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP. Cell Mol Life Sci. 81, 216
Shang, J., Ye, G., Shi, K., Wan, Y., Luo, C., Aihara, H., Geng, Q., Auerbach, A., and Li, F. (2020) Structural basis of receptor recognition by SARS-CoV-2. Nature. 10.1038/s41586-020-2179-y
Shabdar, S., Anaclet, B., Castineiras, A. Garcia, Desir, N., Choe, N., Crane, E. J., and Sazinsky, M. H. (2021) Structural and Kinetic Characterization of Hyperthermophilic NADH-Dependent Persulfide Reductase from . Archaea. 2021, 8817136
Settembre, E. C., Dorrestein, P. C., Park, J. - H., Augustine, A. M., Begley, T. P., and Ealick, S. E. (2003) Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Biochemistry. 42, 2971-81
Serganov, A., Huang, L., and Patel, D. J. (2008) Structural insights into amino acid binding and gene control by a lysine riboswitch. Nature. 455, 1263-7
Seo, M., Kim, J. - D., Neau, D., Sehgal, I., and Lee, Y. - H. (2011) Structure-based development of small molecule PFKFB3 inhibitors: a framework for potential cancer therapeutic agents targeting the Warburg effect. PLoS One. 6, e24179
Senturia, R., Faller, M., Yin, S., Loo, J. A., Cascio, D., Sawaya, M. R., Hwang, D., Clubb, R. T., and Guo, F. (2010) Structure of the dimerization domain of DiGeorge critical region 8. Protein Sci. 19, 1354-65
Seidler, P. Matthew, Boyer, D. R., Murray, K. A., Yang, T. P., Bentzel, M., Sawaya, M. R., Rosenberg, G., Cascio, D., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., and Eisenberg, D. S. (2019) Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples. J Biol Chem. 294, 16451-16464
Seetharaman, S. V., Taylor, A. B., Holloway, S., and P Hart, J. (2010) Structures of mouse SOD1 and human/mouse SOD1 chimeras. Arch Biochem Biophys. 503, 183-90
Seegar, T. C. M., Killingsworth, L. B., Saha, N., Meyer, P. A., Patra, D., Zimmerman, B., Janes, P. W., Rubinstein, E., Nikolov, D. B., Skiniotis, G., Kruse, A. C., and Blacklow, S. C. (2017) Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.. Cell. 171, 1638-1648.e7
Scrima, A., Konícková, R., Czyzewski, B. K., Kawasaki, Y., Jeffrey, P. D., Groisman, R., Nakatani, Y., Iwai, S., Pavletich, N. P., and Thomä, N. H. (2008) Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell. 135, 1213-23
Scott, D. C., Sviderskiy, V. O., Monda, J. K., Lydeard, J. R., Cho, S. Ei, J Harper, W., and Schulman, B. A. (2014) Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8. Cell. 157, 1671-84
Sciara, G., Clarke, O. B., Tomasek, D., Kloss, B., Tabuso, S., Byfield, R., Cohn, R., Banerjee, S., Rajashankar, K. R., Slavkovic, V., Graziano, J. H., Shapiro, L., and Mancia, F. (2014) Structural basis for catalysis in a CDP-alcohol phosphotransferase. Nat Commun. 5, 4068
Schureck, M. A. (2016) Structural and Functional Studies of a Toxin-Antitoxin System Involved in Translational Inhibition. Ph.D. thesis, Emory University, Atlanta, Georgia, PhD, 273
Schureck, M. A., Meisner, J., Hoffer, E. D., Wang, D., Onuoha, N., Cho, S. Ei, Lollar, P., and Dunham, C. M. (2019) Structural basis of transcriptional regulation by the HigA antitoxin. Mol Microbiol. 10.1111/mmi.14229
Schureck, M. A., Maehigashi, T., Miles, S. J., Marquez, J., Cho, S. Ei, Erdman, R., and Dunham, C. M. (2014) Structure of the Proteus vulgaris HigB-(HigA)2-HigB toxin-antitoxin complex. J Biol Chem. 289, 1060-70
Schuhmacher, M. Kirstin, Beldar, S., Khella, M. S., Bröhm, A., Ludwig, J., Tempel, W., Weirich, S., Min, J., and Jeltsch, A. (2020) Sequence specificity analysis of the SETD2 protein lysine methyltransferase and discovery of a SETD2 super-substrate. Commun Biol. 3, 511
Schuermann, J. P., Tan, A., Tanner, J. J., and Henzl, M. T. (2010) Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states. J Mol Biol. 397, 991-1002
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2013) Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 1328-34
Schmier, B. J., Nelersa, C. M., and Malhotra, A. (2017) Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA. Sci Rep. 7, 11085
Schmidt, F. I., Lu, A., Chen, J. W., Ruan, J., Tang, C., Wu, H., and Ploegh, H. L. (2016) A single domain antibody fragment that recognizes the adaptor ASC defines the role of ASC domains in inflammasome assembly. J Exp Med. 213, 771-90
T Schmeing, M., Moore, P. B., and Steitz, T. A. (2003) Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit. RNA. 9, 1345-52

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